sequence
stringlengths
13
8.92k
annotation
listlengths
2
214
description
stringlengths
61
12.1k
labels
int64
0
0
MTNLNATVAAVLVMLAFLAGQSVAGRYYYDKVQDKVRKEVEKAMAKNPSVGPALVRLVFHDCWVYGCDGSVLLDSTPTDGTNTEKKAANNIGLAGFEVIDAIKQKVGTDASCADIVAFAARDAADILSGGKIFYTIPGGRKDGVVSSAAVADANLPHPDFNFDELKDNFNASSRGSSFTVEELVVLSGAHSIGVAHLSSYQDRLGPDSTPIDSDYQEALNKATPPGLLKTGQNPTVTNNVRDETDAFQKDAAYNPVAMGVNPKRGVLDNSYYHNNLVNKVLFKSDWVLRTDDFAASKLDEYKNNPAEWNSDFAAAMVKLSSLPAQGNKLEIRKNCRVPNPQY
[ 507, 8530, 8552, 14337, 24878, 25223, 28462, 30838, 32536, 35522, 36624, 37616, 44655, 52283, 52284, 62128, 86995, 87080, 87244, 87413, 87541, 87599, 87678, 87767, 87873, 87893, 87976, 88008, 88038, 88058 ]
The following text describes a protein: Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. Subcellular Localization: Secreted.
0
MIYPQIMHKPALPWVFRRPTQEDGLSIHELIAQCAPLDQNSAYCNFLQSSHFQTTCLMAEQQELLVGFVSAYRKPEQQNELFIWQVAVHPSARGKGLAYQMLKHLLAREDLADITVLETTITRSNQASWRLFQKLDREQGEQGSVSTFLDETCHFEGEHDTEYLYRIPLQSSN
[ 2519, 11089, 30304, 31485, 36091, 46671, 49230, 87125, 88008, 88153 ]
The following text describes a protein: Function: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A.
0
MAPKKNSAKRPQPSTPKPSAPARIVKVQSSDGHILQADVRALLLSSTLAATIKGYDDENKPLEKLEVNNVVGFTLKLVLEWCEKHKEDDPAIAQAEKDKKNIFIPSWDRHFLTKLPMGNLFDLITAAYHLDITGLINYGCKTVANSAKGKSTEEMRELFGIPEPWEQPSTSTATWDD
[ 10753, 11951, 24917, 24978, 34681, 36964, 45551, 49150, 49151, 49850, 64062, 88008, 88181 ]
The following text describes a protein: Function: Probable essential component of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Regulates cell proliferation during embryonic and larval development.
0
MTEETPGFEEKPDVPSGATPDDAEPQAASEEGAAPAGDASENAGLVAQLDQVRTALNERTADLQRLQAEYQNYRRRVERDRVAVKEVAVANLLSELLPVLDDVGRAREHGELVGGFKSVAESLETTVAKLGLQQFGKEGEPFDPTIHEALMHSYAPDVTETTCVAILQPGYRIGERTIRPARVAVAEPQPGAQTVKPAEDAAEAQDSSGAEDDAGTKESGGPDEG
[ 8171, 24978, 27715, 32074, 33730, 33731, 36550, 43590, 47548, 87285, 87367, 88008, 88086 ]
The following text describes a protein: Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Subcellular Localization: Cytoplasm.
0
MVRIVPSARRTRAPAKLDGRSTPDIAMSLVTTASPLTTADTYTPAADSDAPPAVRGELVINLPMRHAGQRELRLRYELVGAEQAPVVFVAGGISAHRHLAASAVFPEKGWVEGLVGAGRALDPASRRLLAFDFLGADGSLDAPIDTADQADAIAALLDALGIARLHGFVGYSYGALVGLQFASRHAARLHTLVAVSGAHRAHPYAAAWRALQRRAVALGQLQCAEHHGLALARQFAMLSYRTPEEFSERFDAPPELINGRVRVAAEDYLDAAGAQYVARTPVNAYLRLSESIDLHRIDPAAVAVPTVVVAVEGDRLVPLADLVSLVEGLGPRGSLRVLRSPFGHDAFLKEIDRIDAILTTALRTTGETA
[ 2671, 9155, 24978, 28315, 29516, 36010, 42940, 59224, 87125, 87143, 87367, 87774, 88008, 88153 ]
The following text describes a protein: Function: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. Subcellular Localization: Cytoplasm.
0
MEKVKAWLIKYKWWIVAAIGGLAAFLLLKNRGGGSGGGGEYMVGSGPVYQQAGSGAVDNTMALAALQANTQLSAQNAQLQAQMDASRLQLETQLNIETLAADNAHYSTQSQLQLGMAQVDLSKYLGDLQSTTSTALAGMQSDTAKYQSNIQLQAENIRANTSLAEIDAQKYIVGKQADIAKYQAKTERRGQDYGFALGLLNFGGKFF
[ 15813, 25325, 26123, 26481, 87254, 87326, 87411, 87760, 88008, 88159, 88161, 88207, 88220, 88237, 88242 ]
The following text describes a protein: Function: Component of the phage ejection machinery. Pilot protein for the formation of the tube that conducts the genome into the target cell. Probably involved in penetration of the bacterial outer membrane and for making the peptidoglycan layer accessible to the viral transglycosylase. Essential for viral infectivity. Subcellular Localization: Virion membrane; Single-pass membrane protein. Note=Part of the capsid inner membrane.
0
MHNYKLTIQYDGARFKGWQRLGNNDNTIQGKIESVISEMVGKEIEIIGCSRTDAGVHALNQVANFQSDEKLVEHKVKKYLNQYLPNDISITNVEEVHDRFHARYNSKAKTYLYKIWNEEHTNPFMRKYSMHVNKKLNVKSMKAAAKHLVGSHDFTAFSNAKSKKKSMVREVYTLDVMEEAGFVQIRVSGNGFLHNMVRKIVGALIEVGLGQLDAEAIPNILEEKQRNQINCLAEASGLYLENVEF
[ 6178, 11933, 27925, 29669, 35682, 37115, 52557, 52558, 52559, 52563, 87683, 88008, 88278 ]
The following text describes a protein: Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
0
MDTSSVGGLELTDQTPVLLGSTAMATSLTNVGNSFSGPANPLVSRSNKFQNSSVEDDDDVVFIEPVQPPPPSVPVVADQRTITFTSSKNEELQGNDSKITPSSKELASQKGSVSETIVIDDEEDMETNQGQEKNSSNFIERRPPETKNRTNDVDFSTSSFSRSKVNAGMGNSGITTEPDSEIQIANVTTLETGVSSVNDGQLENTDGRDMNLMITHVTSLQNTNLGDVSNGLQSSNFGVNIQTYTPSLTSQTKTGVGPFNPGRMNVAGDVFQNGESATHHNPDSWISQSASFPRNQKQPGVDSLSPVASLPKQIFQPSVQQQPTKPVKVTCANCKKPLQKGQTAYQRKGSAHLFCSTTCLSSFSHKPAPKKLCVMCKKDITTMKGTIVAQVDSSESFQEFCSTSCLSLYEDKQNPTKGALNKSRCTICGKLTEIRHEVSFKNMTHKLCSDHCFNRYRMANGLIMNCCEQCGEYLPSKGAGNNVLVIDGQQKRFCCQSCVSEYKQVGSHPSFLKEVRDHMQDSFLMQPEKYGKLTTCTGCRTQCRFFDMTQCIGPNGYMEPYCSTACMNSHKTKYAKSQSLGIICHFCKRNSLPQYQATMPDGKLYNFCNSSCVAKFQALSMQSSPNGQFVAPSDIQLKCNYCKNSFCSKPEILEWENKVHQFCSKTCSDDYKKLHCIVTYCEYCQEEKTLHETVNFSGVKRPFCSEGCKLLYKQDFARRLGLRCVTCNYCSQLCKKGATKELDGVVRDFCSEDCCKKFQDWYYKAARCDCCKSQGTLKERVQWRGEMKHFCDQHCLLRFYCQQNEPNMTTQKGPENLHYDQGCQTSRTKMTGSAPPPSPTPNKEMKNKAVLCKPLTMTKATYCKPHMQTKSCQTDDTWRTEYVPVPIPVPVYIPVPMHMYSQNIPVPTTVPVPVPVPVFLPAPLDSSEKIPAAIEELKSKVSSDALDTELLTMTDMMSEDEGKTETTNINSVIIETDIIGSDLLKNSDPETQSSMPDVPYEPDLDIEIDFPRAAEELDMENEFLLPPVFGEEYEEQPRPRSKKKGAKRKAVSGYQSHDDSSDNSECSFPFKYTYGVNAWKHWVKTRQLDEDLLVLDELKSSKSVKLKEDLLSHTTAELNYGLAHFVNEIRRPNGENYAPDSIYYLCLGIQEYLCGSNRKDNIFIDPGYQTFEQELNKILRSWQPSILPDGSIFSRVEEDYLWRIKQLGSHSPVALLNTLFYFNTKYFGLKTVEQHLRLSFGTVFRHWKKNPLTMENKACLRYQVSSLCGTDNEDKITTGKRKHEDDEPVFEQIENTANPSRCPVKMFECYLSKSPQNLNQRMDVFYLQPECSSSTDSPVWYTSTSLDRNTLENMLVRVLLVKDIYDKDNYELDEDTD
[ 15387, 24917, 25040, 25366, 29166, 31138, 44874, 45298, 53889, 76937, 87139, 87305, 87412, 87667, 87684, 87767, 87857, 87914, 87976, 88008, 88009, 88148, 88150, 88180, 88261, 88263 ]
The following text describes a protein: Function: Involved in the negative regulation of transcription. Subcellular Localization: Nucleus.
0
MDGSNLTSDGQKELQTFLNFFNLKKQEAMREIELEFKDFSKFQVQDTLYNKDDVQELFKKLEGSLEVLMNKEVSKIIYMCGVYVKIFLSVCSDQDFHADFNFIENVKIIEQMKILEKGGTIVEDKPLQSKVRYSRLPTLDTALQKQMEETVKENDFLKQYNQKLQNELVVLKKEQVQDADQVGSFQDQINQLKQENQQLKQEMEKKLNDCVQFKTLKQMIQEKNQQIKELQMKLQ
[ 22584, 24978, 57513, 87326, 87367, 88008 ]
The following text describes a protein: Function: Regulates ciliary localization of the BBSome complex. Together with the BBSome complex, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. May play a role in neurite outgrowth. May have tumor suppressor function. Subcellular Localization: Cytoplasm.
0
MKDFGSAMLLALETNDHCIQTIRELGEKAEAADAPGNELLQLARWLRAAILGANDRLLSTTSLMLGVNAARDDRQSMVFSGIAGALAGALSMAVGEFVSEAICEEEALPNPYKATAASALAFLCGSLFPLLPAIFVAQHTLRVVIVMVVASVKICLKFESNVKFRIFRIGYVADVRN
[ 11585, 25001, 25325, 28986, 28987, 35350, 42937, 87676, 87678, 87680, 87760, 88159, 88161, 88162, 88186 ]
The following text describes a protein: Function: Vacuolar Fe(2+) uptake transporter. Subcellular Localization: Vacuole membrane; Multi-pass membrane protein.
0
MAKTKYGERHRKGLWSPEEDEKLRSFILSYGHSCWTTVPIKAGLQRNGKSCRLRWINYLRPGLKRDMISAEEEETILTFHSSLGNKWSQIAKFLPGRTDNEIKNYWHSHLKKKWLKSQSLQDAKSISPPSSSSSSLVACGKRNPETLISNHVFSFQRLLENKSSSPSQESNGNNSHQCSSAPEIPRLFFSEWLSSSYPHTDYSSEFTDSKHSQAPNVEETLSAYEEMGDVDQFHYNEMMINNSNWTLNDIVFGSKCKKQEHHIYREASDCNSSAEFFSPSTTT
[ 9337, 9367, 9596, 15388, 24917, 25367, 27904, 27918, 36776, 43624, 50779, 77605, 87123, 87384, 87857, 87923, 88008, 88009, 88148, 88150, 88180 ]
The following text describes a protein: Function: Transcription factor that promotes photomorphogenesis in the light by participating in the transmission of phytochrome A (phyA) signals to downstream responses. Probably acts by activating expression of light-induced genes. In darkness, its degradation prevents the activation of light-induced genes. Subcellular Localization: Nucleus speckle.
0
MGAGTLLNGLEKENFPNNIHSDLPAYPNMDSQEDGNTSKESKRNSPVKQKSQKDEEKSSKMGTASNIFHENKDIHERSEHTDDFNDGLKLAPDSSPSLKECQFKNWESFWCNTEGYKTKHMQPFHFTSGLEEIKEPVMELNISTSPYKGQRPNSAPTEYSAATTAFTKTQLEVSFLKTNLLTYIKKEIDICLSSVPFFDDAVQMQKKFLEYRDIDLDEEYELKILGELLNDLNFFHMQENSLLNRELAVRRFSNQPESQNLPSIRDFRNPLLPIDNRPSPPLGLKRNGKSFEETYDFTSNTSNFWGEKAELQNSITGGTPYFFHPNNIHQTKPFMSFENQNELLFQRKNSDYKQHFNSGRNIHNGVESKSYRGVGLNDSYQKGYAAMTKSFGNIDLNRMPRRSNEEMYSWSRN
[ 11729, 24978, 25029, 26049, 28885, 87367, 87371, 88008, 88074 ]
The following text describes a protein: Function: Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. Probable component of a core structural unit of the scaffold that initiates synthesis of the prospore membrane. Subcellular Localization: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Localizes to the meiotic outer plaque of the spindle pole body (SPB), at the end of the meiotic spindles.
0
MPTAVNVAKQCLTAEASYALEEAVNVARRRGHSQTTSLHAISALLSLPTSVLRDACARVRNSAYSPRLQFKALDLCLSVSLDRIQSGHQLGSDDSPPVSNSLMAAIKRSQAHQRRLPENFRIYQEMSQSQNQNSLSCVKVELRQLILSILDDPVVSRVFGEAGFRSSELKLSIIRPVPHLLRYSSQQPLFLCNLTGNPEPNPVRWGFTVPSLNFNGDLDYRRISAVFTKDKGRNPLLVGVSAYGVLTSYLNSLEKNQTDGMILPTKLHGLTAVNIGSEISDQISVKFDKTYTDTRFHDLGKLAEQGSGPGLLLHYGDLRVFTNGEGNVPAANYIVNRISELLRRHGRRVWLIGATTSNEVYEKMMRRFPNVEKDWDLQLLTITSLKPCLPHNKSSLIGSFVPFGGFFSTTPSELKLPFSGFKTEITGPVSSISDQTQSTLPPWLQMTTRTDLNQKSSAKVVQTKEGLESVCGNKFTSSASASTCSAKSVTTDLNLRVSSVTTGSGLKKHLDSKDFSQPQSVSSYSFDNPRDLNAESFKIIYRRLTDMVSGQDEAARVISCALSQPPKSVTRRDVWLNLVGPDTVGKRRMSLVLAEIVYQSEHRFMAVDLGAAEQGMGGCDDPMRLRGKTMVDHIFEVMCRNPFCVVFLENIEKADEKLQMSLSKAIETGKFMDSHGREVGIGNTIFVMTSSSQGSATTTSYSEEKLLRVKGRQVEIRIETVSSLPMVRSVYGPTSVNKRKLMGLGNLQETKDTVESVKRLNRTTNGVLDLNLPAQETEIEEKYHCEENSNVWLMNLKNHKRLIEVPFKPFDFEGLAEKIKKSVKENFDKCVRSDCLLEVDPKIIERLLAAVYFSDSRKDIKELLENIMSPVFLRIKERYEITTSCVVKLVGRDLDIFLEDQMDLFFVKSQ
[ 22035, 24917, 29033, 30398, 39175, 39366, 58239, 64371, 77303, 87139, 87857, 88008, 88009, 88148, 88150, 88180 ]
The following text describes a protein: Function: Probable component of a transcriptional corepressor complex involved in branching control. Regulates cotyledon expansion and lateral root growth, but not germination or hypocotyl elongation. Promotes auxin transport and PIN1 accumulation in the stem and represses BRC1/TCP18 expression in axillary buds. Subcellular Localization: Nucleus. Domain: Contains 1 EAR motif required for the interaction with TPR2.
0
MDEVQMETARIQSPKSYLYTTLATTHLGEIASCIISILISNGRLTAREISNRTKIPTKNIKSALVSLIQLNCIYYWQEEKDRKFYYSLKETGLLLFVYSGDIINHIKRQYGEDEAEIIQNILIHGHVKIEDYLTQFNHDKSMKIDQENKFLKLFNDNWLIKLQDYHFHSLDDIWHKIFEECLKDTPRSSVTSEIKRVAEAQAKAKVKLNTLLESGTTGGGDIFTEVNGMKKLKPDLVVTFNLSRFQKHLRTNAFVNMVRSKIGVLTAIVYDAALRYIENKSPPMDYPLLDIPGLINDPKDVKEYILSIENKLVNEKKITFSARDIQRLLPKDIDFKNSVITPTFAKPKRPLENGSSPTLKKIKLEDGIASSTSTSTSTSSSTSSNGTSIDLNTLEQHLKLLLNGTNTAFVNEISPGNYTIPFSHLTNILKQNNFEALVKATLGDYAFRILRCVKSMKLCDEKSICNGALLKEKTVRSELYHLIKANIIEIQEVPRSADRAASKTFYLFRHKSNSNFNYLKNCLIYDMAEILNRIQDFKLEHKILLEKYKLVEGQEDQYLLDRELKLLNDLQLREIKNLVKFQRIKSLYSLYSLVD
[ 8118, 8119, 14372, 24935, 27917, 28007, 43422, 47023, 64146, 64148, 67047, 80724, 87386, 87857, 88008, 88148, 88261 ]
The following text describes a protein: Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs (By similarity). Subcellular Localization: Nucleus.
