lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Subcellular Localization:
Cytoplasm.
Sequence:
MPEEKVATKKIKLSALCELCNGRKAVMKRPKNLQKLCKECFYNVFETEIHNTIADANLFQPGDKVAIGASGGKDSTVLASVLKTLNERYDYRLELVLLSIDEGIKGYRDDSLATVKRNQAQYNMALEIISYKDLYNWSMDEIVSCAGIRSSCTYCGVLRRQALDRGAAKLGINHVVTGHNADDMAETVLMNLLRGDTARLEKSCTILTQSTGSPIKRSKPFKYSYQKEIVLYAHYKKLDYFSTECSYAPEAFRGTARELLKSLEAIRPSCIMDIIYSGEHLALAPKKKRTQQYKNKKKTQVDNEHEINADGSITIGTREFKDGNRCENCGYLTSNKICKACVLLAGLEMNRAKVSVDNNTAVDGAAKLTKTLEQLSF
The following text describes a protein:
Function:
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminopimelate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. Can also hydrolyze all N-terminal Asp dipeptides except Asp-Pro. Asp-Ser is the best substrate, followed by Asp-Gly, Asp-Leu, and Asp-Cys.
Miscellaneous:
MISCELLANEOUS: Zn(+2) is usually found in the tight binding site, but the nature of the second cation in the low affinity binding site is different according the activity.
Sequence:
MSCPVIELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMDFGDTQNFWAWRGRGETLAFAGHTDVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNGTVKVVEALMARNERLDYCLVGEPSSTEIVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGNDFFPATSMQVANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLVA
The following text describes a protein:
Function:
Binds bis-(3'-5') cyclic diguanylic acid (c-di-GMP), the ability to bind c-di-GMP is important for its function.
Miscellaneous:
MISCELLANEOUS: Cellulose production is abolished in E.coli K12 / MG1655 and W3110 due to a premature stop codon in bcsQ.
Domain:
The central domain (GIL, residues 153-492) is sufficient for c-di-GMP binding.
Sequence:
MRDIVDPVFSIGISSLWDELRHMPAGGVWWFNVDRHEDAISLANQTIASQAETAHVAVISMDSDPAKIFQLDDSQGPEKIKLFSMLNHEKGLYYLTRDLQCSIDPHNYLFILVCANNAWQNIPAERLRSWLDKMNKWSRLNHCSLLVINPGNNNDKQFSLLLEEYRSLFGLASLRFQGDQHLLDIAFWCNEKGVSARQQLSVQQQNGIWTLVQSEEAEIQPRSDEKRILSNVAVLEGAPPLSEHWQLFNNNEVLFNEARTAQAATVVFSLQQNAQIEPLARSIHTLRRQRGSAMKILVRENTASLRATDERLLLACGANMVIPWNAPLSRCLTMIESVQGQKFSRYVPEDITTLLSMTQPLKLRGFQKWDVFCNAVNNMMNNPLLPAHGKGVLVALRPVPGIRVEQALTLCRPNRTGDIMTIGGNRLVLFLSFCRINDLDTALNHIFPLPTGDIFSNRMVWFEDDQISAELVQMRLLAPEQWGMPLPLTQSSKPVINAEHDGRHWRRIPEPMRLLDDAVERSS
The following text describes a protein:
Function:
Has fibrino(geno)lytic activity on the alpha and beta chains of fibrinogen (FGA and FGB). Inhibits human ADP- and collagen-induced platelet aggregation on platelet-rich plasma but does not affect the thrombin-induced aggregation of rabbit washed platelets. Slightly degrades plasminogen.
Miscellaneous:
MISCELLANEOUS: Negative results: has no hemorrhagic activity. Has no activity toward factor X (F10), prothrombin (F2) and protein C (PROC).
Subcellular Localization:
Secreted.
Sequence:
ERFAPRYIELVIVADHSVATKYNDNVTAILSWVHQLVNNIILFYRDLNVHFTLSAVEVWSNGDLINVQPEATVTLNLFGEWRERDLLNRRMHDNAQLLNNVALDDNTIGLAYDEGMCDPKYSVGIVKDHSAINRMVAATMAHEIGHNLGMNHDGSQCNCGGNGCVMSAVLMQQHSYQFSDCSKDEYQRYLTNHNPQCILNQP
The following text describes a protein:
Function:
Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm.
