Datasets:
lhallee
/
plat_data

Dataset card Data Studio Files
xet
Community
1
sequence
stringlengths
13
8.92k
annotation
listlengths
2
214
description
stringlengths
61
12.1k
labels
int64
0
0
MLKKKLSLEDEDDDRSYNLRSSRSNAKSKPRSSAGTATNPRASKRARLSGASATQEDSSLVDKIRLSFEDFDEALSGFKVSSGYERSKNTDLWVDKYRPRTLEELSVHKKKVDEVKLWFQESLDFLKNGLRNNVLLVTGQAGVGKSATIHLITSILGVTVHEWNAPIPTIWQEHVHNTSSGLKYTSKLDEFENFVESTRKYGVMASSSTDGIKAPVVLLIDDLPLANGRHAFERLQNCLLLLVKSTQIPTVILITDHNNADSSDQTARRMEDTQSSLERAGALKVAFNPITKNSIKKVLQRICREEHCKVTTMEIDQMATASGGDIRHAITSLQLFSVKPELNHTKIKSPRPGMEDNYHGNEQTMYSGLDSGISSCFGRDETLSLFHALGKFLHNKRETDNVIISECSSSLVHDEFARLPLKMDAPEKVLSQAHGQAGRVVDFLHENVLDFVSDGAIEDAWCVSSYLADADLLLADIRGKMSGHNNTEDVPQSAGASVAVRGVLYGNKQPCSSRWHVIRKPKLWQVEQSSIQTKKNLREQRNISYEGSRVADISVMATEYSPVLKWLSYRASPDAFPGMGEETDEEDSDISEDDEIQDW
[ 8065, 8066, 8531, 12016, 24917, 29033, 39731, 58239, 73763, 87110, 87272, 87374, 87855, 87857, 87925, 88008 ]
The following text describes a protein: Function: Seems to be involved in regulation of DNA repair correlated to non-homologous double strand breaks (DSBs) repair. In vitro, involved in rapid but not in slow DSB repair mechanism. Required for effective immune responses that involve activation of DNA damage responses. Subcellular Localization: Nucleus.
0
MVLSRGETKKNSVRLTAKQEKKPQSTFQTLKQSLKLSNNKKLKQDSTQHSNDTNKSVKAKKNGTSSKKTGTQRKRISTQRFSLFTYGNVQVMNSFVPIHNDIPNSSCIRRNSQVSANNVTESSGVFFNDTQSQDSQNTIKLKPTSLMAKGPIEIYQICTGFDKLKENIAPFQKSSKASSHDGHVVNYLSIGRHGDIVHPVLPKLQITRLNGAGFKYFISFYNPERYWEIEFLPLISQSQSELENSVKAFENVISKICQFSHINEGATIGNNESLSDKFKLPPTSDIEPPNTEIINNDDDNDDDDDNYDDDDLNYLLDEEYEQGCTDNSFSVISNTCSNLNASFLYPSDPTDAVSISINEAFKNAIRRTAPVLNIPIAAPSIHSKQQNKRYSSYPFIDSPPYLQDRHRRFQRRSISGLGDL
[ 15016, 25004, 25006, 31013, 56359, 87760, 87894, 87914, 88008 ]
The following text describes a protein: Function: Required for peroxisome inheritance. Miscellaneous: MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium. Subcellular Localization: Peroxisome membrane; Peripheral membrane protein.
0
MNYNDTTEFCFPFGQPSFPTSAMTEGSFDGQFSEFDPTFTSPADTALSDIANLPIDLHKDALFANAPGKGDVDFDSVSMLQLLSDYPLAFNSTENNQKLQTNPSARWSLLDSMDFDNQRQCSDLESAQLGDSGLLKSTILSNSHIDIAALSSSKTSEPTPPFSYVQTPCIPTPSSALIDTPFPGALDSEFGFDESQAPLFPASDGDCQRAFASISYPTNYGCKLSNLGFMSPQSPVKRELNDSTSPSKLSESSSSLTGSSSALLSQSEFLGSVPSLSDSIATVDPFFSFESFETDEKARSLLMDASLKLPQFSTPNLSSNSSSLSLKSTLAEGMKGSTPLAAVKTEKASKAARVMKQKKHREHVCFNCGVTETPLWRRTSDKLNFLCNACGLYNKQYGVMRPLSPRNKGSSKALENLVCANCSSTKTSLWRKDRHGQTVCNACGLYARLHGHNRPIGLKKNKITRRRRGKGPGGEDGMSDEVKSEFPVLSKSVTMAEILSSKGLESPQLTNSVSVSKMPNTDADVSLEHAKISFDSLDNSVIVKKEEEIENKFSVSC
[ 6673, 9909, 15427, 22933, 24917, 25040, 27733, 27735, 27788, 29166, 36499, 46933, 66716, 87123, 87367, 87384, 87767, 87857, 88008, 88009, 88148, 88150, 88261, 88263 ]
The following text describes a protein: Function: Activates genes required for amino acid biosynthesis and acts as a master transcriptional regulator during amino acid starvation. Binds variations of the DNA sequence 5'-GAT[AC]GC-3'. Miscellaneous: MISCELLANEOUS: Functional homolog of the S.cerevisiae GCN4 and mammalian ATF4 bZIP transcription factors. Subcellular Localization: Nucleus. Cytoplasm.
0
MNTFYIFFLFVLTTCFVKGDLPIHALMGDVSGIWKIKQTKKMSQKPEHCGGGIPNRNLDNLNPSIRNYQRFLENEYGNLDMMIVNLTMEKVKIINQEKPRDKWTYLAVRDYERNEIIGHWTMVYDEGFEIRLNGSKYFAFFKYERKSNAHCPTSIEDKSYNDRDCYKTNPTQTHIGWVLNEKVKENTKEKIFYWGCFYAEKKESTPVSSFVLHNGMENKTNLVESHDYHFEEKKKKNLPPIGRRSNYKKFRFSNLQKIYGSTQTHLRDIYGRSGERKYGCRKRDILNLKIRLTLPKQFSWGDPFNDENFEENVDDQKDCGSCYSISSVYSLERRFEILFWKKYKKKVNMPRLSHQSILSCSPYNQGCDGGYPFLVGKHMYEYGIIPEQYMHYENNDYNNCIMDMGNYNHLNKQNRNIKEIYYVSDYNYINGCYECTNEYEMMNEIILNGPIVAAINATSELLNFYNIEDKNVVYDILPKDTHQVCDVPNKGFNGWQQTNHAINIVGWGEQIINQDKIKNDDANNNNNDNNHKLVKYWIIRNTWGKNWGYKGYLKFQRGINLAGIESQAVYIDPDFSRGYPKNILQSDSLE
[ 4519, 8200, 16922, 24907, 24993, 25325, 28218, 28223, 29150, 36082, 36489, 46964, 48384, 57104, 57105, 64244, 66234, 66757, 87063, 87146, 87290, 87413, 87522, 87601, 87760, 87965, 88008, 88058, 88134, 88264 ]
The following text describes a protein: Function: Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Subcellular Localization: Membrane.
0
MATTTSHATNTWIKTKLSMPSSKEFGFASNSISLLKNQHNRQSLNINSSLQAPPILHFPKQSSNYQTPKNNTISHPKQENNNSSSSSTSKWNLVQKAAAMALDAVESALTKHELEHPLPKTADPRVQISGNFAPVPENPVCQSLPVTGKIPKCVQGVYVRNGANPLFEPTAGHHFFDGDGMVHAVQFKNGSASYACRFTETERLVQEKALGRPVFPKAIGELHGHSGIARLMLFYARGLFGLVDHSKGTGVANAGLVYFNNRLLAMSEDDLPYHVKVTPTGDLKTEGRFDFDGQLKSTMIAHPKLDPVSGELFALSYDVIQKPYLKYFRFSKNGEKSNDVEIPVEDPTMMHDFAITENFVVIPDQQVVFKMSEMIRGGSPVVYDKNKVSRFGILDKYAKDGSDLKWVEVPDCFCFHLWNAWEEAETDEIVVIGSCMTPPDSIFNECDEGLKSVLSEIRLNLKTGKSTRKSIIENPDEQVNLEAGMVNRNKLGRKTEYAYLAIAEPWPKVSGFAKVNLFTGEVEKFIYGDNKYGGEPLFLPRDPNSKEEDDGYILAFVHDEKEWKSELQIVNAMSLKLEATVKLPSRVPYGFHGTFINANDLANQA
[ 572, 9300, 9325, 9379, 9397, 9425, 9429, 9430, 9431, 9441, 9491, 9503, 10651, 10653, 16241, 21575, 21782, 25257, 29725, 32453, 32536, 39474, 87008, 87111, 87112, 87296, 87402, 87409, 87476, 87678, 87767, 87873, 87930, 88008, 88154 ]
The following text describes a protein: Function: Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid (ABA) biosynthesis from carotenoids. Required for ABA accumulation upon drought (Ref.2). Required for ABA-mediated regulation of anther/pollen development, including metabolism, cell wall modification and transcription level. Positive regulator of fruit ripening involved in the biosynthesis of abscisic acid (ABA); initiates ABA biosynthesis at the onset of fruit ripening. Modulates the degree of pigmentation and carotenoid composition as well as pectin catabolism during ripening and may regulate the ethylene production and action in climacteric tomato fruit. Subcellular Localization: Plastid, chloroplast stroma. Note=Partially bound to the thylakoid.
0
MNLHTNNNNNNNNYVDENLFWKVYKNLFIRNLIFYKIISTTVIYKYDDDDSLSSGKFIVPSDRVQFKNIISLSWIVKRNLWSLLKYKLISNEELIIKKKAIELLLQECKHDKDLLKLIYQNKYYQMNQIDLILNSIKHSNLMALKLFIEEYNLPTNNNSMDMALEIASKQYYRNEEEQKQSFEVFQFFWEKKKDTLQCTQSELFNQNRNYNAYMLQLILNNPSLYGESLQSNNNNNNNSSSNNIGLMTSREFFNLAVMSVIPEKIKIELLNRGFVKNEKSIYRDGDYIAKTIQKQSPYLPKSIYSYLEKSYQKNELYENRTISVFYFFKILIEYPEKEDSLSILKDFVNVAYKFTDLEIRSYNTLSLNPNSYKAGQKVEILQAISSFNFTLKIKIIESLFPIDSLTLESTRFIFDRLKSSIDNAGTMKHVSKAELIPQSLYHLNIIKTADVELLDQFLNHFHSDAERNLIFKIDDENPLNKDYFKDCSIQDSEKISKFIDKLSSVKEFNSNSKSFLNCLKSKLLPISSELYISSLLKFKETSRKQTYVHAKVLDETLCDFFSEKNNFKSNLTSFIKFINFRSLSITYLVEKVLFSNDFELIELLLNTICNNNNNYGAGIIMVPVSFKTSNPDIIKLIISKSNWHKLFDFKGLIDTVISDSNVCNISNPNTDSQTIELIETVIDFLHSNKIYQRNSKEGFGFGFGFGTTNQQENHTEKTIISNDATKIALLKKKSIKILQLLLKYKNLFDWDSQLFPKLPKLPTIQLDDEILPKSDKPIMSIYEQQELEDQDLYQSRRRKPKNKHGGGRGRRRIDTYNDTAYDGTNNNIPYIGSIGGSVFASTEDSVNGGGSGFYSSSSSIGSISSISSISSISSSNNNNELGSDQSQFILGGNFTGFSGNYQSKSKDKKKIRNLYNTNFLDKFKTHQAQSIFDTMDQLFTRNYTFSFAYTSDSVFQDSIYHSIKNRRIDVIEKLITIQMFTDNHAKLIYSDFLKRIIRNDDGVDLVTFKYLFSHRFLKIFSTEFLQTMSQELLICAVSECCFHLCHWLLSTDNPCNVYVEFLPFKTTYILNVEKKLSYCASPVFKDYMMKKIKPFIKY
[ 8398, 24983, 29172, 46661, 87733, 87785, 88008, 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
MKNIVLASLLGFGLISSAWATETVNIHERVNNAQAPAHQMQSAAAPVGIQGTAPRMAGMDQHEQAIIAHETMTNGSADAHQKMVESHQRMMGSQTVSPTGPSKSLAAMNEHERAAVAHEFMNNGQSGPHQAMAEAHRRMLSAG
[ 26161, 32536, 87411, 87767, 87892, 87926, 88058 ]
The following text describes a protein: Function: Component of the sil cation-efflux system that confers resistance to silver. Subcellular Localization: Periplasm.
0
MKRVIMENIKEKFEFEVNSEYEGMRLDKYLSEQIEEATRSYLEKLIDNNFVKVNSKIINKNGRKLKLGEKIEVLIPEEENIDIEPENIPLNIVYENDDFILINKSYGMVVHPAYGNYTGTLVNALLYYTNNLSSVNGNIRPGIIHRLDKDTSGLILVAKNNYAHAKLASMFIDKTIHKTYLCIVKGNFSEENLSGRIENLIGRDSKDRKKMTIVKENGKIAISNYKVVEQVEGYSLVEVAIETGRTHQIRVHMKSINHVILGDSVYGTEDKNVKRQMLHAYKLEFLNPLDNKKYIFKGKLFDDFIEVAKRLKFNIEKYI
[ 6175, 6755, 27925, 29669, 30353, 35262, 38358, 41140, 41205, 41206, 52563, 64706, 75843, 87683, 87741, 88001, 88008 ]
The following text describes a protein: Function: Responsible for synthesis of pseudouridine from uracil.