0
MNEFSILCRVLGSLYYRQPQDPLLVPLFTLIREGKLAANWPLEQDELLTRLQKSCDMTQVSADYNALFIGDECAVPPYRSAWVEGATEAEVRAFLSERGMPLADTPADHIGTLLLAASWLEDQSTEDESEALETLFSEYLLPWCGAFLGKVEAHATTPFWRTMAPLTRDAISAMWDELEEDSEE
[ 8549, 16923, 19168, 24978, 25040, 53022, 57609, 64167, 75944, 87285, 88008 ]
The following text describes a protein: Function: Acts as a chaperone that increases YcdX activity, maybe by facilitating the correct insertion of the zinc ions into the catalytic site of YcdX. Involved in the swarming motility process. Miscellaneous: MISCELLANEOUS: Does not bind zinc.
0
MGENEDEKQTQAGQLFENFVQASTCKGTLQAFNILTRQLDLDPLDHRNFYSKLKSKVTTWKAKALWYKLDKRGSHKEYKRGRSCMNTKCLIIGGGPCGLRTAIELAYLGAKVVVVEKRDTFSRNNVLHLWPFTIHDLRGLGAKKFYGKFCAGSIDHISIRQLQLILFKVALILGVEIHVNVEFVKVLEPPEDQENQKIGWRAEFLPVDHSLSEFEFDVIIGADGRRNTLEGFRRKEFRGKLAIAITANFINRNSTAEAKVEEISGVAFIFNQKFFQDLKKETGIDLENIVYYKDCTHYFVMTAKRQSLLDKGVIINDYTDTETLLRAENVNQDNLLSYAREAADFATNYQLPSLDFAMNHYGQPDVAMFDFTSMYASENAALVRERQSHLLLVALVGDSLLEPFWPMGTGCARGFLAAFDTAWMVKSWDQGTSPLELLAERESLYRLLPQTTPENINKNFEQYTLDPATRYPNLNSNNIKPNQVKHLYITKELHQYPLERLGSVRRSVGLSRRESDVRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPDLINFDSLNEDHAVENNQLAFDVAEREFGIAPVITGKEMASAQEPDKLSMVMYLSKFYELFRGTPLRPVDSWRKNYEENADLGLAKSSIPHHYLNLTFPRKRTPRVDSRTEENDMNKRRRKGFNNLHEPSAFSSQSLGSNQEGIKEGGNQNKVKSMASQLLAKFEESSRNPSILRQEHRVSGIGKPILRSSSDPPVNSRCPKPEEPTPSPSPPLKRQFPSVVVTGHVLRELKQVSAGGECPARPWRARAKSDLQLGGPENLASLPPTCPGALALSGVLRRLQQVEEKVLQKRAQNLANREFHKKNIKEKAAHLASMFGHGDFPQNKLLSKSLSHTHPPSSPSCLPSPDSAATSSPSTVDSVSPARKLTVGKVSSGIGAAAEVLVNLYLNDHRPKTQATSPDLESVRKTFPLNVGGSDTCYFCKKRVYVMERLSAEGRFFHRECFRCSVCATTLHLATYAFDVDEGKFFCKPHFIHCKTNSQQRKRRAELKQQKEEEGMWKEQEAARRDPPSESSCAAAAIATPEGSPPDEPTSPKKPKSIPEPEPGDVAGGAASPLPSEWTAVRISPGEDVVGQDVLAVRVLVTSDDSSSDAELDRGDSEASSVEPFDERPQQPELQLPPLLKPFTRHSSLREALPRAVSPHDLGEPEAEPALQRANSFQCPTPSEYQSGRRFQSNFMPVNSKMTVSPPKQACPPPPSPSPPSSSSIGDLNALDSPSLPQVTVSNTASQISRGHCSPSTPIFLRRAKAHGPPKDLPLRLPRGQVLERTEYCLVRPGGNGLQSSRPPSPTEMASDGCQEAVAPPRDIRSIHRGPHPVEGKDRCLPDHPLSPWAGEEPGEGSTRPRRVEDGGLELAEEKSGLKKLVLTPEQKTWLLDWNDSNLENLYLETGARLSQKSTRNGSGGHVLKPVHPLLLPLAEKETLPAQRQSQEKMGAPAERAPGERSMAPPKSPLRLIANAIRRSLEPLLPNSDSGRKAWAKPESKTLPTSPPHAYTCSFSFRKSSSSKDSDQPSPKRDVASKASAFFSLGSPTARTAQPSAPSPPAPALCTHSLPSRSSKVFPALVPPPCGKMEDVPTLLEKVSLQETVPDASRVPKKRTSLFSSFRLKDKSFESSLQESGPRKDSQDLFSSPKGKVQPMGNAQPPEKQGQPISSTCLGQRVHPVSPEKDASPTHVPIRAQGTGTVSSTSSSTTSSADEEFHPQPSSRSKERKALRRRRKLEKATKQLVKQEELKRLHKAQAIQRQLEEVEEQQRAFEIQGVRLEKALRGEAADSGTQDEAQLLQEWLKLVLEKNKLMRYESELLIM
[ 826, 7090, 8570, 8912, 11056, 11596, 15427, 24917, 24978, 27940, 30200, 30280, 32536, 34431, 35287, 37370, 37423, 38355, 54668, 63960, 64602, 76195, 87004, 87118, 87367, 87455, 87470, 87700, 87767, 87809, 87823, 87857, 87873, 87914, 88008, 88261 ]
The following text describes a protein: Function: Methionine monooxygenase that promotes depolymerization of F-actin by mediating oxidation of residues 'Met-44' and 'Met-47' on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization (By similarity). Regulates the disassembly of branched actin networks also by oxidizing ARP3B-containing ARP2/3 complexes leading to ARP3B dissociation from the network. Acts as a key regulator of the SRF signaling pathway elicited by nerve growth factor and serum: mediates oxidation and subsequent depolymerization of nuclear actin, leading to increase MKL1/MRTF-A presence in the nucleus and promote SRF:MKL1/MRTF-A-dependent gene transcription. Does not activate SRF:MKL1/MRTF-A through RhoA (By similarity). Subcellular Localization: Nucleus. Cytoplasm. Domain: The C-terminal RAB-binding domain (RBD) (1796-1945), also described as bivalent Mical/EHBP Rab binding (bMERB) domain, mediates binding to predominantly RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound forms).
0
MAAAAQLSLTQLSSGNPVYEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLNKQEFFIALRLVACAQNGLEVSLSSLNLAVPPPRFHDSSSPLLTSGTSVAELPWAVKSEDKAKYDAIFDSLSPVDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKEPVPMSLPPALVPPSKRKTVSISGSMWAIPSSAAKESYHSLPPVGISPTKAPLRQWVVSPAEKAKYDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSTLLAHIWALCDTKNCGKLSKDQFALAFHLINQKLIKGIDPPHSLTPEMIPPSDKSSLQKNTIGSSPVADFSAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLISSLKAEITSQESQISTYEEELSKAREELSRLQQETAQLEESVESGKAQLEPLQQHLQDSQQEISSMQMRLAMKDLETDNNQSNWCSSPQSILVNGAADYCSLSTSSSETANLNEHAEGQNNLESEPIHPESSVRSSPEIAPSDVTDESEVVTAADIEKVSPRFDDDKHSKEEDPFNVESSSLTDAVADTNLDFFQSDPFVGSDPFKDDPFGKIDPFGGDPFKGSDPFASDCFFKQTSTDPFATSSTDPFSASSNSSNTSVETWKHNDPFAPGGTVVAATDSATDPFASVFGNESFGDGFADFSTLSKVSNEDPFNPTISSSASSVVIPKPVLEETPSKSEDVPPALPPKTGTPTRPCPPPPGKRPINKLDSSDPFKLNDPFQPFPGNDSPKEKDPDMFCDPFTSSSTTANKEAEPSNFANFSAYPSEEDMIEWAKRESEREEEQRLARLNQQEQEDLELAIALSKSEISEA
[ 7073, 8497, 8499, 10672, 10919, 12331, 12523, 14078, 15813, 16036, 18324, 20405, 24978, 24997, 25040, 25079, 25093, 25275, 25332, 25337, 25463, 25472, 25476, 25696, 26413, 26499, 27068, 27093, 29025, 30483, 31013, 31137, 32073, 32130, 36158, 37640, 39128, 46081, 51011, 87115, 87244, 87276, 87318, 87367, 87430, 87434, 87760, 87767, 87914, 87974, 87976, 88008, 88009, 88032, 88162, 88180 ]
The following text describes a protein: Function: Involved in cell growth regulation. May be involved in the regulation of mitogenic signals and control of cell proliferation. Involved in the internalization of ligand-inducible receptors of the receptor tyrosine kinase (RTK) type, in particular EGFR. Plays a role in the assembly of clathrin-coated pits (CCPs). Acts as a clathrin adapter required for post-Golgi trafficking. Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2. Subcellular Localization: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, clathrin-coated pit.
0
MFVKNFIHKLKELKQKSLDKFANLLYDYGGYVYDRPCTFIICSLICCLLLTCGFYFKEHEKDIYKLYSISNSYAYETNETINDFFYKSRRCFILVESNVNLLKPKILRELQKFEEGTKDIEVDLSEINECKTNSELPPEQSHVAKELYKTLIQRSEENLKSGKINGSLFDYSDLDENGKSVLSLAGKENNDDTLIEGDNKNDEETSANNNNNEDDNNEDDNNEDDNNEDDNNENDNNNNNEDDNNNDDDDDEDNEEEDEEKQKSLREKLYRKIYEMLKKKKENIVLDENNPNVNFTDYKDDVFYPYQYIPPMLIKADRCKLQNVFGDKNLNIDLREASDGLKKQITYTLEDICEKKYGDCNFSSLFLYYEKGNGYIDYPIKVDNLDFYVNRRTYKEMMFKGILGNMVYEKSGSKYIIKSANAIMTVIPLLNSHTYEPYALAYEKKLIDYVRFYNLDDIIQDEETNDDNDPFIRFHVFTDRSLEDEVDRISKIDNLTRLLLLIGVLLIFMYALFNNVTSVLYRSKPLCAVMGIFCGFLGFLSGSGFLYFLGVKSVPPAETVPFLVIGVGVDDVFVILNSYSLLFMVKDNKKRIQMCLKDSALAITVTTLTNIIAFLISAISPFYSICAFSLFTASSLFFGYLMVLTFLLSFLCIEAKLEKKKRNIFTGTFHLFRSIFMKSSKKNKKENKENNIHDDGDNDNDEKKKDLSLEVKNNEDDYENISIYEWIHNLYLFEESINKKKKNAALVYASNNGMSSNLNNVNEDGFPNPSKIVSMEDVKKRNIKKDDAYINKEDEEGGGYYNKDDNKKKDILGKKQKKNNNNVTLVSKKGEDNELDVYYENLDEKTNDKYKMNNIKSSKLKYDNDKKDGAIINNRPSSDEEYKEEKDKNKINILNDVFNDITIKPNENILLDRGDVIKSSGYDSSYNDLQSSSLPNPSSNEVLNKTTMVYNETDLKDNKKEIKSSKKNVKDIKKSDMIHDDTYDIINSNNKNILLSSNEINNNSNNTNKFNNNSTELATKDTQQFINGHDKNIYLLSSHDNALFYKYIYEEPKGNIGKYFRSLVKNYYVPFLSSRFGKTIVYIMFTIIIAMSIYGCTLMKKGIKYDKAFPVDSYVRRFTTAKIKYFPDFGDFIEVYYFDKHFINKYRGLEKNTKEAASSFLYSDLTDRQIMNSPKINKNVHWENTNLQEELINMHNTLESQEFVTSVANGFTFFLNKNKSSLRKENPQEFYEIFANWLKKDFVGNLFKNDFVFLNGKLVAWRFHYFQKNVDDSEISSKWLKACKQITKLENHNVQMVCFHLSSIFNETDESIIEVTLINLGITILTILVVTAYIIKGFYSCVIIALIIFLIDLCIFGFMCLCGITMNIISMVILVLSVGFSIDHTSHIVQAFSHSMGRTRDEKMKESLHLMIGPVLHSGLSTWFVISTLFFSNKDFTVIFFQTLSLVLFFSITFSSMFLPVLLSSFGPLH
[ 25325, 36544, 38699, 77350, 87103, 87276, 87522, 87732, 87760, 88008, 88159, 88161, 88162 ]
The following text describes a protein: Function: Facilitates cholesterol efflux from membranes in a pH-dependent manner. Required for maintaining normal parasite plasma membrane lipid composition. Required for the proper functioning of digestive vacuole. Required for the viability of blood-stage parasites. Miscellaneous: MISCELLANEOUS: Mutations in the protein confer resistance to three diverse compounds: MMV009108, MMV028038 and MMV019662. Subcellular Localization: Cell membrane; Multi-pass membrane protein.
0
MPKRKAEKNAKGDTANMKNEPQRRFTMLSAEPSSPNIFNKARKAPSKKGKKVPKGKKGKANASKDGNNPAENGDAKTDQAQKAEGAGDAK
[ 8091, 24788, 24917, 27908, 31128, 36014, 87384, 87857, 88008 ]
The following text describes a protein: Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Subcellular Localization: Nucleus.
0
MSEKSIVQEARDIQLAMELITLGARLQMLESETQLSRGRLIKLYKELRGSPPPKGMLPFSTDWFMTWEQNVHASMFCNAWQFLLKTGLCNGVDAVIKAYRLYLEQCPQAEEGPLLALTRAWTLVRFVESGLLQLSSCNCCGGNFITHAHQPVGSFACSLCQPPSRAVKRRKLSQNPADIIPQLLDEQRVQAV
[ 8097, 14958, 15388, 21965, 24936, 24978, 27904, 29166, 42719, 87039, 87103, 87123, 87199, 87367, 87384, 87767, 87855, 87914, 88008, 88148, 88150, 88261 ]
The following text describes a protein: Function: Functions in complex with FlhD as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways. Subcellular Localization: Cytoplasm.
0
MLQSNEYFSGKVKSIGFSSSSTGRASVGVMVEGEYTFSTAEPEEMTVISGALNVLLPDATDWQVYEAGSVFNVPGHSEFHLQVAEPTSYLCRYL
[ 3070, 3078, 25040, 28561, 28664, 29615, 30110, 32074, 33193, 44132, 45325, 48241, 87103, 87525, 88008, 88153 ]
The following text describes a protein: Function: Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions. Is not able to produce D-ribose 1-phosphate from D-ribose and phosphate.
0
MNLLFLFLLLLFFPSLFIAQTTTNSPAPAPTTLALDSTQLNLTHILSTHGCSAFALSLLSSTSAEKAFNDVVEGGFTVFCPNDDVWSEFSPKFKNLTPPAKTSLLEFHGVPIYMPLPVLKSNNGDTNTLATDGAARFDFTVQNEGEDVTVKTSITTAKVDGAGVFDEDPLVVYLIDKVLEPEELFTADVMAPPKGGSDVGAAPSSDSPAESPEESVADQNADGNSGVRVEGGDQFHFMAVALCAWMGFSLL
[ 25079, 27013, 36588, 64136, 71233, 87276, 87489, 87522, 87735, 87760, 88008, 88058 ]
The following text describes a protein: Function: May be a cell surface adhesion protein. Subcellular Localization: Cell membrane; Lipid-anchor, GPI-anchor.
0
MSLQEKFDAAVEIIQKLPKTGPVATSNDQKLTFYSLFKQASIGDVNTDRPGIFSIIERKKWDSWKELEGVSQDEAKERYIKALNDMFDKIAEELDVAAWLEQIDPVIKTNLALIGK
[ 8304, 11234, 24978, 27641, 36418, 48047, 54369, 63778, 87733, 88008, 88162 ]
The following text describes a protein: Function: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters.
0
MKKTVRSLCSTALALTLGFTLLSGPASVQAAGNADYNLAGFSQGNTGGGIISESNTSTYKKVYNATDLALALKKNSGVKVVEIMNDLDLGWNEIPSAAQTSPFAKHNDALTHPVLKQTGVSKITVDGFNGLTIFSANGSKIKHAAITVKRSSNVIIRNLEFDELWEWDESTKGDYDKNDWDYITLEDSSGVWIDHCTFNKAYDGLVDSKKGTSGVTISWSTFKGDDGSANSWVTRQINELEANKASYPMYNYLRSSAVGLSKQDVIAISGPQKKGHLVGATSLESANANLSITLHHNLYKDIQDRMPRLRGGNAHAYNIIMDAADARSAQSRITSAMATAIASKGYKFGITSNGAISTESGAVLVEKSVIKDVQXPCTQQSDRSDQRHVHR
[ 5595, 5603, 15163, 24878, 29025, 30989, 32877, 37622, 45324, 46272, 71260, 86995, 87244, 87258, 87741, 87767, 87937, 88038, 88058 ]
The following text describes a protein: Function: Catalyzes the depolymerization of both polygalacturonate and pectins of various methyl esterification degree, with an endo mode of action. Shows the highest activity on 20 to 34% methylated pectin but retains 67%, 51%, 25%, and 1% of its maximum activity on polygalacturonate and 8.5%, 55 to 70%, and 90% methylated pectin, respectively. Subcellular Localization: Secreted.
0
MDLEHGKKPSAHPAPCTVQQVKDKLIGLRPVMLRASALLATTVAAAVMGLNRQSYTAVVAIVGTKPLTQTFTAQFKDTPAFVYFVIANAIASLYNLVVLAMRRLVQGRVQRLVLHMGDMVIMLLLATGAATAASMAELGKNGNLHAHWNPMCDKFGSFCNRGGLSLVSSFIGVTLMLALNLLSAAANTPRGIVAGQ
[ 18986, 25079, 41421, 41631, 70469, 87276, 87281, 87760, 88008, 88159, 88161 ]
The following text describes a protein: Function: Regulates membrane-cell wall junctions and localized cell wall deposition. Required for establishment of the Casparian strip membrane domain (CSD) and the subsequent formation of Casparian strips, a cell wall modification of the root endodermis that determines an apoplastic barrier between the intraorganismal apoplasm and the extraorganismal apoplasm and prevents lateral diffusion. Subcellular Localization: Cell membrane; Multi-pass membrane protein.
