lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate.
Subcellular Localization:
Nucleus.
Sequence:
MAPKGPTPDKARLGLPDRWLHCPKTGTIVNDLFFPFKTPLCKMYDQQIPERKWKFSPADVFSSPFLNGRRIGLWIDLTNTDRYYFPDEVTEKSCRYVKMAMAGRGMSPTKEETDTFIKIVTEFHEKNADLLVGLHCTHGFNRTGFLIAAYLFQVNEYGLDAAIREFAENRQGGIYKQDYIDDLYTRYEPLEDERVMAPEKPDWEREHHYTDGSNQNNNGTASSSQANFANGFPLLISYFLSKTYQYSGNGNQSASSSNGKNNGAGVKQFMDGLVKGARHVEDPGKKSILQAKVLIALNEIHKMPFQIQELCKWSKQGFPGLQPVSLSRDNINCFEKEPYMVSWKADGMRYIVYINDGEVYAFDRDNEVFEIDNLDFVNNDGSPLKGTVVDTEVIIDKVEEHGILRDHPRMLIYDVMRIGGFNVMKEPFSKRFKIISTEIIDKRDAGFRSGKLRRERQTMSVRRKDFYVLETTWKLFERKFVKNVGHEIDGLIFQPTDRQYETGRCDKVLKWKPPSHNSVDFLLKITKVCREGMLPEWTGHLFVQNQREPFGSMKATASLRQYDGKIIECTLKVNERGQATEWVFMRERTDKSLPNGLRTAQNVLDTMLRPVTEEYLLGSINHALRVLDARKREHLSHEGHSDPKRPRVQ
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Required for respiration and the maintenance of the mitochondrial compartment.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MLRTLRTSQLARSGFGTPSFGLRFNSVGRAFVFSQTGEPKDVIQVLEYPIEKPLENQVLLKSLGFTINPADINQLEGVYPSVPPKSVQINNEDAAIGGNEGLFQVLDPGAKSGLKKGDWVLPRKTCFGTWRSHALVEADTVVKIDNTDLTKVQATTVSVNPSTAYEMLKDLKEGDWFIQNGGNSGVGRAAIQIGHIRGLKSISVVRDRPDLEVLKKELTDLGATHVITEEEASDKLFSKQIKSWTGGKIKLALNCIGGKSATSIMRQLGAGGSIVTYGGMSKKPLTFPTGPFIFKDITAKGYWLTRWADKHPEEKAKTIENIFKFYREKKFVAPPVNISTLDFSKGNDVVLSEFLDALGKAQKGGGKKQLVQWVEY
The following text describes a protein:
Function:
May play an important role in inflammation and regeneration of skeletal muscle (By similarity). Essential for embryonic development (By similarity); [Isoform CKLF1]: Has chemotactic response in monocytes, neutrophils and lymphocytes. Binds CCR4 (By similarity).
Subcellular Localization:
[Isoform CKLF1]: Secreted; [Isoform CKLF2]: Membrane; Multi-pass membrane protein.
Sequence:
MDSPQKVVDHQPFCLSLKCFVKTLRLVVTVASMIFFIVAQAPEPYIVITGFEVTIILFLIALYMCSLDKTMRSFFWPLLDVINSVVTTLFMLIVSVSALIPETSTMIMVGGVFGFLTVICTVADCALMCQKLRFRPHGPYQNRSATDVDDS
The following text describes a protein:
Function:
Probable NADPH-dependent quinone reductase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent. The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD. The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules. The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain. TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1. Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5.