Subcellular Localization:
Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus, nuclear pore complex.
Sequence:
MAICQFFLQGRCRFGDRCWNEHPGARGAGGGRQQPQQQPSGNNRRGWNTTSQRYSNVIQPSSFSKSTPWGGSRDQEKPYFSSFDSGASTNRKEGFGLSENPFASLSPDEQKDEKKLLEGIVKDMEVWESSGQWMFSVYSPVKKKPNISGFTDISPEELRLEYHNFLTSNNLQSYLNSVQHLINQWRNRVNELKSLNISTKVALLSDVKDGVNQAAPAFGFGSSQAATFMSPGFPVNNSSSDNAQNFSFKTNSGFAAASSGSPAGFGSSPAFGAAASASSGISTSAPAFGFGKPEVTSAASFSFKSPAASSFGSPGFSGLPASLATGPVRAPVAPAFGGGSSVAGFGSPGSHSHTAFPKPSSDTFGNSSISTSLSASSSIIATDNVLFTPRDKLTVEELEQFQSKKFTLGKIPLKPPPLELLNF
The following text describes a protein:
Function:
Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
Miscellaneous:
MISCELLANEOUS: Lacks the C-terminal half of the classical GPI inositol-deacylases.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MLSKRLFPYSNLFPRSRKYKFIVYFIICLTIIISALGVYLYSIPIVSPNQPQCDMVWMSPSYARIRAFDETHTKYASKYNLYLYREQDVDKMPNENENEDGNEGFTSLDGIPALFIHGNAGSFEQVRSIAARCSEMYYNDGRFKEKYPHARNIDFFTADFNEELSAFKGLRDQVEYVTQAISFIVDLYPQNPNRNIILIGHSMGGLVARIAASRQQHESNVDIILTLATPHSDPFPWLPKTSDFPDEVGLISIYSSVDLMVPPSVVTPKSKSDHFFSVDAAKLLGVPIDHQGIVWCGQLREKLSEALIGISGLNTLQDRMKVFKKIFSGDRKELGPTPIFGLAKLKLKLLQSWVHLLSLTIFALKWTIIVLAIIQLRKVYTKFNNPPPTH
The following text describes a protein:
Function:
Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate a phosphatidyl-inositol-calcium second messenger system.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MDSEPSWTATPSPGGTLFVPNTTTPWLGRDEELAKVEIGILATVLVLATGGNLAVLLILGLQGHKRSRMHLFVLHLALTDLGVALFQVLPQLLWDITYRFQGSDLLCRAVKYLQVLSMFASTYMLLAMTLDRYLAVCHPLRSLQQPSQSTYPLIAAPWLLAAILSLPQVFIFSLREVIQGSGVLDCWADFYFSWGPRAYITWTTMAIFVLPVVVLTACYGLICHEIYKNLKVKTQAGREERRGWPKSSSSAAAAATRGLPSRVSSISTISRAKIRTVKMTFVIVLAYIACWAPFFSVQMWSVWDENAPNEDSTNVAFTISMLLGNLSSCCNPWIYMGFNSHLLPRSLSHRACCRGSKPRVHRQLSNSSLASRRTTLLTHTCGPSTLRLSLNLSLHAKPKPAGSLKDLEQVDGEATMETSIS
The following text describes a protein:
Function:
May play a role as ligand of RXFP1.
Subcellular Localization:
Secreted.
Sequence:
MAAPALLLLALLLPVGAWPGLPRRPCVHCCRPAWPPGPYARVSDRDLWRGDLWRGLPRVRPTIDIEILKGEKGEAGVRGRAGRSGKEGPPGARGLQGRRGQKGQVGPPGAACRRAYAAFSVGRREGLHSSDHFQAVPFDTELVNLDGAFDLAAGRFLCTVPGVYFLSLNVHTWNYKETYLHIMLNRRPAAVLYAQPSERSVMQAQSLMLLLAAGDAVWVRMFQRDRDNAIYGEHGDLYITFSGHLVKPAAEL
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MASAFLTHQQKVLRLYKKSLRHLESWCVFRDKYRFYACLLRARFDENKNEKDMVKATLMLKAGEEEFWTNQHPQPYIFPDSPGGTSYERYECYKVPDWVLDYWHPSEKTMYPDYFSKREQWKKLRMQSWDREVAQLEAETLPGGPRTEALPPARKEGDLPPLWWQDVTRPRERPT
The following text describes a protein:
Function:
Protein-arginine rhamnosyltransferase that catalyzes the transfer of a single rhamnose to elongation factor P (EF-P) on 'Lys-32', a modification required for EF-P-dependent rescue of polyproline stalled ribosomes.