0
MSVDAKIEFPVIEFRSSDLERGTNGWYRLCKKVREACEIFGCFEVVYDTISTKVREEMFRLMKELVEVPVERKQKNTSPLPYHGWVGPCTQVSLLYEGFGLGDVSNYDSVKNFAQLMWPEGHPRFCDTIHTMGTQLEVLNKLILLMIIDSYGLSEDSLKINYTTSMRMMKYTTPPPGEYETGLFAHTDKPVSTIICEDQIPGLEIEVNDGQWIKLTNLSPSSFVFMVGDPLKAWSNGRLKSTNHRVMMSGDKDRFSIAAFIMPNEGTIIKTPKELIDEEHPQLFKDFDFMKFFFFAFSNPARHIDSGQLLYDFAALSPPVSNGHMDK
[ 30277, 32536, 40223, 58060, 58258, 71100, 75886, 87409, 87678, 87767, 87873, 88008 ]
The following text describes a protein: Function: 2-oxoglutarate-dependent dioxygenase essential for auxin catabolism and maintenance of auxin homeostasis in reproductive organs. Catalyzes the irreversible oxidation of indole-3-acetic acid (IAA) to the biologically inactive 2-oxoindole-3-acetic acid (OxIAA).
0
MTPTGAAAKPSGSRAEPQEMASQPPPPPKPWETRRIPGAGTGPGPGPSFQSADLGPTLLTRSGQPTLTRVPPPILPRPSQQTGNSNLNTFRPAYTSFSSAYGAYGNSFYGSYNPYSYGYGGLGYNRFRMDDLPPSRFVQQAEESSRGAFQSIESIVHAFASVSMMMDATFSAVYNSFRAVLDVANHFSRLKIHFTKVFSAFALVRTIRYLYRRLQQMMGLRRGSENEDLWAESEGTVACLGPEDRAANSAKSWPIFLFFAVILGGPYLIWKLLSTHSEEITATTNWASGEDDHVVARAEYDFAAVSEEEISFRAGDMLNLAPKEQQPKVRGWLLASIDGQTTGLVPANYVKILGKRRGRKTVELNKITEQQRAFTNPALINGTTAADTLEEQEAAFESVFVENNKVPVTSESTSKSGDKQDL
[ 6907, 6982, 7106, 8988, 10750, 10751, 11422, 13074, 17329, 25005, 27507, 29185, 37152, 42079, 63313, 63817, 87760, 87894, 87974, 88008, 88031, 88158, 88159, 88161, 88162 ]
The following text describes a protein: Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix. Involved in the import of PTS1- and PTS2-type containing proteins. Subcellular Localization: Peroxisome membrane; Multi-pass membrane protein.
0
MLQTPESRGLPVPQAEGEKDGGHDGETRAPTASQERPKEELGAGREEGAAEPALTRKGARALAAKALARRRAYRRLNRTVAELVQFLLVKDKKKSPITRSEMVKYVIGDLKILFPDIIARAAEHLRYVFGFELKQFDRKHHTYILINKLKPLEEEEEEDLGGDGPRLGLLMMILGLIYMRGNSAREAQVWEMLRRLGVQPSKYHFLFGYPKRLIMEDFVQQRYLSYRRVPHTNPPEYEFSWGPRSNLEISKMEVLGFVAKLHKKEPQHWPVQYREALADEADRARAKARAEASMRARASARAGIHLW
[ 6673, 8202, 10753, 24018, 24917, 37759, 65111, 68908, 68909, 87976, 88008, 88171, 88181 ]
The following text describes a protein: Function: Enhances ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin ligases. Proposed to act through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. MAGEF1-NSMCE1 ubiquitin ligase complex promotes proteasomal degradation of MMS19, a key component of the cytosolic iron-sulfur protein assembly (CIA) machinery. Down-regulation of MMS19 impairs the activity of several DNA repair and metabolism enzymes such as ERCC2/XPD, FANCJ, RTEL1 and POLD1 that require iron-sulfur clusters as cofactors. May negatively regulate genome integrity by inhibiting homologous recombination-mediated double-strand break DNA repair.
0
MPEIDALFESINVRDLLAGHDLNDPTTPLSAPDLRLLINRLESHSLRIKSKVQSYLVAHHSDFSELFSLCQDTVSRTRLISDDVSDVLQLVSDRPIDVEIRSVVDEITEKTKEVKLKRESLDLVNAIVGICEALQETKEALKNGRFRFAAERIRELKVVLRIGEEEDGEPVAYALLRKEWSNCFDEIQEVLAKFMENAVRFELDSSRIRIKYQLSVGETAGIALSTVLEAMEVIGILDYGLAKAADSIFKHVITPAVTHASTFAAVEDLCKSAGEVTEATLRLEQSSDHKFEDVDGDAMYSGILKVVKFICSSLCFGNVTWIHSFGRLTWPRISELIISKFLSKVVPEDASKLADFQKIIERTSQFEAALKELNFVSSSDAESRLSKYAEDVEVHFASRKKIEILAKARNLLLQCNFTIPQDIAMRNAKHIVCLLFSSERCVVSEAASQLMNLVHKTLEDVCVSSARVASEFYNAARDSILLYEAVVPVKLEKQLDGLNEAAVLLHNDCLYLFEEILGLAFEYRASFPSSIKEYAVFADIAPRFKLMAEEVLQKQVHLVISSLREAIDSADGFQNTHQIKQFKSAEFSIDQVVFSLKNVHMIWEPVLRPKTYKQSMCAVLESVFRRIARDILLLDDMAADETFELQKLIYLMLKNLSSVLDSVRSADETSRPLDDIIPSLRKTRKLAELLDMPLMSITSAWESGELFRCNFTRTEVQDFIKAIFTDSPLRKECLWRIDEVNQ
[ 6695, 8603, 10368, 12377, 16787, 24783, 24917, 25014, 25031, 43870, 72410, 74212, 74213, 80669, 87272, 87273, 87284, 87306, 87367, 87371, 87432, 87695, 87760, 87790, 87974, 88008, 88162 ]
The following text describes a protein: Function: May be required for accurate chromosome segregation. Required for proper maturation of seed storage proteins. Forms a complex with MAG2, MIP2 and MIP3 on the endoplasmic reticulum that may be responsible for efficient transport of seed storage proteins. Subcellular Localization: Cytoplasm, cytoskeleton, spindle. Cytoplasm. Chromosome, centromere. Chromosome, centromere, kinetochore. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=In prometaphase, associated with the kinetochore. At metaphase, mostly associated with the spindle. In early anaphase, found in the vicinity of the centromere. As anaphase progresses, dispersed in the cytoplasm.
0
MSSYKPVAIPTYPKLGEKITQDTLYWKRYKTPVQIKEFGAVTKIHFSPIQPCSYAVTSSTRIHLYGQYSQEPMKTFSRFKDTAYCGTYRGDGKLLGAGCEDSVVQLFDISGKAALRQFSGHSKAVHFVDFTSDKYHIVSGSDDYTSKLWDIPNGIEITSYKEHTDYIRCGCTSPLNNDLFATGSYDHTIKVFDGRTDQSVMSMDHGQPVESVLLFPSGGLLVSAGGRYVKVWDILKGGQLLVSLRNHHKTVTCLSLSSSGQRLLSGSLDRHVKVYSTMNYKVVHSFDYAASILSLALAPDDQIIAVGMTNGVLNIKHRKPEEKKTLQSTAKRHPRYRVFVRGKDYMPKQDDIFVSKPVKAHLTKYDALLKGFHMSKALDAALQVRMKRPEVTVAVMNELKRRGTLKNALAGRDEKELSDLLIFLLKHLINPQFLPILLNVAEHIIDIYSPVVGQSSVIHKQFIRLQEVVEKEINYGEELLKILGMMDTLFATMTTKKESPWEEPKPILSLNSQ
[ 8109, 15426, 24974, 37341, 49061, 51609, 52270, 64085, 87857, 88008, 88009, 88252, 88276 ]
The following text describes a protein: Function: Ribosome biogenesis factor. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. Subcellular Localization: Nucleus, nucleolus.
0
MLAGNMEQANVFRLEEKRYKCRADTIPDMSEVLDPNDPQSFGFEALVEIKPRVFSFQKAPGLLILKNYVSSELQMQLLKSIMFTQIQDPENKTNLSPFYQLPLGNDSIWRRYYNGDGESIIDGLGETKPLTVDRLVHKKLRWVTLGEQYDWTTKEYPDPSKSPGFPKDLGDFVEKVVKESTDFLHWKAEAAIVNFYSPGDTLSAHIDESEEDLTLPLISLSMGLDCIYLIGTESRSEKPSALRLHSGDVVIMTGTSRKAFHAVPKIIPNSTPNYLLTGNKAWDGWISRKRVNFNVRQVRPSR
[ 636, 8065, 23979, 24917, 24978, 25040, 32536, 35944, 39725, 40223, 58263, 64854, 87008, 87367, 87409, 87678, 87767, 87857, 87873, 88008, 88155 ]
The following text describes a protein: Function: Dioxygenase that acts as on nucleic acids, such as DNA and tRNA. Requires molecular oxygen, alpha-ketoglutarate and iron. Mainly acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs, with a preference for N(1)-methyladenine at position 58 (m1A58) present on a stem loop structure of tRNAs. Acts as a regulator of translation initiation and elongation (By similarity). Does not appear to possess DNA repair activity; no activity towards methylated DNA or etheno adducts. Exhibits a weak and unstable DNA lyase activity; this activity is probably not biologically significant and proceeds by a mechanism different from the classical dioxygenase reaction as it does not require 2-oxoglutarate or iron. Subcellular Localization: Cytoplasm. Nucleus.
0
MEPTPMLRDRDHDDAPPTYEQAMGLCPTTVSTPPPPPPDCSPPPYRPPYCLVSSPSPRHTFDMDMMEMPATMHPTTGAYFDNGWKWTFALLVVAILGIIFLAVVFTVVINRDNSTATGTSSG
[ 17112, 25325, 25499, 25884, 63041, 87577, 87586, 87595, 87653, 87760, 88159, 88161, 88211 ]
The following text describes a protein: Function: Plays a role in the inhibition of host innate immune response to promote latent infection. Mechanistically, suppresses viral DNA-triggered signaling by impairing DNA binding and oligomerization of CGAS. Also impairs the translocation of host STING1 from the endoplasmic reticulum to perinuclear punctate structures which is an essential step for its activation (By similarity). Regulates the function of host NEDD4 family ubiquitin E3 ligases through its PPxY motif and thereby prevents the excessive ubiquitination of gB and its degradation by inhibiting these E3 ligases. Subcellular Localization: Host membrane; Single-pass membrane protein. Host cytoplasm. Note=Accumulates in the perinuclear region of the host cytoplasm, with some dispersal into the cytoplasm in a fine-speckled pattern. Domain: Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. Contains one L domain: a PPXY motif which is involved in the interaction with Itch, a member of the Nedd4 family.
0
MAAPVRLGRKRPLPACPNPLFVRWLTEWRDEAASRGRRTQFVFQKALRSLRRYPLPLRSGKEAKILQHFGDGLCRMLDHRLQQHRASGGDHALGSPSGEKSPAPEGPPAEEVQDPSMPVPAQPKAGGSGSYWPARHSGARAILLLLYREHLNPSGHSFLTKEELLQRCAQKAPRMAPGSTRPWPALRSLLHRNLVLRTHQPARYSLTPEGLELAQKLAESEGPTWLNVGIGPEEPPGEQPEVPGAASAELGASEGSVQQPPLELGPGEYRVLLCVDVGETKGVGHRPELLRELQRLHVTHTVRKLHVGDFVWVAQETRPSDPARPKELVLDHIVERKRLDDLCSSIIDGRFREQKFRLKRCGLGRRVYLVEEHGSVHNLSLPESTLLQAVTNTQVIDGFFVKRTADIKESAAYLALFTRGLQRLYQGHTLRSRPWGTPGDPESGAGPSPNPLCSLLTFNDFNAGAIKNKAQSVREVFARQLMQVRGVSGEKAAALVDRYSTPASLLAAYDTCATPKEQEMLLSTIKCGRLQRNLGPTLSRTLSQLYCTYGPLT
[ 4070, 6787, 6798, 8082, 12001, 12083, 12833, 18741, 19369, 24917, 24929, 24974, 26466, 27904, 29458, 32536, 33230, 35850, 41157, 45280, 45553, 58241, 61714, 64146, 69431, 73379, 73380, 87016, 87374, 87379, 87380, 87431, 87601, 87747, 87767, 87850, 87857, 87914, 88008 ]
The following text describes a protein: Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI). Subcellular Localization: Nucleus, nucleolus.
0
MKRKRGEKEEAAEKKMEIVWQTPANPPEKHDYIFRDGRRHVRPYHFEFISHVKNRWAGKTIVDLFAEEFKGRPYDYYVSAVKCGRIQVDGEMVPVSYIVKSSQKISHFVHRHEPPVMAWDVPILDKEDDVVTVWKPATVPVHPCGQYRKNTVVGVLQAEHGLAPLFPVHRLDRLVSGLLILARNATRADLFRQEIEAGKVQKQYVAKVIGVFPEDEQIVDVNVNYNAREGRSTVEVGNSCDGSPIKGKTACTKFTRIGTNGIHSIVLCKPITGRTHQIRVHLQYTGHPIANDILYLSENVTNRSSEGVNADRAAHSPNNCLVPENNSSDKYEDSTEEDFDIDPMCTNCPNIYIYGCICCY
[ 6175, 6755, 27925, 29669, 41140, 41205, 41206, 52563, 75843, 87683, 88008 ]
The following text describes a protein: Function: Responsible for synthesis of pseudouridine from uracil.
0
MARTVDTTGRVVQLLGLLQSRRVWTGEELAERLGVTGRSVRRDIERLRELGYPVHASKGQGGGYQLGAGMALPPLLLDPDEAVAMAVCLRLAAGGSVAGVGESALRALSKLDQVMPARLRSQVAAIHDATVTLGPNATDTAVAPDVLMTLARACRDREHVSTGYTDLRGNQTQRRLEPYQLVTTGRRWYLMAYDRDREDWRSLRLDRMSDVRATGTTFTARPAPDAAAYVGRAISASAYPYVARVRYFAPEKVVAQRFPPGTATFEPDGPDACIVTSGAEYPEQLAMYFATVGHDFEVLEPAEVIDAVGAMADRLRRAVR
[ 14356, 19545, 27750, 27782, 27917, 32074, 36801, 47022, 58014, 64146, 64148, 77187, 87123, 87384, 88008, 88148, 88150 ]
The following text describes a protein: Function: Transcriptional activator. Acts as a transcriptional activator of the MSMEG_1357-56 operon upon genotoxic stress. Controls adjacent genes that belong to the DinB/YfiT-like putative metalloenzymes superfamily by upregulating their expression in response to various genotoxic stress conditions, including exposure to H(2)O(2) or the natural antibiotic zeocin, as well as mitomycin C (MMC), diamide and UVC radiation. Upon genotoxic stress, upregulates two genes encoding proteins of the DinB/YfiT-like putative metalloenzymes superfamily, MSMEG_1357 and MSMEG_1356. Binds different forms of single-stranded DNA (ssDNA) with high affinity, primarily through its characteristic WYL domain. Binds nucleic acids with single-stranded regions, such as polyT 20mer ssDNA, 5' tailed, 3' tailed and fork DNA, but not ssRNA. Miscellaneous: MISCELLANEOUS: May be part of a putative operon containing two genes of the DinB/YfiT-like putative metalloenzymes superfamily, MSMEG_1357 and MSMEG_1356. Domain: The HTH domain binds a palindrome in the promoter of the MSMEG_1357-56 operon; The WYL domain is named after a conserved Trp-Tyr-Leu motif. Mediates binding to single-stranded regions, such as polyT 20mer ssDNA, 5' tailed, 3' tailed and fork DNA, but not ssRNA. May present a signal transducer in WYL domain-containing transcription factors by binding to ssDNA present during DNA damage and playing a role in transcriptional activation.
0
MDKARHQQLFQHSMEPGYRNETVPQPFMPDQTGSASANMRPPNSNGSDVKAVHNFSIQTGEEFSLEFMRDRVIPQRSSNPNGAGDMNYNTGYMELRGLIGISHTGSECASDVSRFSTVENGTSDIERTNSSLHEFGNKLNHVQSAPQALLSKDSSVGNLHGYKNTSSSASGSVTAKVKILCSFGGKILPRPGDSKLRYVGGETHIISIRKDISWQELRQKILEIYYQTRVVKYQLPGEDLDALVSVSSEEDLQNMLEEYNEMENRGGSQKLRMFLFSISDMDDALLGVNKNDGDSEFQYVVAVNGMDIGSGKNSTLLGLDSSSANNLAELDVRNTEGINTIAGDVVGVGASQLMVNGFQQTSAQQSESIPPSSSLHYSQSIPLNAAYQLQQSVPPSSALHYPQSITPGSSLQYPQSITPGSSYQYPQSIIPGSASSYGIYPQYYGHVVQHGERERFPLYPDHSSNYSAIGETTSSIPIQGHVSQQGGWAEGYPYPGSTPKSTQALAEEQKVSSDMKIREEVEPENRKTPGNDHQNPPQIDDVEVRNHNQVREMAVATTPPSQDAHLLPPSRDPRQNTTAKPATYRDAVITGQVPLSGIEDQLSTSSSTYAPVHSDSESNLIDLNYPEPEQSSQRVYCSERIPREQLELLNRLSKSDNSLSSQFVTSESPANTAQQDSGKEAVGKSHDEFKTVNDDANHHTHKDVETIFEKVGVSDETLESEPLHKIVNPDDANKNRVVNGADTEIGVSNLSHVNAAMSHVIPEEQASLQGDILIDINDRFPRDFLSEIFSQAISEDTSTVRPYPHDGAAVSMNVQNHDRKNWSYFQQLAEDQFIQRDVVLDQADSRIPSDRKDGGESSRLPYVSPLSRDGISTNLANPQLTLGQDYGGNFSEKDGGGTGSIPPALENEQMKVTESEEFGAMVENLRTPDSEPKDEKTETRHAALPPLGSEFDYSGLQIIKNEDLEELRELGSGTFGTVYHGKWRGSDVAIKRIKKSCFAGRSSEQERLTGEFWGEAEILSKLHHPNVVAFYGVVKDGPGGTLATVTEYMVDGSLRHVLVRKDRHLDRRKRLIIAMDAAFGMEYLHSKNTVHFDLKCDNLLVNLKDPSRPICKVGDFGLSKIKRNTLVSGGVRGTLPWMAPELLNGSSSKVSEKVDVFSFGIVLWEILTGEEPYANMHYGAIIGGIVNNTLRPTIPGFCDDEWRTLMEECWAPNPMARPSFTEIAGRLRVMSSAATSTQSKPSAHRASK
[ 3604, 8663, 9425, 9426, 10180, 18863, 24978, 28524, 28548, 29033, 36166, 36535, 36977, 45290, 50333, 75822, 87110, 87139, 87196, 87367, 87694, 87855, 87914, 88008, 88052, 88153 ]
The following text describes a protein: Function: RAF-like protein kinase acting, together with RAF24, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process. Subcellular Localization: Cytoplasm. Note=Broadly distributed to both membrane-associated and intracellular punctate structures.