Sequence:
MHAALVPTWSSPCPIYTEIPDPGPPPPEQLQLKVLAVGIPRVVRLRARGIHPTAKSASLPYDPSIDGVGIDEQTGIMYYILPLSASCLAEKVNVDRDNLVPLQPGAPKPQPRNGPENGYGIALGDAADHRAETLDPIAIAGLVNPVSSSWMALRTRVDGEITGKTVLVLGATSKSGRAAVLVARFLGANKVIGVARREEGLRSVEGLDGWVTSGDMLPGETGVRFALPDWVGPVHIVLDYVGGSVAAGVLGSAEIEEGRELQYVQVGNLALELGTGEKHMFETLPGHLISRKPICIRGSGMGSFSRRDLVREMPGLVAFLARMKAPFGIASAPMCEVASVWQDEDTKGSRVVIVP
The following text describes a protein:
Function:
Transcriptional regulator that activates expression of the aaeXAB operon, which is involved in the efflux of aromatic carboxylic acids such as p-hydroxybenzoic acid (pHBA). In the presence of the effector pHBA, acts by binding to a single target within the aaeXAB-aaeR intergenic region. In the absence of pHBA, binds more than 50 sites along the E.coli K12 genome, including genes related to biofilm formation and several genes involved in stress response, suggesting that it might play a role in quorum sensing in the absence of pHBA.
Sequence:
MERLKRMSVFAKVVEFGSFTAAARQLQMSVSSISQTVSKLEDELQVKLLNRSTRSIGLTEAGRIYYQGCRRMLHEVQDVHEQLYAFNNTPIGTLRIGCSSTMAQNVLAGLTAKMLKEYPGLSVNLVTGIPAPDLIADGLDVVIRVGALQDSSLFSRRLGAMPMVVCAAKSYLTQYGIPEKPADLSSHSWLEYSVRPDNEFELIAPEGISTRLIPQGRFVTNDPMTLVRWLTAGAGIAYVPLMWVINEINRGELEILLPRYQSDPRPVYALYTEKDKLPLKVQVVINSLTDYFVEVGKLFQEMHGRGKEK
The following text describes a protein:
Function:
3'-5' exonuclease that prefers single-stranded DNA and RNA. May play a role in the H(2)O(2)-induced DNA damage repair.
Subcellular Localization:
Cytoplasm.
Sequence:
MFDIGVNLTSSQFAKDRDDVVACAFDAGVNGLLITGTNLRESQQAQKLARQYSSCWSTAGVHPHDSSQWQAATEEAIIELAAQPEVVAIGECGLDFNRNFSTPEEQERAFVAQLRIAADLNMPVFMHCRDAHERFMTLLEPWLDKLPGAVLHCFTGTREEMQACVAHGIYIGITGWVCDERRGLELRELLPLIPAEKLLIETDAPYLLPRDLTPKPSSRRNEPAHLPHILQRIAHWRGEDAAWLAATTDANVKTLFGIAF
The following text describes a protein:
Function:
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MRNILPFLTRIPVKGDFEKARNELWAFPLVALVSSALPTLILYLGLPLSNLLAVLALYWTIGLLHLDGLADWADGIMAKGDRERKIEVMKDVNTGIAGLFAVVIVLLLQVYSLQLLPFYALFLAELNSKYAMLLALATKRPLGKGLGAYFMEGMNGRQLALGTLLYVLLGLSVVLFEPRALAGILGLLFGVHIIRISLKNFDGLNGDCLGATAEITRAGTLVVMALVWWYL
The following text describes a protein:
Function:
Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MSSFKKAQKAAQKSHRERSQPSSRARFGLLEKKKDYQLRARDYHKKQDALKLLRQKAQDRNPDEFYYKMISTRMIEGVHTRLKKDEPTTEEQVKMMDTQDLRYVNHKMTVESKKIEKLKSSLHMLEDTEEKPKNKHTFFVDTVREANEFDPAKHLNTHPALLHRTHNRPTLSMLSDPSMLKAIAGGSAEEGTSSGILAVGKEKKKRYHELSQRIEREKQLNIIAQKMEAKKHFKDKTRKRLVKEETQESAPVFKFHMQRKR
The following text describes a protein:
Function:
O-linked mannose beta-1,4-N-acetylglucosaminyltransferase that transfers UDP-N-acetyl-D-glucosamine to the 4-position of the mannose to generate N-acetyl-D-glucosamine-beta-1,4-O-D-mannosylprotein. Involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MHLSAVFNALLVSVLAAVLWKHVRLREHAATLEEELALSRQAPEPAPALRIDYPKALQILMEGGTHMVCTGRTHTDRICRFKWLCYSNEAEEFIFFHGNTSVMLPNLGSRRFQPALLDLSTVEDHNTQYFNFVELPAAALRFMPKPVFVPDVALIANRFNPDNLMHVFHDDLLPLFYTLRQFPGLAQEARLFFMEGWGEGAHFDLYKLLSPKQPLLRAQLKTLGRLLCFSHAFVGLSKITTWYQYGFVQPQGPKANILVSGNEIRQFARFMTEKLNVSHTGAPLGEEYILVFSRTQNRLILNEAELLLALAQEFQMKTVTVSLEDYAFADVVRLVSNASMLVSMHGAQLVTALFLPRGATVVELFPYAVNPDHYTPYKTLAMLPGMDLQYVAWRNMMPENTVTHPERPWDQGGITHLDQAEQARILQSREVPRHLCCRNPEWLFRIYQDTKVDIPSLIQSIRRVVKGRPGPRKQKWTVGLYPGKVREARCQAAVQGASEARLTVSWQIPWNLKYLKVREVKYEVWLQEQGENTYVPYMLALQNHTFTENIKPFTTYLVWVRCIFNKTLLGPFADVLVCNT
The following text describes a protein:
Function:
May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
Subcellular Localization:
Cell membrane; Lipid-anchor. Membrane, caveola.
Sequence:
MSYKIARASEYLAITGGGIKDIKLAKSSWVLPWQSCTVFDVSPVNYTFEVQAMSSEKLPFVIPAVFTIGPRVDDPHALLLYAMLMSQHDKHSNHVNELVQGVIEGETRVLVASMTMEEVFKGTKEFKKEVFEKVQLELNQFGLVIYNANVKQLVDVPGHEYFSYLGQKTQMEAANQAKIDVAEAKMKGEVGAKERTGLTIQNAAKIDAESKIISTQRKGEGTKEEIKVKSEVQVFQNEKEALVAKADAALAIQKAALTKSSRVAEVEAAKAVAMREAELQTQVEKMNALTRTEKLKAEFLSKATVEYETKVQEANWELYNKQKKAEAVLYEKQKQAEATKAAADAAFYAKQREAEGIVAMANAQGTYIKTLLGAVNNDYSAMRDFLMINNGVYQDIAKTNAIAIKDLQPKISVWNQGGADQGMSGGGMKDIAGLYKMLPPVLDTVYEQTGMQPPAWIGTLRGAEPSR
The following text describes a protein:
Function:
Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria; (Microbial infection) May serve as a receptor for adhesin A variant 3 (nadA) of N.meningitidis.
Subcellular Localization:
Cell membrane; Lipid-anchor. Cell membrane; Single-pass type II membrane protein. Membrane raft. Secreted. Note=A secreted form also exists. Localization to membrane rafts requires palmitoylation.
Domain:
The cytoplasmic region is required for subcellular sorting on the cell surface; The C-type lectin domain mediates the recognition and binding of oxLDL.