0
MATTSTGPLHPYWPRHLRLDHFVPNDLSAWYIVTVLFTVFGALVVTMWLLSSRASVVPLGTWRRLSVCWFAVCAFVHLVIEGWFVLYQKAILGDQAFLSQLWKEYAKGDSRYIIEDNFIICMESITVVLWGPLSLWAVIAFLRQHPSRYVLQFVISLGQIYGDLLYFLTEYRDGFQHGEMGHPIYFWFYFFFMNVLWLVIPGVLFFDSVKQFYGAQNALDTKVMKSKGK
[ 4473, 6122, 8361, 11608, 14761, 24918, 25008, 25014, 25636, 25708, 26230, 27670, 28592, 31584, 32073, 33044, 42688, 61633, 87298, 87299, 87369, 87411, 87432, 87601, 87683, 87728, 87731, 87760, 87857, 88008, 88077, 88078, 88081, 88082, 88159, 88161 ]
The following text describes a protein: Function: Isomerase that catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers; Component of the microsomal antiestrogen binding site (AEBS), a multiproteic complex at the ER membrane that consists of an association between EBP and 7-dehydrocholesterol reductase/DHCR7. This complex is responsible for cholesterol-5,6-epoxide hydrolase (ChEH) activity, which consists in the hydration of cholesterol-5,6-epoxides (5,6-EC) into cholestane-3beta,5alpha,6beta-triol (CT). The precise role of each component of this complex has not been described yet. Miscellaneous: MISCELLANEOUS: Binds to the phenylalkylamine calcium-ion antagonist emopamil, an anti-ischemic drug. Subcellular Localization: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus envelope. Cytoplasmic vesicle. Note=During interphase, detected on the endoplasmic reticulum and the nuclear envelope. During mitosis, detected on cytoplasmic vesicles.
0
MGPKLFKPSIDWSRAFPDSVYWVGKAWTISAICVLAILVLLRYLTPWGRQFWRITRAYFVGPNSVRVWLMLGVLLLSVVLAVRLNVLFSYQGNDMYTALQKAFEGIASGDGTVKRSGVRGFWMSIGVFSVMAVLHVTRVMADIYLTQRFIIAWRVWLTHHLTQDWLDGRAYYRDLFIDETIDNPDQRIQQDVDIFTAGAGGTPNAPSNGTASTLLFGAVQSIISVISFTAILWNLSGTLNIFGVSIPRAMFWTVLVYVFVATVISFIIGRPLIWLSFRNEKLNAAFRYALVRLRDAAEAVGFYRGERVEGTQLQRRFTPVIDNYRRYVRRSIAFNGWNLSVSQTIVPLPWVIQAPRLFAGQIDFGDVGQTATSFGNIHDSLSFFRNNYDAFASFRAAIIRLHGLVDANEKGRALPAVLTRPSDDESVELNDIEVRTPAGDRLIDPLDVRLDRGGSLVITGRSGAGKTTLLRSLAELWPYASGTLHRPGGENETMFLSQLPYVPLGTLRDVVCYPNSAAAIPDATLRDTLTKVALAPLCDRLDEERDWAKVLSPGEQQRVAFARILLTKPKAVFLDESTSALDTGLEFALYQLLRSELPDCIVISVSHRPALERLHENQLELLGGGQWRLAPVEAAPAEV
[ 6620, 24878, 25079, 29033, 30398, 35372, 38739, 38873, 45676, 50737, 58239, 64383, 76490, 87103, 87110, 87276, 87760, 87855, 88008, 88157, 88159, 88161, 88162 ]
The following text describes a protein: Function: Multi-solute ABC transporter that mediates uptake of unrelated hydrophilic compounds. Can transport vitamin B12 and related corrinoids, and antimicrobial peptides such as bleomycin. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Contributes to maintenance of chronic infections. Subcellular Localization: Cell membrane; Multi-pass membrane protein. Domain: Contains a large occluded hydrophilic cavity that spans the entire thickness of the membrane and extends into the intracellular part of the protein. It consists of two connected chambers. The larger chamber is located in the transmembrane domain, and the smaller chamber is formed by the part of the protein that connects the NBDs and transmembrane domains.
0
MLDFIKGKVITVKPDKIVIQTGGIGYSVKIPIRVSRYINRDEETQIFTSLIVKEESIEIYGFLESSERDLFEELIKIAGIGPKMAINILSTYDRETLYKIIDHEDIKSLSKIPGIGKKTAQRILLELRGILPSLQYEKDQKYDDILSALLNLGYKRLEAKEVLDKIYNNEKDEATIIRESLSILAGKDGK
[ 8065, 8084, 9304, 24978, 25206, 26466, 27696, 29033, 29631, 36019, 38868, 45278, 45378, 46277, 47579, 64034, 87367, 87374, 87379, 87380, 87384, 88008 ]
The following text describes a protein: Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA. Subcellular Localization: Cytoplasm. Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
0
MANVKKVCVIGAGVSGLSAIKSCLEEGFQPTCYEQHDDLGGIWYYTEDPRPNQGAAMFKSVVSNISKSMLSYSDFPFPEDAPMYPSHERVHQYLREYADHFNLLPHIRFGTQVIKVEEAKDHVTSGQWMVHTSGNGGKHETFDAVILSNGSAFGRPVSPDVPGYETFKGVKLHSYQYRTNKPFEGKRVLIVGSGNTAFDLAVDVCRVATQVDLALLKGTWVVPRLHKKGTPIDLHAFRRVYSDIPVSWLNGIFKDFSNNRFDHDKYGVAGRQQPITQSTPTINDDIGLCLASRKVSIKPQLVKLFGTSARFADGTTVGDVDAVIFATGYVNSCSFLDHELEADIKKLDLYKLVFPTRLAHPTLALVGAGQSNGPLFPLMELQARWAARVFKGVHKLPNSDTMKANTEVYKDMVLATFGRLKPVTNNVVYRDDIAAEIGAKPNLLWLIIKDPLLAYMYYFGPAYPFHHRLVGPNPWKGAAAASKHAYYNTLSGVATSFTPKDSGSVWLHTKMMFTCVIIGVICALVIITRL
[ 0, 25014, 28380, 28382, 33679, 33680, 36736, 53023, 63960, 76001, 87004, 87432, 87455, 87470, 87760, 87809, 87823, 87873, 88008, 88159, 88161 ]
The following text describes a protein: Function: Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics. Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytoprotective and developmental processes. In vitro, catalyzes the N-oxygenation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) and could therefore participate to the detoxification of this compound that is generated by the action of gut microbiota from dietary precursors such as choline, choline containing compounds, betaine or L-carnitine. Subcellular Localization: Endoplasmic reticulum membrane; Single-pass membrane protein.
0
MQDVSTCYVFKSRLQEYAQKVGLPTPVYETTKEGPSHEPMFTSTVIVNNVRYESLPGFFNRKAAEQSAAEVALMRLVNSGSMENLSQPVVIYFILHHLRQNNCASALICTVILTVLYSNQKPQCQHETGLCKNLLQEYAQKMNFAIPKYECRRYDPEGKVITFSCTIDVGGMRYVGAAARTKKEAEIKAARTALLAIQSSSTGPNGYSAYTVLPMKKVTDLSISNQESAAALKPKKNRFKKKKKRNVCTRNTGDVQVQMVNQGTESPAPLAPTMGDPAPFNISSSVENRTALVVSQNDRGTSTLGINSQFGGAGTAEGNAVIGVEQVTSEVHSSTVVITWRNNSHVR
[ 8125, 9888, 24917, 27927, 28406, 48249, 70724, 88001, 88008, 88009 ]
The following text describes a protein: Function: Binds double-stranded RNA.
0
MPFLWLCWALWALSLVSLREALTGEQILGSLLQQLQLDQPPVLDKADVEGMVIPSHVRTQYVALLQHSHASRSRGKRFSQNLREVAGRFLVSETSTHLLVFGMEQRLPPNSELVQAVLRLFQEPVPRTALRRQKRLSPHSARARVTIEWLRFRDDGSNRTALIDSRLVSIHESGWKAFDVTEAVNFWQQLSRPRQPLLLQVSVQREHLGPGTWSSHKLVRFAAQGTPDGKGQGEPQLELHTLDLKDYGAQGNCDPEAPVTEGTRCCRQEMYLDLQGMKWAENWILEPPGFLTYECVGSCLQLPESLTSRWPFLGPRQCVASEMTSLPMIVSVKEGGRTRPQVVSLPNMRVQTCSCASDGALIPRRLQP
[ 6673, 7607, 8802, 9050, 9052, 9557, 12376, 14058, 21278, 21287, 24878, 24907, 28832, 28864, 29073, 31969, 36864, 37466, 39161, 48918, 50791, 59202, 87363, 87402, 87413, 87522, 87532, 88008, 88038, 88058 ]
The following text describes a protein: Function: Required for left-right axis determination as a regulator of LEFTY2 and NODAL. Subcellular Localization: Secreted.
0
MQFQLTFFLHLGLLSYAKAQDECHRGACHPTTGNLLVGRGAQLTASSTCGLDGAQKYCILSYLEGEQKCFICDSRFPYDPYAQPNSHTIENVITSFEPDREKKWWQSENGLDHVSIRLDLEALFQFSHLILTFKTFRPAAMLVERSTDYGHTWKVLKYFSKDCAASFPNVTSGQAQGVGDLVCDSKYSDIEPSTGGEVVLKVLDPSFEIEDPYSPHIQDLVTLTNLRINFTKLHTLGDTLLGRRENDSLDKYYYALYEMVVRGSCFCNGHASECGPMQTVRGDVFSPPGMVHGRCVCQHNTDGPNCERCKDFFQDAPWRPAAGLQDSTCRACSCNGHSDRCHFNSTVYLASGGLSGGVCEDCQHNTEGQHCHRCRPLFYRDPLKAISDPYACIPCECDPDGTISGGICVSHSDPAVGSVAGQCLCKDNVQGAKCDQCQPNHYGLSAADPLGCQPCDCHPHGSLPLSPCDVDTGQCLCQPSATGPRCDECAVGYWGLENHLHGCSPCDCDIGGAYSNVCSPKDGQCECRPHITGRSCTEPAPGYFFAPLNFYLYEAEEAMPLQGLAPLGSATFGQVPADHGVFPEPVPGSPVTWTGPGFARVLPGAGLRFTVNNIPSAMDFAVAIRYETQSADDWAVQIMVNPPRGSKHCTRKTPWPKPQSFALPAASRIVLLPTPICLEPDVQYSIDVYFSQPLEGRSHAHSHILVDSLGLIPQINSLENFCSEQDLDEYQLHNCVEIASEARPRVLPSACERLIVSVSARLHEGAVACKCHPQGSVGPSCSRLGGQCQCKPHVAGRCCDRCSAGSYGLGHHGCHSCHCHPEGSKSIVCDQITGQCPCQGEVAGRRCDRCLAGYFGFPNCRPCLCNGFAELCDPETGSCFNCGGFTTGRNCERCIDGYYGNPSSGQSCRPCPCPDVPSSNQYFAHSCYQNPWGSDVICDCLQGYTGKQCEECSAGFYGNPRISGAPCQPCACNNNIDLSDPDSCSRVTGECLRCLHNTHGPNCQLCKPGHFGSAINQTCRRCSCHPSGVNPAECRPDQGACLCDPDTGTCPCLPNVTGQACDHCADGYWNMIPGRGCQPCDCDPQTSHSRHCDQVTGQCLCKLGYDGKRCSECKENYYGDPQGRCIPCDCNQEGTQKPVCDQATGMCRCQEGVSGPRCDRCARGHNQEFPACLPCHSCFDQWDHTISSLSKAVQGLIRLAATMDDKRETLPACEADFKDLTENMSEIERILKHPVFSSGEFLKVKDYHDSVRKQIEQLSGQLKTVYEFQDLKETTERMRNEADLLLADLQEEIDLRSGARNASIVDSLESIKKYYQSSSYAEKETNETTLIISNSEKTRNDLLTNLDTLTSKGNLSREKLKQIKIPDIQILNEKVCGERGGAPCVVSACGDPRCHGSLTLSRDALQKAQEAESTTHNLSNQFQGLKNQIKNISKLAEVSKNNALQLSEKLRNMKNQSESEEEKLNLLIKKLKKFLLEENVPPEDIEKVANRVLDIRLPVTSQNLTHELDKIRKLTQLCEDYRADENRLNKAAEGARKVLVKAKGAKKAAHVLLNLDKMSNTLQQVRITQGRANSTITQLTAEITKLKKNVLQAENQAKETKNELHLAKQQSALEDGLSQLWTKLQRNRDQASRVKAQAESARRQAGGLEEEFVELKNQYAVLQRKTSATGLTKETVGKVKQLKDAAEKLAGDAEDKIRRITDLEKKIQDLNLSRQEKADQLKQLEDQVIAIKNEIVEQENKYATCYS
[ 8835, 9520, 9521, 10729, 13029, 18639, 24878, 24904, 26236, 36552, 37641, 42933, 46893, 76095, 87214, 87270, 87326, 87413, 87453, 87522, 87706, 88008, 88009, 88038, 88058 ]
The following text describes a protein: Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Subcellular Localization: Secreted, extracellular space, extracellular matrix, basement membrane.
0
FGFINYEVGDSKKLFFHVKEVQDGIELQAGDEVEFSVILNQRTGKCSACNVWRVCEGPKAVAAPRPDRLVNRLKNITLDDASAPRLMVLRQPRGPDNSMGFGAERKIRQAGVID
[ 12862, 24818, 25296, 27925, 37649, 45392, 46277, 56259, 87367, 87914, 88001, 88008, 88009 ]
The following text describes a protein: Function: RNA-binding protein involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Required for efficient formation of stress granules. Subcellular Localization: Cytoplasm. Cytoplasm, Stress granule. Cytoplasm, P-body.
