UniProt ID
stringlengths 6
10
| Protein Sequence
stringlengths 5
15.6k
| Functional Description
stringlengths 6
12.4k
|
|---|---|---|
Q9P260 | MAAMAPGGSGSGGGVNPFLSDSDEDDDEVAATEERRAVLRLGAGSGLDPGSAGSLSPQDPVALGSSARPGLPGEASAAAVALGGTGETPARLSIDAIAAQLLRDQYLLTALELHTELLESGRELPRLRDYFSNPGNFERQSGTPPGMGAPGVPGAAGVGGAGGREPSTASGGGQLNRAGSISTLDSLDFARYSDDGNRETDEKVAVLEFELRKAKETIQALRANLTKAAEHEVPLQERKNYKSSPEIQEPIKPLEKRALNFLVNEFLLKNNYKLTSITFSDENDDQDFELWDDVGLNIPKPPDLLQLYRDFGNHQVTGKDLVDVASGVEEDELEALTPIISNLPPTLETPQPAENSMLVQKLEDKISLLNSEKWSLMEQIRRLKSEMDFLKNEHFAIPAVCDSVQPPLDQLPHKDSEDSGQHPDVNSSDKGKNTDIHLSISDEADSTIPKENSPNSFPRREREGMPPSSLSSKKTVHFDKPNRKLSPAFHQALLSFCRMSADSRLGYEVSRIADSEKSVMLMLGRCLPHIVPNVLLAKREELIPLILCTACLHPEPKERDQLLHILFNLIKRPDDEQRQMILTGCVAFARHVGPTRVEAELLPQCWEQINHKYPERRLLVAESCGALAPYLPKEIRSSLVLSMLQQMLMEDKADLVREAVIKSLGIIMGYIDDPDKYHQGFELLLSALGDPSERVVSATHQVFLPAYAAWTTELGNLQSHLILTLLNKIEKLLREGEHGLDEHKLHMYLSALQSLIPSLFALVLQNAPFSSKAKLHGEVPQIEVTRFPRPMSPLQDVSTIIGSREQLAVLLQLYDYQLEQEGTTGWESLLWVVNQLLPQLIEIVGKINVTSTACVHEFSRFFWRLCRTFGKIFTNTKVKPQFQEILRLSEENIDSSAGNGVLTKATVPIYATGVLTCYIQEEDRKLLVGFLEDVMTLLSLSHAPLDSLKASFVELGANPAYHELLLTVLWYGVVHTSALVRCTAARMFELTLRGMSEALVDKRVAPALVTLSSDPEFSVRIATIPAFGTIMETVIQRELLERVKMQLASFLEDPQYQDQHSLHTEIIKTFGRVGPNAEPRFRDEFVIPHLHKLALVNNLQIVDSKRLDIATHLFEAYSALSCCFISEDLMVNHFLPGLRCLRTDMEHLSPEHEVILSSMIKECEQKVENKTVQEPQGSMSIAASLVSEDTKTKFLNKMGQLTTSGAMLANVFQRKK | Regulates intracellular cholesterol distribution from recycling endosomes to the trans-Golgi network through interactions with RAB11 and OSBP (PubMed:29514919). Functions in membrane tethering and promotes OSBP-mediated cholesterol transfer between RAB11-bound recycling endosomes and OSBP-bound Golgi-like membranes (PubMed:29514919). Translocated to the trans-Golgi network area in an OSBP-dependent manner (PubMed:29514919). Colocalizes with RAB11A in recycling endosomes (By similarity). Found in a complex composed of RELCH, OSBP1 and RAB11A (By similarity). |
E4US45 | MQFVAVLAALGALVAPAAAYPHAPMNETLVDVQLTAVGNTMVKATITNKGDSVLNMLQFNTIMDENPTRKVMVFQDGVEVPFTGMMPRYLMSDLTEEFFTTLPPQASVEHTFDIAATHDLSAGGKYVISASGAVPTAEEHSTTITSTALYESNELHMEVDGVQAAAVEQAMNFTPEMQSIHARALEKRTKIVSGSCNQNTLRATMNALGNSARLAQAASRAASQNPRKFQEYFRTNDANAKQRVIARLNSVARESSSANAGVTTYYCSDTMGGCKPRVLAYTLPSRNLVVNCPIYYNLPPLTKQCHAQDQATTTLHEFTHNPAVASPHCQDYAYGYQQCISLPAAKAVQNADNYALFANGMLSNLFVFTLN | Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine. May be involved in virulence (By similarity). Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain. Binds 1 zinc ion per subunit. Belongs to the peptidase M35 family. |
Q96LY7 | MRHEELLTKTFQGPAVVCGTPTSHVYMFKNGSGDSGDSSEEESHRVVLRPRGKERHKSGVHQPPQAGAGDVVLLQRELAQEDSLNKLALQYGCKVADIKKVNNFIREQDLYALKSVKIPVRNHGILMETHKELKPLLSPSSETTVTVELPEADRAGAGTGAQAGQLMGFFKGIDQDIERAVQSEIFLHESYCMDTSHQPLLPAPPKTPMDGADCGIQWWNAVFIMLLIGIVLPVFYLVYFKIQASGETPNSLNTTVIPNGSMAMGTVPGQAPRLAVAVPAVTSADSQFSQTTQAGS | Truncated N-terminus. |
D6VPR0 | MASRVDETTVPSYYYYVDPETTYTYQQPNPLQDLISVYGLDDISRQVARTNLDGTKAVKLRKSYKNQIADLSGKFSTIPTRENGKGGQIAHILFQNNPDMMIQPPQQGQNMSEQQWREQLRNRDIALFQPPNFDWDLCSSVLSQFERSYPSEFANQNQGGAQAPFDIDDLAFDLDGTGKSQSGSNSGNNSKKRKNKSSGSSMATPTHSDSHEDMKRRRLE | 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. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. Component of the Mediator complex, which is composed of at least 21 subunits that form three structurally distinct submodules. The Mediator head module contains MED6, MED8, MED11, SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules interact directly with RNA polymerase II, whereas the elongated tail module interacts with gene-specific regulatory proteins. Present with 6116 molecules/cell in log phase SD medium. Belongs to the Mediator complex subunit 19 family. |
D6VRZ9 | MYGDLGNKLVLEAKRTKQLYARSNQDVNLPMYHEDIIRNILKEVSNLRKNTEYLKEQQQLGMLDDKVAKCQYFVTLLCMERNKRCLLAYQRLRTDILDSMAWNNNGLDLMSSITFSQQDTNNLSHQEQEYLKEYCDLITDLKSGDLVDIDLSGSLVPPSDVFIDVRVLKDAGEIQTEYGVFNLIKDSQFFVRQSDVERLIQQGYLQKI | Required for DNA replication. Functions as part of the GINS complex which plays an essential role in the initiation of DNA replication by binding to DNA replication origins and facilitating the assembly of the DNA replication machinery. Required for the chromatin binding of CDC45. Component of the GINS complex which is a heterotetramer of SLD5, PSF1, PSF2 and PSF3. Interacts with PSF2. Associates with autonomously replicating sequence (ARS) regions in S phase. This association requires SLD3 and DPB11. Present with 1431 molecules/cell in log phase SD medium. Belongs to the GINS1/PSF1 family. |