Sequence:
MTFDDLKIQTVKDQPDEKSNGKKAKGLQFLYSPWWCLAAATLGVLCLGLVVTIMVLGMQLSQVSDLLTQEQANLTHQKKKLEGQISARQQAEEASQESENELKEMIETLARKLNEKSKEQMELHHQNLNLQETLKRVANCSAPCPQDWIWHGENCYLFSSGSFNWEKSQEKCLSLDAKLLKINSTADLDFIQQAISYSSFPFWMGLSRRNPSYPWLWEDGSPLMPHLFRVRGAVSQTYPSGTCAYIQRGAVYAENCILAAFSICQKKANLRAQ
The following text describes a protein:
Function:
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
Sequence:
MTRRQRVAENLNSALHHLLGAHPGTYLIGEDVADPYGGAFKVTRGLSDRFPDRVLSSPLSEGGIAGVGAGLALAGNRSVVEMMFSDFAALAFDPLLNFAAKSVSMYGRRVPMSMVVRCPTGGNRGYGPTHSQSLQKHFLGIPSLHLREVSPFHDNRRVLTAMLDREEPGVLFEDKVLYTRAMYQAGVVDDLFRYEVLADPSETARVFAPDCGPPDWIVLAPGGLTERAVTALRTLLLEEEITCELLVPSQLYPFDSKALLPVLSRADRICVMEDSTADGTWGELLAQQLHEELWSRLARPVLPLTAEPSIVPTAAHLEHGVLLQPSTIHRAIVEATK
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MKSNTASFEKSSKSTQEEQQPSMKMKSLRIHIKKEVLEEIQSPSLQYDAVQSSSAHQEQSKNGRDEELESGIAEGYKIYTYCIKEEEPDETPSSPFDNATQSLTHQDVCSPSNVPQSFGNRMQIPSPPHAVSESQKSSQTDVKGSCDRAINSDSSNSIQSEKCPEENDSKRVECRNNIKDADSEDQNTSHTNVEGSCDRTINSDSSNSIQSEKCPEENDSKRAECRNNIKDADKVSSKLNGEATRSLGIHSGKKYHQCSECGKKWSSKSNLARHLRTHTGEKPYPCPECDKRFSDKSSIPQHMLIHSGEKPYQCSECSSRFNCKSNLRQHMNHHSTTNLHQCPKCNKKYDSKYTLAQHLITHTDERPFKCPECNKTFTAIKYLKRHQKLHAKDKAYECTYCNKKFHSACYLKFHIRTHTGEKPYQCPECSKRCATKSRLNVHMLTHTCTDEKPYQCPECSKKSATKSNLNKHMLTHTGEKPHSCSMCNKKYRSSSDLKIHLRTHSGEKPFLCSFCGERCTDIGSLANHTIRFHREWTQQCPQCSKKFVSKSHLRTHMRTHTGEKPYQCPECSKRSATKSSLNQHMLTHNGEKRYECSECKKTYANKGDLDTHKKVHTGVKHAQCSHCDQGFDSKYYLKKHVRTHTGEKPYRCSECNRDFTFQSNLKRHMMIHTGEMPYQCDECNKKFRQKETLISHMRTHTGEQPYSCSECGRRFASKGNLSKHNLVHTGEKPFECSECKKTYAYIGALNRHKKVHTRVKHTQCSHCDQMFDSRYYLQKHMLTHTGEKPYRCSECNRGFTFQSNLKRHMVIHTGEMPINVTSVIRNVDKKKL
The following text describes a protein:
Function:
E3 ubiquitin protein ligase that acts as a positive regulator of RPM1- and RPS2-dependent hypersensitive response (HR), in association with RIN2. Probably not required for RPM1 degradation during HR.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MGITYLHISVATTALSFVGLQVWTELSLDRLRADGIITKNISLGNSENTLELLLSSHTTIALLASFVLNIYILLVLSLKTLFFGDLYAIETRKLVERLANYIIYKGTFLPFVVPRTVFQGVLWTIWLTVLCTLKMFQALARDRLDRLNASPSSTPWTYFRVYSALFMVLSTDLCWIKLSLMIYNTVGSSVYLLLLFEPCGIAFETLQALLIHGFQLLDMWINHLAVKNSDCQRSKFYDSMTAGSLLEWKGLLNRNLGFFLDMATLVMALGHYLHIWWLHGMAFHLVDAVLFLNIRALLSSILKRIKGYIKLRVALGALHAALLDATSEELRDYDDECAICREPMAKAKRLHCNHLFHLGCLRSWLDQGLNEVYSCPTCRKPLFVGRTESEANPSRGEVSSDEHLARQFERQNNSVHALTTGMFPTETPNFTESDPWRNSEVDPSWLQTWSDQGVDVVGSSAGSRSVGLGQVQLMMRHLASVGEGSAQTTLDDASWGLWPMNPSQASTSSTYVPPGAGGRTGGLHLRTVSRAANNMASILAMAETVREVLPHVPDEIIFQDLQRTNSVSVTVNNLLQM
The following text describes a protein:
Function:
Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
Subcellular Localization:
Nucleus. Mitochondrion.