0
MKLLVCYLLAITCVLVDADKGERILKLTEVIKELKALNRTVTHNSVMSNAPSMDTEECCSQSALKCFRAMVPHLKAKNKTLQRKVIKNLNNRMILGSLDSCSQEEREKTVCQGCDSYPKDSQKCVQQLESLLQKAISRLA
[ 8534, 9989, 24907, 28832, 28833, 38743, 43641, 87363, 87413, 88038, 88058 ]
The following text describes a protein: Function: Cytokine with immunoregulatory activity. May promote the transition between innate and adaptive immunity. Induces the production of IgG(1) and IgG(3) in B-cells. Implicated in the generation and maintenance of T follicular helper (Tfh) cells and the formation of germinal-centers. Together with IL6, control the early generation of Tfh cells and are critical for an effective antibody response to acute viral infection. May play a role in proliferation and maturation of natural killer (NK) cells in synergy with IL15. May regulate proliferation of mature B- and T-cells in response to activating stimuli. In synergy with IL15 and IL18 stimulates interferon gamma production in T-cells and NK cells. During T-cell mediated immune response may inhibit dendritic cells (DC) activation and maturation. Subcellular Localization: Secreted.
0
QSWSSILYLERNRPQPTGTATALNSPCAETAWPAAASPGARGGAARQPGPGHHASPAGRAAGLRGWKSPSPTEQSVSPGLDGGEQSSPRAPPGLLHKARPGRLPPGRRHPRPRPPARRVARLVRAAVAAAGRLPSPEACPYLRWQRRRRRPTWGPAANGLPACAAGPAREAEVPRAAASVSAAAPAGYITRLGLRAAPRLGCLRPQDALSPTTASAAAGSRPRYPDSWYRDITSNKKFFSLAATYRGAIVGMIVAEIKSRTKIHKEDGDILASTFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALANLSPCSIPHRIYRQAHSLLCSFLPWSSISTKGGIEYSRTM
[ 2607, 2673, 8603, 24724, 28307, 28460, 36091, 49230, 71362, 87125, 87302, 87307, 87528, 87760, 88008, 88153 ]
The following text describes a protein: Function: N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues of the transmembrane proteins, with a strong preference for N-termini facing the cytosol. Displays N-terminal acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. May also show histone acetyltransferase activity; such results are however unclear in vivo and would require additional experimental evidences. Subcellular Localization: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
0
MPNLIILVFVGGAFGAMCREFIMLSVPRLADGFPMDIFVANIIAAFLLGLTTSFFKKDKINQYVHLMVGTGIMGGLSTFSSFVFGAVEMMKNPTEVLVSICYLVASLIVGFIAVELGLMIGPKEKPKDPQVASE
[ 20858, 22507, 25079, 32536, 34177, 35774, 38943, 87274, 87276, 87674, 87676, 87760, 87767, 88008, 88064, 88159, 88161, 88162 ]
The following text describes a protein: Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. Subcellular Localization: Cell inner membrane; Multi-pass membrane protein.
0
MLTIGQLARIFEISTKTLRHYDAIGLFVPARTGSDNGYRYYQPEQIEQLSRILALRRLDVPLEAIDRLKRDGALDDPQRLRHFLQRHQHTLREEISARQRLLAELDRTLATLAHWRIRNMHARIVERPAFSVVGMEYFGSAPGDTIGQLWERFIPREHEIAGKHDPEVSYGICAQQPNGEFHYVAGFEVQEGWPVPEGMVRFQVPAQKYAVFTHKGTAPQIAESFQAIYSHLLAERGLEPKAGVDFEYYDQRFRGPLDPNSQVDLYIPIY
[ 8101, 15387, 15388, 25809, 27656, 27731, 27782, 27918, 36394, 43626, 44867, 45480, 59593, 73036, 87103, 87123, 87384, 87855, 88008, 88010, 88148, 88150 ]
The following text describes a protein: Function: Transcriptional regulator. Responsive to the second messenger cyclic di-GMP (c-di-GMP) and to the virulence factor pyocyanine, which both enhance gene expression and promoter DNA binding of BrlR. Activates expression of operons encoding the multidrug efflux pumps MexAB-OprM and MexEF-OprN and several ABC transport systems, acting by direct binding to their respective promoters. Also acts as a repressor of the two component regulatory system, PhoPQ. Binds to promoter of its own gene. Contributes to the antimicrobial tolerance exhibited by biofilms, acting, at least in part, by activating expression of multidrug efflux pumps and ABC transporters. Miscellaneous: MISCELLANEOUS: Biofilm bacteria exhibit a profound tolerance of various antimicrobial agents, rendering biofilm cells 10- to 1,000-fold less susceptible than the same bacteria grown in a planktonic (free-floating) culture. Second messenger cyclic di-GMP (c-di-GMP) has been associated with controlling the transition between a motile and biofilm lifestyle; increased levels contribute to resistance of exponential-phase planktonic cells to tobramycin and norfloxacin.
0
MEQYEILEQIGKGSFGSALLVRHKHEKKKYVLKKIRLARQTDRVRRSAHQEMDLISRVKCPFIVEYKDSWVERGCYVCIIIGYCEGGDMAEAIKRANGVQFSEERLCTWLVQLLMALDYLHVNHILHRDVKCSNIFLTKNQDIRLGDFGLAKMLTSDDLASSVVGTPSYMCPELLADIPYGSKSDIWSLGCCLYEMTAHKPAFKAFDIRALINKINKSMVAPLPTMYSSAFRGLIKSMLRKNPEFRPSASELLTHPHLQPYVLKIHLKSSSPRCDNFPTRWSDSSFMKKTKFVENDSMRFSDIGRRRSFSNDRALNPSVSETEQDSLSGIRRVQEIPSYLFEKFTEFSVGIDNEDITADKSTATKFSAVAKTPRLTPAVSVTPRKHIIPSKISKTGQKHDLVPVSQTPSSKSSYSSRRVSLPLPSRTAAIVTPYGANVGSLPTTNSPDVSVNAPRIDKIAEFPLASSNDPVLPIRQTSKCASSSSSIDSADRSITKDKCTVQILEKAVATSNVSDQSLGVAQDGSEGGSEHNRAAVSIHSSSESRQRRFDTSSYQQRAEALEGLLEFSARLLKQQRYDELGVLLKPFGPEKVSPRETAIWLAKSFKETQV
[ 3604, 28524, 29033, 36535, 42974, 45290, 50333, 76315, 87110, 87694, 87855, 88008, 88052, 88153 ]
The following text describes a protein: Function: May be involved in plant development processes.
0
MRGEERWQEQPALASHPSRATLRPRGWPRLGLAPTGVGSSCPPAPASELARHLARRAPVSASPPVLPPIKDQGARPPTLAASAAAASSPPPPPPPPIPPLPPSTSTSAARPTDMAGVTSKRRSSSASTSSSSGDGAAVSDRPRGVTRKRRSGGRCPRPAASLRPAAPRPSSHHTAGLRVILQKELRYSDVSQLGRIVLPKKEAEAYLPILTSKDGKKSLCMHDLQNAQLWTFKYRYWPNNKSRMYVLENTGDYVRTHDLQLGDSIVIYKDDENNRFVIGAKKAGDQQAATVPQVDEHISTLFPIFPIAQVDDYLSPMAPQVDISAFVPHADENHEIFDGILNSLPEIPVANVRYSDFFDPFDDGMDMANTLNANANQSASLHVTDDKSGHSLIPNPKSGPHM
[ 8101, 9535, 16188, 24917, 27731, 27918, 38654, 48767, 71043, 87384, 87472, 87857, 88008, 88010, 88148, 88150 ]
The following text describes a protein: Function: Transcription repressor involved in flowering time regulation. Represses the flowering activator EHD1 by binding specifically to the DNA sequence 5'-CATGCATG-3 of its promoter. Miscellaneous: MISCELLANEOUS: Plants overexpressing LFL1 show a late-flowering phenotype. Subcellular Localization: Nucleus.
0
MGNKNKEKKKARKRQLSNSKTNEDLEVIEVSLQKKRLLDDSVDIVQAGNVRCAEKGTKKTVKSVLQHLFKDKPLETLPTRELIGNQLVAAIRNRHFAIVEGPLGCGKTFLGLYASSVLGLPIHVMQMGDQIDSKTLFGSYHCTEVAGQFVWKESTFAKWLQAPGVILLEDIDAANADVVSKIVDIATYRQTDASNSEKNLDFHNEVRIIATMSGKGKKTAVLDGVPVRIRVESLSDDELKRLASKSYPRIAHLSRTLISTFRKIENVPGTGNSRQLTSTDFLRGCARLALLPNISANVETFAELIDTWCLADPRQRANQLCNIVASSLNVNPDRVNTHLSVRQPEVKYDEHVVSVGRSKIPRKMSMIKTGRHRLGHTRDVVQLMERIGVCVSHNEPLLLVGETGVGKTSIVQAVADLIGVTLDVVNVSPTSDSDELIQGYKPTTIGRLMEPFTKFYMEVFTKNFDSKNNQKFVDNLEKCLSSGRFKDYLSLVEATAIKALQRKCTNKENDGQNFWFVQDKFAMVSKKEQLRSLSRKALFWRLRKKDIGFLLMRLTWLHQSVLTQSLTHYQHPEHIQASTLESVVFHQEYERGLIVFIFKSSRFYRFTEFFVSETSDPFQLALIVSAYLPTVSQPFVENLVKFYMSAKQLYPSSYSLRTLCRALNFTADNMFGSVDQSIYEAVSMAFLTNLESEEKGVMRSKIQTAFRCKVGVMPEPKESHNYVKIGGYYVQKGTLLPENDPKYVITKTVKGNLAEIARIVCSGRFPILLEGETSAGKTSIICHLAKVTGNKIVRINNHEHTDVQEYMGSYVADSGGRLVFREGALVQAVRDGSWVILDELNLAPTDVIEALNRLLDDNRELFVSEINETIKAHPRFRLFATQNPAGSYAGRKRLSRALMSRFIVLRFLHLPIDELSEMVRARCGISPNAALKMIEVLNELRNRRSLSGLFSARDGLMTLRDVFRWAKRLSTDETTDDWLQILVNHGYFLLAGRCRNEKDEATVVETLEKIIKRNINKDELFSMESPYMPIDVITDKVVLTLGMRRMLVLTEQAWLRNEAVLMVGETGGGKTTLSELVGRGKLRSINCHEKTETADLLGRLRPKHDGGFEWSDGVVISAMREGAPLLVDEISLAEDSVLERLNPLFEEDRALLLSDAGTETEVVQSQSGFQIIATMNPGGDYGKKELSKALRNRFTEVWTSSDYTTSELATIFDHRLARVEATREESRISPTKTATSIVTWISQFFGKYSHVFRHAPSVRDVVACAELYSSAVTAQIDSPIAIRDALCAVFLDSLAGLTTRLHIDAEEVFDDALTMLHTKLVKTELVSQFSDVSNFIQEAKKTVLIEQTSNCLIVAHLRVPFGSIPPKVPKAFSLKAPTCSENFYRIARGLLINKPILLEGAPGCGKSSTVMALAQLTGNPITRLNLSDQTDLSDLFGSDVPVLTEDGTMTFRWEDGPVLKAIKKGEWILLDEMNLASQSVLEGLNACFDHRKVLYIAELNREFVIPATSNCRFFACQNPRVQGGNRRALPKSFVNRFTNIYTNDLTKEDIVIVLNGVDEKNLLSDEQQRAMVTISEQCEKESERGTLLGGPYSFNLRDLLRWYDLIAAGRSLGEGFELVYMARIRREEDKELIRSIYEKTTNEKLVSRSVLLTVDAKDMRIGKCTLKRNPQTTPIASKRRLLASQMTLTHSVATCVELNWLTLLVGPRNCGKRTVIENIANICNRKLKSITLNADTDAQELIGNYEQVVDEDCLPDAKKKIIEIFQKKNVPVDRVQQVDDLNKLEATVELILSEIGNDEEIREVISIANLSSMRFEWTDSVFVDAYLHGDWLLIEDVNLCSAAVLDRLNSCLESGGKLVVAERQNSYEPLEPHPDFRVFLSMDARVGEVSRAMRNRSLEIYIDETSRWSSWPADVQAIVGSEISMELSKNVSRDLTTEQQLHFAALLEENGENFSTDVAWKLVGGQKDSSMEDDDEDDEVIVQKLACAPRIDQICELSGDYERYLISTWKHAAEKAKVSNVEAALMTFLSTSSWSIQNLLGDFQTIFGYDLVDSIVKRIPANLLNPFNRHLIDAEASSGFPTDQSSKFSRSILFEWIIQMISKIPIDQGSAEHLCNTLTKYEIATCDVTFNNLPQISQLVRSIIEMFKTSTTVSRHAHREVCISISYLLLIAASRRKLTTRTGCAAVYLAWNDLKNEATKAIGITCTESLTSVSAKIDEGWTSESYEKFVTEFIHRWRKFAVCSPFSTEDQARLFLEHIETILREENTDNDVEMIEEDSDEEVEHKNTPIPVSPIELSNKVVESVDALFEFLSSGIVNQKDDVFKKSNVYSGVDWKDPKSSQWIRTAAVFCVSVAACKIQEEDDENVLVSDLLMIGGGAHCIATRLFFSSLNYNPALSSLNMAHLQKFPIKELGTKLWRLAVNSSSIRNVMKHALEHLGVGIEGWTNGDKNGIECGVEMMERALPPKETLDPVIFEEERSLFIRAKRRIVERQLSYLAEWRELVGRQSSDCDFSSSQVIIRGLNDLRKELADLDCEDGQHEDVIYRQSATQYNQICAEMRSFLDLVKSTISDMRSSSDESNDKMTVIRMARLKSFAMSAENFRISILRKFVSFVDVSMPFVAGLLIVEIAFNEMALKWKQEAKRQHATLSSAFPRFIKFYSTPSGLVSNEVSSWAIRDGSPMPLQLKSAVVRRKLSEIEDENLSSSITEIQWTRAQWKKWYEKNIAKAEQKDFIYRTKTEEEKDEMDIEEFFAKQEQDSQVLPDSDVSLLLEAVEQKKFSLVDDKSRKQSDERYEMALAWMRYVMSEVGAIPVEDSLWTQCIDGDQKLFEVLASHEGLSDDVDGEDTKVIDVYRNSSLRECRRVAVILERLSTRTKEVLERWPEVVSLKTIITTIDEFFTVSVSTPHIKVATQIENLIEVCEQWEMMADRANSLKDPLGELRRMLVDWKKMEVRCWSSLLVNCENEAKQRAQLVAFPLFESLFEATTPEMEASIIPMSIEWMHNATLVDFSTRVLTIKSLSRWAKIAGKGVLAKQLEAASRHFAIFTERVEQRLKDAREPAEKGLKDYLRVVKYNDLNLWNIRVSSIKAHAQLYKIVRRFKDAINAELHEDFGILQKIEEWKRKVFDQDASTSDEDLTGNDCEKRIKQVRKFATEINEKFSHLCGTTAIEELYEQTKAADEAIRTMINYVGEDEEKEKQQGYARNSRQRQVAMMIKESQAIGLNARKAVLLVQEDINKSSILDVVSKEECEKEMRICSSGRNIVIQKVNKIDQQVGISTRKHLSGMIGLFFKITVIYNIIFLSEYGMSYMISLQQSIGDLKSSISKMHSFSAHLKVLSENQRSGWIIDHEIVKGRIEKVAGLISSMEVFVGSMKRRLEAIPYHSDEFIRSKSHLHQLSKLSQSDEIAQKLVNWSAKLSTLIENMKRINENFGNTSIFKSIEYAIWRSQLNEDSKALLDILNLFDGFFESEKQQISKNLEEMSLWTKEFDSSVPVEECETDVTQLLLLVQNIYKKLNAVKVNEEPKALDQINILRDILKQSDVETVVKYLAEIVQKHSSGETCGRNIEGLAELSKMTASIIESGVTHLSNCLGYFCVFYHSMLSMTMQLYEKGYVNSIPKAEKQESGDGQTDDTGEGGGIGEGGTAKDAKDVTDEMEETGQIEGLEDEQPADSEEHESKNDNERPIDMEDDFAEDLEDIDKNEKGNQDEGEDQSDEEPDVEDQMGDVEEEDEKQLDPKMWDEEEKEQEQQKNMDQEQQAADNQTDEMVAKEDDAQTKDEDQDKAGKDEEKNDQPEEDEQENMDERDRENDERAEDQMDTSEPNVDDEHPEKGEIDETEDGDDGDETDKEDEEAIEGDGEEDQNEQQDLVDVEDSTQKNEEAEEQKKEDEALEQGTGGEQNDQDDKQDAADGGLAEEEEKEDQEDKDEKGEGKSKSDPNGDGSKGEAPKEQTKKEDEEKEEEDDEEKVERKRELATDDAPMEEAEMGEGEENESGQQMENAEISDRQQVGKGTIEEAQQTKREDKREEEKKKRRELKDAVEGTSGENDGGEVEDEDAEETKDAHIHMAAQDMFTVIEETTKDLVTGMIDEPESPERPDQSTVRRINEKADEQWAAMSRTVGMLAAELAENLRLILEPQRANKMQGDYRSGKRLNMRRLIPYIASEYRKDRIWMRRTKRAQREYQIMIAVDDSESMNENGIHQSTCESVCIVEDALRRCDAGRVSVCSFGANVETIIPFGEASASSSIEMLKQMTFSQKKTDLLLLLKNAKQQLDEIRTATSEQMLIVISDGRGALSQGADKVRALYSALQGVTVLFIILDSGKKSIEDHTVASFKDNKVILTPYLSIFPFPFYALVKSVQQLPSVIAESIRQWFEMTTQHS
[ 6648, 24917, 24926, 24974, 29033, 30398, 37630, 38873, 45806, 46148, 57106, 58239, 64214, 67936, 68247, 87110, 87285, 87855, 87857, 88008 ]
The following text describes a protein: Function: Nuclear chaperone required for maturation and nuclear export of pre-60S ribosome subunits. Subcellular Localization: Nucleus, nucleolus. Nucleus, nucleoplasm.