Q7TTW6 | MAERTLVGLALKVGPLGEHDRLLSLLSDAEGVTRLAVPGARRPKSSLAAAAPLTLLELQVGGRSGLARVRQLRVLHSHAGLGRQLETLSAAQAFCDLCLQIGREDPVEGLLATLQLHLERLDQRSDCLDELLASSVQGAIHLLTLGGYSLPLQSCCLSGAPLEPPIGTWEWRCSLLPMDGFAIDRQPGAAMTLNPSELALLQRLTRADLPRRRDGELMGPRPVWLRLLAVVEIWIRTHLQRGNPALAMLRECVTAKQVSQHGADAANS | Involved in DNA repair and RecF pathway recombination. Belongs to the RecO family. |
P30797 | MSAALGIVLRPEGQRLAVSLTPPDPLPVAALLLGKPPGQVAELLPRLFNLCGAAQGHAARLALGLPAEAAPARREILRDHLAKLCLIWPKLLGLAPQPLPEHWAEGGAALQHWLWGGAKPADLWPFLTSGQGVAPLLATLGHAFAPGEAVAVLPPLSDPMALTAQENSPAGRVADDPLMRQAEARFGRGPFWRALGRIVDLHAFALAPPAAATPRPGLALVAAARGTYALSARAEAGMVTALSRVTPTDHLLAPCGALALSLASLPAAKAGLAALVIDILDPCVAVSVQELAHA | Belongs to the HupK family. |
Q6NNH8 | MEKLLIICMLLISVLVATSQSQTDPETFLRCLVREGSNPQVFISDVTYIPSNSSFTTVLRRRIPNLRFDKPTTPKPIAIITPTTWSHISPVLACARLFPVQVRIRSGGHDFEGLSYTSTAPFFLIDLLNFKSVDVNLTEGTAWVDTGATLGELYYKIAEKSNVLGFPAGLCTTLGVGGHISGGGYGTMMRKYGLSVDNVVGSRIIDSNGNTYFDRMSMGEELFWAVRGGGAASFGIVMGYKIRLVPVPEKVTVFSVGKTVGEGAVDLIMKWQNFSHSTDRNLFVKLTLTLVNGAKPGEKKVLATFIGMNLGGFDKTLNVMNRDFPELKLKKTDCTEMRWIDSVLFWAGYPVGTPTSVLLNPTVTKKLFMKRKSDYVKRPVSRTGLGLILKKLVELEKVEMNWNPYGGRMGEIPSSRTPFPHRGGNLFNIEYIIDWSEAGDNVEKKYLALANEFYRFMTPYVSSNPREAFLNYRDIDIGSSGNSTYEEGKIYGAKYFKDNFERLVDIKTKFDEINFWRNEQSIPVRK | Binds 1 FAD per subunit in a bicovalent manner. The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage. Belongs to the oxygen-dependent FAD-linked oxidoreductase family. Truncated N-terminus. |
Q54PJ0 | MNQSQNFHNIDLGHYGAQGSNQSFNNNNNGNNGMMMNQQQMQQHVVPHLHHLQQQQQQPQQQQLRNVPDYSNSPNGTTNGSTMSPNCINTNNNNNNNNNNNNNSNNNNNNNNNASNNLTSNKSSSTNTPQIGQLQASPANLTNSPSAISSPITISNNSSLNSPSTTSSPNLLLNGTSNKRIMISQQTCLVEEKFSKNGVQKNVHVVVKNNPFLLTLSLLDSSLNFHQLTPEVQLVYDSESLKEVDSATVKPLEYKTRANEEGDQLTIELRIKVLSSQLEDMLFRAKVKIVDPRTRKETHGLSVITHPIRVVSKPDQVKKKAKKRKRAPTDSLMDTLNRIEHQQKEQQRLLKKLCYHDKENNIIQLIQQQQQQQQLLNNVTNNINNNNNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTTSTTTTTTTTTSSCNNNNNNNNENNEHIVKIENTECNNNNNNIINNTENDENINKPILNSKDEFQSAFKEFIGAFKQLQCLDPDGADGAFKINTCANDAQTMCEILEMVKVELKKDENFKDKCGGSSGGACGENNPDNPCSCKVCPYKQKVDHINQSYETYFNMFNPSNSNSVVPQQSQQLQQQQIQQQQQSQQQVQQQQQQQMQQQPQQQQQQPQQQQQNQQQGQQPQQQQQQGQLDYTTYIDPQLQMQQQLQMQQAAQQQYMQQTMDQQQQQQYYMQQYHLQQQQQQQQAQRYLMQQQYMQQQAQQQQQQHQQVAIQQQQQQNQQQNQQQNQQQQNQSPQNQQSLDFQNANNFIDFNSGLGFMNFPNINFGDMGFSAV | Essential for normal culmination. May function as a transcriptional regulator. Expressed in the prestalk cells that constitute the slug tip (pstA cells) and in prespore cells (at protein level). Not expressed in the band of prestalk cells that lies behind the slug tip (pstO cells). Highly expressed in pstO derived papilla cells during culmination. Accumulates during aggregation and remains constant throughout culmination. Induced by acaA in the slug tip. Induced by dstA in prestalk cells, but not in prespore cells. Mutants fail to culminate. Development is normal until migratory slugs are formed, but slugs lacking cudA fail to culminate in the dark or in low level unidirectional light. In overhead light slugs lacking cudA eventually form defective fruiting bodies that lack both mature stalk cells and mature spore cells. |
Q8D3Z2 | MATPHINAQPGDFAETVLMPGDPLRAKYIAETFLEDVKQVCDVRNMFGFTGTYKGKKVSVMGHGMGIPSACIYVHELIAEYGVKNVIRVGSCGAVRDDVNLMDVVIGMGASTDSKVNRIRFNDHDFAALADYGLLEEAVKQARAQNVPVKVGNVFSADLFYTPEADIFEKMEKLGILGVDMEAAGIYGVAADLKAKALTILTVSDHIIRGEKLSSEDRQKSFNDMMKVALETAINL | Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + a purine nucleobase Homohexamer; trimer of homodimers. Belongs to the PNP/UDP phosphorylase family. |
P30894 | HPVHNQGEFSVCDSVSVWVANKTTATDMRGNVVTVMVDVNLNNNVYKQYFFETKCKNPNPVPSGCRGIDAKHWNSYCTTTDTFVRALTMERNQASWRFIRINTACVCVISRKNDNFG | Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. It stimulates division and differentiation of sympathetic and embryonic sensory neurons as well as basal forebrain cholinergic neurons in the brain. Its relevance in the snake venom is not clear. However, it has been shown to inhibit metalloproteinase-dependent proteolysis of platelet glycoprotein Ib alpha, suggesting a metalloproteinase inhibition to prevent metalloprotease autodigestion and/or protection against prey proteases (By similarity). Binds a lipid between the two protein chains in the homodimer. The lipid-bound form promotes histamine relase from mouse mast cells, contrary to the lipid-free form (By similarity). Homodimer; non-covalently linked. Expressed by the venom gland. Belongs to the NGF-beta family. |