Sequence:
MKAEPKPPEPGLRMGKTSVEETPAAADPFLKKMAAAFTDGILRRGVDNRYLVLKVNTVQNEGSQEKHLIITAAQSLEDQELCILRDEWDDLSVEPGDIIHLEGEYKADAWIIDKDFGYLILYPDMLISGTSVANSIRCMRRAVLNENFRSCDSSSHQMLIGTVLHEIFQKAINDSFTQEKLQELALQTIQEIKHLKEMYYLNLKEDVFKQEIEDYLPSFSKWAEEFMHGPMSADLPMMQQTLLSDRNKNESPYRIQVTEALDIEENIWSPRFGLKGKIDVTVNVKIHRGSKATCRVMPLELKTGKESNSIEHRSQVVLYTLLSQERRADPEAGLLLYLRTATMYPVPANRLDRRELIKLRNQLAFYLSHSVTKSIAEKEQTQLTPLPPVINDSFACKYCSQTYNCALYSRAVEQPMDKSLAAGATLPKIEKMTQHLKYSHLQYFSLWYLMLTLESQSKDTRKSHRNIWLMSAAEREKTGDCIGNLMRTEDVQTICNGQYLHTFQHKHGTIPNTNLMTGDRVMLSGEERRLLALSSGYVKAITRTTVTCLLDRNLSKLPRVTLFRLDHEERIGGIETPLGNLSKLMENTPVSEKLRDLIIDFREPQFIQYLSSVLPHEAKDTVANILKGLNKPQRQAMKKVLLSKDYTLIVGMPGTGKTTTICALVRILYACGFSVLLTSYTHSAVDNILLKLMKFKVGFLRLGQTQKVHPNIQKFTEEEICREKSIKSLTSLEELYNSQPIVATTCMAINHPIFSRKRFDFCIVDEASQISQPVCLGPLFFSSKFVLVGDHLQLPPLVLNSEARGLGMSESLFKRLEQKQNAVVQLTVQYRMNSTIMSLSNKLVYEGKLECGSDRVANAIVSLPFLKNVMLDLQARTDHSQTSWLKEAFEPNNPVCFLNTEKIPAPEQAEKGGVSNIIEAKLIVFLASVFIKAGCNPLDIGIIAPYRQQLKIITHLLNHSSVNTVEVNTVDKYQGRDKSIILVSFVRSNKDGNLGELLKDWRRLNVAITRAKHKLVLLGCVPSLSQYPPLEKLLRHLHLEHKIFNLPLGAHESICQYNVR
The following text describes a protein:
Function:
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
Sequence:
MRVNGVDLSEIAELFGTPTYVIDLDRVKENYLRLDKAIKCPHVIAYAYKANHEPELVKLLAKLGSGATVPSAFGVILARISGVPPEKTVLVGPSPSRGDLIEAMDFGAIISIESHSQANALRSIGRANVMVRVNPGVGAGAYPGLVTGGKRSKFGLPPEEALSLFNSLKKDMRALGFHTHIGSQIFSTDPFRAALDVIKGLAERVGGVEIVDLGGGLGVPYSNESPFPLEEYAELVCERVREMGTKLFLETGRYIVADAGYLLSRVNYVKEVGGEKWLLIDAGMNDLIRPALYGARHEIICEGEGRERVLVAGPVCESSDFFGEYELPKLKEGDLIAFKNAGAYGFSMASRYNLRPLPAVVGIEGGRFRLLRPREDFCRAVFG
The following text describes a protein:
Function:
Through its association with the EHMT1-EHMT2/G9A and PRC2/EED-EZH2 histone methyltransferase complexes may function in gene silencing, regulating repressive post-translational methylation of histone tails at promoters of target genes.
Subcellular Localization:
Nucleus.