Domain:
Adopts a GT-B fold and acts as an inverting enzyme that converts the beta-configuration in the dTDP-beta-L-rhamnose donor to the alpha configuration in the N-linked (Rha) arginine product.
Sequence:
MNTPPFVCWIFCKVIDNFGDIGVSLRLARVLHRELGWQVHLWTDDVSALRALCPDLPDVPCVHQDIHVRTWHSDAADIDTAPVPDAVIETFACDLPENVLHIIRRHKPLWLNWEYLSAEESNERLHLMPSPQEGVQKYFWFMGFSEKSGGLIRERDYRDAVRFDTEALRQRLMLPEKNAPEWLLFGYRSDVWAKWLEMWQQAGSPMTLLLAGAQIIDSLKQSGIIPQNALQNDGDVFQTASVRLVKIPFVPQQDFDQLLHLADCAVIRGEDSFVRAQLAGKPFFWHIYPQDEHVHLDKLHAFWDKAHGFYTPETASAHRCLSDDLNGGEALSATQRLECWQILQQHQNGWRQGAGAWSRYLFGQPSASEKLAAFVSKHQKIR
The following text describes a protein:
Function:
A tubulin-like, filament forming GTPase; the motor component of the type III plasmid partition system which ensures correct segregation of the pBtoxis plasmid. Filaments may seed from the centromere-like site (tubC) when bound by DNA-binding protein TubR; the tubC-TubR complex stabilizes the TubZ filament. Filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling. TubR-tubC complexes track the depolymerizing minus end of the filament, probably pulling plasmid within the cell. Required for pBtoxis plasmid replication/partition. Binds the TubR-tubC complex; GTP is not required for binding to TubR-tubC. TubZ alone does not bind DNA. Has a high GTPase activity in the presence of Mg(2+); in the presence of GTP assembles into dynamic filaments which upon polymerization bind almost exclusively GDP. Filament formation is cooperative, requiring a critical concentration. Formation occurs very quickly and is followed by disassembly as GTP is consumed.
Miscellaneous:
MISCELLANEOUS: N-terminally tagged protein does not form filaments, C-terminally tagged protein does so, but not as well as untagged protein; MISCELLANEOUS: The pBtoxis plasmid encodes all the major endotoxin proteins (Cyt1Aa, Cry4Aa, Cry4Ba, and Cry11Aa) responsible for the mosquito larvicidal activity of strain 4Q2.
Subcellular Localization:
Cytoplasm. Note=Forms long, dynamic filaments.
Domain:
Consists of two domains: a nucleotide-binding N-terminus that hydrolyzes GTP and a C-terminus domain necessary for polymerization. The domains are bridged by a long, central helix. The C-terminus is required for binding to the TubR-iteron DNA complex; its gradual deletion leads to decreasing binding to TubR-DNA. Interactions between the C-terminus and the following monomer drive polymerization (By similarity). The C-terminus is required for filament formation. In the absence of GTP's gamma phosphate the intersubunit interface is weakened, linking GTP hydrolysis to treadmilling.