0
MIHLMIMMLERVGIIVILGFILAHTKLFRQALQNQDGYKGKAILISIFSLFSIISNYTGIEIQRNMIVNNDWVFTIDPSGSIANTRILGVEIGGLLGGPFVGAGIGILAGLHRFSLGGSTALSCAVSSILAGVLAGLIGRYFTKRYRMPTPRIAALVGIGMESLQMIIILLMAKPFSDAWELVSMIGIPMILINGTGSFIFLSIIQAIIRKEEQARALETHRVLTIADQTLPFFRQGLNENSCKSVAAIIHKLTGTDAVSLTDKEKILAHVGAGMDHHIPSKSLITGLSKKVIKTGHIMKAISQEEIECTHAECPLHAAIVLPLTSNGNTIGTLKMYFKSPAGLSQVEEELAEGLAMLFSTQLELGEAELQSKLLKDAEIKALQAQVNPHFLFNAINTISALCRTDVEKTRKLLLQLSVYFRSNLQGARQLLIPLSKELNHLNAYLSLEQARFPGKYKIELNIDSRLEQIEIPPFVLQVLVENALRHAFPKKQDICKVTVCVLSDDASVYMKVADNGRGIPPDVLPELGKKPFPSKEGTGTALYNLNQRLIGLFGQQAALHISSEVHKGTEVSFQVPMQQMKEGEEHAQGVNS
[ 3639, 8663, 18986, 25079, 27654, 29033, 38412, 40530, 44917, 45732, 59186, 64620, 76295, 87110, 87276, 87694, 87760, 87855, 87914, 88008, 88153, 88159, 88161, 88174 ]
The following text describes a protein: Function: Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism. Subcellular Localization: Cell membrane; Multi-pass membrane protein.
0
MATFSLGKHPHVELCDLLKLEGWSESGAQAKIAIAEGQVKVDGAVETRKRCKIVAGQTVSFAGHSVQVVA
[ 8138, 25040, 27925, 64706, 87103, 88001, 88008 ]
The following text describes a protein: Function: Its structure and the presence of conserved basic residues indicates that it probably binds RNA.
0
MTSPHFSSYDEGPLDVSMAATNLENQLHSAQKNLLFLQREHASTLKGLHSEIRRLQQHCTDLTYELTVKSSEQTGDGTSKSSELKKRCEELEAQLKVKENENAELLKELEQKNAMITVLENTIKEREKKYLEELKAKSHKLTLLSSELEQRASTIAYLTSQLHAAKKKLMSSSGTSDASPSGSPVLASYKPAPPKDKLPETPRRRMKKSLSAPLHPEFEEVYRFGAESRKLLLREPVDAMPDPTPFLLARESAEVHLIKERPLVIPPIASDRSGEQHSPAREKPHKAHVGVAHRIHHATPPQAQPEVKTLAVDQVNGGKVVRKHSGTDRTV
[ 15044, 16457, 24926, 24978, 25026, 25027, 26230, 32073, 66826, 67518, 87139, 87166, 87326, 87367, 87371, 87595, 87616, 87662, 87914, 87976, 88008 ]
The following text describes a protein: Function: Interferon-stimulated protein that plays a role in innate immunity. Strongly inhibits ebolavirus transcription and replication. Forms a complex with viral RNA-bound nucleocapsid NP and thereby prevents the transport of NP to the cell surface. Subcellular Localization: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm.
0
MSSGANITYASRKRRKPVQKTVKPIPAEGIKSNPSKRHRDRLNTELDRLASLLPFPQDVINKLDKLSVLRLSVSYLRAKSFFDVALKSTPADRNGGQDQCRAQIRDWQNLQEGEFLLQALNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALNPSQCTDSAQGVDEAHGPPQAAVYYTPDQLPPENASFMERCFRCRLRCLLDNSSGFLAMNFQGRLKYLHGQNKKGKDGALLPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGCDAKGQLILGYTEVELCTRGSGYQFIHAADMLHCAESHIRMIKTGESGMTVFRLLAKHSRWRWVQSNARLIYRNGRPDYIIATQRPLTDEEGREHLQKRSMSLPFMFATGEAVLYEISSPFSPIMDPLPIRTKSNTSRKDWAPQSTPSKDSFHPSSLMSALIQQDESIYLCPPSSPAPLDSHFLMGSVSKCGSWQDSFAATGSEAALKHEQIGHAQDVNLALSGGPSELFPDNKNNDLYSIMRDLGIDFEDIRSMQNEEFFRTDSTAAAAGEVDFKDIDITDEILTYVQDSLNNSTLLNSACQQQPVTQHLSCMLQERLQLEQQQQLQQPPPQALEPQQQLCQMVCPQQDLGPKHTQINGTFASWNPTPPVSFNCPQQELKHYQIFSSLQGTAQEFPYKPEVDSVPYTQNFAPCNQPLLPEHSKSVQLDFPGRDFEPSLHPTTSNLDFVSCLQVPENQSHGINSQSAMVSPQAYYAGAMSMYQCQPGPQRTPVDQTQYGSEIPGSQAFLSKVQSRGVFNETYSSDLSSIGHAAQTTGHLHHLAEARPLPDITPGGFL
[ 7545, 7557, 8101, 8110, 8436, 9297, 12548, 15387, 15388, 15427, 23109, 23146, 24917, 24978, 25976, 28686, 32074, 32577, 34371, 35927, 35965, 37281, 45714, 47419, 47522, 61734, 63761, 64381, 66505, 87106, 87123, 87220, 87272, 87367, 87384, 87857, 88006, 88009, 88010, 88148, 88150 ]
The following text describes a protein: Function: Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer. Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation. Xenobiotics can act as ligands: upon xenobiotic-binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists. Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands. Acts as a negative regulator of anti-tumor immunity: indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity. Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1. Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1. The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription. Subcellular Localization: Cytoplasm. Nucleus. Note=Initially cytoplasmic; upon binding with ligand and interaction with a HSP90, it translocates to the nucleus. Domain: The PAS 1 domain is essential for dimerization and also required for AHR:ARNT heterodimerization.
0
MITTNLKSLIRYIVVHFVTTKITPSDLLRHASGISGNSRKPIKDIARHSVLITYIIRILTTLKEEIDVALTTEAFSTSVSTNASSCEESLVTAATVESKDGDRVQEVGCSTSDTISNEHHMKVAAEAMDKITESAASCSQLQGDVENKVLGGSSLSTKKHSISVPVYVDELVKVESVSETLSTKVVLEIALHVNQARLKGLVKDLPDLVPSPQPPLAPPWLQHSVYLEPLYPTPSSKMYEELQRLSPIVSIRESYFLRYCTQIEQGLWAVVDVSGRHSLRKMFGSVVTLQGAHKSLPRSCTNHLNPKLCFFSQHLIAIVRTPLFLVKAAYDTCQIQASLAPSSADYHWNWKMIEWGRVRVPMVLFKWKTFPPSVLMSLIYGATNFGKEANEECMVIGVYNSRVEAMRNTTLSYLPPFD
[ 3922, 18986, 24878, 25223, 29172, 33957, 38337, 40072, 87280, 87281, 87601, 88008, 88038 ]
The following text describes a protein: Function: Hydrolyzes acetyl esters in homogalacturonan regions of pectin. In type I primary cell wall, galacturonic acid residues of pectin can be acetylated at the O-2 and O-3 positions. Decreasing the degree of acetylation of pectin gels in vitro alters their physical properties. Subcellular Localization: Secreted, cell wall.
0
MAFRQSEHEMSVTSLDSSVELRSRSPSPQVFNPRKLRFADDDFDKDTPEGASPQHPLQQRPKLSSGEEQQLDSKIGKEGGDGDVSMSPPCQKVRALRLFSTPATPKTILQKSTTQCSNHLSAAAAAVNASRRSDDLFRLSERPRSLPLHNRKLPTQDTANVNPFTPDSLMAHNKKRCRTQFGRENLNLNVNAMQKYLLSDACDDDVTEEAGDSMREIHQQAPKRLALHDTNISRFKREFMQVNVIGVGEFGVVFQCVNRLDGCIYAIKKSKKPVAGSSFEKRALNEVWAHAVLGKHDNVVRYYSAWAEDDHMLIQNEFCDGGSLHARIQDHCLGEAELKIVLMHVIEGLRYIHSNDLVHMDLKPENIFSTMNPNAHKLVEVQPQQTKDDDGMDSVYEELRHSENLVTYKIGDLGHVTSVKEPYVEEGDCRYLPKEILHEDYSNLFKADIFSLGITLFEAAGGGPLPKNGPEWHNLRDGKVPILPSLSRDFNELIAQMMHPYPDKRPTSQSIFSHPILSAVDSKSKLQLGLELTVEKRKNEILMNKLREAKKQIKLLEQRVNLLAVTNNPDSLDGQRCLRSFTRRMRTPFSSHGKFDSISDRNKNVITNI
[ 3602, 6695, 6946, 10209, 16737, 16785, 16787, 16942, 24917, 24978, 27681, 28549, 28551, 28674, 29033, 36535, 45290, 50083, 50333, 75994, 87016, 87110, 87272, 87273, 87694, 87747, 87767, 87790, 87855, 87857, 87914, 88008, 88153, 88177 ]
The following text describes a protein: Function: Acts as a negative regulator of entry into mitosis (G2 to M transition). This kinase specifically phosphorylates and inactivates cyclin B1-complexed CDC2. Subcellular Localization: Nucleus.
0
MRSVCFCFCLALLLPRCIQSQRSRPAFAQLDEDTQRDVLAVDILNRSGVLNSLLRSEHHLVFRRARPPRPASQVPKRAQQGSRFALSLDVPTSILSVLIDLAKNQDMRTKAAANAELMARIGKRK
[ 8681, 8956, 9443, 12125, 24907, 28880, 33766, 33768, 36096, 55928, 87567, 88008, 88038, 88058 ]
The following text describes a protein: Function: Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress. Subcellular Localization: Secreted.
0
MERDFLGLGSKLSPITVKEETNEDSAPSRGMMDWSFSSKVGSGPQFLSFGTSQQETRVNTVNDHLLSSAAMDQNQRTYFSSLQEDRVFPGSSQQDQTTITVSMSEPNYINSFINHQHLGGSPIMAPPVSVFPAPTTIRSSSKPLPPQLTIFYAGSVLVYQDIAPEKAQAIMLLAGNGPHAKPVSQPKPQKLVHHSLPTTDPPTMPPSFLPSISYIVSETRSSGSNGVTGLGPTKTKASLASTRNNQTAAFSMAPTVGLPQTRKASLARFLEKRKERVINVSPYYVDNKSSIDCRTLMSECVSCPPAHHLH
[ 9296, 9506, 9512, 24917, 44782, 51147, 67538, 87139, 87686, 87857, 87925, 88008, 88148, 88150, 88180 ]
The following text describes a protein: Function: Repressor of jasmonate responses. Interacts with and suppresses RHD6 and RSL1 transcription factor activities to negatively regulate jasmonate-stimulated root hair development. Subcellular Localization: Nucleus. Domain: The jas domain (259-284) is required for interaction with COI1.
0
MFRVCRRLYHPNTLEHAVGNRLRPLAYEQDSPQYKVLQRALEAHVPVLGFNERAIVRAAGDLGYGSAVLSALAAPNSPALLNVPSAVLELVKFHLVTKRVALADAAAQGNVSMEQLFLQRVEADRPLAGQLTQLLSILSLPGEFLVNTAMPELFRLSDDLIYYSGEKDHPDLAWYSKRAAVAMAYVSTNLFMARDRSPALEETLHFARRRLQQVDSLGTAYNNVEEFAWYQLLMAMNLVKSQLTRG
[ 8398, 24983, 25807, 29172, 46661, 47479, 87733, 87785, 88008, 88154, 88179 ]
The following text describes a protein: Function: Membrane-associated protein that warps the membrane surface to access and bind aromatic isoprenes with high specificity, including ubiquinone (CoQ) isoprene intermediates and presents them directly to COQ7, therefore facilitating the COQ7-mediated hydroxylase step. Participates in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Subcellular Localization: Mitochondrion.
0
MGKGAAKYGFKSGVFPTTRSILKSPTTKQTDIINKVKSPKPKGVLGIGYAKGVKHPKGSHRLSPKVNFIDVDNLIAKTVAEPQSIKSSNGSAQKVRLQKAELRRKFLIEAFRKEEARLLHKHEYLQKRTKELEKAKELELEKLNKEKSSDLTIMTLDKMMSQPLLRNRSPEESELLKLKRNYNRSLLNFQAHKKKLNELLNLYHVANEFIVTESQLLKKIDKVFNDETEEFTDAYDVTSNFTQFGNRKLLLSGNTTLQTQINNAIMGSLSNEKFFDISLVDSYLNKDLKNISNKIDSKLNPTSNGAGNNGNNNNTTNL
[ 12385, 24979, 24983, 24992, 27932, 87103, 87785, 88008, 88020, 88022 ]
The following text describes a protein: Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. Miscellaneous: MISCELLANEOUS: Present with 2010 molecules/cell in log phase SD medium. Subcellular Localization: Mitochondrion. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1.
0
MMRIALFLLTNLAVMVVFGLVLSLTGIQSSSVQGLMIMALLFGFGGSFVSLLMSKWMALRSVGGEVIEQPRNERERWLVNTVATQARQAGIAMPQVAIYHAPDINAFATGARRDASLVAVSTGLLQNMSPDEAEAVIAHEISHIANGDMVTMTLIQGVVNTFVIFISRILAQLAAGFMGGNRDEGEESNGNPLIYFAVATVLELVFGILASIITMWFSRHREFHADAGSAKLVGREKMIAALQRLKTSYEPQEATSMMALCINGKSKSLSELFMTHPPLDKRIEALRTGEYLK
[ 4761, 8200, 9257, 25079, 25325, 28225, 29166, 37534, 54815, 75738, 87039, 87191, 87274, 87276, 87601, 87760, 87767, 87770, 87965, 88008, 88086, 88159, 88161, 88261 ]
The following text describes a protein: Function: Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins. Subcellular Localization: Cell inner membrane; Multi-pass membrane protein. Note=Bioinformatics programs predict 4 transmembrane helices, however PhoA and Bla fusions as well as other experiments only confirm the first 2.
0
MTEILSQDEIDALLSAISSGEVSESDYASVSEQKKVKIYDFKRPDKFSKDQIRTLQMMHETFARLATTGLSAQLRALVSVHVASVDQLTYEEFIRSIPNPTTLAVINMDPLRGSAILEIDPSISFTIIDRLFGGKGEQAKISRELSEIEMSVMEGIIVRILGNMRESWSTVIDLRPRLGNIETNPQFAQVVPPNDMVVLITLETKIGEVEGMTNLCIPYITIEPIINKLSAQYWYSSIRKGELDENRAVIQERLDQVAIPLIAEVGSVDVSINDFMNLSIGDVVKLENTSTRSEMIVKVGERKKFKCLPGRVGSRLAIQIGERVEDIPDELLGSTRSEQEY
[ 16578, 19168, 25079, 25214, 27938, 37225, 37347, 59156, 64185, 87198, 87276, 87278, 87287, 87311, 87467, 87468, 87760, 88008 ]
The following text describes a protein: Function: FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Subcellular Localization: Bacterial flagellum basal body. Cell membrane; Peripheral membrane protein.