Q818U0 | MINFNFFMNDVVRQAREEIVSAGYTELTTPEAVEEAFKRNGTTLVMVNSVCGCAGGIARPAAAHSVHYDKRPNHLVTVFAGQDKEATARAREYFEGYPPSSPSFALLKDGKIVTMVERHEIEGHEPMQVIAKLQSYFEENCEEL | Belongs to the UPF0403 family. |
A1TUE2 | MSALDVIIMAAGKGTRMKSRIPKVLQRLAGRPLLGHVLDQARGLQARRAVVVTGHGAAEVEPFIARAADGLDVRCVRQEPQLGTGHAVQQAVPALQGDGTVIVLSGDVPLTRTDTLRALVAAGGGGQLALLTVTLPDPAGYGRIVRGSDGAVRGIVEHKDATEAQRAIDEVYSGIMAVPAGLLAGWLARLTNDNAQGEYYLTDIVAMAVADGVPVVAHRIADALQVAGVNSPLQLAELERAHQLAQARALMEQGVRLADPARFDLRDDARTGVRGELACGQDVEIDVNCIFSGRVELGEGVRIGAHCCIANARIAAGAVVHPYTHIDGEQPAGVQVGEGALVGPFARLRPGAQLGREVHIGNFVEVKNSSLAEGAKANHLAYLGDATVGERVNYGAGSITANYDGANKHRTVIEADVHVGSNCVLVAPVTIGAGGTVGGGSTITKSTPAGALSVARGKQVTKENWQRPAKLPKA | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine Binds 1 Mg(2+) ion per subunit. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2. Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. Homotrimer. In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family. In the C-terminal section; belongs to the transferase hexapeptide repeat family. |
A9N6Y0 | MNSLFASTARGLEELLKTELEKLGAVGCQVVQGGVHFQGDTRLIYQSLMWSRLASRIILPMGECKVYSDLDLYLGVQAINWTEIFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRKNLPRPNVDRESPDLRINVWLNKETASIALDLSGDGLHLRGYRDRTGLAPIKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMWATDRAPGLHRGHWGFSGWAQHDETIWQEVKAEAQTRARKGLAEYSSHFYGSDSDARVIERARSNARRAGIGELITFEVKDVAQLSNPLPKGPYGTVISNPPYGERLDSEPALIALHSLLGRTMKNQFGGWNLSLFSASPDLLGSLQLRADKQFKAKNGPLDCVQKNYHIAETTADSKPATVAEDYANRLRKNLKKLEKWARQEGIECYRLYDADLPEYNVAVDRYGDRAVIQEYAPPKTVDAQKARQRLFDIIAATLSVLGIPPNKLVLKTRERQKGKNQYQKMSEKGEFLEVSEYNARLWVNLTDYLDTGLFLDHRIARRMLGEMSKGKDFLNLFSYTGSASVHAGLGGARSTTTVDMSRTYLEWAERNLRLNGLSGRAHRLIQADCLGWLREANEQFDLIFIDPPTFSNSKRMEESFDVQRDHVALMKDLKRLLRKGGTIMFSNNKRGFRMDLEGLAELGLTAQEITQKTLSPDFARNRQIHNCWLIRAA | Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. guanosine(2445) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(2445) in 23S rRNA + S-adenosyl-L-homocysteine guanosine(2069) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(2069) in 23S rRNA + S-adenosyl-L-homocysteine Belongs to the methyltransferase superfamily. RlmKL family. |
B5XQD2 | MALTKAEMSEYLFDKLGLSKRDAKELVELFFEEIRRALENGEQVKLSGFGNFDLRDKNQRPGRNPKTGEDIPITARRVVTFRPGQKLKSRVENASPKDK | This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. Heterodimer of an alpha and a beta chain. Belongs to the bacterial histone-like protein family. |
Q2J0F2 | MTDLPPHALQPAEPVSVEQHMALSSLFTTLEDLTAWSRKHSLWPFNFGLSCCYVEQVTALTPVYDQARFGAEVIRASPRQADLLVVSGTVFHKMAAPLLRLYEQMRAPRWVIAMGACACSGGMYDIYSVVQGVDRFIPVDVYIPGCPPRPEAMLDALIMLQQQVGSERRPLGVTVGNSAGLGFDAPRRRDERHDQRMAQTLLDPPETL | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+) Binds 1 [4Fe-4S] cluster. NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex. Belongs to the complex I 20 kDa subunit family. |
P94948 | MGTPEGIDVITVVISEAPYGQERAYTALRFALTALVEGEEVKIFLIEDGVFLGKKGQNPDEVPNYLELLEQCIEQGAEVKACGPCSKARGLSEEDFIEGVELATMHDLVNWVKESDNVIFF | To M.jannaschii MJ0989. |
B8E520 | MKTAHEIRPGNVIMLDGSPWVVQKTETTRSGRNAAIVKLKLKNLLLNSGTETTFKGEDKLEDIILDRLDCTYSYFADPMFVFMDAEYNQYDVEAENLGDAAAYIVDGMEETCQVTFYDGKAISVEMPTTIVREVIYTEPSARGDTSGKVMKPATITGGGTVTVADFVKVGDKIEIDTRTGEFKKRV | Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. Protein biosynthesis; polypeptide chain elongation. Belongs to the elongation factor P family. |
Q04HN0 | MDLSKLTTEARNKRTMNLDRMTIHEFATIMNQEDQSVPLSVANSLATIENAIDSITKHFKQGGRLFYIGAGTSGRLGVLDAVECVPTFGIEAEMVRGLIAGGPSAMTLAVEGAEDDDKLASSDLKKRALTAADVVVGIAASGRTPYVIGGLDYADSLGAATISLACNQNSEISKHAQIAIEVPVGPEILTGSTRLKAGTAQKLVLNMLSTGAMVGIGKVYKNLMVDVRPTNEKLLIRSKRIICQATNCDEATAAEVFEKADRNVKLAIVMILTNLPKKEANEQLRKADGFISKTIPE | Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate Amino-sugar metabolism; N-acetylmuramate degradation. Homodimer. A lyase-type mechanism (elimination/hydration) is suggested for the cleavage of the lactyl ether bond of MurNAc 6-phosphate, with the formation of an alpha,beta-unsaturated aldehyde intermediate with (E)-stereochemistry, followed by the syn addition of water to give product. Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily. |