Sequence:
MLLNSNELEHIHSTNHSVNDISIRWGVIGAGQKGNKEADLFAGYKFSNGTTCYPTLAVNFAESDMMHLQNIIKEDRIHFDGLKGAARTPSVVTDLFDPETNPNANGYLDKLAQELGRKFTNEEGEVIVDQFLICLGAGGGVGTGWGSLVLQLIREQFFPCPVSMLISLPSGDPDEINNALVLLSEIDEFMREQDRLFGNSDIKPLANVIVNDNTQMQRIIESQKGTKDLKNRYVNWKEVANDNVVSTLHEINIIPENYGSDNVTYDPSDLIKLLSIPGRFLTIGKARIAKFDLHSLENSIKRSLDEGFFSAEHQFETATMYGGFVLRPSNADFFKDVNTENRIRNTLGEYKRLDEIAGKFGDPIWDNEYAVCYTIFAGMTMPKRYISLAREGKELAEKQEQLRAEAQRKQDEEKVDISFATNRVQKNTFNPYNKNQGFGGASRFSGGKNSAFKRQTSEATSTQNQQEEENIISTLKTSNPFKKR
The following text describes a protein:
Function:
P450 monooxygenase that plays a major role in cholesterol homeostasis in the brain. Primarily catalyzes the hydroxylation (with S stereochemistry) at C-24 of cholesterol side chain, triggering cholesterol diffusion out of neurons and its further degradation. By promoting constant cholesterol elimination in neurons, may activate the mevalonate pathway and coordinate the synthesis of new cholesterol and nonsterol isoprenoids involved in synaptic activity and learning. Further hydroxylates cholesterol derivatives and hormone steroids on both the ring and side chain of these molecules, converting them into active oxysterols involved in lipid signaling and biosynthesis. Acts as an epoxidase converting cholesta-5,24-dien-3beta-ol/desmosterol into (24S),25-epoxycholesterol, an abundant lipid ligand of nuclear NR1H2 and NR1H3 receptors shown to promote neurogenesis in developing brain. May also catalyze the oxidative metabolism of xenobiotics, such as clotrimazole.
Subcellular Localization:
Cell projection, dendrite. Endoplasmic reticulum membrane; Single-pass membrane protein. Microsome membrane; Single-pass membrane protein. Postsynapse. Presynapse.
Sequence:
MEGNLIVFGLCLLVTAFSFIFLGIFFYVSYNRNIYSHIPHPKPLHFLLGHLPLFKEVAKNGPVSKKMVEWSKELGPVYCLHIVFRTLIMCNDSTVIKELLTRSKYLKSPDNYRGLKSVYGAMTLGNGLLSEMNHEVWMKKRALFNPAFHRKYLMGLMNEFNSCSAKLVNHLIPLSDGQTEVVMLKEFERLTLEIIGKVGFGMEDDIIGNPDSPLCQLLPKVLSGVNSVYRRPLLKYSILPKDIKYKHEVRAAANEIRAVGRRCILARIDALRRGDQVPQDILTYILQESNNLEGIKDFDLEDMVDEFVTFFGAGQETTANLLSFTLLHLGRNPQVMKKLRDEIDTVLKGRNYVEYSDVGKMKYLTLVLKETLRINPPVGHLHRLLPHEMDICGYKVPKGSVVMVPIYGMGRNEKHFKNPEKFDPERFTRDEDSPLFAYMPFSLGARSCIGQTFTMIEFKVVICKLIQQLEFQLVPNQSFEFVEETLTFKPKDGCKSYITMRNI
The following text describes a protein:
Function:
Transcription factor that binds promoters containing the CryR2 element, 5'-ACATAWCT-3'. The DNA-binding activity is decreased upon direct physical interaction with the mediator subunits and is modulated by redox conditions. The oxidized protein is the preferential binding form.
Subcellular Localization:
Nucleus.
Sequence:
MAPKKAEEVVESPPVSSEEEESGSSGEESESSAEVPKKVESSQKPESDSEGESESESSSGPEPESEPAKTIKLKPVGTKPIPETSGSAATVPESSTAKRPLKEAAPEAIKKQKTSDTEHVKKPITNDEVKKISSEDAKKMFQRLFSETDEIALLQGIIDFTSTKGDPYEDIDAFCIYVKKLIDFDATKNQIVTKLQRLKKKFNNAVKNSLKKGKTEDDIEFAKDLEQKGFELSRKIWGSNGVLVTGKSSRKKVGGTPAPKEMKLVAHSTPKKQQEEAKKPERTEAKVVNTGLSIGKEIASFLNADNGSSCGLDESTLTAVWAKVADGAEKREVEEKWKKLKAKQFELCLQRSGLVNETAKMIFKAYES
The following text describes a protein:
Function:
Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Required for the proliferation and viability of hematopoietic cells.