0
MEVYFSGTIERIIFENPSNFYRILLLEIDDTDAEDFDDFEIIVTGTMADVIEGEDYTFWGQIVQHSKYGEQLQISRYDRAKPTSKGLVKYFSSSHFKGIGLKTAQKIVDTYGENTIDEILQHPEKLEGIAGLSAKNREAFVSTLRLNYGTEMVLAKLANYGIPNKLAFQIQDFYKEETLDVVENYPYQLVEDIKGLGFTIADQLAEELGIESQAPERFRAGLVHSLFQACMETGDTYVEARDLLEQTLTLLESSRPVELDPSQVAQELSYLIEEDKVQQIDTKIFDNSLFFAEEGIRSHLIRILEKGEQKRQDLETIQKHITTVEQELGIEYDNIQKQAICDAIQNKVFILTGGPGTGKTTVINGIIAVYALLEGLDFRKKSNLPILLAAPTGRAARRMNELTGLPSATIHRHLGMTGDDDTSHLEDYLDAEFIIVDEFSMVDTWLANQLFSNISSNSKILIVGDSDQLPSVSPGQVLADLLHIPLIPQTRLEKIYRQSKESTIVTLASQIRQGILPADFTQKKADRSYFEIASGHIPATIEKILGAALRNGIPARDIQVLAPMYRGTAGIDAINQLMQDLLNPPQKDQLSFEAPQCHYRKRDKVIHLVNDAEINVFNGDLGAITDLIPGKYTESKQDEIVIDFDSNEVSYPRNEWYKIRLAYAMSIHKSQGSEFPVVILPITSASRRMLERNLIYTAITRAKSKLILLGELQAFDYATQHIGTARKTYLIERFSDLLENVEEKQQAVSETVTSSASEQSYILTEENWDRIPAMIGITDTDLKEIFGK
[ 6281, 8084, 25186, 27904, 28408, 29033, 30398, 30481, 32134, 41321, 58239, 58458, 59640, 68492, 76189, 87110, 87384, 87449, 87539, 87601, 87683, 87850, 87855, 88008 ]
The following text describes a protein: Function: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase. Has no activity on blunt DNA or DNA with 3'-overhangs, requires at least 10 bases of 5'-ssDNA for helicase activity.
0
MNMQITKILNNNVVVVIDDQQREKVVMGRGIGFQKRAGERINSSGIEKEYALSSHELNGRLSELLSHIPLEVMATCDRIISLAQERLGKLQDSIYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHLVSAQMSGNMEDVAGVTQLMREMLQLIKFQFSLNYQEESLSYQRLVTHLKFLSWRILEHASINDSDESLQQAVKQNYPQAWQCAERIAIFIGLQYQRKISPAEIMFLAINIERVRKEH
[ 15388, 27925, 37231, 39517, 45724, 64377, 64393, 76316, 87123, 87914, 88001, 88008, 88009, 88148, 88150 ]
The following text describes a protein: Function: Mediates the positive regulation of the beta-glucoside (bgl) operon by functioning as a transcriptional antiterminator. This is an RNA-binding protein that recognizes a specific sequence located just upstream of two termination sites within the operon.
0
MSAEEQRTTEEVPEWKRQEVAELVDLLETYDSVGVVNVTGIPSKQLQDMRRGLHGQAALRMSRNTLLVRALEEAGDGLDTLTEYVEGEVGLVATNDNPFGLYQQLENSKTPAPINAGEVAPNDIVVPEGDTGIDPGPFVGELQTIGANARIQEGSIQVLDDSVVTEEGETVSDDVSNVLSELGIEPKEVGLDLRGVFSEGVLFTPEELEIDVDEYRADIQSAAASARNLSVNAAYPTERTAPDLIAKGRGEAKSLGLQASVESPDLADDLVSKADAQVRALAAQIDDEDALPEELQDVDAPAAPAGGEADTTADEQSDETQASEADDADDSDDDDDDDDGNAGAEGLGEMFG
[ 7224, 25435, 27932, 34265, 37431, 54806, 67740, 69830, 69852, 75978, 88001, 88008, 88020, 88022, 88277 ]
The following text describes a protein: Function: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Miscellaneous: MISCELLANEOUS: Was called L10e in this organism; in this case 'e' is for E.coli-like, not eukaryotic-type protein.
0
MPSTPTTPTTTTPITASYWCYSCTRFVSVWADQGTTTVGSVACPHCDGGFIEQINDSSSAATELTIPASTEVRSINNNRRSVIRRRRSGRRPSFNPVIVLQGGAGEREEGEEGDAARDRRAFEFYYDDGSGSGLRPLPDSVSEILMGSGFERLLEQLSQIEASATGIGRSGNPPASKSAIESLPRVEISDCHIGSEANCAVCTEIFETETEAREMPCKHLFHDDCIVPWLSIRNSCPVCRFELPSEPNRRSNNNEEDNAVGMTIWRLPGGGFAVGRFNAAMRDGERVLPVVLTEMDGGGIGNSQDGPRRISWVRSHGTLESDSNGTGSGSGSGGRLRRMVRGMVSLMRRVRPNRSSSSSSAAISTSSDNLDLNIEVESRVLDRSNSVMRRYFRRNRSNRDSSSSVLH
[ 2741, 9300, 9429, 9430, 17018, 25040, 28656, 29166, 34103, 37468, 44906, 46929, 66851, 87112, 87367, 87767, 88008, 88086, 88153, 88181, 88261, 88263 ]
The following text describes a protein: Function: E3 ubiquitin-protein ligase involved in the positive regulation of abscisic acid-dependent drought stress responses. Possesses E3 ubiquitin ligase activity in vitro. Subcellular Localization: Cytoplasm, cytosol.
0
MRAERLRLSEEQGQRILRLYHLYRLTIGLVLVLLISSELEDQVLKLVHPELFHVGSWCYLVFNILVALFLPPSRQLLPIFILALTDVLMLCGLFYAGGGVPSGIGSLLVVAVAIANILLRGRIGLVIAAAASLGLLYLTFFLSLSSPDATNHYVQAGGLGTLCFAAALVIQALVRRQEQTETLAEERAETVANLEELNALILQRMRTGILVVDSRQAILLANQAALGLLRQDDVQGASLGRHSPMLMHCMKQWRLNPSLRPPTLKVVPDGPTVQPSFISLNREDDQHVLIFLEDISQIAQQAQQMKLAGLGRLTAGIAHEIRNPLGAISHAAQLLQESEELDAPDRRLTQIIQDQSKRMNLVIENVLQLSRRRQAEPQQLDLKEWLQRFVDEYPGRLRNDSQLHLQLGAGDIQTRMDPHQLNQVLSNLVQNGLRYSAQAHGRGQVWLSLARDPESDLPVLEVIDDGPGVPADKLNNLFEPFFTTESKGTGLGLYLSRELCESNQARIDYRNREEGGGCFRITFAHPRKLS
[ 3639, 17580, 25079, 27654, 29033, 35965, 38915, 39532, 40530, 63875, 64620, 87110, 87274, 87276, 87694, 87760, 87855, 87914, 88008, 88153, 88159, 88161, 88174 ]
The following text describes a protein: Function: Member of the two-component regulatory system PilS/PilR that regulates the expression of multiple genes including the type IV pilus (T4P) major subunit PilA. Thereby, plays a major role in the regulation of multiple motility pathways. Functions as a membrane-associated protein kinase that phosphorylates PilR in response to environmental signals leading to activation of specific gene promoters including the pilin gene. Subcellular Localization: Cell inner membrane; Multi-pass membrane protein. Note=Localizes at both poles of P.aeruginosa. Also accumulates at the septum of dividing cells, so when the daughter cells separate, PilS is already in place at both poles. Domain: The linker domain is the critical region for polar localization.
0
MNSIHGHYHIQLSNYSAGENLQSATLTEGVIGAHRVKVETALSHSNLQKKLSATIKHNQSGRSMLDRKLTSDGKANQRSSFTFSMIMYRMIHFVLSTRVPAVRESVANYGGNINFKFAQTKGAFLHKIIKHSDTASGVCEALCAHWIRSHAQGQSLFDQLYVGGRKGKFQIDTLYSIKQLQIDGCKADVDQDEVTLDWFKKNGISERMIERHCLLRPVDVTGTTESEGLDQLLNAILDTHGIGYGYKKIHLSGQMSAHAIAAYVNEKSGVTFFDPNFGEFHFSDKEKFRKWFTNSFWGNSMYHYPLGVGQRFRVLTFDSKEV
[ 4666, 8200, 24878, 28223, 39169, 41435, 66234, 87601, 87926, 87965, 88008, 88038, 88134, 88240 ]
The following text describes a protein: Function: Cysteine protease, which is translocated into infected cells and plays a central role in pathogenesis by cleaving the C-terminus end of the human small GTPase RhoA/ARHA, a regulator of cytoskeleton. Once cleaved, ARHA loses its lipid modification, and is released from the cell membrane, leading to the subsequent disruption of actin cytoskeleton of the host cell. Subcellular Localization: Secreted. Note=In infected cells, it is cytoplasmic. Translocated into the host cell by the type III secretion apparatus with the help of the SycT chaperone.
0
MASTMIRTSASLRTLNLTRVFCTTACARAPTMWSITKNQASVTFTWLFGKLGRFSVMRRPSKPPHDFVVPVGNPILRGQALAVDNRNIKSKETQEVLDQLVKVMRKKGAVGLSAPQVGVGLQIIAVECTRKQLDLVPQEIRKIREMQEFPLKIFINPKLKVTDYSTVVFPEGCESLPGYQANVPRYYGVTITGLDREGKPVAWQVTGWPARILQHEVEHLRGDLYIDIMDSRTFIDSSWERKNF
[ 4938, 8138, 14743, 24979, 32054, 32536, 55392, 64554, 87601, 87767, 87968, 88008 ]
The following text describes a protein: Function: Removes the formyl group from the N-terminal Met of newly synthesized proteins.
0
MAEPGRTFNTAFAPPPPLWKHFTPENLQRLENIKKEASKGEDGRRRKKEWSPAELRSLKIPPELRFLVPPEIPSEQYSIFGEVQNLSTALPSLEEQGITQLYPSSPKPDTKSGDSSQPAQPLNHAYYLLKISKSLLLNFLEFVGILSVAPEQFEPKVEDIRNLFINAHHLLNLYRPHQARESLIMMMEAQLARTKDEIQQMDKLKEEVNAVLDQLAAEGADVGSTIQSTTKDKKGVKPEDQIPEDSKLLWDILDGKLDD
[ 8103, 25361, 26679, 27921, 43767, 64907, 71125, 87123, 87857, 88008, 88148, 88150 ]
The following text describes a protein: Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). Subcellular Localization: Nucleus.
0
MWVLGIAATFCGLFWLPGLALQIQCYQCEEFQLNNDCSSPEFIVNCTVNVQDMCQKEVMEQSAGIMYRKSCASSAACLIASAGYQSFCSPGKLNSVCISCCNTPLCNGPRPKKRGSSASAIRPGLLTTLLFFHLALCLAHC
[ 6931, 8732, 13174, 19410, 20043, 22354, 25079, 25325, 26413, 27013, 30983, 31365, 49135, 72017, 87276, 87413, 87489, 87522, 87735, 87760, 88008, 88058 ]
The following text describes a protein: Function: Believed to act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro increases receptor desensitization and decreases affinity for ACh of alpha-4:beta-2-containing nAChRs. May play a role in the intracellular trafficking of alpha-4:beta-2 and alpha-7-containing nAChRs and may inhibit their expression at the cell surface. May be involved in the control of anxiety. Subcellular Localization: Cell membrane; Lipid-anchor, GPI-anchor.
0
MSLSLYAIQALFILDSSGKRIFSKYYTAPHIDSSEHTNEFQTTEEELAFEKAVFKKTWKTQNDVSVVMKHKVVAVQTLDMVFYVVGSSDENEMLLYECVCSVRDALELLLKGVPDKKTLLENYGLLVLTVDETIDDGIILESDPVLIAGRVTKAPTSDAQALVSDIKEMGFMSSLQKARDKFAERILRGAF
[ 8490, 8493, 8494, 24724, 25467, 45293, 54700, 66963, 87367, 87369, 87420, 87528, 87760, 87974, 88008, 88162 ]
The following text describes a protein: Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex. Subcellular Localization: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
0
MPKLLGSFISFKAPNYFVQSAQDAIAIDATALMVFLGPPHSAYRVPFNKMQFSLGYELLKTKNINSNGLVVHAPYIINCASKDPLKQQNAISVLTNEIQLCNLAGAHYLVLHPGSAVAQTTNEALDNLVKVLNQVINKTKTTVICLETMAGKGNEIGRDLTELKYVIDRIVDKDRIGVCLDTCHFHDSGIDFSDLTGVFNTITTKLGFEFLKVIHLNESKNNCGSKKDRHANINAGMIGFENLMKFISHPQIKDLPIILETPSTSLNYPTIYREEISQIRSWFKTYQPDAN
[ 4064, 8068, 27904, 28010, 29072, 29166, 29468, 37373, 46898, 51010, 64004, 87039, 87374, 87380, 87431, 87601, 87767, 87850, 88008, 88261 ]
The following text describes a protein: Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
0
MKVYDDEDNIGVLEQTIFPDKGVLYQQRIVCAEQKINLVQCRLFLTKLIAVFNRGDTFTQEEATELFFATTKLFYSPNVPLRQLLFTALRSVIPYACDVFVVMNSLSKDATSTYDFQRSSALRTLGMILTDQTINSLERHYKQGIVDKIPNVSVSALSTACKLALTHADVVAKWMPEISTALSSSNHLVQYQAIRLLHILKKHDRVALIRCVVTYGKEKPLRSPYAHVELLKICKDILIGERAFSKTVLPLVEYIQTSMRPNNDLVALEAIKLASQLELDAAPQSLSAQLMNSIQVYLQSNKTILRFEAIRVVSEMSYRYNELVSTVRIDVESLLRESNRAILTLAIATSLNICNESSIDGLLNKVAKFMSELPDSFRTKVVNTVEKLAERYPSKYLTLLSFLSHSLTIKGVKFQTAVVNTIRRLCIIQPRCRETSLTTLADYIEDCEYPEIIMKVFSFIGEEGPHSKKPMKYIRSIYNRLLLESPIIRAAGITTLSKFAEIPELKPNIIEILKKCAYDEDQEVRDRACFYSVFLDTPKVETPVITSQTDIDALQHVLEQYINGDCETPFDLEEESKKTIIIEPIKEEEVSNEVKKEQEIIEGFGEVIKKSEVTLTTTGSEYDVVCKKMIYKNNVVLLYSITNTLTDYCLSNVSIEIGIEKGDYKIIEQSTISSLPAQGSDIIKVVLDRPDSLIGTFSNKLIYTLKENIEDDTGDEDEYIIDNVSLNLSDFVSPVEIEDWNVQFESLSKEANKTQIFKFPAFKNLQIAVDKLKELFGLNVINGSDDAKKAVKKHVLLLAGNILLKEPATTFIRLRMLCDEKGVTVEVCIRSTNTLIPDMLLALL
[ 8490, 8492, 8494, 9275, 24724, 25008, 25017, 25467, 28885, 38056, 43603, 46078, 46245, 46911, 46912, 49116, 50029, 60963, 64780, 87367, 87369, 87420, 87528, 87760, 87974, 88008, 88009, 88162 ]
The following text describes a protein: Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. Subcellular Localization: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
0
MNKMLSNDCLGTQEPHTFCKTTETLEHSHLQEITLDKTAAGSTLISHQNVCCIAELSGENTEIMEISLLHNESDAGSTSLLPLPLLSYGPRSMVPIQVPPSSDFESILSPEPIYSDLQLKEMNYNAAAMDESTEFLHLILSGNDEGYNSTTELQVWDVVDFYVSENFSALQFDSLMGFTNEVSTSYNDCMNLVDMVERPVARLSLDDTPKPSNSDDAVPADNVTMDPDETSLYLQTKPTDSETESSSAAGDVETEYLDLKLLSRCMPDLMDVDSPNCLSKTPVKKKHVTLVLDLDETLVHSTLDHCDNADFTLEVFFNMKNHTVYVRKRPYLKMFLEKVAQMFEVVIFTASQRVYAEQLIDKLDPDGKYISRRIYRESCVFSDGCYTKDLTILGIDLAKVAIVDNTPQVFQLQVDNGIPIKSWFDDPSDQELIELLPFLESLVDSEDVRPIISKTFHDKLEQN
[ 24917, 28554, 39455, 46037, 55054, 64168, 76020, 87601, 87970, 88008 ]
The following text describes a protein: Function: Probable phosphatase.
0
MVLESIARIIKVQLPAYLKRLPLPETVGGFAKLTVSEWLRLLPLLGILALLGYLTIRPFLPKKKKQKDSLINLKIQKENPKVVNEIDIEDLKSTNACYCRCWRSKTSYLLIHFGSLGVLHLITRLRRDSSVRAFPVCDKSHIKHNELTGDNVGPLILKKKVL
[ 6740, 9907, 24981, 25014, 32536, 33778, 51593, 52128, 69197, 71352, 87040, 87102, 87194, 87432, 87678, 87681, 87760, 87767, 87785, 87788, 88008, 88159, 88161 ]
The following text describes a protein: Function: Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of BCL2 with BECN1 and is required for BCL2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy. Subcellular Localization: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion outer membrane; Single-pass membrane protein.
0
MSEAPAVMSAEQLLREAVIRIARSDAEPLLLHALGRDRAWLFAHGRDPVPAEQAQRFGALVERRHQGEPVAYLTGSRGFWTLDLAVSTATLIPRADTETLVELALERLELTAGVRVVDLGTGSGAIALAIASERPQAQLIATDASADALAIARHNAHAHGLHNVECRLGHWLQPLAGERFDLIASNPPYIAAADPHLQQGDLRYEPASALASGSDGLDDIRLIVADTPAHLLAGGWLLLEHGWDQGEAVAALLIARGFAAVATHQDLEQRDRVTLGQWPHAAG
[ 2266, 8141, 12244, 27903, 31862, 34958, 37643, 39708, 42637, 52361, 59229, 67851, 75975, 87777, 88008, 88026, 88153 ]
The following text describes a protein: Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
0
MENLQSKFSLVQGSNKKLNGMEDDGSPPVKKMMTDIHANGKTLTKVKKEHLDDYGDASVEPDGEHAKRNRVSLPETLNLNPSLKHTLAQFHLSSQSSLGGPAAFSARYSQESMSPTVFLPLPSPQVLPGPLLIPSDSSTELTQTLLEGESISCFQVGGEKRLCLPQVLNSVLREFSLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQRLCNALLRPRTFPQNGSILPAKSSLAQLKETGSAFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGFESAKWHCYLHVNQKYLGTPEEKKLKIILEEMKEKFSMRNGKRIQSKTDTPSGMELPSWYPVIKQEGDHVPQTHSFLHPSYYLYMCDKVVAPNVSLTSAASQSKEATKAETSKSTSKQSEKPHESSQHQKTVSYPDVSLEEQEKMDLKTSRELYSCLDSSISNNSTSRKKSESAVCSLVRGTSKRDSEDSSPLLVRDGEDDKGKIMEDVMRTYVRQQEKLNSILQRKQQLQMEVEMLSSSKAMKELTEEQQNLQKELESLQSEHAQRMEEFYIEQRDLEKKLEQVMQQKCTCDSTLEKDREAEYAAQLAELRQRLDHAEADRQELQDELRQEREARQKLEMMIKELKLQIGKSSKPSKD
[ 6673, 7021, 7267, 8675, 8742, 9114, 9118, 11620, 11751, 12875, 15195, 16480, 16982, 18440, 21892, 21978, 24841, 24917, 25807, 27733, 27787, 27908, 32467, 38687, 43626, 45219, 48392, 55055, 64718, 87139, 87326, 87684, 87914, 88008, 88180 ]
The following text describes a protein: Function: May have regulatory role in cell division or differentiation in response to extracellular signals.