0
MAGNIVKWWKHKILGGYKQFTVLQECATDSEELIYPGRAPSACSAPPDLLLTSDREQMLKVKSSASTGSGTGQTKTSFQHSHHHHHHGHHHQSPSSNGHNHSGTSHQQQQQQQHHHHHKSQKDAFRKCTNGKAGGGNATAGGASGAGATNTINTTAATIRSDPDRVRLEEFTCDVSLEDGKKPQPLQFSFTLYDLDGHGKITKDDIAGIVSTIYESIGKSVVVPHYGSKTINVRLTVSPDGKTATTKPASAAVKKAIITPRRRYRSRKLISDDDGSDTSENCPRLLRNRTAATAVTNNGETANNNQAALQNQQQQQQQQHHHHHHHHSNGSSGKLKESNLSKATALAGDNQVNRSIGLSNSSEGSSAVGQLLVEAYHKNNLSPGAANAGAGKGVLNNAPNATKSKANENVYESINNLKCCNLQQQQQQHTASNNTSLQTTASSLPVTATGLNQSTTSTAALICHDCVDGGAPTTTLLPPLSTLETVVIPAPSAGVTGRAKRKLVRKTRASRKTAIAAKMMSEDFARRPRARSLSVGNENCYENVIGRMAAAQEECWKSSLCRRELIEIIRESMVKNSLCFQPNRRKEHHRLAAAVGATRSTQPTPVKLSTALLNQQYPNLSAEQKLTRSINQVEQWLDHRSPKLVPKVKLADDMQLQRTVVSRPLKRSKSKEELTPSNLLLLENLKISEDIAEIAVVTPKKVYNKESLIASATKKNIKTHHQHQHSPSRQPTAVPTVAIGAEKPSAPLTVVNKQSIPVGDAQLVQLQYGSVPINADPSECENLIRMSDDGEDVEQHQHQQHQQQQQTAPMAATKHSYRHHQPQSRSQPQSPQHHQHHHQQEPRYCGSGRAHSVSSASAASTTAVHRYVHEHIHHHYHHFENDPDES
[ 10615, 11631, 19705, 24917, 24978, 25079, 29025, 37640, 46081, 67333, 87276, 87367, 87402, 87760, 87767, 87857, 88008, 88256 ]
The following text describes a protein: Function: Cell autonomous antagonist of the canonical Wnt signaling pathway. May activate a second Wnt signaling pathway that controls planar cell polarity. Required for neuroblast specification (By similarity). Subcellular Localization: Cell membrane. Cytoplasm. Nucleus.
0
MTGGVMSQKFVVGAGLLVCSVCSLSAMAGSKPVDLILRVLVDAPPPCSIKGSQVEFGNMIADNVDGTNYRQDAKYTLNCTNSLANDLRMQLKGNTSTINGETVLSTNITGLGIRIENSADNSLFAVGENSWTPFNINNQPQLKAVPVKASGAQLAAGEFNASLTMVVDYQ
[ 8653, 14755, 25169, 36156, 43555, 64662, 75918, 88008, 88058 ]
The following text describes a protein: Function: Part of the yfcOPQRSUV fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. Miscellaneous: MISCELLANEOUS: The operon is cryptic under classical laboratory conditions, but is functional when constitutively expressed.
0
MKMKKTDDILLKRLLLSVGILLFIRMGTFLPIPGINHGHLAFYIQQHPITKNLVSTFSGNDTFVIGLFTLNIFPYINASIMVQLITGLIPSISKLQKEGGGEGRRAITRLTRLITFGWALIQSSSIAFYLKRALFDWSPLLAFEIIVWLTTGAMIVLWLSELITEYGLGNGASLLIYTNIISSLPNLGKKLITENNGSLTLVSGFGIAILFFIAISGIITLQESARIVPLISSKQLSQSQPVVSKVTSNNYIPLRFNQAGVMPIILTTALLVLPNYITNLGVFPLLTLPIFLKSSKIIYWISYFILILIFSSFYSTIVLNPKDIAQELQKMAVSIPGVRPGLATTFYLKQVMKRVTFFGAIILAILATLPNVIEGILNVSSFNGLGTTSLLILVGVVLDISREMKSIILSNIYNERFD
[ 8293, 25248, 28802, 29185, 37773, 55042, 57856, 59898, 87296, 87760, 87930, 87974, 88139, 88158, 88159, 88161, 88162 ]
The following text describes a protein: Function: The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. Subcellular Localization: Membrane; Multi-pass membrane protein. Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
0
MKVDSMGNEIEKLKTKEVKLKSKAANQLTQQCAKLCRSEDIKISELEGDVGTLHKTHNVYQSTIVGYSANHRFDAENRNLVSNSPGNGIESGAKHIYNQQQVYGTLVEVAHGSVKDPTARYLKDTDTSKAKVPKKPCYKWGHGGWQSACCITTISMHRLPQISSKYYSRVGGRKMSGRAFSKLLNCLVAQDYELSIPLDLKDHWDKNGTNLYSILK
[ 9420, 24917, 27918, 32185, 44791, 87384, 87857, 88008, 88148, 88150 ]
The following text describes a protein: Function: Transcriptional regulator that specifically binds to GA-rich elements (GAGA-repeats) present in regulatory sequences of genes involved in developmental processes. Subcellular Localization: Nucleus.
0
MASQDQNTGTTHVELQGGENSKKLFSKYDLWSKAMDEKKLSSSLFTVNDTQEFLELCEACRRGDLEVVKSLVENYNTPINQVDQFDYSPLVLASLCGHEPVVKFLLENGALCERDTFQGERCLYGALNDNIRRMLLSYDITKAIDESQPYASHITSLLSNSALHFTTDIVFAGQYGRVFAHKFYLAARSSYFKSKFSKLGPSEHEIEVKHFAKEFESILRYLYLDTNAVFTKQYNNALLSIGKKFQLNDFIALYEKDREQLHSRDWKKIQLAKTQNDLGEFLDYIISNYKVPIESLNQPSDQYSFHDAYLQSYTHRYPVHRAIMCRCEYFLDMLAGPFLESNQELPVLSLPFSSSVVEIVLKFLYTDKTDIAPELALDVVYVADMLSLDKDRSLKSLASIVITKQEEPIDSIYDILRTAWDTSTPRLEQYASEYMANHLEHLIDDPEFCELVKESADRILQRQETDTIELIDDIRYFLSKRFGIYHEDLCIDGVVDTLTPYESEYNQKMEMIDDLLDKLELQA
[ 10753, 14521, 24729, 24917, 24978, 25040, 36115, 37690, 45551, 64507, 70787, 87108, 87367, 88008, 88009, 88180, 88181 ]
The following text describes a protein: Function: Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Subcellular Localization: Cytoplasm.
0
MYVSSSIHIKPNFNSSFSVSKTLSKSSSAYCSSGYSSLGFSSTFRSPRWSYGVDWKSPISLKAQIRTAAVTPVLNNFHRKLTTMASENPFKGILTSLPKPGGGEFGKYYSLPALNDPRIDKLPYSIRILLESAIRNCDNFQVKKEDVEKIIDWENTSPKLAEIPFKPARVLLQDFTGVPAVVDLACMRDAMNKLGSNADKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSNAFRNMLVVPPGSGIVHQVNLEYLGRVVFNREGLLYPDSVVGTDSHTTMIDGLGVAGWGVGGIEAEATMLGQPMSMVLPGVVGFKLSGKLRSGVTATDLVLTVTQMLRKHGVVGKFVEFYGDGMGELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVSMIEAYLRANNMFVDYNEPQHEKVYSSCLYLDLAEVEPCVSGPKRPHDRVPLKEMKSDWHSCLDNKVGFKGFAVPKDAQEKVVKFSFHGQDAELKHGSVVIAAITSCTNTSNPSVMLGAALVAKKACDLGLNVKPWVKTSLAPGSGVVTKYLLQSGLQKYLNEQGFHIVGYGCTTCIGNSGDLDESVSSAISENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVDIDFEKEPIGVGKDGKNVFFRDIWPSTEEIAEVVQSSVLPDMFKSTYEAITKGNNMWNQLSVPATSLYSWEPSSTYIHEPPYFKDMTMDPPGPNGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLNERGVDRRDFNSYGSRRGNDEIMARGTFANIRIVNKLLNGEVGPKTIHIPSGEKLSVFDAAMKYKSAGQDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIVPLCFKAGEDADSLGLTGHERYTIDLPDNISEIRPGQDVTVRTDTGKSFTCIVRFDTEVELAYFNHGGILPYVIRQLSQQ
[ 5531, 7947, 7948, 7949, 24979, 28076, 30949, 32536, 33780, 36411, 36797, 41228, 49052, 49054, 50931, 63799, 70437, 87042, 87105, 87678, 87681, 87741, 87767, 88008 ]
The following text describes a protein: Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
0
MIIPDINLLLYAVITGFPQHRRAHAWWQDTVNGHTRIGLTYPALFGFLRIATSARVLAAPLPTADAIAYVREWLSQPNVDLLTAGPRHLDIALGLLDKLGTASHLTTDVQLAAYGIEYDAEIHSSDTDFARFADLKWTDPLRE
[ 3921, 15413, 25079, 27681, 28418, 38184, 41207, 54804, 59226, 87016, 87601, 87747, 87767, 87850, 88008, 88147 ]
The following text describes a protein: Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB33.