Subcellular Localization:
Cytoplasm.
Sequence:
MSGRLWSKAIFAGYKHSLWNQREHTAVFLKIEDETEFYLGKRCAYVYKAKDSTVTPGGKPNKTRVVWGKVTRAHRNSGKVRAKFRNNLPAKVSTNEKSTNKSGFVGGKRSLEVRLFNRVGLQQMPVGSLGVLLPV
The following text describes a protein:
Function:
Dual methyltransferase. It catalyzes N-terminal methylation of target proteins via its C-terminus. It catalyzes dimethylation on lysine residues of target proteins via its N-terminus.
Sequence:
MNLLPKTREEFAQTDYWNEFFKKRGEKAFEWYGEYLELCDQIHKYIKPADRILMLGCGNSKLSMDMYDTGFRDITNIDISPIAVKKMLELNAKSRPEMKFLQMDATAMTFPDESFSVSLDKGTLDALFADDEPETRAVVENYFKEILRTMRNGGRYVGISLLQEHILNFLLDFLPKHNCMLRIVHCLGVEQANKEKNADDALTLPVFVVVATKFKSLPMPVLEFGFGNDKMQRFTTVSELNSAVSSVQKAALVCNGLARSNIAGHNEVIMDLHRPSEQTPRYTIHILDKPPARGLGKYAAFIVPQGREVEWIFSTPAGRKKLQDSANFQRLAVVTLHRDQVYSTLDEVKQELADSIKNLSPAGLTDQIPYLSLGSDVGKRETLICGFSKISGDFRIEEVEANGKTLRRLIFLSNQFVVQSEALVKTVKIKGKKDRKKIDFGYLACQHHLYMSVGVQLATTVQHPKRDVEKDVLVVGLGGGGLCSFLHAALPQARITAVEIDPIMLEVAEQYFELKQDKRFHVVIDDGLDFVERCRNEDIHFDAVLFDVDSKDLSLGMSCPPQSFLATKILQHIKEIIGPKGLFMLNLVCRDESLRTEALNNLHKVFPAVCSYKLEEDINEIIYCANDEKYKTVEQWKKNMGTAGRGLNSAVKETKLASEDALEVAEFLSELKI
The following text describes a protein:
Function:
Stress-inducible actin-binding protein that plays a role in synaptic and cognitive functions by modulating actin filamentous (F-actin) dynamics. Mediates polymerization of globular actin to F-actin. Also binds to, stabilizes and bundles F-actin. Involved in synaptic function by regulating neurite outgrowth in an actin-dependent manner and for the acquisition of hippocampus-dependent cognitive function, such as learning and long-term memory. Plays a role in the actin and microtubule cytoskeleton organization; negatively regulates focal adhesion (FA) assembly promoting malignant glial cell migration in an actin-, microtubule- and MAP1A-dependent manner. Also involved in neuroblastoma G1/S phase cell cycle progression and cell proliferation inhibition by stimulating ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B degradation in a COMMD1- and actin-dependent manner. May play a role in tumor development.
Subcellular Localization:
Cell junction, focal adhesion. Cell membrane. Cell projection. Cytoplasm, cytoskeleton, stress fiber. Nucleus. Synapse.
Sequence:
MQSGDCVRVCVCACVLVCLKDVHPLQLLLLLCRKIAGRIQPKLCFLEQLGIGIMGVTHGKKADHNLQSHNSACAQPLIGPGESDLVSDLGSLIDPDQRWAREEDLDHSKLLPEHTDYEELIRPKKLHNPIKASKSHRELQRELIITHKRGVVVEEKPELQRVLEQRNRAQALKQEQKQEEEKSPLEQELLKRQMRLEKFEKEAEEQRERLKCAPEFIRVKESLKRTAITSAAEKEL
The following text describes a protein:
Function:
Necessary for the splicing of pre-mRNA. Probably active at the 3' splice sites.
Subcellular Localization:
Nucleus speckle.