0
MKIMVAIKRVVDYAVKIRVKPDKSGVETKNVKMSMNPFCEIALEEALRVKELGLASEVVAVSVGPSQFTETLRTGLAMGADRAIHVEAPENIYPITIAKILKALVDVEKPGLLFLGKQAIDNDQNQTGQMVAGLLKWPQGTFASKVVLDKEKQVATVDREVDGGIETLCLNLPAVITTDLRLNQPRYATLPNIMKAKSKPIKKFTLQDLNIEIKSDLEVVEVTEPPKRKSGVIVSSVDELIDKLKNEARVI
[ 12776, 24979, 24988, 29629, 35990, 46227, 48255, 48256, 62163, 87425, 87785, 88008, 88162 ]
The following text describes a protein: Function: The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). Subcellular Localization: Mitochondrion matrix.
0
MSYAGQSSKASSSLDPRSIRTASSSAYPNHAGVGTHHDSEVAFAELQMLSQNQRKLATLTGRMTTILSGFDKRLIKLEGSILPIHKGTQKLARMSDNIDLTLSALNKTLGHYDVVIDEQPLLKQGPDASDTRPYMDTIDRVIKGLDYLQKSNLKSQEGVMKRMNDLIELGARNLCTVISDWVRADSEAIDLSEYSRNAHYPVLSETTHNAIVPIFNYLSTLPQHPRTGFAPMSAGLAVYASVRGDYLKQCLAPLAARLQQHALEQIGTGVTGAGMVMVTQDDDFDSHSNYRRGQAGAVELFEAYYGMLDNDYRILQGLMTSAELDKQTLLLASTFSQLASQPLTALIESLGTVQSHVRRHLATHTSFLLDLIGALSGIVLTGRWDVLLRAMEDSPEAPLHSTSPIDRAELDLNTGFAPAAEVLEIYSKLKNTAIGIFPRFIEDVKAIPARKVSEVPSTSVNEITYLGLQFIRQITEYSDVVSPLLHTLGNGNWMMSSGVAPILSLGLDSDASKQSIVGDYLNDVVAVVLTSLEARSRAIRQPSTASVFLLNNIGHLRRSVSAPLPSYLGAAEDGSSVSIISLHLGEMGNDLLGTALRQANTSYLDAWSPVVAPLMDDQPLNATQYHRHATSKLIGVGSGSEKNQVKDRFARFYEALEDLERLHRAYPVNREDHELKERLTRDVTRLVCPMYARFLAKHKASDFTKNPSKHIRMTEQEVEDKIASLFC
[ 8491, 10368, 24727, 25112, 29046, 39333, 49212, 72412, 87448, 87974, 88008, 88162 ]
The following text describes a protein: Function: Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Also plays a role in the assembly of the exocyst. Subcellular Localization: Bud. Bud neck.
0
MNPQDAPQQDLIYRDFLERFLSNIDIAQIEAMRQQNKIRFPINLDLLRSESRQQYPNLVDDLIRNPTDFIRVFQQKLCQICKQLQDQQEDDDKKGVQTDKTYKIYFEGKLGKNYVTPRGLGAAQINQLVCTQAIVTKMSLVLLKLSKSVHFIEKKNQFKQVEYFNNMDPSARTSARQVRVVQKKDEEGNPMIFEFGLSDLNDMQTLVVQELPERTPTGMLPRSLEVILDQDLVDRVKPGDRVEITGVYKCIPNSTTKANGTFRTTLIAQNIKVMNAVQETKISEIDIRHIKEIAKKSNLLEYMSKSIAPSIFGHGIVKQSILLQLLGGTEKNLETGTHLRGDINVLLIGDPSTAKSQLLRYVMGTAPLVVTTTGRGTSSVGLTAAVKRDNETGENTLEAGAMVLADGGVILIDEFDKMNEIDRVAIHEVMEQQTVTIAKAGIHCSLNARCSVLAAANPLYGEYQQDMAPTKNIGLPDSLLSRFDLLFIILDEKKKDIDRKVAERVTKNHRYKGQYDDEENIGDIIQPMAQMSIKQEISPFVQQSAIYHSNDQKDLLTQSFLKKYIMYAKENYPNVVLDDEAAEEVTRQWTKMRQNDLLEKQIRTQPITIRSLESLIRLASAHAKLRLSNVVTKQDVKIGAKLMKISLQMDQEDEVEDNKKPSGRKSSLQRLKSEQPLSAGRQKLESEQLKQEEQENQLIVKSDKKKQKQDDPKEKEAEFHLFLQQAHSQNITRDQLKAVHKVLRDFKEKLHQDVVDIDIIWGELQSQSRIIIADYLQFLKCLLELDKQEKVQFDDKKRTVQLL
[ 5173, 6798, 8056, 22297, 24917, 26144, 27917, 28298, 29033, 30398, 36945, 38873, 42807, 46277, 58239, 58587, 60237, 62000, 68595, 87110, 87381, 87384, 87539, 87601, 87855, 87857, 88008 ]
The following text describes a protein: Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Subcellular Localization: Nucleus.
0
MDERECLEEKLDFGFAFDSKNFSDRKLHIHIIEELNSSDAESEGEGESKGNDQDDGKDVDNQSFPDICETFETQDGEIFLVTEGDDEYDKFKGEDMIIKPDLHLDMEYKHVLRVEKVYINSAILAANSPFFYKLFSNGMKESVQQHVTLCVYESEEDALIDILRYIYTGKLTSTSASELLTVLIIADRFEVFSCMGYCSRLLCKLPMTLEFAINSLELPCSVSIATSVQPLIDAAKEYLVDRYMNILKCQDELMELPLAAIQSILSSDDLYVASEDVLYDVIVKWVRLKYPIVAERRQVFCTYLCPLIRFPMMSCRKLKKVLRCSELFSEFATKVVLEALFFKADAPHKQRALAQAETLSHRFIERGYKYRPVKIVEFQSPLKQCIVYLNLHRSECSKLFPSGRIYSQAFHIDGQAFFLSAHCNMDQENMFHCFGLFIGMQDKNASALTVDYEFAARTKEEDHEDFVSKYKGYYTFTGGKAVGYRNLFTTQWSKFLSEDSPYFINDVVHLRAELTIKRT
[ 9677, 24917, 36115, 43560, 45551, 45807, 72046, 88008, 88181 ]
The following text describes a protein: Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
0
MLTEEWYELEGWTQDICGIISIVNNLFLMYLILIKSPVALGSYKWLMMFTTCFELAYALVNLIAGSSVRTFGSAWIVFQKSRYRHEITLFLIVVYCACFGFSLAIIACHFVFRYGSVELEFRNKYLSGYKQIFLYVFPFFISIVWGIICWVYCGETPQRTDYLRNKMMDNYHLKIEDVGYVSSYYWPVDENGQVHPDFDSFFGTSLMWVIVGISVMSVLYFGIGCYTWISKKLEFMSSQSVAMKSLQKQLFNALVVQSAIPFILMYVPIGMAFVFPMLNIELNLKYPFISLTVAIYPAIDPLPSILIIASYRKACIDMIRSLKCWGDKGKVTANNTRVDSIAMFTIK
[ 8522, 8678, 14042, 25079, 26499, 31957, 51972, 87276, 87278, 87287, 87311, 87522, 87760, 87860, 88006, 88008, 88045, 88159, 88161 ]
The following text describes a protein: Function: An odorant receptor which affects chemotaxis to the volatile odorant diacetyl. Specifies AWA neuronal cell fate via the odr-7 pathway. Subcellular Localization: Cell projection, cilium membrane; Multi-pass membrane protein.
0
MAASMCDVFSFCVGVADRARGSVEVRYVDSIKGKGLFATQLIRKGETIFIERPLVAAQFLWNALYQYRACDHCLRALEKAEENAQRLTGKPSQILPHPELCSVRKDLHQNCPHCQVMYCSAECRLAAAEQYHQILCPGPSHDPRHPLNKLQEAWRSVHYPPETASIMLMARMVATVKQAKDKDHWVRLFNHFCSRTANQEQAIVHKLLKGKFKDQLELLLGLFKEALYEEALSLWFTPEGFRSLFALVGTNGQGIGTSSLSQWVHACDALELTPQDREQLDTFIDQLYKDIEAATGEFLNCEGSGLFVLQSCCNHSCVPNAETSFPENNFVLHVTALEDIKPGEEICISYLDCCQRERSRHSRHKILRENYLFNCSCPKCLAEADDPNVTSEEEEEEDEEEGEPEDAELGDEMTDV
[ 2070, 2328, 2342, 12244, 15339, 21054, 24011, 24441, 24978, 29166, 30153, 32071, 35565, 35577, 36951, 46079, 70697, 72391, 87367, 87767, 87777, 88008, 88026, 88153, 88180, 88261, 88263 ]
The following text describes a protein: Function: Protein-lysine N-trimethyltransferase that specifically catalyzes trimethylation of 'Lys-22' of the RPL40/eL40 subunit of the 60S ribosome, thereby promoting translation elongation and protein synthesis (By similarity). May also act as a histone methyltransferase in the context of histone octamers, but not on nucleosome substrates: trimethylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4 to form H3K36me3 and H4K20me3, respectively. The histone methyltransferase activity, which is independent of its SET domain, is however unsure in vivo (By similarity). In association with the NCoR corepressor complex, involved in the repression of toll-like receptor 4 (TLR4)-target inflammatory genes in macrophages, possibly by catalyzing the formation of H4K20me3 at the gene promoters. Plays an important role in embryonic stem (ES) cell self-renewal and differentiation. Maintains genome stability of ES cells during differentiation through regulation of heterochromatin formation and repression of endogenous repetitive DNA elements by promoting H4K20me3 marks. Acts as a regulator of the hypothermia response: its degradation in response to mild hypothermia relieves the formation of H3K36me3 at gene promoters, allowing expression of the neuroprotective gene SP1. Subcellular Localization: Cytoplasm.
0
MKFFALFIYRPVATILLSVAITLCGILGFRMLPVAPLPQVDFPVIIVSASLPGASPETMASSVATPLERSLGRIAGVSEMTSSSSLGSTRIILQFDFDRDINGAARDVQAAINAAQSLLPSGMPSRPTYRKANPSDAPIMILTLTSDTYSQGELYDFASTQLAPTISQIDGVGDVDVGGSSLPAVRVGLNPQALFNQGVSLDDVRTAVSNANVRKPQGALEDGTHRWQIQTNDELKTAAEYQPLIIHYNNGGAVRLGDVATVTDSVQDVRNAGMTNAKPAILLMIRKLPEANIIQTVDSIRAKLPELQETIPAAIDLQIAQDRSPTIRASLEEVEQTLIISVALVILVVFLFLRSGRATIIPAVSVPVSLIGTFAAMYLCGFSLNNLSLMALTIATGFVVDDAIVVLENIARHLEAGMKPLQAALQGTREVGFTVLSMSLSLVAVFLPLLLMGGLPGRLLREFAVTLSVAIGISLLVSLTLTPMMCGWMLKASKPREQKRLRGFGRMLVALQQGYGKSLKWVLNHTRLVGVVLLGTIALNIWLYISIPKTFFPEQDTGVLMGGIQADQSISFQAMRGKLQDFMKIIRDDPAVDNVTGFTGGSRVNSGMMFITLKPRDERSETAQQIIDRLRVKLAKEPGANLFLMAVQDIRVGGRQSNASYQYTLLSDDLAALREWEPKIRKKLATLPELADVNSDQQDNGAEMNLVYDRDTMARLGIDVQAANSLLNNAFGQRQISTIYQPMNQYKVVMEVDPRYTQDISALEKMFVINNEGKAIPLSYFAKWQPANAPLSVNHQGLSAASTISFNLPTGKSLSDASAAIDRAMTQLGVPSTVRGSFAGTAQVFQETMNSQVILIIAAIATVYIVLGILYESYVHPLTILSTLPSAGVGALLALELFNAPFSLIALIGIMLLIGIVKKNAIMMVDFALEAQRHGNLTPQEAIFQACLLRFRPIMMTTLAALFGALPLVLSGGDGSELRQPLGITIVGGLVMSQLLTLYTTPVVYLFFDRLRLRFSRKPKQTVTE
[ 10408, 14414, 20911, 25079, 27021, 27474, 29812, 32089, 36802, 55658, 58272, 87274, 87276, 87760, 88008, 88159, 88161, 88162 ]
The following text describes a protein: Function: The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function. Subcellular Localization: Cell inner membrane; Multi-pass membrane protein.
0
MLTIPFLSNYIEKVVTKQLLADNVDTLNYYVTSLLLAFFSFAISCKQYFGTPIQCWVPNEFKGGWEKYAEDYCFISNSYHVPMDEQIQDHHRGDHISYYRWVPIVLALQAVFFFLPNYLWNLMSNNTAFNPRHYVEEASKLKTLTGVAREKEIDALADQFMEGVAVFGRDEYAPRSVFARSGWNCTYLYLLTKALYVLNVVGQMCILNAFLGGTYWSWGADVIGDMLTGREWQEAEVFPRVILCDFSVRAMAQKHTYTVQCVIMMNMINEKLYLFIYLWFIFLIALTLANFFYYLVSLSVPSLRTRLVFCSMDGKRLRLSRRESARFALDCLHPDGVLLIIFIREHVGGRVANELTQKLIQKHYANGSSVSSRSSDGDHCTMESLEKKPFISGMPLTHFDRYDPPPKNHQMSAPKYPHISPNHTMNQTMESAPPVDEFDRYTTMRMDDRSILPRPSPRTTHQGTVLDHTDHPAARNSSPTDV
[ 12938, 25079, 25103, 28908, 36763, 87275, 87276, 87497, 87674, 87676, 87760, 88008, 88159, 88161, 88162 ]
The following text describes a protein: Function: Structural component of the gap junctions. Subcellular Localization: Cell junction, gap junction. Cell membrane; Multi-pass membrane protein.
0
MDMMGKAMFSHQVGKFKEDLGLKGDEEEKTSNYDPRKEAEEEEQLAEQRQRRKEAQGKKQAERAVNRNKIREKYGLKQNKHDQQLVTNHGKPNPSAKEPSRDDSSLTRSGSSSSSQDKKDDKCAVM
[ 10632, 12101, 16500, 25594, 26212, 27652, 30815, 43460, 87448, 87837, 88008, 88162 ]
The following text describes a protein: Function: Positively regulates a late step in synaptic vesicle exocytosis.
0
MRWLPQISFSSPSSSPSSSLKPVASYSESPDPDRNQDRDRFHRRLFRFNRGRLTRQRKLRHLTDDDVLLGERRASTSSSTFDSGLTRSPSAFTAVPRSPSAVPLPLPLPLPEVAGIRNAANARGLDDRDRDPERLISDRTSSGPPLTSVNGGFARDSRKATENSSYQDFSPRNRNGYWVNIPTMSAPTSPYMSPVPSPQRKSTGHDLPFFYLPPKSNQAWSAPDMPLDTSGLPPPAFYDITAFSTDNSPIHSPQPRSPRKQIRSPQPSRPSSPLHSVDSSAPPRDSVSSPLHPRLSTDVTNGRRDCCNVHPLPLPPGATCSSSSAASVPSPQAPLKLDSFPMNSQWKKGKLIGRGTFGSVYVASNSETGALCAMKEVELFPDDPKSAECIKQLEQEIKLLSNLQHPNIVQYFGSETVEDRFFIYLEYVHPGSINKYIRDHCGTMTESVVRNFTRHILSGLAYLHNKKTVHRDIKGANLLVDASGVVKLADFGMAKHLTGQRADLSLKGSPYWMAPELMQAVMQKDSNPDLAFAVDIWSLGCTIIEMFTGKPPWSEFEGAAAMFKVMRDSPPIPESMSPEGKDFLRLCFQRNPAERPTASMLLEHRFLKNSLQPTSPSNSDVSQLFNGMNITEPSSRREKPNFKLDQVPRARNMTSSESESGQQQQQQQYRSPDLTGTVNRLSPRSTLEAIPSPCPSQRPKPSSSDRRRTGVTSDHL
[ 3621, 6680, 7241, 15045, 15833, 16517, 21306, 21390, 24040, 25040, 25079, 28524, 28546, 29033, 35176, 36535, 45290, 50333, 76193, 87110, 87276, 87367, 87694, 87760, 87855, 87914, 87925, 88008, 88153 ]
The following text describes a protein: Function: Mitogen-activated protein kinase (MAPK) involved in the transduction of signal between the host cell surface chitin receptor complex CERK1-LYK5 and the intracellular MAPK cascade that leads to chitin-induced immunity. Phosphorylates and activates MAPK targets (e.g. MKK4, MKK5, and possibly MKK2) when phosphorylated by PBL27 after elicitation by chitin. Required for resistance to the fungus A.brassicicola. Subcellular Localization: Cell membrane. Cytoplasm, cytosol.