P43669 | MNTFFRLTALAGLLALAGQSFAVEDITRADQIPVLKEETQHATVSERVTSRFTRSHYRQFDLDEAFSAKIFDRYLNLLDYSHNVLLASDVEQFAKKKTVLGDELRTGKLDVFYDLYNLAQKRRFERYQYALKVLERPMDFTGNDTFNLDRSKAPWPKDEAELNALWDGKVKFDELSLKLTGKSDKEIRETLTRRYKFAIRRLAQTNSEDVFSLAMTAFAREIDPHTNYLSPRNTEQFNTEMSLSLEGIGAVLQMDDDYTVINSLVAGGPAAKSKSISVGDRIVGVGQAGKPMVDVIGWRLDDVVALIKGPKGSKVRLEILPAGKGTKTRIITLTRERIRLEDRAVKMSVKTVGKEKVGVLDIPGFYVGLTDDVKVQLQKLEKQNVNSIVIDLRSNGGGALTEAVSLSGLFIPSGPIVQVRDNNGKVREDSDTDGVVYYKGPLVVLVDRFSASASEIFAAAMQDYGRALIVGEPTFGKGTVQQYRSLNRIYDQMLRPEWPALGSVQYTIQKFYRVNGGSTQRKGVTPDIIMPTGNEETETGEKFEDNALPWDSIDAAKYVKSDDLAPFGPELLKEHNARIAKDPEFQYIMKDIARFNAMKDKRNIVSLNYAQREKENNEEDALRLARINDRFKREGKPLLKKLDDLPKDYQEPDPYLDETVKIALDLAHLEKEKPAEQAAANK | Involved in the cleavage of a C-terminal peptide of 11 residues from the precursor form of penicillin-binding protein 3 (PBP3). May be involved in protection of the bacterium from thermal and osmotic stresses (By similarity). The enzyme shows specific recognition of a C-terminal tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus. A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala. Belongs to the peptidase S41A family. |
Q01679 | MHTFLRSTALVVAGLSARALASIGPVTDFHIVNAAVSPDGFSRQAVLAEGVFPGPLIAGNKGDNFQINVIDELTNATMLKTTTIHWHGFFQHGTNWADGPAFINQCPIASGDSFLYNFQVPDQAGTFWYHSHLSTQYCDGLRGPFVVYDPADPYLDQYDVDDDSTVITLADWYHTAARLGSPFPAADTTLINGLGRCGEAGCPVSDLAVISVTKGKRYRFRLVSISCDSFFTFSIDGHSLNVIEVDATNHQPLTVDELTIYAGQRYSFILTADQDVDNYWIRANPGIGITTGFAGGINSAILRYDGADVVEPTTTQATSPVVLSESNLAPLTNAAAPGLPEVGGVDLALNFNLTFDGPSLKFQINGVTFVPPTVPVLLQILSGAQSAADLLPSGSVYALPSNATIELSLPAGALGGPHPFHLHGHTFSVVRPAGSTTYNYVNPVQRDVVSIGNTGDNVTIRFDTNNPGPWFLHCHIDWHLEAGFAVVFAEDIPDVASINPVPQDWSNLCPIYNALDASDH | Lignin degradation and detoxification of lignin-derived products. 4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O Binds 4 Cu cations per monomer. Belongs to the multicopper oxidase family. |
C3MJ88 | MVTIVLNKYKLLDKIHIGQQKLEDLLFNLKSEVKPIDENNIEIEINADRLDLLSSDGIARAIKGLLEKELGEAKYNVTDTEYTLIVDNVRTRPYALAAIVYNAKIDLEELIQFQEKLHGTIGRKRKKVAIGIHDLRKVDSKTIEYKEVPLSYKFVPLYGNKELTISEILEKTEQGKLYGNISIANGVSPAIVQDDGEVLSIPPIINSNKTRLDENTKDFFIDVTGTSFEAVAQTLDIIVSNLAEAGGTIGRVKVLKSANSSQLSSPLFLHKIQNVREEYVKKILGIKTSKEEICKHVMRMRMNCDIENGVIRVTVPQYRVDILNEIDVVEDIAMSIGYNNLEPSKYISTNYGSYDYMTLLERKIRELGIGAGYVEISNFVLIKDEKLFSNKYVKILNPVTEEYNAVRNSLIPGLLDFLSKNQHAKFPIRVFETGDVVVYDSSTDTGFRNDKRAAYAIMDNKVSYEDIQAPIHYILKSLGLEVNYKEENNNIFIEGRSASIFYENEKMGVIGEVNPDVLIRFGIEYPAVIAELYISEIAKRLTNQR | ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe) Tetramer of two alpha and two beta subunits. Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 2 subfamily. |
A4FWV5 | MADVLTELPGVGPSTAEKLIEAGYLDFMKIATSTIGELTDIEGISEKAAAKMIMAARDLCDLGFKSGVELLKQRQSVWRLSTGSKELDTVLAGGLESQSVTEFAGMYGSGKTQIMHQTCVNLQMAEKIFADLEGVVEEEMENPKAVYIDTEGTFRPERVVQMAEGAGIDGQTVLDNTFVARAYNSDMQMLFAEKIEDLIKGGNNIKLVIIDSLTSTFRNEFTGRGKLAERQQKLGRHMATLNKLADLYNCIVLVTNQVAAKPDAFFGVAEQAIGGHVVGHAATFRFFLRKSKGDKRVAKLYDSPHLPDSEAVFRITEKGIQD | Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules. Belongs to the eukaryotic RecA-like protein family. |
D1Q180 | MFDIGFSELLLVLVIGLVVLGPERLPVAVRTVSGWIRTLRSLAATVQNELAQELKLQELQDSLKKVEQAGLQNLTPELKASMDELKEAAEALKRSYHVDAGSEAPHTIHNPLVTEPEAIHDGVTPAEPATQVSALAQAPNILEAGTASVVDSVVEAAPVTTVKSVVQGEVLVKSTPVQEVGLADVMDKPVTKQQIDTIDSHGTDLSSAGPSRIHQPGGDQ | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation. The Tat system comprises two distinct complexes: a TatABC complex, containing multiple copies of TatA, TatB and TatC subunits, and a separate TatA complex, containing only TatA subunits. Substrates initially bind to the TatABC complex, which probably triggers association of the separate TatA complex to form the active translocon. Belongs to the TatB family. |
Q49L05 | MDIVSLAWAALMVVFTFSLSLVVWGRSGL | Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, PetD), cytochrome f and the Rieske protein, while the 4 small subunits are PetG, PetL, PetM and PetN. The complex functions as a dimer. Belongs to the PetN family. |
B1KRQ5 | MNPIVKSFEYGQHTVTLETGVIARQANAAVLASMGDTTVLVTVVGKKAEDVGRDFFPLTVNYQEKTYAAGKIPGGFFKREGRPSENETLIARLIDRPIRPLFPNGFKNEVQVIITVVSVDPEINPDVISMIGTSAALSISDLPFNGPLGVARVGYTNGEYVLNPNVSQLAESDLDLVVAGTQGAVLMVESEAASLPEEVMLGGVVYGHDQQQVVINAINELTAEAGKTKWDWTAPAEDTDLVEKIKGLAEAELTNAYQIADKHERRDAVIALKNAAVAKLVEENADVDLREVDKLLGSLEKKVVRSRIISGSPRIDGREPDMVRALNVMAGVLPRTHGSSLFTRGETQALVTCTLGTERDAQKVDSIMGEYTNRFMLHYNFPPYSVGETGMVGSPKRREIGHGKLAWRGINAVMPTAEEFPYSVRVVSEITESNGSSSMASVCGTSLALMDAGVPIKTSVAGIAMGLVKEGDDFVVLSDILGDEDHLGDMDFKVAGTRDGITALQMDIKIEGITKEIMQIALQQAYGARVHILNVMDQAISGHREDISDHAPRITTLKINPEKIRDVIGKGGATIRALTEETGTTIELEDDGTVKIASANGEATKEAIRRIEEITAEVEVGTVYNGKVVRIVDFGAFVTILPGKDGLVHISQIAEERVANVSDYLQVGQEVKVKVMEVDRQGRVRLSMKEAQPKAEAAPAAE | Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate + RNA(n) Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Belongs to the polyribonucleotide nucleotidyltransferase family. |