0
MFALRRNSIVTIQRIFPIAAAVRYGSSTTATGAYGTHNTPVASNETLSREDNKLLDQVIRVDHAGELGANRIYKGQHFILRVTNPRVAPTIQHMWDQEKYHLSIFNKYCTEHNVRPTVLRPLWDVAGFALGVGSALLGTRAAMACTEAVETVIGDHYNNQIRETAHLEDKHPEFSKLREKLAELRDDELGHLNAAVDDWEAQKAPAHGLFTNAIKLGCKTAIWLCKRF
[ 1270, 8398, 24983, 25624, 29347, 32536, 43640, 45706, 87007, 87678, 87760, 87767, 87785, 87786, 87809, 87873, 88008, 88178, 88179 ]
The following text describes a protein: Function: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides. Subcellular Localization: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
0
MSAENKIEEITEDQVPQIEENSTIVIKKEEKAARALISKLNLQKVEGITRVVLKRTRQHIFVIANPEVYKTPTGNSYVVFGEAQHEDMQATARAAQIAAAQAQQAAAETGSVSEAAAAGEVGAELASKDPASITADLEAASLSKDEDAEDEAEADATGLEDSDIKLVMEQANVSRNKAINGLKKNDSDVVNTIMDLCK
[ 8290, 8291, 10368, 24917, 24978, 25056, 31302, 33730, 34276, 34284, 34476, 38183, 49627, 65702, 70343, 87367, 87857, 87974, 88008, 88162 ]
The following text describes a protein: Function: Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. EGD2 may also be involved in transcription regulation (By similarity). Subcellular Localization: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic, may also transiently localize to the nucleus.
0
MFKWVTPASTATLSRCTLPATTAATTTTTAMAATRTATTTTRTTRPQLLSIALTSLIIIVASFVPTTSGFRSIETNGGGRKLFGGYRITPKHCRATKTLPSSDPRANGPTICMFNHECAQRGGEVVGACMDGFLFGACCQIPPTHELASTLINEAQNAYFQQHQQQTKLQQSAAQSSFESYGEQQQSLSEEQVAQQPSQNIYDQQNLDKVYQQLDSSSSISPPNGAYGDEPQQQEYQSESEQPVRDENAYPTSSSSTEATQSQSSSASVEFEQEPSQPADASNDQTTQKINKQPVQPPNFHVHKHSVTINSPSSPPQNDDFVMQVLSTLPPEHADDHHIVFTTEVPTKITSGLQDQTSSESNSFEEVSSTPAATQKPKPKPTQMPTQKTTQKATQKPTPKPTQKAKPKPVPQLAESMKRPIQQKPQQVAKPKPSPKPAQSTNNHHHNHLILDGGEFTHSDITHPGADADLVEDLQFSTGYGPQPVYAEPPKQQQQQQPAEQSYISSSTSAKRPTTGHNSPTTVSSITTHVDSIESIILQLNNTSHGPSYNVVSQQTPSYGYPGAAVVQTEPAAQNPTFYQENESEKVQESDSQSDYGYTTTVNYESFYDKVSDEQDASAAVSQSAEMPTARPGYGEDVSAVLEDHTMPANGYHDAEAPVAPQTSEFNKMPVMGIAYPVDMSYMEEEGNLPATAAGYGQMSSDSYEASTESTYQKLSTVQTEEPQPTYVRPTTNANKQNRPVASYIGMVTMQHYNPQPGNGDYQAQVPPEVSVSSHTTKVQEQMDETSNGYQQSETTSGYVSPPTAVPAPAQRPQYDAVQGDASSERPVLVTASPRPRPKPSTKRPAVKRPISGESTKKKPQPQPSAGAYNQEKISEHSTRKPVSNGYDKVPESPITHIQIKKPSATQHKEQEQTGYPRPASPAGYEQTTAAAPAPAAPSLNYDKPDAPPSQYDQPSAPSASYDQLAPMPSLNYNEQHASSPGRKPSTAKPISTSYVTGPSTPRPPATVDYHYDNVPPLFMADDKLDAFIQSTAENIVGSTPGNYQPPLVATASTPAYAHRPTSSGSYGHKKPGFVQINGTPKPPRPTVLITPKPTAINLVTYSSLSDDSNKLASSTSSYVTGRPGVQGVSSNDFKDPGYFGSSPVHVAFTQSTTEAVYAVPSDDKPAFPGYFGPTPSYPAFSVPGEKVGQNVMEETYTSPNDFVNFPPVRNPNLNMSAASSAVTSDLDLSTPAFVEDVVLKDKMHTLVHKLVASLQGNFEALADMIEEPGSNKTVATYQAGAGGTAKPVRVVTTRKPVRTATTTRPKVTTKKPVTRVTTKAPNKKTSAVSTTTRKPATRRTTVAAKVTTTTRRPATKKPTRRVSSTVKTTTVSSARPADDEIVDEEDEEDVNPNPSDNEIDQGATLSSYGGANGRKIHSTSRTLPTPNLAFHSPSTECGVRPHVKSGRIVGGKGSTFGAYPWQVLVRESTWLGLFTKNKCGGVLITSRYVITAAHCQPGFLASLVAVMGEFDISGDLESKRSVTKNVKRVIVHRQYDPATFENDLALLELDSPVQFDTHIVPICMPNDVADFTGRMATVTGWGRLKYGGGVPSVLQEVQVPIIENSVCQEMFHTAGHNKKILTSFLCAGYANGQKDSCEGDSGGPLVLQRPDGRYELAGTVSHGIKCAAPYLPGVYMRTTFYKPWLRSITGVK
[ 4571, 8200, 13203, 17537, 25079, 27031, 28227, 36986, 37036, 43583, 50917, 61632, 69992, 87139, 87276, 87413, 87522, 87601, 87760, 87965, 88008, 88049, 88061, 88159, 88161 ]
The following text describes a protein: Function: Probable endopeptidase. In tracheal terminal cells, acts downstream of ich to regulate seamless tube growth and/or maintenance probably by processing lumenal matrix proteins. Subcellular Localization: Cell membrane; Single-pass type II membrane protein.
0
MKMKLHVEISSVFLFVFEHRNMKCISCEGKYDGDAGACRQCYEDLKAKVAFLAMSNRYPLTFCTDVVLLASDNGHPEGPAGGMAHEAVLASRSPVFKALLHNETKEIHINELWPQELGAFINYLYTAEICLDQDLARKLLVVAEKYQVHHLKDLCQKFLVSNLNRDNSLATYTFGHHHNDKQIIDAALMLITNNIEKLASSDEYAELKRSHPQLVIEIYEHIVASSTAPSVQALLLEELL
[ 11623, 14521, 24978, 31139, 36115, 45551, 71027, 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
MRRRRLQLRYSSDEEEEDETGTSGVGDSVQSFGIASSIQPETSVSSNSNPNPGERIAISEVEIIDVFGNPQPTPPDSSIPTPYPVYPSESVSGNDYESPISEVLSRMGIKLKREWWVSCLSGLETSIPQFSYLDVAAKAKHCFEQFMFFDMNLCGGGVLPPNVASMNRIELAGPFVLQVDEIVNIGCPLKGRYENANAGLKRCLKLSMTDGVQRVFGMEYRPIKDLQVLAPAGLKIVVSSVQVRHGLLMLVPEIVEVLGGMVEELEEARKRLVVEVNKPPRGKRTRVGVVPSLTTRATLAAWSLNGNDTGNHVHDTGNHVNSSASGNASHTQANQGIPVHVTRTHNSSRAMDEPLASTNVGATVSRVEHMQIDTASAHGERTFSDIHSTSSNIHRAASTAGTGTSCSGACSGARSFANNVGGNSLDQTSNVTSFVEEMHIDTGRVRDTTTHIYGSDSGGVAAEFSNMVVDLEGPSVLSTNTEKPFTYLAELSQKWAVMKDTIHFVQGRIKCFLTGVKKFQFKQQSTYELLCYVDDGSLICEILLHNDVVQKRIGHSSMEVTAALSSSAPTSLNAMMKEKLKRFQLFLADFEGIMVVEMNRSSQYPVAIEMNQGCSLTDARLLLDRIKSSSRTSSSLNPVVVLSP
[ 6787, 27656, 47620, 61001, 69379, 75114, 87139, 87757, 88008 ]
The following text describes a protein: Function: Essential component of the RMI complex, a complex that plays an important role in the resolution step of homologous recombination, in a process called Holliday Junction dissolution, to limit DNA crossover formation in cells. Together with TOP3A, is essential for the resolution of meiotic recombination intermediates, a step that prevents entanglement of the parental chromosomes.
0
MKLSIHGRKITLTDAIRKYAEEKISKVEKFNDSIIKIDATLAASKLKTGNAHVTEILAYLSGSTLKATATESDLYASIDKAVDIMESLLKKHKEKRSRAKVQDDTRKKSYSFDYIVEPEEKLSDEKKLVRVYLPLKPMEISEAILQLEYLNRVFFAFTNTTTGKMAVVYKRKDGDYGVIED
[ 15393, 25437, 32120, 38785, 61276, 62737, 64310, 65912, 76229, 87367, 88008, 88155 ]
The following text describes a protein: Function: Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth. Subcellular Localization: Cytoplasm.
0
MKGQQKTAETEEGTVQIQEGAVATGEDPTSVAIASIQSAATFPDPNVKYVFRTENGGQVMYRVIQVSEGQLDGQTEGSGAISGYPATQSMTQAVIQGAFTSDDAVDTEGAAAETHYTYFPSTAVGDGSGGTTSGSTTAVVTTQGSEALLGQATPPSTGQFFVMMSPQEVLQGGSQRSIAPRTHPYSPKSEAPRTTRDEKRRAQHNEVERRRRDKINNWIVQLSKIIPDCSMESTKSGQSKGGILSKACDYIQELRQSNHRLSEELQGLDQLQLDNDVLRQQVEDLKNKNLLLRAQLRHHGLEVVIKNDSN
[ 6746, 6932, 7884, 9298, 9774, 10933, 12513, 15388, 15427, 17193, 18840, 24788, 24926, 24936, 25018, 27788, 27904, 27918, 30811, 32074, 32079, 32170, 32382, 32577, 35927, 45714, 64381, 77385, 87384, 87684, 87857, 88008, 88148, 88150, 88180 ]
The following text describes a protein: Function: Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters. Subcellular Localization: Nucleus.
0
MEALRTRASAQPLQDADDLIDSVETFIFDCDGVIWKGDSLIDGVPETLDMLRSKGKRLVFVTNNSTKSRKQYGKKFETLGLSVTEEEIFASSFAAAAYLKSINFPKDKKVYVIGEDGILKELELAGIQYLGGPEDGGKKIELKPGFYMEHDEDVGAVVVGFDRYFNYYKVQYGTLCIRENPGCLFIATNRDAVTHLTDAQEWAGGGSMVGAIGGSTQREPLVVGKPSTFMMDYLADKFGIQKSQICMVGDRLDTDILFGQNGGCKTLLVLSGVTSLSMLQSPDNKIQPDFYTNKISDFLSLKAATV
[ 4110, 9500, 24978, 25225, 29569, 30335, 32536, 41322, 41330, 55054, 64168, 87016, 87115, 87296, 87601, 87747, 87767, 87914, 87918, 87930, 88154 ]
The following text describes a protein: Function: Photorespiratory enzyme that dephosphorylates the 2-phosphoglycolate produced by the RuBisCO oxygenation reaction. Subcellular Localization: Plastid, chloroplast.
0
MATFTPLNAASEDLDKEKRTLEIRIEEAVQIYQNALSAQKQGDDNAATKYYDELLNVRILRELPFTVNSNYKKNNALLLLHYLTRKNHGLFLLSKLQSLLSLDPSTDPIPVYRDALLDFAIALACDYNDIELWSFVAELAEKLEMPRIQRFALESSFYTGYEPFDAERVFTNIDDLNPGKLISLQNLYNLLKKLGGIAEPLPQLDLSISSLYTLPSFFPQLPTPSFHRRSINLCPKIKKLQLSHDTLHGFLDLVLYALQINEKKTPTRGFPSTLIIHVHSLNLSTAESHDLESTDSELWSEISDAGPDTNTINTAAKLSEPVYAKDIVPPPSDNLPKPQLLKRPIDDSDVRISKRSRGRDLRTPSESNLFSLIASITSDINEQIQKRFPDATSPFSGESMFREYSSIFEDYHQLLVNFPSEGSIPDLDVSTDSAANGAFSKMILIDLAMHSANRLEHMQVPDGYLLQLLSEVNSLNMVPAELATFFVESMLRPRKLEPPFYLQQCWGKIFKKKFTTICERIESTLHELVKASLQTPEVFNISQSLFELFLDDYFLALKFSSNDQKDDNVSEIPTESLEYKKLRCLRWKSLTEQVVELQPSCKSSSQRHLIIRNSWARNLLLRLTGCSSEAIVENFKQLRCLLQENSDSLELLNSQCMADLSVQVVDFELSKLQTVEFFNTLFMNTKNLDFNAVIKNLEPVLSPENKFAEDPQAKFISQFLEKTSTEFQIHLWYLLYQAYSSAHRPYNSLLCAFQSLKIILIRLCSSSFSIQDAGRRQAELLGMLNFSSNLFRIIWQKLHEQPDILSPCNEMTVIDCIRIILIYLRTFAIYVGIDEDISDQRIPKPSNPEFDSYAQTVKDSLMSGWCIFYTLFAHLLHYDFIKADAQKLLPQILTAIHSQYSFRGYCSSSNQSFLELSQTECQRLDAWENENEILQCVCCRFNLIIGSEYYVPQSHQSDSVNLTSNDAIKIIPFILGFAVKRSHGWVMPRSDQKNALEIICKVIRFPGENNADVYFNKCAIKEFLERDISPQLTKMLLKSNDILGLREIGSKVVDDRVRGLYYAQSQVLFGYYRSRLKGSRCINDLLVIIKYFLLDLYLNPRRQDSWYTCSSVFSSLADEELGWSAEQICLADDVINEYRRKAILCNLMALSLPFTQDKLFKANVYFDFAMNLYASARPPLEMAAFLPSETRVFSGASGLYNLSMKPIEVSKVIALAADYFGMSAELSNDWRALYMLGKACRKCGDMENALVHFEAAAALAPTKSGSGSQQALLIEPHYALLSNLSKAAIEGSVEIVQILSYLRRIRHPPKDSGSLLEVKNEDVNIYKRNALLFILKALAEMRILDKQSWHHRPTYRIAKIMEHLGNVQQAKEEMETLFSYKTSGKSLLNIWRTPNERPGRHFYYGATYSRYLLSLFYKTNDKVNFLQFLKRFRRSSSTIYEHRQIWLDIMIKYLEDLRLQHSVKETQINDLPLVEFKYVYKEISLLDEQKLSLLHQVYEIRKLNNGLYPTIKVDDFLIDCFMSLYNEVKSSISPLDANIPNSPSTITAKPLNDEKAINNENSVKQKTVITRKDVVSKVLALFRPHRETYYRETQNKILQKLASTSSSLVRSFTEDSSQAGESPGIHEEIQ
[ 8603, 20990, 24768, 24917, 46079, 52236, 61618, 87307, 87857, 88008, 88009, 88114, 88148, 88150 ]
The following text describes a protein: Function: Has a role in a nucleosome assembly pathway that is required for the integrity of heterochromatin and proper chromosome segregation. Required for transcriptional silencing in the outer repeat (otr) region of centromeric repeats and the Tf2 long terminal repeat retrotransposons. Subcellular Localization: Nucleus.