0
MPVPNPTMPVKGAGTTLWVYKGSGDPYANPLSDVDWSRLAKVKDLTPGELTAESYDDSYLDDEDADWTATGQGQKSAGDTSFTLAWMPGEQGQQALLAWFNEGDTRAYKIRFPNGTVDVFRGWVSSIGKAVTAKEVITRTVKVTNVGRPSMAEDRSTVTAATGMTVTPASTSVVKGQSTTLTVAFQPEGVTDKSFRAVSADKTKATVSVSGMTITVNGVAAGKVNIPVVSGNGEFAAVAEITVTAS
[ 20285, 20460, 25499, 27003, 38657, 61244, 87103, 87577, 88008, 88207, 88215, 88220, 88228, 88230, 88233, 88235, 88237, 88242 ]
The following text describes a protein: Function: Forms the phage's tail tube composed of 32 hexameric disks. When it encounters the appropriate initiation complex gpM and gpL, it assembles in hexameric rings that stack on top of each others. Multimerization ceases when the correct tail length is achieved through a mechanism dependent on tail terminator protein. Subcellular Localization: Virion. Host cytoplasm.
0
MAWKLFVFFLLFHVFSVFVVVLAASPPENVTIGALLALRTRIGRAARVAIQLAVKEINEDQTLLNGTRLLVQISDDNCNAVQGAAAAVELMQRNRVVAIAGPQTSEVAHFVAHMGTVTKIPIVSFSATDPTLSESQYPFFIRNTHSDRIQMEAIADFVKLFEWKEVVALYSDDNFGTNGIMELHDELSKVGATIPFRAAVSRSMNKDDIGEILAKFGDAGGRIFVVHTDASVGRAVLTEAYDLRMLTTGFVWIVTETLSSVLDGVYSDDEFVAAAQGIVGTRSFIPGSPQLERFKSSWRSFNVNRTRGGYRSSNVNLYGLYAYDTIWMIAYAIDGFLAANGSFEYEAMKCPPGGERRLDLARLSVAKFGARVLREIVKTKFSGISGKVELSAGGELKGSDLEVVNMYGRGLRTVGYWNKGTGFSVDAPSEDRPQMESVSRLQKKLHHIVWPGDNLHVPRGLMIPKTGRELVIGVPLKQGYKEFVDLTIDVSNVSTFHGFCIDVFKAALSSLPYTVTYSFVGFGDGNSTPSYDELVEKVANKKFDAAVGDITITRKRAKLVDFTQPYTISGLVLVVPVTETHAHQAWAFLQPFSNSMWYTTAAFFFFTGTVVWILERDKNRDFGGRPRKQVVTTFWFIFSTLFFSQRERINSILGRIVVIIWLFVVLILISSYTASLTSILTVRRLRPTIQGLSRLVGSDVRIGYQEGSFVKDYLLQLNVESDRLVPLKSIATYSTALSSNEVGAVVDELPYVQLLLSSDCRFAISGEEEFSKSGWGFAFPKGSALAADVSTAVLTLAETGELQRIHETWLHTTRCSGKVVEVKFDKLDLRAFSGLFGFFAVVVVVATLSHALRSYCQNYKTALLAAAPFQWPSHFSRGSRFVRSFRSYVWQTGKNVSVA
[ 25079, 29911, 31958, 37041, 37304, 37459, 48945, 50026, 58725, 70714, 87413, 87522, 87674, 87676, 87721, 87760, 88006, 88008, 88058, 88159, 88161, 88162 ]
The following text describes a protein: Function: Glutamate-gated receptor that probably acts as non-selective cation channel. Subcellular Localization: Membrane; Multi-pass membrane protein.
0
MPPCPPQPNRNRLPQLPTGELGEMELTWQEIMSITELQGLNVPSEPSFEPQAPTPYPGPLPPPTYCPCSIHPDAGFTLPPPPYELPASTPHAPDLPYSYGNIAIPVSKPLTLSGLLNEPLPDPLALLDIGLPVGQPKPQEDPESDSGLSLNYSDAESLELEGTEAGRRRSEYVDMYPVEYPYSLMPNSLAHPNYTLPPTETPLVLESSSGPVRAKPAVRGEAGSRDERRALAMKIPFPTDKIVNLPVDDFNELLAQYPLTESQLALVRDIRRRGKNKVAAQNCRKRKLETIVQLERELERLGSERERLLRARGEADRTLEVMRQQLTELYHDIFQHLRDESGNSYSPEEYVLQQAADGAIFLVPRGTKMEATD
[ 6818, 8103, 8728, 9050, 9052, 9887, 9888, 11689, 11746, 12947, 17715, 24917, 24978, 25366, 25809, 26821, 27733, 27735, 27904, 32073, 33690, 35927, 39957, 39958, 43523, 72396, 73140, 87123, 87367, 87384, 87684, 87857, 87914, 88008, 88148, 88150, 88180 ]
The following text describes a protein: Function: Component of the NF-E2 complex essential for regulating erythroid and megakaryocytic maturation and differentiation. Binds to the hypersensitive site 2 (HS2) of the beta-globin control region (LCR). This subunit (NFE2) recognizes the TCAT/C sequence of the AP-1-like core palindrome present in a number of erythroid and megakaryocytic gene promoters. Requires MAFK or other small MAF proteins for binding to the NF-E2 motif. May play a role in all aspects of hemoglobin production from globin and heme synthesis to procurement of iron (By similarity). Subcellular Localization: Nucleus, PML body. Cytoplasm. Note=The sumoylated form locates to the nuclear bodies PML oncogenic domains (PODs). Translocated to the cytoplasm through interaction with ITCH. Domain: The PXY motifs are required for binding WW domains. PXY1 is required to promote transactivation of beta-globin and for hyperacetylation of histone H3, but not for binding to the HS2 promoter site.
0
MPNEDNELQKAIENHHNQLLNQDKENADRNGSVIEDLPLYGTSINQQSTPGDVDDGKHLLYPDIATNLPLKTSDRLLDDILCDTIFLNSTDPKVMQKGLQSRGILKESMLSYSTFRSSIRPNCLGSLTDQVVFQTKSEYDSISCPKYNKIHVFQAVIFNPSLAEQQISTFDDIVKIPIYHLKVSVKVRQELERLKKHVGVTQFHSLDHLHEYDRVDLSTFDSSDPNLLDYGIYVSDDTNKLILIEIFKPEFNSPEEHESFTADAIKKRYNAMCVKNESLDKSETPSQVDCFYTLFKIFKGPLTRKSKAEPTKTIDSGNLALNTHLNPEWLTSKYGFQASSEIDEETNEIFTEYVPPDMVDYVNDLETRKIRESFVRKCLQLIFWGQLSTSLLAPNSPLKNTKSVKGMSSLQTSFSTLPWFHLLGESRARILLNSNEQTHSPLDAEPHFINLSVSHYYTDRDIIRNYESLSSLDPENIGLYFDALTYIANRKGAYQLIAYCGKQDIIGQEALENALLMFKINPKECNISELNEATLLSIYKYETSNKSQVTSNHLTNLKNALRLLAKYTKSDKLKFYVDHEPYRALSQAYDTLSIDESVDEDIIKTAYSVKINDSPGLKLDCDRALYTIAISKRSLDLFNFLTEECPQFSNYYGPEKLDYQEALKLLQVNENASDETILKIFKQKWFDENVYEPDQFLILRAALTKISIERNSTLITNFLLTGTIDPNSLPPENWPTGINNIGNTCYLNSLLQYYFSIAPLRRYVLEYQKTVENFNDHLSNSGHIRRIGGREISRGEVERSIQFIYQLRNLFYAMVHTRERCVTPSKELAYLAFAPSNVEVEFEVEGNKVVDQTGVLSDSKKETTDDAFTTKIKDTSLIDLEMEDGLNGDVGTDANRKKNESNDAEVSENEDTTGLTSPTRVAKISSDQLENALEMGRQQDVTECIGNVLFQIESGSEPIRYDEDNEQYDLVKQLFYGTTKQSIVPLSATNKVRTKVERFLSLLINIGDHPKDIYDAFDSYFKDEYLTMEEYGDVIRTVAVTTFPTILQVQIQRVYYDRERLMPFKSIEPLPFKEVIYMDRYADTENPLLLAKKKETEEMKQKLKVMKNRQRELLSRDDSGLTRKDAFLESIKLLESDTIKKTPLKIEAANDVIKTLRNNVQNIDNELMKLYNDINSLEEKISHQFDDFKEYGYSLFSVFIHRGEASYGHYWIYIKDRNRNGIWRKYNDETISEVQEEEVFNFNEGNTATPYFLVYVKQGQEGDIEPLKRILK
[ 4562, 9996, 10221, 10754, 12115, 14521, 14522, 18436, 24917, 24978, 25040, 28657, 34086, 37104, 50970, 56774, 59082, 66234, 70893, 87601, 87914, 87965, 88008, 88134, 88181 ]
The following text describes a protein: Function: Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to ubiquitin. Hydrolyzes polyubiquitinated 'Lys-63' polyubiquitin chains in RPO21, producing mono-ubiquitinated RNA polymerase II. Removes ubiquitin chains that initiate proteolysis of FZO1 and inhibit mitochondrial fusion. Miscellaneous: MISCELLANEOUS: Present with 2420 molecules/cell in log phase SD medium.
0
MTRFTDTLWSSITDIYQAIIYHPFNEELARGILPREKFAFYMQQDALYLADFARALAIMAGRAPDEAAIIQFVRFAEGVAVVERALHHTYFREFGIETPTRQPAPACFTYTNFLLATAACRSYEEGMAALLPCFWIYREVGHDIYRRAAPNNPYQKWIDTYAGQEFDEVVTQAIALTDTIAEQASATQQQRMRDAFIYSARLEWMFWDSAYRLEQWLP
[ 5043, 9225, 9226, 25040, 33469, 39484, 49154, 58373, 76622, 87601, 88008, 88128 ]
The following text describes a protein: Function: Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, a reaction that is part of a thiamine salvage pathway.
0
MTKDMETIVSLAKHRGFVFPGSDIYGGLSNTWDYGPLGVELKNNVKKAWWQKFITQSPYNVGIDAAILMNPKTWEASGHLGNFNDPMIDNKDSKIRYRADKIIEDYMLNEKGDENFVADGLSFDEMKRIIDEEGIVCPVSGTANWTDIRQFNLMFKTFQGVTEDSTNEIFLRPETAQGIFVNYKNVQRTMRKKLPFGIGQIGKSFRNEITPGNFIFRTREFEQMELEFFCKPGEEIEWQNYWKTFASQWLKDLNLSEEATRLRDHDADELSHYSNATTDIEYRFPFGWGELWGIASRTDFDLKKHSEHSGEDFQYHDQETGEKYIPYCIEPSLGADRVTLAFLCDAYDEEGVEGSKDSRTVLHFHPALAPYKAAVLPLSKKLSGDAIKVFEELSADFAIDFDESQSIGKRYRRQDEIGTPYCITFDFDSLEDEKVTVRDRDTMEQVRMPITELKSFLAEKVKF
[ 6297, 8151, 24978, 28636, 29033, 30298, 32578, 35318, 37864, 37865, 39345, 41180, 54850, 58077, 61977, 64364, 72021, 87110, 87145, 87367, 87722, 87855, 87968, 88008 ]
The following text describes a protein: Function: Catalyzes the attachment of glycine to tRNA(Gly). Subcellular Localization: Cytoplasm.
0
MEREMAASYEPKLNSEIRIFESSDEIVTDLAEYISQVSEISVKERGYFAIALSGGPLVSFLRKLCEVPYNKTLDWSKWYIFWSDERAVAKNHADSNYKLTKEEFLSKVPILSGHVYSINDGATVEDAATDYEFVIRQLVKIRTIGVSESNDCPKFDLILLSMGSDGHVASLFPNHQALELKDDWVTYITDSPQPPPERITFTLPVINSASNIAILATGVDKANAVHSAVSDSSDGLDAAAPLPARMVQPTDGKLVWFLDKAAASSLEALSDDAYQQQHL
[ 3961, 7854, 9131, 25040, 30456, 40925, 41142, 64872, 66515, 87601, 88008 ]
The following text describes a protein: Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
0
MKRYIALDIGDVRIGVARSDIMGIIASPLETINRKKVKSVKRIAEICKENDTNLVVVGIPKSLDGEEKRQAEKVREYIEKLKKEIENLEIIEVDERFSTVIADNILKELNKNGAIEKRKVVDKVAASIILQTYLDMKK
[ 3921, 6853, 24978, 28400, 40317, 41585, 46274, 64743, 87367, 87601, 87850, 88008, 88023 ]
The following text describes a protein: Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. Subcellular Localization: Cytoplasm.
0
MKYVLVTGGVVSGLGKGVTASSIGVVLKACGLGVTSIKIDPYLNTDAGTMSPFEHGEVFVLDDGGEVDLDLGNYERFLDVTLTKDNNITTGKIYQSVLDKERKGDYLGKTVQVVPHITDAIKDWIESVSLIPVDGKEGQADVCVIELGGTVGDIESMPFIEALRQLSFSVGPDNFCLIHVSLIPVLGVVGEQKTKPTQHTVRELRALGLTPHFLACRSAQPLLESTKAKLSQFCHVAAANILNIHDVPNIWHVPLLLRNQNAHHSILKQLNLTNVATAPDLDSWNKMAETFDNLTNHVQIAMVGKYIGLTDSYLSVVKALLHACIACSLKPHIEWIAASDLEDESEKSTPEAHAAAWKILKSAECILVPGGFGDRGVSGMVLAAKYARENKIPYLGICLGMQIAVIEFARSVLGLERANSTEFDAQTSDPVVIFMPEGSRTHMGSTMRLGSRRTHLHNRDSLTSKL
[ 6488, 14820, 25040, 26898, 28001, 29033, 39625, 50342, 50777, 58239, 59228, 62053, 87110, 87511, 87722, 87855, 87976, 87988, 88008 ]
The following text describes a protein: Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
0
MTHSLKPWNTFGIDHCAKHIVCAENEQQLLSAWQQATREGLPVMILGEGSNVLFLENYAGTVILNRLKGIEVNETADAWHLHVGAGENWHQLVRYALDNNMPGLENLALIPGCVGSSPIQNIGAYGVELQRVCDYVDCVELETGKRLRLSAAECRFGYRDSIFKNEYQDRVAIVAVGLRLSKQWQPVLTYGDLTCLDPKTVTAQQVFDAVCHMRTTKLPDPKVNGNAGSFFKNPVVAADIAMELLERFPNAPHYPQADGSVKLAAGWLIDQCQLKGVTIGGAAVHRQQALVLINANDATSKDVVALAHHVRQKVGEKFNVWLEPEVRFIGRSGEVNAVESIA
[ 1634, 9079, 9244, 16787, 18986, 25040, 29408, 33679, 34431, 38538, 41093, 45717, 49218, 49219, 49220, 64081, 64378, 87004, 87272, 87273, 87279, 87281, 87367, 87455, 87470, 87823, 87873, 87890, 88008 ]
The following text describes a protein: Function: Cell wall formation. Subcellular Localization: Cytoplasm.
0
MNSYLLAFKSGFGFLTTIPVGISMEGIDELMKKIYFYPVVGAVLGLLIGAIAYIGQLIFPDPVLAALIMGSVYYFTGFNHLDGVTDMGDGFMAHGSHEKKIKALKDTTLGTGGVAFGMLVLLAFYGSIRSIQDEGINVFGSNLPLLMFASMFIAEVSAKQSMLTIAAFGKPLPRPENQAYPGLGEMTINGATRKNFLIGFIFGAFVCFLPFGLIGLIPYLAACISALVLLNRSYAHFGGLNGDGIGTANEIGRITALIIIAVTLELSLNTGGLEWTLL
[ 3800, 9231, 25079, 29455, 33728, 39045, 87016, 87276, 87320, 87747, 87760, 88008, 88153, 88159, 88161 ]
The following text describes a protein: Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate. Subcellular Localization: Cell membrane; Multi-pass membrane protein.
0
MDARLTVLTAFPPAAGIDNEEYYQNSQQHAKRVRELVRDNAQWIRESADDILKHVNPAVYSLSYLMILEFLLQSPGWTSQQAHESLASYMAQFFLQFDARQIRCKGSTWSDVLKEAYSERGLFPASVAVELVTAALLRLDPSGSIITSHHCNLVELAYNTGNVGALLPLIEKPIIYMPAKGMSTAQPLCDMSLPPPAYINPDSQLTDALTSAAVLQYDFLCGLCFIERRMWQQAFDAFERCVTYPTRDGGCSKIMTEAYNKWILVGLLLTGKPPTLPETTSQAAKKIFATQGKPYKLFAQAFKSETAGDLVREFEVINSELLPNEGNVELAKLVLAHYQRWQIINLRNIYTNISLEKIQERTQSAETGAPLPTVEAVDQLVQSMIADGSLQGAIERPKDGSPAYLTFLSSPAQGMSEVEFSAQVNKVMQGIKALEPIIEATNKRLASNREYISHTVKRQFDAAREHKLGLQSAGGGFEESSFHIEEEEDLMSGLPAH
[ 8202, 24978, 25142, 36533, 76411, 80613, 87367, 87857, 88008, 88062 ]
The following text describes a protein: Function: Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex is involved in the regulation of the circadian clock through its control of the stability of the SCF(FWD1) complex. Subcellular Localization: Cytoplasm. Nucleus.
0
MIKYLSAHLRLARHDKPIGALLLHIPCVWGTILGQPTFNFQEIIWYSSVFGVGSFTMRAAGCVVNDMWDRNIDNKVERTRQRPLASGELQMKDAWISLFAHCSVGLLVLTQLSWSTIAASFGIVPIAFLYPLAKRYFSYPQLVLGIAFNWGVVVGGLQLAGMLNPTIMLGYAAGIVNTLIYDTVYGHQDKEYDKSLGLYSTAYTLPKNTPLYLTWVFSGLIGLTCYAASYHPGVYPLIVLNQLDMYLRLKATDFDNPESCGKFFRDFKWFQITIALIFGAGSYMKQ
[ 3238, 8398, 9059, 24983, 29219, 30317, 36382, 41343, 59825, 66964, 71116, 87016, 87685, 87760, 87785, 87786, 88008, 88153, 88159, 88161, 88179 ]
The following text describes a protein: Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate. Subcellular Localization: Membrane; Multi-pass membrane protein. Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side.