Q59LW4 | MDLKLPPTNPTNPQQAKTFMKSIEEDEKNKAEDLDIIKKEDIDEPKQEDTTDGNGGGGIGIVPTLQNIVATVNLDCRLDLKTIALHARNAEYNPKRFAAVIMRIRDPKTTALIFASGKMVVTGAKSEDDSKLASRKYARIIQKLGFNAKFCDFKIQNIVGSTDVKFAIRLEGLAFAHGTFSSYEPELFPGLIYRMVKPKIVLLIFVSGKIVLTGAKKREEIYDAFESIYPVLNEFRKN | General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. Belongs to the TFIID complex together with the TBP-associated factors (TAFs). Binds DNA as monomer. Belongs to the TBP family. |
Q8TVL8 | MKTGTWRVKTGFARMLKGGVVMDVTNVEQAQIAEDAGAVAVMVLEKVPADIRAAGGVARMCDPAKIEEIMDHVTIPVMAKCRIGHVAEAQVLEAIGVDMIDESEVLTPADEEHHINKWEFEVPFVCGARNLGEALRRIAEGAAMIRTKGEAGTGNVAEAVRHMRIIRREISELTRLDKEELYGKAKEYGVPFDLVAEVASLGRLPVVNFAAGGIATPADAALMMQLGADGIFVGSGIFKSDRPQEMAEAIVEATAYYDDPEVVAEVSKNLGDEVAMRGLEISEIPEEERMQLRGE | Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis. In the presence of PdxT, forms a dodecamer of heterodimers. Belongs to the PdxS/SNZ family. |
Q2TWM9 | MRVTTLSTALFALASTAVSAPTAGSSSPGLEVKLTQIDNTRVKAVVKNTGSEEVSFVHLNFFKDAGPVKKVSIYRGQDEVQFEGIKRRLRSSGITKEAVTSLGAGETLEDEFDIASTSDLASGGPVSIRSHGFVPIVVDGKITGYIPYKSNDLTVNVDGGKAAKVTKALSQLTRRTEVTDCKGDAESSLTTALSNAAKLANQAAEAAESGDESKFEEYFKTTDQQTRTTVAERLRAVAKEAGSTSGGSTTYHCNDPYGYCEPNVLAYTLPSKNEIANCDIYYSELPPLAQKCHAQDQATTTLHEFTHAPGVYQPGTEDLGYGYDAATQLSAQDALNNADSYALYANAIELKC | Metalloprotease that shows high activities on basic nuclear substrates such as histone and protamine. Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain. Binds 1 zinc ion per subunit. Thermostable. Belongs to the peptidase M35 family. |
P86350 | MKISQVFIFVFLLMISVAWANEAYEEESNYLSERFDADVEEITPEFRGIRCPKSWKCKAFKQRVLKRLLAMLRQHAF | Disrupts cell membranes through the formation of pores (Probable). Has antibacterial activity against Gram-positive bacteria S.aureus (MIC=10 uM) and B.subtilis (MIC=0.5 uM) as well as Gram-negative bacteria P.fluorescens (MIC=1 uM) and E.coli (MIC=0.5 uM). Has hemolytic activity against human erythrocytes (EC(50)=7 uM). Probably forms a transmembrane alpha-helix in the target cell membrane. Expressed by the venom gland. |
B5FG51 | MSENSNHHCIIVGIAGASASGKSLIASTIYNELRAKVGDHQIGVITEDSYYKDQSHLTMEERVKTNYDHPNALDHELLCEHLEQLMRGEAVNIPTYSYTEHTRTSEVDVMTPKKVIILEGILLLTDPRLRNLMHASVFMDTPLDICLLRRARRDVEERGRTMESVFEQYQKTVRPMFMQFIDPSKQHADIIVPRGGKNRIAIDVLKAHISRLLKA | ATP + uridine = ADP + H(+) + UMP ATP + cytidine = ADP + CMP + H(+) Pyrimidine metabolism; CTP biosynthesis via salvage pathway; CTP from cytidine: step 1/3. Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1. Belongs to the uridine kinase family. |
B4SXX2 | MANFPASLLILNGKSADNQPLREAITLLRDEGIQIHVRVTWEKGDAQRYVDEARRLGVETVIAGGGDGTINEVSTALILIRDGVAPALGLLPLGTANDFATSAGIPEALDKALKLAIAGNAMEIDMARVNDKTCFINMATGGFGTRITTETPEKLKAALGGVSYLIHGLMRMDTLTPDRCEIRGENFHWQGDALVIGIGNGRQAGGGQQLCPTALINDGLLQLRIFTGEELLPALFSTLTQSDDNPNIIDGASAWFDIHAPHEITFNLDGEPLSGQEFHIEVLPGALRCRLPPDCPLLR | Probably phosphorylates lipids; the in vivo substrate is unknown. Binds 1 Mg(2+) ion per subunit. Ca(2+) may be able to substitute. Belongs to the diacylglycerol/lipid kinase family. YegS lipid kinase subfamily. |
A4G0Z4 | MRAFLIGRWQPFHKGHLEIIKKISKEVDEIIIGIGSCQKSHTLTDPFTAGERMMMITKTLENYDINYYAIPINDIDYNAVWVSSVESLTPPFTTVYTGNSLVRELFSEKNYAVKKPELYNRTDYSGTKIRKKMLDGSTWEHLVPEEVVKVIEEIDGINRIRRLNEKDYDEE | ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+) Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1. Belongs to the archaeal NMN adenylyltransferase family. |
P35853 | MPHEPKGLNEECGVFGVWGNPNAASITHLGLHTLQHRGQEGAGIVGLTKDGMRRHYGLGLLSEVFTNTDQLTPLIGRAALGHVRYSTAGGRVLENIQPLLFRFSDEAIALAHNGNLTNAISLRRQLEDQGAIFQSTSDTEVLMHLIRRQVGQPWLTQLKTALNEVHGGFAFVLLTEHGLYAAVDPHGFRPMVVG | Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2. In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family. |
H2BXL5 | MHIIFQYPIVDLRDIVSGGNGRLNDPKWPDPQERRQSFVSGFGKVKSRNLGGSDNFTGESYYCDSHSAIKFKELQHQGFSEGITTPASIFNSYRRYYNDGRFVGKVEIGLIDNLEKIIRNYPGSEGIQISSILKHYSNLEATVEDEQVKLYKAGPRLSKKYQRESTLREKHFQINPDYVQTGELTIVLTYSSHERLIVPRRSFSLEKIELPNDAGSIELFGYKLKQDGYPTKVWIIKIPANFRSKSGKHKTILRDLRMNLLRIHLEKETIKILLNAIKYKQIELEKESAEAKQVNAYFEQTSKKLFRKSRYDIKQENLLDFALQSEKSMDKGSFNSLKENITYFQDEFMLDNLGKLVGSMAVKPMLFVCSNPRDSNFIDFDKEYKDLKYNLQRAIDRDHYDIEIELSVTKDEFKDILDRYKPQFLHLSMHATVKDGLHFEDKNKAILPMSVKEFKQIIERYTKKHELKLVLISACNSKNHAKAIKEYCDFAIGTKAVFPVPAALIYSNNFYTTLFNGYQKDLEYCHSGAINAIEFNNPKFDDLDYKNKKIRVHEIPVLIKNSKYV | Probably a dedicated protease for substrate gasdermin bGSDM; cleaves the bGSDM precursor, releasing the pore-forming moiety, which integrates into the membrane and triggers cell death. Involved in defense against bacteriophages (Probable). Expression of bGSDM and this neighboring protease is not toxic in E.coli (PubMed:35025633). |