0
MVSFRFPFSFSQPPRATTSFSGFSISAVAVSVTVGAAAAGAAIAASRNPSHPILEWAFSSHRSSLSPWGSITLADESVVEPKTGFSFPASIGDSRRLLGVGLRKKSLLGLKNIDVYAFGVYADCDDVKKLVGDKYANLPASEIRGNKSFMDDLMEADIKMTIRLQIVYGKLNIRSVRNAFQESVGNRLKKFGGSDNDELLQSFTSLFKDEYKIPRNSTIDLTKDPGHVLSVAIEGNHVGSVKSHLLCRSILDLYIGEEPFDKNAREDFLDNAASLAFDN
[ 8304, 25040, 25225, 25249, 25257, 25277, 29022, 30387, 49156, 49157, 49158, 64064, 70521, 87103, 87296, 87930, 88008 ]
The following text describes a protein: Function: Fatty-acid-binding protein. Interacts preferentially with saturated fatty acid. May be involved in alpha-linolenic (C18:3) metabolism. Subcellular Localization: Plastid, chloroplast stroma.
0
MKRLTLKNLKRSLHHQSKQGGGEGGEGIEEAYNSDSETACREEDSDESAEVPGRRLRRAGTLPYPSRRRREREGFMSTIRHRLKIGKGSQDQENCTEEVKDEEKEDGEVVEEETVTTRRPTRSKSMRVRKKESATTVALRPANSEENLSQRKDSQYWTRKLHEKNRKDLPPAPHDGEGDENGEITMDICHKKVERKDSSDSRSSKSSKSKNSPFSVSSINCTQEKPISSEKSRLKALRSFLTLPRRGSKKKGSKEKEEPDSPDTISSNGVSPRALPPCPSLTESHDIFNSASSTVPRPRNGNNGSSYEPYDDEDNERKIASYEQVGGRAHVNHSLTEELRKLVRHGWYWGPISRAEAEEKLAHLSNGSFLVRDSSDDRYLLSLSFRSYDRTFHTRIEHCNGIFSFYSQVESEGHKSIVDLIEHSMRESQSAVFCYSRSRTPGAPSFPVRLTNPVSRFTQVRTLQYLCRFVIRQYTRIDHIQLLPLPTKIREYLQECHY
[ 9577, 13402, 24917, 24978, 25079, 31818, 36753, 37186, 63821, 64590, 87276, 87367, 87534, 87760, 87857, 88008, 88030, 88060, 88181 ]
The following text describes a protein: Function: Substrate-recognition component of a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex, also named CRL5 complex), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as DAB1 and IRS1. Specifically recognizes and binds phosphorylated proteins via its SH2 domain, promoting their ubiquitination. The ECS(SOCS7) complex acts as a key regulator of reelin signaling by mediating ubiquitination and degradation of phosphorylated DAB1 in the cortical plate of the developing cerebral cortex, thereby regulating neuron positioning during cortex development. Functions in insulin signaling and glucose homeostasis through IRS1 ubiquitination and subsequent proteasomal degradation. Also inhibits prolactin, growth hormone and leptin signaling by preventing STAT3 and STAT5 activation, sequestering them in the cytoplasm and reducing their binding to DNA. Subcellular Localization: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Nucleus.
0
MPWKEESEFTKQDKAARVIQQAWKSFLNVAIFQHFKSLIDLRRQGEPRQIVKYINPKEAELLDAAAGIHVRFRLGGVKFPPDIYYKIFTHRPIEDLCANSPRNYAKLPAKHTSHNKNDHLQEEDHSGWYHRIENNGWRPVSDTFWLSTDGMVVEDKKESEFHFSKLKRRQDLEKKRKLRKIEWMRQMYYSGSLEAKSTHHETLGLIHTATKGLIRAFEDGGIDSVMEWEVDEVLNWTNTLNFDEYIASWKEIATSNSSANFKGFRFNQAQKNIYNYGGDISKMQMGIPDDTYYENVYQEPNVTRLTPDSTYGL
[ 19816, 22398, 24981, 25040, 87139, 87367, 87760, 87785, 87788, 87976, 88008 ]
The following text describes a protein: Function: Acts as an inhibitor of mitochondrial fission. Interacts with MFF and prevents DNM1L recruitment to mitochondria, promoting a more fused mitochondrial network. Subcellular Localization: Cytoplasm, cytosol. Mitochondrion outer membrane. Note=Predominantly localizes to the cytosol, with a minor fraction at the outer mitochondrial membrane.
0
MHPPPPAAAMDFSQNSLFGYMEDLQELTIIERPVRRSLKTPEEIERLTVDEDLSDIERAVYLLSAGQDVQGTSVIANLPFLMRQNPTETLRRVLPKVREALHVAGVEMQLTAAMSFLTILQDESVSIHAYTHSFLQVILLHLEHRDTGVSNAWLETLLSVIEVLPKETLRHEILNPLVSKAQLSQTVQSRLVSCKILGKLTNKFDAHTIKREILPLVKSLCQDVEYEVRSCMCRQLENIAQGIGTELTKSVVLPELIELSRDEGSSVRLAAFETLVNLLDIFDTDDRSQTILPLVKSFCEKSFKADESILISLSFHLGKLCHGLYGIFTPDQHLRFLEFYKKLCTLGLQQENGHNENQIPPQILEQEKKYISVRKNCAYNFPAMIVFVDPKNFHMELYSTFFCLCHDPEVPVRYTIAICFYEVSKLLNSGVYLIHKELITLLQDESLEVLDALIDHLPEILELMSTGGESSVQENKLSSLPDLIPALTAAEQRAAASLKWRTHEKLLQKYACLPHVISSDQIYYRFLQRMFTIMMTNNVLPVQKAASRTLCIFLRYNRKQEQRHEVIQKLIEQLGQGKSYWNRLRFLDTCEFIIEIFSKSFFCKYFFLPAIELTHDPVANVRMKLCYLLPKVKSTLKIPADKHLLQQLEMCVRKLLCQEKDKDVLAIVKRTVLELDRMEMSMDAFQKKFYEKDLLDQEKEREELLLLEMEQLEKEKQQNDGRPMSDKMFEKKRRDTKTPTQSLPKNIPISVPGPSSVTPSTSKEIKKSKLIRSQSFNNQAFHAKYGNLEKCASKSSTTGYTTSVSGLGKTSVLSLADDSFRTRNASSVPSSFSPNTPLPSTSRGTGNSVDPKSSGSKDTQPRKATLKSRKSNP
[ 7031, 24978, 25040, 25108, 25151, 26070, 26230, 28676, 28677, 30807, 46078, 49116, 53199, 67168, 87139, 87326, 87367, 87914, 87976, 88008, 88009 ]
The following text describes a protein: Function: Putative regulatory subunit of serine/threonine-protein phosphatase 4. Subcellular Localization: Cytoplasm.
0
MSAMLRAALRRLPLPCRGGRPGPSAALRALGGAASARAGKENRSPSLGKDKADTVIIGGGCVGVSLAYHLAKAGLQDVVLLEKSELTAGSTWHAAGLTTYFHPGINLKKIHAYSIKLYEKLEEETGQAVGFHQPGSIRIASTPTRVDEFKYQMTRAGWHPTEQYLITPEKVQELFPLLNMDKVLAGLYNPGDGHIDPYSLTMALAAGARKYGAQLNYPVQVTNLNSRSDGTWEVETPLGVIQAKRIVNTAGFWAHEIGKMIGLQHPVIPVHHQYVVTSTVPEVKALKTELPVIRDLEGSYYLRQERDGLLFGPYESQEKMKLQDSWVTNGVPPGFGKELFESDLDRIMEYVEAAMEMVPVLKKANIINTVSGPITYSPDILPMVGPHQGVRNYWVAIGFGYGIIHAGGIGKYLSDWILEGEPPFDLIELDPNRYGKWTTTEYTAAKARESYGFNNIIIYPKEERFAGRPTERTSGLYDLLKTKCSMGFHAGWEQPHWFYKPGDETGYKPSFRRTNWFDPVGREYKQVMERVGVIDLSPFGKFKVKGTDSVKLLDHLFANVVPKVGSTNISHMLTPKGKVYAELTVSQLYPGEFMLVTGSGSELHDLRWIEEEVVRGGYKVEIENMTDEMGVLGVAGPYARQVLQRLTAEDLSDGSFKFLQSRHLKLSDIAVTAIRISYTGELGWELYHRKEDSVALYNAIMDAGQKEGIDNFGTYALNALRLEKGFRAWGAEMNCDTNPLEAGLEYFVKLNKPADFIGKKMLKQIKEKGLKRRLVYLTLETDDVDPEGNESVWHNGKVIGNTTSGSFSYSAKQSLAFAYVPTELSKVGQKLEVELLGKNYSATIIQEPLVLTEPTRTRLQRKGQSPKI
[ 1880, 14212, 24978, 24979, 24988, 33113, 41080, 41203, 47701, 58150, 59087, 59210, 61253, 63960, 87004, 87115, 87455, 87470, 87785, 87873, 87976, 88008, 88154 ]
The following text describes a protein: Function: Catalyzes the demethylation of N,N-dimethylglycine to sarcosine. Also has activity with sarcosine in vitro. Subcellular Localization: Mitochondrion.
0
MDSSAAASSSSSAGPLSVVHVAFPEVTGALLESLNQQRLEGKLCDIAIQVQGRVFRAHRAVLAASSPYFHDQVLLKNMTSVVLPSVMDPVAFEAVLGSAYTGHLSMAADEIVNFLTVGSVLQMWHIVDKCTELLKERRGALLLGSAAAPSSSLAPSSSSSSLAPSSKFILEMEDDEGSDGGEPGCSVPPGGSRRPPLHRPAYLRPSIVPQRQWVFVKKERPQEDLVLTCEEEDEDPVEEVELEEQVNFCESSEDFPSPYEGNHVVLFPAGSGPAAGASLAASTVEHGAVQLASGSGGDGNKIFMCHCGKAFSHKSMRDRHVNMHLNLRPFDCPVCNKKFKMKHHLTEHMKTHTGLKPYECDVCAKKFMWRDSFMRHKGHCERRHRLEPDGGQTWTFIMRDNRFFVWAPFSLS
[ 8103, 15388, 24917, 24957, 27733, 27735, 29166, 36115, 45551, 46932, 64003, 76112, 87384, 87767, 87857, 87914, 88008, 88009, 88148, 88150, 88261, 88263 ]
The following text describes a protein: Function: May be involved in transcriptional regulation. Subcellular Localization: Nucleus.
0
MYEVIQKRKTKIINVLQSPELMRLIEDPSNLGISLHFPVSSLLKSNKCTPMPKLSTYSLASGGFKDWCADIPLDVPPEIDIIDFYWDVILCMESQFILDYNVPSKNKGNNQKSVAKLLKNKLVNDMKTTLKRLIYNENTKQYKNNNSHDGYNWRKLGSQYFILYLPLFTQELIWCKLNENYFHVVLPSLLNSRNVHDNHSTYINKDWLLALLELTSNLNQNFKFEYMKLRLYILRDDLINNGLDLLKNLNWVGGKLIKNEDREVLLNSTDLATDSISHLLGDENFVILEFEC
[ 17964, 19492, 24605, 24978, 29069, 88008, 88021 ]
The following text describes a protein: Function: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis in response to increased intracellular polyamine levels. Binds to ODC/SPE1 monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome.
0
MVRMEDIISLAKRKGFVFQSSEVYGGLSGAWDYGPLGVELKKNIKKEWWKSMVYLHENIVGLDSAIFMRPEIWRASGHVDGFSDSMVDCKDCKSRFRADFIDLSKNCPNCKVGNNFTSPRSFNLMFKTHIGVVEDSSSEVYLRPETAQGIFVNFRNVLDSSRLKIPFGIAQVGKAFRNEIVTKNFIFRTCEFEQMEMQFFVHPKQIDEWFCYWQQNRMNFFIETLKISPDRLRFKAHDSTQLAHYAKAAFDIEYEFPFGFQEVEGIHNRGNYDLTQHAKFSNKPKVFEYHDLLTKEKYVPYVIETSAGLTRSVLMTLCDAYSEEELSDGDKRIVLRLHPKLAPYKIAIFPLVKKVELTEIARRIYMELCDDFHIFYDDSGTIGKRYRRQDEIGTPYCVTIDYNTIEDETVTVRERNNMTQKRIFINDLYSYIKTEILNYKEDFNK
[ 6297, 8151, 24978, 28636, 29033, 32578, 37864, 37865, 39345, 41180, 54850, 58077, 61977, 64364, 72021, 87110, 87145, 87367, 87722, 87855, 87968 ]
The following text describes a protein: Function: Catalyzes the attachment of glycine to tRNA(Gly). Subcellular Localization: Cytoplasm.