0
MHPISACRRASPLSTPRFQDIFVDASLKADRAGIGVNYHTRREFEKYSLVRRPDRRPDSNHAELAAIFVALLHSRGSRKTRIFTDSQTSIDLIREGTLDPRFAVLVGCSRWLLAESEETLLFKVKGHSGVPGNEVAHRLAAMGRRDGAIVLPDYLIGRAECRDRLIPALIDECARLNQWQIESFKRTQAGASSQAEIMSSSSVCTKKRTMPTISGEVPSSEAASSRSSLTRLLTSSASTPTSFLESESNLLGLMLASLSYAADNMTFDFKPHFHKAFQLAEEIGSGSFGRTHVAFARKMGDGDGKRVAVKVIPKRRMSSQVEIDDVVREVEILRVLQRNENVVEFIDAYEDAMNVYIIMELCSGGDLSDRILDAGGRCSEESAVPLVWQILSAVAYMHRRGVIHRDIKPENFLFASDDENSILKAIDFGLSDYCREGDVLSDIVGSPYFVAPEVLKKAYDLKADEWSIGVMTYIMLVGARPFYGRTQSEVFRSVLDEKPNMEEVEITAEARDFIEKLLTRDVRGRLTAAQALTHPWMSEVRNR
[ 13402, 24917, 24978, 27903, 28405, 28529, 29026, 29033, 29662, 36535, 37731, 42974, 45290, 46274, 50333, 64155, 75860, 87110, 87694, 87855, 88008, 88052, 88153 ]
The following text describes a protein: Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner.
0
MNQEAASNLGLDLKLNISPSLDSSLLTESSSSSLCSEEAEGGGGEAKSMVVVGCPNCIMYIITSLENDPRCPRCNSHVLLDFLTGNHSKKSTS
[ 9379, 9515, 24235, 87441, 88008, 88086 ]
The following text describes a protein: Function: Involved in ethylene-dependent salt stress responses by reducing reactive oxygen species (ROS) accumulation.
0
MNAISLAVDQFVAVLTIHNPPANALSSRILEELSSCLDQCETDAGVRSIIIHGEGRFFSAGADIKEFTSLKGNEDSSLLAERGQQLMERIESFPKPIIAAIHGAALGGGLELAMACHIRIAAEDAKLGLPELNLGIIPGFAGTQRLPRYVGTAKALELIGSGEPISGKEALDLGLVSIGAKDEAEVIEKAKALAAKFAEKSPQTLASLLELLYSNKVYSYEGSLKLEAKRFGEAFESEDAKEGIQAFLEKRKPQFKGE
[ 5513, 8306, 28229, 37402, 51112, 59212, 87460, 87729, 87731, 87741, 88008 ]
The following text describes a protein: Function: Involved in the degradation of long-chain fatty acids.
0
MEAQDYFVGGYYGAGENQFSPEKRHGDQKPPCEPFAIDDLLDFSNADVIMSDGFFDNNVAGNSTDSSNVTAVDSCNSSGSGGDNRFGGTIVPYGFSGDVQLTGELCVPYDDMAELEWLSNFVEDSYSAEEELKTLQLLSGAGAVKPQTPESSSSTDTLPSFSTDETARNASFLRPETPLPGKARSKRSRAAPGDWSTRLLHLPDAPPKNYPIVKKREDPNVECSGRKCLHCGTDKTPQWRTGPMGPKTLCNACGVRFKSGRLVPEYRPAASPTFVSAKHSNSHRKVLELRRQKEMQRSSQHHHHHQHQQLLSHSSIFGVSSNGGDDFINYHHHCGPEFRHVI
[ 8103, 11620, 15388, 24917, 27731, 29166, 36499, 46933, 49664, 76794, 87123, 87384, 87767, 87857, 88008, 88148, 88150, 88261, 88263 ]
The following text describes a protein: Function: Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters. Subcellular Localization: Nucleus.
0
MDPSRYGRQQEWDNNSAPEGYGTQHDPNHRFGVSYDDGYPDERLMRDDVYNYPPGHNTLGDLPQSRKRNYEENYPSELRRQEKPYIDSNYAADYYHDSEAGSRNGHYRDHEHERSSRYDGCDDYSCNDNNYRSKNYHHSRDDGREKDYDYTRRSYDSEYERASVRDGSRKSRDPQDRERNSRDREWDSRDREWDKRCYSRERDESPHKRYEKSRSRSTGRGEFSRSRSPRGRSHGRSYREDSYEGDHWNESERRREYEDRHNQDHFSATPSATVVVKGLSMKSTEEDLYQILAEWGPLHHVRVIREQNSGISRGFAFIDFPTVDAARTMMDRIEHDGIVLDGRKLMFHYSQPTGRAGVSRRQEHASRRSYGGSRNMIVPTDWICTICGCINFARRTSCFQCNEPKTKDSPSADVGLSNSAAGKRISETGPTHVLVVRGLDEDADEEMLRYEFSKHAPIKDLRLVRDKFTHVSRGFAFVHFYSVEDATKALEATNRTALERNGKILRVAYAKSVHGSGTGISAPSHSNNLAAAAIEAATFSQQYDGVGWAPKEYNTGEKQNTGGQAQGVGEIESQKGTSAPQSGYVWDEASGYYYDAASGYYYDGNSGLYYDSNSGLWYSYDQQTQQYVPCPDQNNESKVTENQPDSAKKEKSSQQKVIISAATTPNVEKVLSLPDAVQAAAAAAIASEKREKERVKEIKLASKTSLLASKKKMSNVLTMWKQRSHETQIQRPSPSLGDNPPTVSAEARSSFSTGQSMGKLKSDVIIAKERSTSNHGVSALTTAESSSSSTTGGTLMGVMRGSFGGTLGGASSSASVQMPPILPSASPASVSVSGSGRRRFSETPTAGPTHREQPQTSYRDRAAERRNLYGSSTSSGNDVIDSSEDLMGLRKGSSDPTPFPPGVGGRGITTSTEVSSFDVITEERAIDESNVGNRMLRNMGWHEGSGLGKDGSGMKEPVQAQGVDRRAGLGSQQKKVDAEFEVQPGDTYRTLLHKKALARFRDMSDNN
[ 6736, 8126, 14660, 24917, 24945, 27925, 29166, 36320, 36354, 37500, 46581, 63444, 63774, 64198, 68619, 87139, 87767, 87857, 88001, 88008, 88009, 88072, 88261, 88263, 88273, 88274 ]
The following text describes a protein: Function: Splicing factor that controls alternative splicing of the developmental regulator ABI3. Reduces splicing of a cryptic intron in ABI3, leading to a decreased in ABI3-beta transcript. Regulates the splicing of the receptor-like kinase SNC4/LRKL-2.6. Subcellular Localization: Nucleus.
0
MNDQLTEVYASIDALIDYALAHLDLDPRNADWTRNQIFALFRLDSYPGPKTTTSAASVSDVVQDIVGSRSQAPYGEKTPDPLLAAFRAAATTAGLFKPEEGPAYADTIMGILSANPADLDDRFLLVEHRDGGMAAMQWFYDYCVANNYVKRAQLDRNPRFDSHGLTVTINLAKPEFKNMKKAAAGNAVAGGYPKCTICHENEGFAGRDKRTLRTLPVTLGGESWFWQFSPYGYFDQHGICVNTDHTPMHVDRDTFGHLLDFVDRFPGYFLGCNAALPRIGGSVLAHDHYQGGGELLPMHKAATWAAFTLADYPDAVVEILDWPGTAVRVVSKSRQSIIDVSDIIREAWVGYDDAANGIASHDADGNRQSALSPSAIITERGYEMSLIFRNNAISDEYPEGIFHAHPEYWPVKQEPIGLIEAQGLFILPGRLVDQLGIVEEALAEGRDLPDEVSEFSLEWGELAETLAGNHDREAIRQAVHDELGSVCYRILGNTAVFKQKATTQTFLESLGFAAR
[ 3703, 7854, 7887, 24978, 29083, 36573, 40875, 87258, 87367, 87494, 87856, 88153 ]
The following text describes a protein: Function: Transfers the UMP unit from UDP-glucose (UDP-Glc) to Gal1P. Can also transfer the UMP unit to GlcNAc1P and GalNAc1P. Involved in the general galactose metabolism, and also involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria. Subcellular Localization: Cytoplasm.
0
MERQPKRFVGASVRNVDEIYKRIKPLFREISSCSRCEERRSASKGTPKAYCVTVDVERCFDTIRPRKLYQVLKKAIQEDEYLIRKHWVGHQVAPISDSDESLPSSSFFFKLERPAYPSGELLGFEELAAQSKKENAMFVDGVLYDYLTKAKALELLKEHLSTNVVQVDGRDYVQRCGIPQGSVLSTTLCNMYYAHFERRVLGKRLPELYVNYEKLSSSLLQASIPFNETKAAQEFFVTKVVSAIRQRWHALYFDPELLSEDTIRVNLFQMQIVAAHRFTILIEMLPFVNRDMHFFHECIHRILKKMTKGIHRSLELAAQPSSGLSLSSYHAQKHQVRKYSNLSTYILPLTCLFVPLVQVWTIGLRAFQLMIQAKRDQAKTSNAQRKQQCNWVDWQKLLDAIQSEQKEFKQQEKKTRSTGPAFDFAWLMSDRRNASMLKRCLGVGSVDRS
[ 3731, 8564, 24761, 24785, 25325, 27924, 32009, 32536, 34243, 36329, 38838, 69990, 87306, 87747, 87760, 87767, 87856, 87857, 88002, 88008, 88125, 88153, 88159, 88161 ]
The following text describes a protein: Function: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Subcellular Localization: Nucleus. Chromosome, telomere.
0
MGITSPPTEDSGGGGGELSEPMPFKFVAWAGSADASFWHRLADFKLDTQKLTEVPISISGFFAPCNQPHAPSYLQLMMESLPLDTGASNEPTEVPYNRNRLPVPGMLYNTNTLESYNALDKPALLRATADQIWDDIKSGRAEEDTSLLSRFLVVSYADLKKWTFTYRFAFPGLRMSPQATAAACQAARDFFSKDEIAGVLAACTEWRALPSGASLTSFLINITPDGSIKSQSLKEWHTAQQEGGKIVLTFYDPSNLPANPGWPLRNLLALASVRWGVSRLQVLCYRENRSGQLDLEHSPVLDIILPAKIEWMEPVGWELNARGGKGSKFVDLGQSMDPLKLAESAADLNLKLMRWRLLPSLDLPRMASTKCLLLGAGTLGCQVARTLMAWGMRHITLVDYGRVAFSNPLRQSLFTHEDSLHNGKPKAEAAAENLKRIFPGVNAVGVQMSIPMPGHSVGKNEIAGVVEDCRRLKELVDTHDVVFLLTDTRESRWLPTLLCADANKVAINAALGFDTYLVMRHGAAPSLDSNSSSDGQPRLGCYFCNDVVAPLDSTANRTLDQQCTVTRPGLAPIAASLAVELAVALLHHPLGVSAPGDQATSLTDNTEHPLGIMPHQVRGFIAHYAQLVVTGQAFDKCTACSASVVREFREKGVEFILEVLNRPNYLEDLTGLTELLRITDDEPLVWDDDADF
[ 6653, 6741, 8558, 9701, 10368, 12329, 13102, 16517, 21241, 24766, 24978, 30766, 30767, 36429, 41263, 60999, 63779, 69423, 69424, 72043, 87194, 87367, 87974, 88008, 88162, 88181 ]
The following text describes a protein: Function: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for autophagy. Subcellular Localization: Cytoplasm. Preautophagosomal structure.
0
MLKYPDYISKLISFLKKLPGIGFKSAEKIAFELLEWDPSQIEAMAQALQEFSTSHATCSNCFCLKISQTSPCNFCSESRDSSSLCIVATPKDVFALEKSKIFKGHYFVLGNLLSPITGKHLSLEKLAILKQRIEACSPKEMIIALDATLEGDATALFLKQEFSYLPIKISRLALGMPVGLSFDFVDANTLARAFSGRNCF
[ 6797, 8078, 27904, 29166, 36025, 41162, 49082, 55388, 62320, 87374, 87379, 87380, 87767, 88008, 88261, 88263 ]
The following text describes a protein: Function: May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
0
MTPRSRLATLGTVILLVCFCAGAAHSRGDTFQTSSSPTPPGSSSKAPTKPGEEASGPKSVDFYQFRVCSASITGELFRFNLEQTCPDTKDKYHQEGILLVYKKNIVPHIFKVRRYRKIATSVTVYRGLTESAITNKYELPRPVPLYEISHMDSTYQCFSSMKVNVNGVENTFTDRDDVNTTVFLQPVEGLTDNIQRYFSQPVIYAEPGWFPGIYRVRTTVNCEIVDMIARSAEPYNYFVTSLGDTVEVSPFCYNESSCSTTPSNKNGLSVQVVLNHTVVTYSDRGTSPTPQNRIFVETGAYTLSWASESKTTAVCPLALWKTFPRSIQTTHEDSFHFVANEITATFTAPLTPVANFTDTYSCLTSDINTTLNASKAKLASTHVPNGTVQYFHTTGGLYLVWQPMSAINLTHAQGDSGNPTSSPPPSASPMTTSASRRKRRSASTAAAGGGGSTDNLSYTQLQFAYDKLRDGINQVLEELSRAWCREQVRDNLMWYELSKINPTSVMTAIYGRPVSAKFVGDAISVTECINVDQSSVNIHKSLRTNSKDVCYARPLVTFKFLNSSNLFTGQLGARNEIILTNNQVETCKDTCEHYFITRNETLVYKDYAYLRTINTTDISTLNTFIALNLSFIQNIDFKAIELYSSAEKRLASSVFDLETMFREYNYYTHRLAGLREDLDNTIDMNKERFVRDLSEIVADLGGIGKTVVNVASSVVTLCGSLVTGFINFIKHPLGGMLMIIIVIAIILIIFMLSRRTNTIAQAPVKMIYPDVDRRAPPSGGAPTREEIKNILLGMHQLQQEERQKADDLKKSTPSVFQRTANGLRQRLRGYKPLTQSLDISPETGE
[ 10917, 15813, 25325, 25398, 25414, 26307, 26310, 26481, 36134, 63241, 63243, 66110, 87103, 87413, 87522, 87569, 87573, 87581, 87586, 87595, 87760, 88008, 88058, 88159, 88161, 88194, 88203, 88237, 88242 ]
The following text describes a protein: Function: Envelope glycoprotein that forms spikes at the surface of the virion envelope. Participates in viral entry through an RGD motif that binds ITGAV-ITGB3. Membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. Subcellular Localization: Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein. Host endosome membrane; Single-pass type I membrane protein. Host Golgi apparatus membrane; Single-pass type I membrane protein. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN).
0
MFNSFSKSSLEFILTETQCTTMEQFSASSMSRHHAPYDRRFGSIYPLFQLLGFTPVPLHGQALTSLRTLTIVFVSFYTTGEIIVLSYSLIKPEAVFFLSDATGTFADAIQFVIPLAVPLVTLTLSLLKRSTQKRIALLMDQIDGSIEAHGAAPGCLERFNHQLADDIFSTMFVFNVIPAVSEFFIISRISGNPVWHRNWLLKVWFFILIRLGDSFFLVHVLYLRNRYRVLNNELQQTASTVGRAISPEAIHRRLVHLKAMQNLLKDLTGEVSDRFGWQLFAVITMLFICTTIDGYWMYASLHYDGNLYKVESFLCGISPVLMFFVLFNTCQKCVDEGEITFYYLHSVLNRVLPQTTITLIENFSKQLDNEQINFSAANFFDIRLSSLTTIFGSITSYLVIYINFIPKTDTFNDYNKEHNLVTT
[ 8663, 8996, 9008, 16569, 25079, 25494, 25495, 26197, 47375, 87276, 87760, 88006, 88008, 88152, 88159, 88161 ]
The following text describes a protein: Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. Subcellular Localization: Cell membrane; Multi-pass membrane protein.
0
MTDKLTLTPLERALQCARFALDKKALDVKVLEIGRISSIADYLVLATGRSDKQAQAIADSVKKGLKKYGKVIDMEGLREGNWIVIDYGDVIVHIFREELRSYYDLDGLWSAAGQVAIPAEYLWEGKEGGGE
[ 10779, 14126, 19692, 24978, 32119, 39562, 70002, 87367, 88008, 88010, 88155 ]
The following text describes a protein: Function: Functions as a ribosomal silencing factor. Interacts with ribosomal protein uL14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation. Subcellular Localization: Cytoplasm.
0
MSRGRGVPMMDLKRSYDVEDRVVSVSIPSIIEADEADLWPLPEIDTKKSKFPCCIVWTPLPVVSWLAPFIGHIGLCREDGVILDFAGSNFINVDDFAFGPPARYLQLDRTKCCLPPNMGGHTCKYGFKHTDFGTARTWDNALSSSTRSFEHKTYNIFTCNCHSFVANCLNRLCYGGSMEWNMVNVAILLMIKGKWINGSSVVRSFLPCAVVTSLGVVLVGWPFLIGLSSFSLLLFAWFIIATYCFKNIIT
[ 9420, 9671, 24724, 25008, 25014, 25018, 43165, 87432, 87528, 87760, 88008, 88159, 88161 ]
The following text describes a protein: Function: Acts at an early step in the ethylene signaling pathway. Positively regulates ETR1, leading to the negative regulation of ethylene responses. Subcellular Localization: Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
0