E0T5H9 | MNDFDPTTLSSPAAIGHNLRRRPLVRKKLSEMVEEELEQMIRRREFGEGEQLPSERELMAFFNVGRPSVREALAALKRKGLVQINNGERARISRPSADTIIGELSGMAKDFLSHPGGIAHFEQLRLFFESSLVRYAAEHATDAQIALLEQTLALNSQSLDDNALFIRSDVDFHRVLAGIPGNPIFMAIHVALLDWLLAARPAVADADLYEHNNTSYQQHIEIFNAIRRHDPDQADRALQTHLNSVFASWHTLSAQSSSDE | Transcriptional repressor that controls expression of the genes required for the catabolism of sialic acids. Belongs to the NanR family. |
Q87R12 | MAQFIDRRLNGKNKSAVNRQRFLKRHKEQIKESVADAVNRRSITNTETGEDVSIPHKDINEPIFHQGKGGVRERVHPGNDQFITGDKIERPKGGGQGSGSGEGNASPDGEGQDEFVFQISKDEYLDILFEDLELPNLEKNQIAKITEWKTHRAGFQTAGIPSNISVIRSLQQSLARRTAMTAGKKRLLKELEDELTRIKNIEPAQQLEENRLKKEIEELRKKIENVPFIDTFDLRFKNYEKRPVPSSQAVMFCLMDVSGSMDQATKDIAKRFYVLLYLFLTRTYENVDVVFIRHHTQAKEVDEHEFFYSQETGGTIVSSALKLMDEIVKERYPVGQWNIYAAQASDGDNWADDSPRCRDLLVNKLLPNCQYYSYIEITRRSHQTLWHEYEKLTDEFPNFAMKNIRSVEDIFPVFRELFQKETA | Belongs to the UPF0229 family. |
P0DKR7 | MAHPCATDPELWFGYPDDDGSDGAAKARAYERSATQARIQCLRRCPLLQQRRCAQHAVEHRVEYGVWAGIKLPGGQYRKREQLAAAHDVLRRIAGGEINSRQLPDNAALLARNEGLEVTPVPGVVVHLPIAQVGPQPAA | Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA (By similarity). Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit. Essentially constitutive during exponential and early stationary phases, decreases in late stationary phase. 3-fold induced by starvation, 3-fold by cumene hydroperoxide and 5-fold by diamide (oxidzing agents), 15-fold induced by SDS, 200-fold by heat shock. Repressed by SDS and diamide. Not induced by hypoxia, NO, cAMP or in mouse infection, slightly repressed in macrophage infection. The Fe-S cluster can be nitrosylated by nitric oxide (NO). Upon Fe-S cluster removal intramolecular disulfide bonds are formed. Belongs to the WhiB family. |
Q5HVQ1 | MTKKEMLYEGKGKKLFKTDDENLLISEFKDDLTAFNAEKRGNESGKGALNCRISTEIFHLLEKNGIKTHLVETISDTEQVVKKCKIVPIEVIVRNVATGSLTKRLGIKDGTVLPFALVEFCLKDDALGDPFINDEHCLILNLVQNEAQISEIKNMARKINSILTPFFDNKNLRLIDFKIELGLTKDNELVLADEISPDSCRFWDKFSNEKLDKDRFRQDLGNVKMAYEEVLKRILN | 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2. Belongs to the SAICAR synthetase family. |
M1WG92 | MASTTGTEATPSRISLSQDHLGILHDVKVNTASIEIANSLLQKNHEEWHMFFRDRAGHNHISHSILTCLALGGSPEDIQRAYDDGLEIQRPMPPLDDALVARLGDDNVMYESLGSISQYRSFLAYFQHHMEEHGWKATVTKYLFSHTKLSEKMLARMYEGAYHPVIHLGLGFEFQQPAIVAEALAQAAAHDDSNLYTYFIACEEESEIAYPLQQAKTLLQIMADASSSKTIRNAPHWEDYGNKMRDGVLGRACRETANVASKFVIRKTPESLRRRTAEMIDTCAYVAASSQRSGRKRKIDFFYMHMVTSSLFFSVIGEQDWIPLNDRIRMVEWKARLDVAWYVVCGCADIQQLALTAYNDPVTDGMGWEELYAAVVKEHDDGHVSKMIRALKNGQEAARPFENGPYRNAFPLHGDMWLKAARMTLGTTTGCDEDTKFVMFTGFDIPWETRPDLQ | Baeyer-Villiger oxidase; part of the ergochrome gene cluster responsible for the typical purple-black color of the ergot sclerotia (PubMed:28955461). The ergochrome gene cluster produces several ergot pigments including the yellow ergochrome secalonic acid and its derivatives, as well as the red anthraquinones endocrocin and clavorubin (PubMed:28955461). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) CPUR_05437 (By similarity). The atrochrysone carboxyl ACP thioesterase CPUR_05436 then breaks the thioester bond and releases the atrochrysone carboxylic acid from CPUR_05437 (By similarity). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (By similarity). The next step is performed by the anthrone oxygenase CPUR_05434 that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving CPUR_05427, CPUR_05428, CPUR_05429 and CPUR_05430 (By similarity). The short chain dehydrogenase/reductase CPUR_05418 then catalyzes the C-5 ketoreduction to give the xanthone skeleton of the monomeric units (PubMed:32105084). Ergochromes formation requires further dimerization steps of different xanthone units, probably catalyzed by the cytochrome P450 monooxygenase CPUR_05419 (PubMed:28955461). CPUR_05425, CPUR_05426 and CPUR_05431 are unique to Claviceps, thus it is likely that they are involved in further modification of xanthone units or in their dimerization (PubMed:28955461). The yellow ergochromes and the red anthraquinone pigments endocrocin and clavorubin are products from the same PKS derived precursors and the latter are likely shunt products in the pathway of xanthone biosynthesis (PubMed:28955461). It is proposed that atrochrysone carboxylic acid released from the PKS CPUR_05437 can also0 be converted to endocrocin anthrone which is further oxidized into endocrocin by CPUR_05435 (By similarity). Endocrocin could be then modified to clavorubin, possibly by CPUR_05423 and CPUR_05431 (PubMed:28955461). Clavorubin is the principal anthraquinone metabolite produced by the cluster with a much higher yield compared to endocrocin (PubMed:28955461). Pigment biosynthesis. Expression correlates with the formation of the sclerotia and thus the pigment production and is directly regulated by the cluster-specific activator CPUR_05433 (PubMed:28955461). Belongs to the questin oxidase family. |