Sequence:
MPSEQKHLFFDEKQNTLKKDYDVKNEIVDTVRSVLKPKISESHFHYELKNVKIVLPRINIPNEVLLKHEVDKYRKLFQHKPQTARKSISIKTVNCIEECVLLHKSERVEEGIKMSAKILNFNCLKCRDSTRYSPNDLQKHFQMWHHGELPSYPCEMCSFSANDFQVFKQHRRTHRITLVKCDICNNENLYTLLDLTKHFSSTHCVNGNFQCEKCEFSTQDVGTFVQHIHRHNEVLYKCDKCHYICLTKGELQKHLHIHSGTFPFTCQYCSYGATRREHLIRHVITLHKEHLYAKEKLEKDKYEKRMAKTSTGLKLILKRYKIGASRKTFWKRKKINNGSDRSIEKNTQVLKKVNKTQAKSEDQSRLVQEHINEEKDERLYCENNDKPAESESEKPTLLSTGQCNRAEEGSNSTTGFLKTALQGPTVLMVKNNRITIPANYSAKFMGFKMVDGKQHIVIKLLPTSKQNLYLPGSQSGATRHSTANLQPQTLDTTAFLTGVTTELNDTIYMKASTPFSCSSPIRSGKVTSEKEVALLSQTSNMLPTMDDEKSVSSLPTTSELITASVNLTTKVETRDNVDLWGSHIAQCHPEVSGTAIKSPDKVTCTVKPNPYSSGDMHNYCINYVNSELPVESSNQGSLPFHNYSKVNNSNKRRRFSGTATCENPQKESSLSKTVVQQPISESVLSLVRKESSNPDSLLASISLLNTKDGTLKTQAEMEEQCVLEKGQNIDGQNLYTNENQNLESLTEKPKWDDISSDESPMMPRITSVFSLQSQQASEFLPPEVNQLLQEVLKAKPDVKQDSSNTPSKDLRLHCDQSFQKHEREDKIVECSKDLKGQGLFPVPSCSMGINGPTNDPNLKCGGKEKQMLSMSQDVRDSEKTPRISGFGTLLKTQSDAIITQQLVKDKLRATTQNLGSLYMQSPLLNSEPKKALFVQTPRGFFVPLHIANKPGLHASGKPLPLVNTQGVPASLLLNKKPGMILTFNNGKLEGVSAVKTESAQACGTTTKEPCRPPILKVEPSSNCLTPALCSSIGSCLSMKSSSENTLSLKGPYIIKTPASSSVKAVPTPNTVSEHQGTKLNISDSVKQQNKIFPKPPLYTLLPDGKQAVFLKCVMPNKTELLKPKLVQNSTYYKNIQPKKPEGTPQKILLKIFNPVLNVTAANNLSVSNSASSASSSQKDNVPSHPATGGEQKEPESSRDALPFLLDDMMPANEIVITSTATCPESSEEPVCITDHSEARVLRRKTNCTIERCVNKKKTLKKNFSRIKTHLRSKDSETAFVSRNRNCKRKCRDSYQEPPRKKALHRKCKEKAKPEDISESFGYSKPRLSKDSVRTLRLFPFSSKQLVKCPRRNQPVVVLNHPDADAPEVVNVMKTIAKFNGRVLKVSLSKRTINALLKPVCCNSSKTICDDFPKRHKTFKPVSSVKERFVLKLTLKKTSKNNYQIVKTTSENVLKAKFNCWFCGRVFDNQDTWAGHGQRHLMEATRDWNMLE
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.