0
MPGSSLWLIPPPSHPLYPILSFLISQHLPSDFPSEAGAADARLIPEFFAPHMTLSSGISPDLYGDDPQRWLDSIPWPSADEVQVRFEGISSQDTYYRRCYARVKLDEGIKKIAGLARARGVNGEDDAKGAKTQEWLEWWRKEFGPHVSLMYGDVPISDDRLKEVAKVVEEAGVKLAEPEGNVEGNGWNGGVVWLVPTDRDIRDWKPIAKRVL
[ 4201, 9207, 25018, 28164, 43654, 46309, 87528, 87601, 88008 ]
The following text describes a protein: Function: Involved in the metabolism of ADP-ribose 1',2'-cyclic phosphate which is produced as a consequence of tRNA splicing. Subcellular Localization: Golgi apparatus.
0
MTRNPFMVEPSNGSPNRRGASNLSKFYANANSNSRWANPSEESLEDSYDQSNVFQGLPASPSRAALRYSPDRRHRTQFYRDSAHNSPVAPNRYAANLQESPKRAGEAVIHLSEGSNLYPRDNADLPVDPYHLSPQQQPSNNLFGSGRLYSQSSKYTMSTTSTTAPSLAEADDEKEKYLTSTTSYDDQSTIFSADTFNETKFELNHPTRQQYVRRANSESKRRMVSDLPPPSKKKALLKLDNPIPKGLLDTLPRRNSPEFTEMRYTACTVEPDDFLREGYTLRFAEMNRECQIAICITMYNEDKYSLARTIHSIMKNVAHLCKREKSHVWGPNGWKKVSVILISDGRAKVNQGSLDYLAALGVYQEDMAKASVNGDPVKAHIFELTTQVSINADLDYVSKDIVPVQLVFCLKEENKKKINSHRWLFNAFCPVLQPTVVTLVDVGTRLNNTAIYRLWKVFDMDSNVAGAAGQIKTMKGKWGLKLFNPLVASQNFEYKISNILDKPLESVFGYISVLPGALSAYRYRALKNHEDGTGPLRSYFLGETQEGRDHDVFTANMYLAEDRILCWELVAKRDAKWVLKYVKEATGETDVPEDVSEFISQRRRWLNGAMFAAIYAQLHFYQIWKTKHSVVRKFFLHVEFLYQFIQMLFSWFSIANFVLTFYYLAGSMNLVIKHGEALFIFFKYLIFCDLASLFIISMGNRPQGAKHLFITSMVILSICATYSLICGFVFAFKSLASGTESHKIFVDIVISLLSTYGLYFFSSLMYLDPWHMFTSSIQYFLTLPAFTCTLQIFAFCNTHDVSWGTKGSTQESKQLSKAIVVQGPDGKQIVETDWPQEVDKKFLEIKSRLKEPEFEESSGNEKQSKNDYYRDIRTRIVMIWMLSNLILIMSIIQVFTPQDTDNGYLIFILWSVAALAAFRVVGSMAFLFMKYLRIIVSYRNKVEGSGSWEVSKLDLPNVFHKKG
[ 2822, 7898, 18986, 22054, 25112, 25325, 25498, 26774, 28153, 39962, 39963, 47387, 59211, 87281, 87522, 87525, 87760, 87914, 88008, 88153, 88159, 88161 ]
The following text describes a protein: Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (Probable). Required for septum formation (Probable). Subcellular Localization: Membrane; Multi-pass membrane protein.
0
MDLQQVYLAAVVLAALALTLADEEAKKLWDRLDHLDPNHDGVVTQEELKNFAFWERTKDLREDAAEQWDTLEVPPGEKLTFGHYKEKSYGEDFSEDDDLGPYGRTVQQDHARFNASDQNKDGALDKEEFLAFLWAEEYPHMHDIITLETMEDLDKNGDGAISFTEFAGDDEGVMEDSVDHMEFKESDKNQDGQLNHAEVKEWLLGPTLKEDDERVATVLSKLDKDEDGKLTRSEIEADPEVIETLMYEEDGGEYLHDEF
[ 10368, 25008, 25013, 29025, 37640, 46081, 51011, 87244, 87285, 87432, 87522, 87767, 88008, 88009, 88058 ]
The following text describes a protein: Function: Probable molecular chaperone assisting protein biosynthesis and transport in the endoplasmic reticulum. Required for the proper biosynthesis and transport of pulmonary surfactant-associated protein A/SP-A, pulmonary surfactant-associated protein D/SP-D and the lipid transporter ABCA3. By regulating both the proper expression and the degradation through the endoplasmic reticulum-associated protein degradation pathway of these proteins plays a crucial role in pulmonary surfactant homeostasis. Has an anti-fibrotic activity by negatively regulating the secretion of type I and type III collagens. This calcium-binding protein also transiently associates with immature PCSK6 and regulates its secretion. Subcellular Localization: Endoplasmic reticulum lumen.
0
MEALGDLLAPHSELIAKVAGTITTLQFLSGVVLMNDIRKKGSSDVYPVGPFLFGVVLTVLSLKLANIMNDAAMINTNLIGLVINFVFLFGFYYYASSASRSKIWKQIGYSSVFLLAITAYANFEDPAKIEFRLGMLITGILVWMVGSPLLHLPKIIEKKSTEGMPFPIIFAGNLVAFSWTLYAISIKNTVMVLQNLLLLVLGGIQLSMFAIYPNKPAAEKPKDSKKDK
[ 9122, 12937, 24724, 25018, 25079, 25325, 33737, 39494, 73582, 87276, 87528, 87760, 87976, 88008, 88009, 88087, 88159, 88161, 88162 ]
The following text describes a protein: Function: Mediates sugar transport across membranes. Subcellular Localization: Cell membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
0
MSSKDNTCPPPGPGHINGFHVPHYAFFFPHMLGGMSXTGGLPGVQHQPPLSGYSTPSPATIETQSTSSEEIVPSPPTPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKESPKPEAIESYILSPETQDLIEKVQKAHQETFPALCQLGKYTTSFSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKSACLDILILRICTRYTPDQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQPVPLEMDDAETGLLSAICLICGDRQDLEQPDKVDKLQEPLLEALKIYVRTRRPQKPHMFPKMLMKITDLRTVSAKGAERVITLKMEIPGAMPLIQEMLENSEGLDTLGGGASSDAPVTPVAPGSCSPSLSPSSTHSSPSTHSP
[ 8097, 8103, 11498, 16093, 16477, 18874, 24917, 24936, 27733, 27735, 28686, 29166, 31775, 36381, 37295, 37376, 38460, 46933, 63346, 73132, 73133, 87384, 87767, 87857, 88006, 88008, 88148, 88150, 88261, 88263 ]
The following text describes a protein: Function: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Required for primary neurogenesis and for anteroposterior neural patterning. Subcellular Localization: Nucleus. Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain; The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
0
MEVIEVSGEDGGMYIENGDSFLIHFLHSFPRIDFSLTVVNSTFDLESTKYKESLLFWASLPVLGLLIVLISLLAYLIFRCICKSAYDDESTNRSRISESECEKTNKCISCVKWSISCLVLLACGSSAFGFYGNNEIRKGSNIVSDAIASTAINLYYAQTQVSQLRNLINSTNAEIKSLRETLKRHFGQYRHLNTTANEELGKHLELMSRRMTEVWNHVRDLVDRDEKRDETDSKVAIYSKLFEDFDLYRWITCISIFVWLIVLSLMLLLGAVKSSKCLLLVLILIGAIFKFTTFQILYMWYSNSCGLLVVMQLTSRINSSFTEYYIKCNPTKHPNPLVHHIKGAQNGVSEMNSNINEAANYIKNFLPQSEYTSGSICRQYSGLLNLSENCSTMRESIA
[ 25079, 25966, 28902, 34436, 41895, 87276, 87290, 87291, 87522, 87674, 87676, 87760, 88008, 88159, 88161, 88162 ]
The following text describes a protein: Function: Probable chloride channel. Subcellular Localization: Cell membrane; Multi-pass membrane protein.
0
MEPESILDFHTEQEEILAARARSVSRENQISLAIVLVGSEDRREIKEGIEILEDVVSDTAHSEDSRVCVHYLALAHARLKNYDKSINLLNALLRTEPSNMQATELRRAVEKKMKREGLLGLGLLGGAVAVVGGLVIAGLAFRK
[ 6691, 8512, 8549, 10749, 24981, 25005, 29172, 34060, 46079, 49536, 58702, 58705, 61987, 87170, 87374, 87760, 87785, 87788, 87894, 88008, 88159, 88161 ]
The following text describes a protein: Function: Involved in the fragmentation of the mitochondrial network (By similarity). Involved in perinuclear clustering of the mitochondrial network (By similarity). Plays a role in removal of ultraviolet C radiation-induced mitochondrial DNA damage. May act, redundantly with fis-2, downstream of mitochondrial fission, before the fission products participate in either mitochondrial homeostasis, mitophagy, or apoptosis. Subcellular Localization: Mitochondrion outer membrane; Single-pass membrane protein. Peroxisome membrane; Single-pass membrane protein. Domain: The C-terminus is required for mitochondrial or peroxisomal localization, while the N-terminus is necessary for mitochondrial or peroxisomal fission.
0
MEEKTHHHHHSTNKHIPSSKSRTPLLHKPYHHHVQTNPPPFLLHPSSHQNLNLVASNLPSSYYYYYYCYFYSQFHNSLPPPPPPHLLPLSPPLPPLLPLPPPHSMTRFHKSLPVSQVVERKQQHQQKKKIQVSNNKVSGSIAIEEAALVVAKRPDFGGQDGSVIYLLANHFLVKFDSSQRIYHYNVEISPQPSKEIARMIKQKLVETDRNSFSGVVPAFDGRQNIYSPVEFQGDRLEFFVNLPIPSCKAVMNYGDLREKQPQKKIEKLFRVNMKLVSKFDGKEQRKEGEDWAPLPPEYIHALDVILRENPMEKCTSIGRSFYSSSMGGSKEIGGGAVGLRGFFQSLRHTQQGLALNMDLSITAFHESIGVIAYLQKRLEFLTDLPRNKGRELSLEEKREVEKALKNIRVFVCHRETVQRYRVYGLTEEITENIWFPDREGKYLRLMSYFKDHYGYEIQFKNLPCLQISRARPCYLPMELCMICEGQKFLGKLSDDQAAKIMKMGCQKPNERKAIIDKVMTGSVGPSSGNQTREFNLEVSREMTLLKGRILQPPKLKLDRPRNLKESKVFKGTRIERWALMSIGGSSDQKSTIPKFINELTQKCEHLGVFLSKNTLSSTFFEPSHILNNISLLESKLKEIQRAASNNLQLIICVMEKKHKGYGDLKRISETRIGVVTQCCLYPNITKLSSQFVSNLALKINAKIGGSMTELYNSIPSHIPRLLRPDEPVIFMGADVTHPHPFDDCSPSVAAVVGSINWPEANRYVSRMRSQTHRQEIIQDLDLMVKELLDDFYKAVKKLPNRIIFFRDGVSETQFKKVLQEELQSIKTACSKFQDYNPSITFAVVQKRHHTRLFRCDPDHENIPPGTVVDTVITHPKEFDFYLCSHLGVKGTSRPTHYHILWDENEFTSDELQRLVYNLCYTFVRCTKPISIVPPAYYAHLAAYRGRLYIERSSESNGGSMNPSSVSRVGPPKTIPLPKLSDNVKNLMFYC
[ 9625, 9783, 9964, 13237, 13284, 14027, 16925, 24978, 26098, 27616, 27925, 38476, 38534, 46274, 48322, 61225, 61227, 63866, 64155, 71461, 87925, 88001, 88004, 88008, 88010, 88020, 88148, 88150, 88155 ]
The following text describes a protein: Function: Involved in RNA-mediated post-transcriptional gene silencing (PTGS). Main component of the RNA-induced silencing complex (RISC) that binds to a short guide RNA such as a microRNA (miRNA) or small interfering RNA (siRNA). RISC uses the mature miRNA or siRNA as a guide for slicer-directed cleavage of homologous mRNAs to repress gene expression. Required for the processing of 21 nucleotide trans-acting siRNAs (ta-siRNAs) derived from TAS3a transcripts. Associates preferentially with the microRNA (miRNA) miR390 which guides the cleavage of TAS3 precursor RNA. Seems to act as miR390 specific slicer. Associates mainly with small RNAs of 21 nucleotide in length and with a 5' terminal adenosine. Acts in the RDR6/SGS3/DCL4/AGO7 trans-acting siRNA pathway involved in leaf developmental timing. Does not seem to act on leaf polarity. Required for the production of the 30-40nt bacterial-induced long siRNAs (lsiRNA). Involved in antiviral RNA silencing by contributing to efficient viral RNAs clearance. Targets less structured viral RNAs than AGO1 which is capable of targeting RNAs with more compact structures.