P12626 | MSDQATFEFDTDYFVEEFSHCFTGECRVKMLPILYKISQIITGNADLADALSIVLGVMQQHLKMQRGIVTLYDMRAETIFIHDSFGLTEEEKKRGIYAVGEGITGKVVETGKAIVARRLQEHPDFLGRTRVSRNGKAKAAFFCVPIMRAQKVLGTIAAERVYMNPRLLKQDVELLTMIATMIAPLVELYLIENIERVRLENENRRLKHALKERFKPSNIIGNSKPMQEVYELIHKVASTKATVLILGESGVGKELVANAIHYNSPNAEAALVTSNCAPLPENLAESELFGHEKGSFTGALTMHKGCFEQADGGTIFLDEVGELSPTVQAKLVRVLQNRTFERVGGSKPVKVDVRIIAATNRNLVEMVEQGTFREDLYYRLNVFPITVPPLRERGSDVIALADHFVSAFSRENGKNVKRISTPALNMLMSYHWPGNVRELENVMERAVILSDDDVIHSYNLPPSLQTSKESGTAFGLTLEEKIKAVECEMIVEALKNSSGHIGEAAKELGLARRMLGVRMERYGISYKSFSRYA | AnfA is essential for nitrogen fixation under Mo- and V-deficient conditions. It is required for the regulation of nitrogenase 3 transcription. Interacts with sigma-54. |
Q7C5U6 | MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLEAGARLTVNALTFIPQFTVWVNEGMLTLVEGPFDETLLDSCWLAIAATDDDTVNQRVSEAAESRRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVARYAGQLRARVKKQFATMGERRRFWEKFFVNDRLAQSLANADEKAVNATTEHLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCHAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGGELDWENLAAEKQTLVFYMGLNQAATIQEKLIAFGMEANMPVALVENGTSVKQRVVHGVLTQLGELAQQVESPALIIVGRVVALRDKLNWFSNH | Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. 2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) + precorrin-2 + 2 S-adenosyl-L-homocysteine NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin 2 H(+) + siroheme = Fe(2+) + sirohydrochlorin Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. In the C-terminal section; belongs to the precorrin methyltransferase family. |
Q4FRS8 | MKVREILVTSALPYANGDIHLGHLVEYIQTDIWVRSMKAQGHKVTYVCADDAHGTAIMLKAEDNGVTPEQQIANVQAAHEADFAKFLINFDNYHSTHSEENREFSELIYRRLRDTGHISTRDVEQLFDPEKQLFLADRFVKGTCPECAAPDQYGDNCEVCGTTYDATELKDPYSTLSNATPILKTSKHYFFDLPEFEQFLKDWTRSDNRLQVSVANKLQEWFDAGLTSWDISRDAPYFGFQIPDTPSDEPDKYFYVWLDAPVGYMASFKNLCDKRAGTDDALDFDHYWAQENEHKTEVYHFIGKDIVYFHALFWPAMLAGSELRTPTAVFAHGFLMVNGEKMSKSRGTFIKADTYAEHLHPEYLRYYFASKLSDKVEDINLDLEDFMQKVNSDLVGKVVNIASRSAGFLLKKYDGMLTDVCAEPSLLEDITKTGDEIAAAYENREFSRAMRLIMQCADKANEYIDEKKPWALAKVEGAEQEVQDVCSVAINIFRQLMVYLAPVLPELTANAKEFLNINDLSFASRNEWLLGHQINKFKPLMQRIDEKDVAAMVDASKASLTQVDAPTASQDDKMVAKNTAPAATPSSTEQADYIGIEDFAKVEMKVAHVIACSYVEGADKLLQFTLDVGEAQPRNVFSGIRKFYEPEQLLDKKVICVTNLAPRKMKFGISEGMILSSGDPKTQLTVVTLPDNCVIGDLLA | Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met) Binds 1 zinc ion per subunit. Homodimer. Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily. |
C9E258 | MATEAPVEATEIPSVAAAETVEKQPHKLERKWTFWFDNQSKPKQGVAWGSSLRKAYTFETVEEFWSLYDQIFKPSKVTVNADFHLFKAGIEPKWEDPECANGGKWTATSSRKANLETMWLETLMALVGEQFDESEDICGVVASVRRSQDKLSLWTKTATNEAAQMGIGRKWKEIIDAEKISYSFHDDSKRERSAKSRYTV | Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses (Ref.1). (Microbial infection) Susceptibility host factor required for viral infection by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). EIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G. EIF4E is also known to interact with other partners. In higher plants two isoforms of EIF4F have been identified, named isoform EIF4F and isoform EIF(iso)4F. Isoform EIF4F has subunits p220 and p26, whereas isoform EIF(iso)4F has subunits p82 and p28. (Microbial infection) Interacts with viral genome-linked protein (VPg); this interaction is possible in susceptible hosts but impaired in resistant plants. Mostly expressed in roots and leaves, and, to a lower extent, in stems, flowers and immature green fruits. According to the redox status, the Cys-99-Cys-138 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. Variant present in strain cv. Zhongshu 5, confers an increased resistance to potyvirus cucumber mosaic virus (CMV) and tobacco mosaic virus (TMV) and tolerance to plum pox virus (PPV). No obvious growth defects (PubMed:22242134). Plants lacking eIFiso4E, eIF4E1 and eIF4E2 exhibit a semi-dwarf phenotype (PubMed:22242134). Displayed sequence is from cv. Heinz 1706 and cv. Ailsa Craig, and is associated with susceptibility to cucumber mosaic virus (CMV), tobacco mosaic virus (TMV) and plum pox virus (PPV). Belongs to the eukaryotic initiation factor 4E family. |