Sequence:
MEDLLGEKHYDEWGHHNAEFDHRAFIGEEDDTFHEYSEEDASDRLITVFDEIDTNMDEYIDKNEMKARIKGNQLKRLEKESREKFKVLDVNEDSMLPWEEYKQVMFANDLAENNGKLSDSMQSMYTNDHRKFIDADQDNDGMLTLTEFAAFNFPHNFPHMQNALAMESLDTYDKNKDGKISWKEYISSMYNSEDNKEQPGWVRDEEKIYLLRHDKDGDELLDLSEIKSWIAPEENNDEEEEANHLIESADLDQDGKLTREELLSHQSLFAGHTKKSRKYEDPDFDFDYHADRYHDEL
The following text describes a protein:
Function:
Peptidyl-alpha-hydroxylglycine alpha-amidating lyase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Mediates the dismutation of the unstable peptidyl(2-hydroxyglycine) intermediate to glyoxylate and the corresponding desglycine peptide amide. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
Sequence:
MYTKQEKIFSHLRQMVPFLAGLLIFSVHFTCTVEARPQTVSSNGNNASNARFGAHEYAYVSSWPIVDRKLGSVSAVALDGDGNVVIFHRGSHVWQLSSFDTENRYQEATGGPIAQPTVLKFNRNTGELLQQWGENLFYMPHGLTVDHEQNYWLTDVALHQVFKFDLNHSTTEPVLTLGTRFEPGNDAYHYCKPTAVAVLKSGEFFVADGYCNGRIVKYSAEGIPLLSWGRNSFVLTRSFTLPSGQPVPASFFAIPHALALVPDRDLLCVADREQGRVQCFHTRNGTFHSQYSSPEIGSRLFSVKYISSDGGLLYTINGPQFVLNPVPVAGHIIELASGNVIGRFQPNNPKHAFSNPHELAVTDDGSEVYVAELNPQMVHKFRRISPARLTGSTTTTRESAKEDAAKNSPAKQAKPQQQHHPQGNTSKTSVTRSWLLHIAVAAAVRICVLISKRLIRWVVCRRPPQAEKGRAKDPCVSATVLSKVSPSVVGRKSSECRLLVHCGLSLRLRGVIVVLFGCLAAVIGTLREWKKSNFSR
The following text describes a protein:
Function:
Collagen-binding adhesin that mediates bacterial adherence to collagenous tissues such as cartilage. Participates in the infectious process by acting as a virulence factor in many different animal models of staphylococcal infections including arthritis, endocarditis and keratitis. Inhibits the activation of the classical complement pathway by interacting with host C1q and interfering with the association between host C1r with C1q.
Subcellular Localization:
Secreted, cell wall; Peptidoglycan-anchor.
Domain:
Composed of a N-terminal A-region and a number of B-repeats depending on the strain. At the C-terminal end are features required for surface targeting and covalently anchoring to the peptidoglycan. The collagen binding activity is located in the A-region.
Sequence:
MNKNVLKFMVFIMLLNIITPLFNKNEAFAARDISSTNVTDLTVSPSKIEDGGKTTVKMTFDDKNGKIQNGDMIKVAWPTSGTVKIEGYSKTVPLTVKGEQVGQAVITPDGATITFNDKVEKLSDVSGFAEFEVQGRNLTQTNTSDDKVATITSGNKSTNVTVHKSEAGTSSVFYYKTGDMLPEDTTHVRWFLNINNEKSYVSKDITIKDQIQGGQQLDLSTLNINVTGTHSNYYSGQSAITDFEKAFPGSKITVDNTKNTIDVTIPQGYGSYNSFSINYKTKITNEQQKEFVNNSQAWYQEHGKEEVNGKSFNHTVHNINANAGIEGTVKGELKVLKQDKDTKAPIANVKFKLSKKDGSVVKDNQKEIEIITDANGIANIKALPSGDYILKEIEAPRPYTFDKDKEYPFTMKDTDNQGYFTTIENAKAIEKTKDVSAQKVWEGTQKVKPTIYFKLYKQDDNQNTTPVDKAEIKKLEDGTTKVTWSNLPENDKNGKAIKYLVKEVNAQGEDTTPEGYTKKENGLVVTNTEKPIETTSISGEKVWDDKDNQDGKRPEKVSVNLLANGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVEELTKVKGYTTHVDNNDMGNLIVTNKYTPETTSISGEKVWDDKDNQDGKRPEKVSVNLLADGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVEELTKVKGYTTHVDNNDMGNLIVTNKYTPETTSISGEKVWDDKDNQDGKRPEKVSVNLLANGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVDELTKVNGYTTHVDNNDMGNLIVTNKYTPKKPNKPIYPEKPKDKTPPTKPDHSNKVKPTPPDKPSKVDKDDQPKDNKTKPENPLKELPKTGMKIITSWITWVFIGILGLYLILRKRFNS
The following text describes a protein:
Function:
Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3.