Sequence:
MYQRPDMITPGVDAQGQPLDPRKIQEHFEDFFEDLFEELGKFGEIESLNICDNLADHMIGNVYVQFKEEDQAAAALQALQGRFYSGRPIIADFSPVTDFREATCRQYEENNCNRGGYCNFMHVKLVSRELRRKLFGRYRRSYRRGSRSRSRSRSISPRNKRDNDRRDPSHREFSHRDRDREFYRHGSGKRSSERSERQERDGSRGRRQASPKRGGSPGGGREGSEERRARIEQWNREREEKEEGGA
The following text describes a protein:
Function:
Invertase inhibitor (Probable).
Subcellular Localization:
Secreted. Secreted, cell wall. Endoplasmic reticulum. Note=After 5 minutes in germination medium, detected as a soluble protein and released from apertural and non-apertural regions of pollen grain wall. In mature, non-hydrated pollen grains, predominantly associated with the endoplasmic reticulum (ER) concentric cisternae, which are situated between the vegetative nucleus and the generative cell. After 5, 15 and 30 minutes as well as 2 hours of hydration, localization to this ER region is noticeably decreased.
Sequence:
MKLSFSLCIFFFNLLLLLQAVISADIVQGTCKKVAQRSPNVNYDFCVKSLGADPKSHTADLQGLGVISANLAIQHGSKIQTFIGRILKSKVDPALKKYLNDCVGLYADAKSSVQEAIADFKSKDYASANVKMSAALDDSVTCEDGFKEKKGIVSPVTKENKDYVQLTAISLAITKLLGA
The following text describes a protein:
Function:
Regulator of sister chromatid cohesion in mitosis stabilizing cohesin complex association with chromatin (By similarity). Antagonizes the action of WAPL proteins (WAPL1 and WAPL2) which stimulates cohesin dissociation from chromatin, particularly during somatic division in root cells and meiocytes during anaphase I. Required for centromeric sister chromatid cohesion during male meiosis (microsporogenesis). Cohesion ensures that chromosome partitioning is accurate in dividing cells and may play an important role in DNA repair (By similarity).
Miscellaneous:
MISCELLANEOUS: Named sororin after the Latin word 'soror', which means 'sister', because of its critical role in sister chromatid cohesion.
Subcellular Localization:
Nucleus.
Sequence:
MEAPRSVGGRIQRKPLADCTNTVSRSSQQSSSSVKFANPSLTSSLKRLVEQTTLKEKPKDVNTSATAPEIASRPITTDVRPVTRRMSADLASPASAPSRPQTSRSDMGVSDKDFTEPWSVYTVRRKASGQKRSKDASSSTSAAARIRLDLSSSSGKKTRQASENKKKTLKVAPKKRQRTVKQEKEDPVSAACQDYIEKQKAYFAEIDAFELPVEEVSNSDSD
The following text describes a protein:
Function:
Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
Subcellular Localization:
Cell outer membrane. Membrane.
Sequence:
MPSIMKFRKRFLFAITFIIFCIPFTLTAYGFVVRSIQIQGLQGISADTVRSYLPIHEGQEYTAQRGQRILQSLYRTGFFETVRLARRGDALIISVKERPIISLIRISGNKAISTKKLRPILNKLNISEGQPYDPTKLHEIEVGLEQQYGAMGYHAATVSTRVVKETKNRVALYIHINEGGIAKVGSIQFVGNRAFSARTLRNQFKLTTPGLFTWISHRDRYSQVKLEEDLQQLSEFYLNHGYLRFRVVSHDVQWSPDKKHVYITIHLVEGPIYHLSGYTITGETYGFKDQLYRLVKLKRGDIFSRQVIINTNKAIGDFLGDRGYAFARVNVIPTIDDQQHLVHLTFNVAPGERVYVRRISFFGNQRTDQEVLRREMRQYEGSLYSLSKIEESKRRLELLGYLSDVKYTPQIVPNSPDQVDLNYHVKEIAAGRASIQGGYSDVYGFLYGASISEPNFMGTGKYVSIGFQNSQYQQNYSFVYNNPYYTTWGLQRGFSIYYSRVKPNTKFNLSSYVEDGYGADVTYAYPISERNSIGFGYGFEHIKISQLDPAIAAPSVLAFLGTTNGVQNTSRDYNQFKLNGGWTYNGLDRAIFPTKGLYTGIGLEIGVPVLKSSLGYYLATYSAKYYQPIWHGFILNLLATVGYGDGFGHDRLPFFKNFYAGGIGSVPAFSPNSLGPKNRYNSFGAIGGNLETIFGVHLILPQFISERVRTAIVFDAGNVFQVPRFPGDIAVPARATIPDPEAATRPQIIQNDRFSLKNLRPSLGLAVEWYTPLAPIDLTLAFPLNRRPGDNFQAFQFSFGVSL
The following text describes a protein:
Function:
VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MKAITTTIGTLWILSAHWTKADTNAADNEPDFTVLCSVLDVATGKPALNDIPTKWRNLRQQLTDINISLSTGDWTKHLLDTDGNVQEWTKAQQAGKLPEDWATEWPAWAAAAKRSAKGGETHDKLQASGIPSLDAEQRKEAAQLIKHLLNSTQPLMDALQGVETAEAATTAAALAATLDQSVYGDKPEAHPGKQASAAVRRTATRGICASGAKIGTSQALADALLCLCWTDTGSPPQGQGSVCRKNLGNTLTSTWDTASATVNAAYAQIKGACKLQTGHTITAANIAEALAAVKHKIAQHKEGGYLGKYEGDFSCDGKNANGVCIKYADFSDKGNKAFEEIEWVKKLRSVETALRKREAAVARVDTLTTALETQTAAAWLIPQRAKSSQQKREGVSPKQHTSTGNGNKQQADQCEAIKKATECKEKQPNCEWQGKNDEDGPHCKVNKTHITKEAAQTGTNRGNEETTTDKCSQAKTSDECAAVKGDIPKDKKSVCGWIEGKCQNSRFPVNKKLTLMVSAFVSIAAF
The following text describes a protein:
Function:
Probable thiol-disulfide oxidoreductase that may participate in various redox reactions.
Sequence:
MAEALLHHLPRRFGASTSASSSPSSHVVLSPAPRADLRVTRLAAAAPPGRPRRLMAHAAVRSETGEQPKWWEKNAGANMIDIHSTQEFLDALRDAGDRLVIVEFYGTWCGSCRALFPRLCRTATDNPNIVFLKVNFDENKPMCKRLNVKVLPFFQFYRGADGQLEAFSCSLAKFQKLKDAIAVHNTDRCSIGPPVGVGDVLDSSSSQEKPTEAAS
The following text describes a protein:
Function:
May bind amino acids.
Sequence:
MAMKGYLDEYEKLVIRMNTPRVVIDNGVCSSATIVKVDSSRRNGILLEAVQILTDLNLSIKKAYISSDGTWNMDVFHVTDLNGNKLNDQSVLRYIEQSIETVYYGENIEVNGLTALELTGTDRIGLLSEMFAVLSDLNCDVVDAKLWTHNGRVASVIYLKDCISGAPILDSHRISKIEGRLKNVLNGDNDVNSAAKTCVTVDSMMHIERRLHQLMFEDRDYERRSKKHERSPMVVVTVQNWAERGYSVVNVHCRDRTKLLFDVVCTLTDMEYAVFHATINTAEDQAHLEFYIRHKDGSPISSEAERQRVIQCLEAAVERRALEGVRLELRHPDKQGLLAEVTRTFRENGLNVTRTEISTSSDMATNIFYVTDANGDEPDFKLIESVREKIGLECLRVKEMPTMYHKKGDGEEQQQTKAVLVSLGSLVWRNLFNFGLIKSCS
The following text describes a protein:
Function:
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MAVTAAQVKELREKTGAGIMDAKRALVETDGNMEAAAELLREKGIAKAAKKADRVAAEGLTGIAVNGNVAAIVELNSETDFVAKNDQFVALVKETAELIASKKPATNEEALALETASGITLEAELVQATATIGEKITFRRFAVIEKTDAQHFGAYQHNGGKIGVVSVVEGADETLAKQVSMHIAAMNPTVLSADELDSEFVKAELAQMNHKIDEDNASRVLVNKPELPHHEFGSKSQLTEEVLAAAKASFEEELKAEGKPEKIWDKILPGKMAKFIVDNTKVDQQFALLAQLYIMDDSKTVEAFLESKGAKAIAFTRFEVGEGIEKAETDFAAEVEAAKAGL
The following text describes a protein:
Function:
Probable transcription factor with a role in the retinal determination (RD) network. Contributes to differentiation of antenna-specific characteristics (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MPMSSSGYSRTTTHFKMMMATKGKRPLRHLTATDKIDAIQRIHDGESKASVARDIGVPESTLRGWCKNEEKLRYMSRQSAENADKLTSEATAAALTAVAAAELFNGPPEKRMKLEQGLFGKKYDESFYKSPRGMNGLDLSGGGDKGLGVSGGDIIMNGLHGADFSAFAKTAAEISAMGKAKDRYGADLSRNGGGDPGKAELSMAAISPLTSLSHLSGMGGLAQSPLALSFNEIATNLNLIAQLNNNHNLATMSNLGGLTAAQSLRNARPKGNASQSPRASLPDSSGSGGGTPGDKSTPSLTVRNLAKLQQKTSSELQNNGRDPNAPVDEALWYWLKSQQAMLGLNNLYSQMPRPSSPQQPQSTPPTTTTTQQQQPQSSTPPTATPPIVSTPQPTPPSSAPSLTPEDTKNSSWFWQWYKTFGASLMPGDKSCNNNSINATNANNSKYENILYSQLTKGQSPPTTADSLNNNAQPINLNISSNGVVDHLKSEPEDLTTTTNPSMLPPEDHTRFNPSPSTSIKSELKPEVDEDEDEDDEVAKCNGANTAVKQVLDNLLYSQSSPGPVATAPSPLSPSSSTHENGHATPTPLADDLKSTCSEDTDLKSSAEAVEHGEKFLKWLEACSDPNVTAMQVMQFKYLLNSIKLSAERQNGGGEERTRRRRK
The following text describes a protein:
Function:
Binds to the TGF-beta receptors sma-6 and daf-4, and enhances TGF-beta signaling activity in vitro. Has a role in regulation of body size.
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Cytoplasmic vesicle membrane; Lipid-anchor, GPI-anchor.
Sequence:
MIVYSLLLLILYDFLPKVVTFDTVCIGLCHCVGNVVDCSSLDLSEIPTTIPNNTRILLLSDNEIESIDKSRLKGFYFLQTLDISNNIIRHIDFEFFYNLPNLKILNIRKNRLARIPRGSHELGHLEKLDLRSNLISTVTSEELSYLAAVRSVDLSRNLISYLPKPTTSAKVNIEKLDLASNSITDIGTDHFSSFNTLVTLKLARNHITTLNQFSFSRLRKLESLDLTRNMIREVRFLAFNQLPSLQNVSLARNDVYRLDDGMFYACEGLKHLNLSTNRVQAVTEGWMFGLTSLEVLDLSYNQIQSFHISSWSHTPKLKWLSLHSNRIQSLPSGSFRVLRQLEELILSANSIDSLHKFALVGMSSLHKLDLSSNTLAVCVEDGAVLYNTSMPFLRSLRFTNNQLRVIPKRAFERFPALEELDLTDNPIATIHPEAFEPLELKRLVMNSSSILCDCQISWLASWIYRLKLDKSSIIAKCSYPPPLADLYVVAIDTANLTCHNDSPRAKIVRQPVEVSTLIGEKARFTCNVYGASPLSIEWRVMENGQPRVLVQDSATFLSINRTAVVNGTFDERELAAAELLLDNVAMTDNSEYQCVARNRFGSDFSTHVKLQVYQAPKFTYTPEDMPLLVGQTAKFLCAATGTPRPEIKWAFEQIPFPAAEARRLYVTPNDDHIYIMNVTKEDQGAYTCHATNVAGQTQASANLIVFENFFHYPESPDLSPMLIKKRDALKIDCSCDLISSRQRMVWKRQQQVILFLKKAKFSDNDQILTLTQTTFSDSGEYSCELWVDDTILMRKITMVKVVNEDEFVSSEATLTQRVQRIRAMASKLVDNIKSTGNGIYLMASCSAFGLMILGVITSICICIAKCSCNQNHVFNVLPVQV