0
MSTSTSPAAMLLRRLRRLSWGSTAVQLFILTVVTFGLLAPLACHRLLHSYFYLRHWHLNQMSQEFLQQSLKEGEAALHYFEELPSANGSVPIVWQATPRPWLVITIITVDRQPGFHYVLQVVSQFHRLLQQCGPQCEGHQLFLCNVERSVSHFDAKLLSKYVPVANRYEGTEDDYGDDPSTNSFEKEKQDYVYCLESSLQTYNPDYVLMVEDDAVPEEQIFPVLEHLLRARFSEPHLRDALYLKLYHPERLQHYTNPEPMRILEWVGVGMLLGPLLTWIYMRFASRPGFSWPVMLFFSLYSMGLVELVGRHYFLELRRLSPSLYSVVPASQCCTPAMLFPAPAARRTLTYLSQVYCHKGFGKDMALYSLLRAKGERAYVVEPNLVKHIGLFSSLRYNFHPSLL
[ 2773, 8198, 24724, 30311, 59686, 87413, 87528, 87760, 88008, 88153, 88159, 88161 ]
The following text describes a protein: Function: Golgi-resident glycosylphosphatidylinositol (GPI)-N-acetylgalactosamine transferase that catalyzes the N-acetyl-beta-D-galactosamine transfer from an UDP-N-acetyl-alpha-D-galactosamine to the 4-OH-position of first mannose of the glycosylphosphatidylinositol (GPI) of a GPI-anchored protein (GPI-AP). This modification occurs after the fatty acid remodeling step of the GPI-anchor maturation. Subcellular Localization: Golgi apparatus membrane; Multi-pass membrane protein. Domain: Contains three transmembrane domains, including a tandem transmembrane domain insertion into its glycosyltransferase-A fold. Transmembrane domain 1 functions as a signal for Golgi targeting; The conserved DXD motif is involved in enzyme activity.
0
MARQFVVLVLLTLTIATAFAADAPSASPKKSPSPTAAPTKAPTATTKAPSAPTKAPAAAPKSSSASSPKASSPAAEGPVPEDDYSASSPSDSAEAPTVSSPPAPTPDSTSAADGPSDGPTAESPKSGAVTTAKFSVVGTVATVGFFFFSF
[ 9505, 9739, 25079, 25571, 27013, 87276, 87489, 87522, 87735, 87760, 87975, 88008, 88058 ]
The following text describes a protein: Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death (By similarity). Plays an important role during the formation of the nexine layer of the pollen wall. Subcellular Localization: Cell membrane; Lipid-anchor, GPI-anchor.
0
MRPLKPGAPLPALFLLALALSPHGAHGRPRGRRGARVTDKEPKPLLFLPAAGAGRTPSGSRSAEIFPRDSNLKDKFIKHFTGPVTFSPECSKHFHRLYYNTRECSTPAYYKRCARLLTRLAVSPLCSQT
[ 8667, 10213, 18470, 18474, 24878, 24907, 25079, 28832, 30934, 30935, 31074, 59517, 87103, 87139, 87276, 87363, 87413, 87760, 87976, 88008, 88038, 88058 ]
The following text describes a protein: Function: Cytokine that acts as a physiological ligand for receptor tyrosine kinase LTK, leading to its activation. Monomeric ALKAL1 binds to LTK, leading to LTK homodimerization and activation. In contrast to ALKAL2, does not act as a potent physiological ligand for ALK. Subcellular Localization: Secreted. Cell membrane. Note=Following interaction with receptor tyrosine kinase LTK, associates with the cell membrane, membrane-binding is required to activate LTK.
0
MVMDIRVLTPDRVICSTTADEVILPGLTGQVGVLDGHATLITALDTGLLRIKLADKWTPIILCGGLAEIDRNRVTVLVNDVEELVAVELSEATKELEKATSAIENAETSKARLDASVELKKATARLEGINYLS
[ 10591, 25248, 26421, 29033, 32555, 37166, 52803, 64508, 87109, 87239, 87296, 87598, 87676, 87760, 87930, 88139, 88162 ]
The following text describes a protein: Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. Subcellular Localization: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein.
0
MLTRKQMELLDFIKTRMDRDGVPPSFDEMKDALDLRSKSGIHRLITALEERGFIRRLAHRARAIEIVKLPEAMERAGFSARAAKAAAAPLPKGAVTVETAGALDLPLMGRIAAGLPIEAINGGPQSVTVPGMMLSGRGQHYALEVKGDSMIAAGINDGDIVVIREQQTADNGDIVVALVADHEATLKRYRRRGGMIALEPANDSYETQVYPEQMVKVQGRLVGLIRSY
[ 4653, 8047, 8065, 8200, 9304, 15387, 25809, 27731, 27783, 28227, 41182, 41183, 41184, 49051, 64053, 64146, 64148, 66762, 75732, 87191, 87374, 87380, 87381, 87384, 87601, 88008, 88010, 88034, 88148, 88150 ]
The following text describes a protein: Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Has been shown to bind to the direct repeat sequence 5'-GTT-N(7)-GTTC-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
0
MDLSTILGLVLAVASISLGDILEDGNPLHIIHLSSVIIIVPTSLFAAMTGTHARYVKAAYKEIKIVFLNPKINLNETIKNLVELATLARKDGVLSLEGRVAQIEDDFTRNGLSMIIDGKDLKSVKESLEISIEEMEEYYHGAAHYWETAGETAPTMGLVGAVMGLMLALQKLDNPAEMAAGIAGAFTATVTGIMCSYAIFGPFGHKLKAKSKDIIKEKTVLLEGILGIANGENPRDLENKLLNYIAPGEPKKSQFEG
[ 8522, 19168, 22130, 25079, 36385, 38325, 73034, 87274, 87276, 87287, 87467, 87598, 87676, 87760, 88008, 88159, 88161, 88162 ]
The following text describes a protein: Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity). Subcellular Localization: Cell inner membrane; Multi-pass membrane protein.
0
MQDIRQETLNECTRAEQSASVVLWEIDLTEVGGERYFFCNEQNEKGEPVTWQGRQYQPYPIQGSGFELNGKGTSTRPTLTVSNLYGMVTGMAEDMQSLVGGTVVRRKVYARFLDAVNFVNGNSYADPEQEVISRWRIEQCSELSAVSASFVLSTPTETDGAVFPGRIMLANTCTWTYRGDECGYSGPAVADEYDQPTSDITKDKCSKCLSGCKFRNNVGNFGGFLSINKLSQ
[ 20285, 20460, 25499, 26995, 32536, 33780, 41449, 87042, 87103, 87105, 87577, 87678, 87681, 87708, 87767, 88008, 88207, 88215, 88220, 88228, 88230, 88233, 88237, 88242 ]
The following text describes a protein: Function: Part of the distal tail tip complex which plays a role in DNA ejection during entry, and in tail assembly initiation during exit. The tail tip complex is assembled successively with three tail tip proteins J, one tail tip protein I, one tail tip protein L and one tail tip protein K. The tail tip complex interacts with tail measure protein to initiate tail tube assembly. The formation of the tail tip complex is completed by the addition of tail tip protein M, which is followed by tail tube polymerization. Subcellular Localization: Virion. Host cytoplasm. Domain: The C-terminus coordinates an iron-sulfur cluster.
0
MEDCIGHDNGVEILVEINMICKSGPMKIEGKVAIVTGGGQGIGERFCIALLEKGANVVIADIKTRQGESLSKQFNQKYGLNHLINYTKSTFGNVDILCNNAGVPEMEQWEKVLNINLNSVIRGTKLAMEAMSTKNGGRGGIIINTASMGGILPMPSGPVYCASKFGVVGFSRSLDTCYESDGIRVNAICPSFAPTSLFEASIDSLVNANQHEEARKMKAIIISIDQVARGMIQLVEDDTKNGAVMRITAAKGIDYQPYRSSKL
[ 39, 108, 24978, 30232, 37894, 64058, 87873, 88008 ]
The following text describes a protein: Function: Catalyzes the NAD-dependent dehydrogenation (oxidation) of a broad array of hydroxylated polyunsaturated fatty acids (mainly eicosanoids and docosanoids, including prostaglandins, lipoxins and resolvins), yielding their corresponding keto (oxo) metabolites. Decreases the levels of the pro-proliferative prostaglandins such as prostaglandin E2 (whose activity is increased in cancer because of an increase in the expression of cyclooxygenase 2) and generates oxo-fatty acid products that can profoundly influence cell function by abrogating pro-inflammatory cytokine expression. Converts resolvins E1, D1 and D2 to their oxo products, which represents a mode of resolvin inactivation. Resolvin E1 plays important roles during the resolution phase of acute inflammation, while resolvins D1 and D2 have a unique role in obesity-induced adipose inflammation.
0
MLIKSQRLTLFSPLLSKTRRIPVNSHQTLVAESVITRRTLGAITATPSFHKNPVVIRRRIKLERVTRNCVRIDREIDEEEEEEEKERGDLVKQSIWEQMKEIVKFTGPAMGMWICGPLMSLIDTVVIGQGSSIELAALGPGTVLCDHMSYVFMFLSVATSNMVATSLAKQDKKEAQHQISVLLFIGLVCGLMMLLLTRLFGPWAVTAFTRGKNIEIVPAANKYIQIRGLAWPFILVGLVAQSASLGMKNSWGPLKALAAATIINGLGDTILCLFLGQGIAGAAWATTASQIVSAYMMMDSLNKEGYNAYSFAIPSPQELWKISALAAPVFISIFSKIAFYSFIIYCATSMGTHVLAAHQVMAQTYRMCNVWGEPLSQTAQSFMPEMLYGANRNLPKARTLLKSLMIIGATLGLVLGVIGTAVPGLFPGVYTHDKVIISEMHRLLIPFFMALSALPMTVSLEGTLLAGRDLKFVSSVMSSSFIIGCLTLMFVTRSGYGLLGCWFVLVGFQWGRFGLYLRRLLSPGGILNSDGPSPYTVEKIKSI
[ 8531, 9356, 9406, 9441, 12017, 14335, 15044, 25249, 25277, 25711, 29924, 32089, 38034, 70900, 87296, 87326, 87616, 87662, 87760, 87925, 87930, 88008, 88154, 88159, 88161, 88162 ]
The following text describes a protein: Function: Functions as a multidrug and toxin extrusion transporter in the export of salicylic acid (SA) from the chloroplast to the cytoplasm. Plays an essential function in plant defense via the pathogen-induced salicylic acid (SA) accumulation. Also acts as a key component of the Age-related resistance (ARR) pathway. Subcellular Localization: Plastid, chloroplast membrane; Multi-pass membrane protein.
0
MHLLVATAVSVERDAVARAFPAPGTEVSRPGITLHRLPDGWDLLAAGVGPARAAASTAAALTAAALDGRPYDLVVSAGIGGGFAPEAPVGSLVVADAITAADLGAETADGFLPVTDLGFGTVTHLPPAPLVRAAAEATGARPGTVLTGSTVTGTAARAALLRERHPGALAEAMEGFGVAEAAAAHGVPVLELRAVSNPVGPRDRAAWRIGEALAALTDAVGKLAPVLESWKPHER
[ 4451, 9178, 9229, 10981, 25040, 29420, 29544, 36645, 52446, 63787, 87601, 87762, 88008 ]
The following text describes a protein: Function: Catalyzes the hydrolysis of futalosine (FL) to dehypoxanthine futalosine (DHFL) and hypoxanthine, a step in the biosynthesis of menaquinone (MK, vitamin K2). Does not accept aminodeoxyfutalosine (AFL) as a substrate.
0
MAEPQSRAPAPLCAGATDIVVAASAGISVNARLCKHLLLQGSSLTQPQPLTNSVFLDALARYPLPVVSAATAHDVAGSEQQLQLHQPSAHSPLQPPSEASSEPTTAASAAPVRIRRSTASPLGERHMSFRGAAPHAASDLTSAINQFWALSPAPAAPHSPLLATTEGDAQGPVHTAAVAPCGSAPQPTPPPPPPWVAFSPFRFCADPSFHAALQRLSRHRSGTADTHQRRQRAVAPPSPPSRHMPGLSSLGPPVGGVAPASRPAGEGPHGTPSSGSAAVAVNVSAPDGGSVSFDAPLGAPWTVMDAWCHGFAATAVDGGRSRKRARTASATAASPTSAEPTTFARLHVSDTYHGGSARMGSKNSPPPTVTTVAAHDTFRTNPSPDSIATLLPWASPKTPHETVDVPQSRVPEKDDLLDLLLGVRQNASRSPEFAGGLPCSRAQLMEATGMTGAEVHTEGEGERNALAKHNGSAMLSSSRTVSRLGTSAARAGADGLATSCVQRNQATTSLALTAAATATAMPRGPALSASADADFSCGAVDPNNGEHVLVSTVRELRSTCARLGLLSTGSKTTLQQRLRFYYASAPASQQSGVRVPLAATAANLSAALHVPLDPGATRTGGEVGASRSTGSPPRTVFRYHSPSQSPGSVLPASAAAVAVGQPRTCATEAVSGPATRVAGPAVWEHAAVSTSPAAAASGQRGRFVPSPTQFLHDLASWTTRTPHTALATLCDAHSPPSATAARAQQEELTSETGRVRWQWLVDFRERSSAHRGGGGSGRRQHEGMLDVFRKQHVPCTSMMLPAGDFMLSVELSNEEAAAMHVYGVAASTEVDPGVPSASAPAEGAAPVLSHVCSLVVERKTAADLDASVKGARYTEQRRLLAASPFRLVVWLIEGVNVAGGSGSGFSRHGQRHYQGGDGTESDTQPGSRSPSPAPSSRAESARQRVDSACASLGLHGKGWLVVRTRNTTESVQFLKLLATHVARQLASYRLRRRCMGEGNSGMVAGTDGCAACQTAAQDPSAQRVARADGGDVHCGNIFRSTGNGASTTSMAAAVALLQLTTTKTCLQSVSALQRHLRAKTAFPRMLMCVRGCSAALASLLSSKYGTLLRFWRELRRRGQEVCDADPDIQRLTTAQKKVYILLTEFLLAKDYF
[ 4070, 6787, 6798, 8082, 12083, 24917, 26466, 27904, 29458, 32536, 33230, 38425, 41157, 45553, 61714, 87016, 87374, 87379, 87380, 87431, 87601, 87747, 87767, 87850, 87857, 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.
0