Sequence:
MTASKRVAKELEDLQKELPKYLRNLCSEEDNVLVWHALLLPERPPYNLKAFRLCISFPREYPFQPPTVKFTTRIYHPNVDRDGRVCLPIISKKNWKASTRTCQVLEALNMLVNQPEPGQPVRLELAEQLTQDPELFDQMAQEFTLQFGVDRPS
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MVTVPSASPKPKRAESIDAATTLLYVPLTFSLTLIPPPRPQDVGKLVVVLDLDETLVYSRDNTVYKRPGVVQLLRTLKGKCEVIVWTAGTREYALDVIRTIDSVCAVQYCVYRHPMWWTGDIGCTKDLRLLGRPMDRVLLVDNTPSVFRANPLNSLLVEDFIVPHPRAYNAQEKTLLVLADIFEHVFRRFTSPCIADVLASKRISRQAIRLERGEFVDLNVLTPI
The following text describes a protein:
Function:
Catalyzes the adenosylmethionine-dependent methylation of the exocyclic amino group (N(2)) of guanosine at position 10 of various tRNAs. Acts via a two-step process that leads to the formation of either N(2)-monomethyl (m(2)G) or N(2)-dimethylguanosine (m(2)(2)G).
Subcellular Localization:
Cytoplasm.
Sequence:
MKSCLLLDLESFEGLPHILSERLSFTRSFGKLLGLFHCSEFPGALNELEKIPISGRFKATCVRVEGSCEWIGRKDLEERIGGWVIDNNEGAKVDLENPEIEIIAVITSDHVVVYLKEGEVDRSLFKVKEVSARPYAHPASMRPTLARAMVNLARTRGGDLVLDPFLGVGGIALEILSVGARLIGVDINEKLVIQAKNNLMTYGFLEGYELRVGDALSLELGVRVDRIVTDPPYGRMSSSPYAPRELASKFISKVPDYLRRGGWISISLPKEFLDRRDFEDAGIDIVNFFDLREHRSLVRRIWVGKLP
The following text describes a protein:
Function:
Catalyzes the carboxylation of beta-amyrin at the C-28 position to form oleanolic acid. May be involved in saponin biosynthesis in fruit skin.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MEVFFLSLLLICVLSVSIRLYLLLYKHRSHFTGPNLPPGKIGWPMVGESLEFLSTGWKGHPEKFIFDRISKYSSEVFKTSLLGEPAAVFAGAAGNKFLFSNENKLVHAWWPSSVDKVFPSSTQTSSKEEAKKMRKLLPQFLKPEALQRYTGIMDHIAQRHFADSWDNRDEVIVFPLAKRFTFWLACRLFMSIEDPAHVAKFEKPFHVLASGLITIPIDLPGTPFHRAIKASNFIRKELRAIIKQRKIDLAESKASKTQDILSHMLLATDEDGCHMNEMSIADKILGLLIGGHDTASSAITFLVKYMAELPHIYEKVYKEQMEIANSKAPGELLNWDDVQKMRYSWNVACEVMRLAPPLQGAFREAITDFVFNGFSIPKGWKLYWSANSTHKSLECFPQPEKFDPTRFEGAGPAPYTFVPFGGGPRMCPGKEYARLEILIFMHNLVKRFKWDKLLPDEKIIVDPMPMPAKGLPVRLHPHKP
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MSDKLTQIQDELDALLNMMQRQIAHIVLQAPPSVPPGQHRVDTMPEIKGKAASENPQSNPPQPAEPPVPEKISPEQFNQDLKEFSRDIVVKQQQVELLIASLPGLNVSEEQQVARMKELEKELEGLEDERAQAVREKEVLLKKVEDKIMSVGRSR