Q6LD29 | MLGIVKMEGHETTDWSNYYQDTQEAYSSVPVSNMTQGLASMNTYMTMNPMSSSSNMTAAGSFNMSYGNSGLGAGLSPSGMSGMGAGAASAMNGMGSGVPSMGTALSPSNMNAMSAQQASMNSLSYSSMNPGMSPMAYGSSNMNRARDTKTFRRSYPHAKPPYSYISLITMAIQQAPSKMLTLSEIYQWIMDLFPYYRQNQQRWQNSIRHSLSFNDCFVKVARSPDKPGKGSYWTLHPDSGNMFENGCYLRRQKRFKCEKTQGGKGNQDGRKDHSGPSSPLQRVHGKSSQMDSSSSMSNPSSSPQALEHNGSNGEMKPQVAAGPSPLSSHQNHSTHSLAHESHIHLKGDPHYSFNHPFSINNLMSSSEQQHKLDFKAYEQALQQYSSYGGGLPGMPLGSPSMSGRGNIEPSALEPTYYQGVYSRPVLNTS | Probable transcription factor. At neurula stage, expressed in the notochord but not in the neural floor plate. During tailbud stages, expressed in the neural floor plate. At stage 35, expressed in the rhombencephalon, mesencephalon, pharyngeal pouches, foregut and pronephros. At stage 44, expressed in a region of the gut on the right hand side of the embryo. Expressed in the adult lung and liver. Expressed zygotically. Expression begins in the blastula stage. Levels increase throughout gastrulation before decreasing at the tadpole stage. |
A3PCF5 | MLSESLTKTKLTDPLILDLLQNIRKHRSMLEDLKSIKIDPNLTNIISNEIGRELYIENEFHKAKGFRKLHIEVAEFSKNLRILHCVFFPDPKFDIPIFGMDLVKINDIVSAAIVDLSPASQNQALKYEKLLSGVDKSSFTSLREIPKWGRIFSNNVFFASLRNKSEKNDFCSVVDQYLSILIKLSKKAKPEFNEEIIQERIDFQKNYCAQQMKNEKTSMVLLKYFDEKWVNNYIKTVLFDF | Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin. (2R,3Z)-phycocyanobilin + 4 oxidized [2Fe-2S]-[ferredoxin] = biliverdin IXalpha + 4 H(+) + 4 reduced [2Fe-2S]-[ferredoxin] Belongs to the HY2 family. |
Q12S25 | MSISSLHRGYQVLRTLLHYGLDELLAKDKRPKLFPLIRGCFFWIRNQHKDKSAAERLKLAMQELGPVYIKLGQMLSTRRDLLDDEWAYQLAMLQDRVPPFDSALAREAIETELNASIDSLFDDFDDVPLASASIAQVHSATLKSNGKAVVLKVLRPNVEALILADLQLMSHCAALLERILGDGNRLRPAEVIEDYRLTILGELNLKLEALNAIKLRNNFLDSDALYVPYIYEDLSFTRLIVMERIYGIAVSDLSALKAQGTNLKLLAERGVELFFTQVFRDNFFHADMHPGNIFISRDHPDNPYYIGLDCGIMGTLTDVDKRYLAENFLAFFNRDYQRIAQLHLESGWVSEHTDIVAFEQAIKIVCEPMFNKPLAEISFGHVLLALFRTARQFNMVVQPQLVLLQKTLLYIEGLGRQLYPQLDLWQTAKPFLEQWMAKQVGPKALFDKFKSNAPFWAEKLPELPELVYDNLKLGRKLLGTQQQMLDKYLKYQHKAHKSNYLLITSAVFVICGTILFTQAVTLWASLLCLGTGAGLWLLGWQARPKNRKL | Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. Cofactor biosynthesis; ubiquinone biosynthesis [regulation]. Belongs to the ABC1 family. UbiB subfamily. |
Q758W7 | MLESTALFSATTIHLDRLMCAFNCMTPFGQRDDVLITIDRDGLTFIRQNNHAAEIQLFLAKELFQYYSIREGFEGEIQLCMKLNHLLDTVSVANRDKDDVVECTLSYDGEGTPFMLILEDSMITEQVEYATYLVGEMDRTGLELDRARLEFECILKGDVLYSALRDLREIGCKECYLYIVTSSRARPMFALVSRGQLGLSKIILPSERSVLEKLEVYENDSTTLIHDAPVIGLFDFAALDKLRPSTKIASKVLIRKDVHGLLAVNILSDTNAILVPEKRELIRASRSVSAEYPTVVIEVFLLEKASVGDIDVRDVHQLMLTSPAHRRSGFADSGSRIVSVTPTATSAAHTGAGSLLGLAPPSAFPAEETQDPDESYHPAPSNTDIPLFL | Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Component of the checkpoint clamp complex composed of DDC1, MEC3 and RAD17. Belongs to the rad1 family. |
Q2MBK4 | MIWKRHLTLDELNATSDNTMVAHLGIVYTRLGDDVLEAEMPVDTRTHQPFGLLHGGASAALAETLGSMAGFMMTRDGQCVVGTELNATHHRPVSEGKVRGVCQPLHLGRQNQSWEIVVFDEQGRRCCTCRLGTAVLG | Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Displays esterase activity toward a wide range of substrates, including acyl-CoAs and aryl-CoAs. Siderophore biosynthesis; enterobactin biosynthesis. Homotetramer. Dimer of dimers. Interacts specifically with the aryl carrier protein (ArCP) domain of EntB. Induced by iron starvation. Belongs to the thioesterase PaaI family. |
P49460 | MTATLERREGVSLWERFCAWITSTENRLYIGWFGCLMFPTLLTATSCYIIAFIAAPPVDIDGIREPVAGSLLYGNNIISGAVIPSSNAIGMHFYPIWEAASIDEWLYNGGPYQLIVLHFLLGVASYMGREWELSYRLGMRPWIFVAFSAPVAAASAVFLVYPIGQGSFSDGMPLGISGTFNFMLVFQAEHNILMHPFHMAGVAGVFGGSLFSAMHGSLVTSSLIRETTENESTNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRALHFFLAAWPVVGIWLTAMGVSTMAFNLNGFNFNQSVVDSQGRVINTWADIINRADLGMEVMHERNAHNFPLDLASGDVLPVALNAPAVNG | Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. 2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2 The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids. PSII is composed of 1 copy each of membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3 peripheral proteins of the oxygen-evolving complex and a large number of cofactors. It forms dimeric complexes. Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z. C-terminally processed by CTPA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth. 2 of the reaction center chlorophylls (ChlD1 and ChlD2) are entirely coordinated by water. Herbicides such as atrazine, BNT, diuron or ioxynil bind in the Q(B) binding site and block subsequent electron transfer. Belongs to the reaction center PufL/M/PsbA/D family. |
Q9RX92 | MKLSDVQKRLQAPFPAHTVSWKPAAFNAERTRALLLAHVDARAVQDRLDAVCPDDWSFEMEVVSGAEVPTVKGRLTVLGVTREDIGEAPEGSMAAYKAAASDAMKRCAVQFGIGRYLYDLPKQWADWDDARRGPKHLPELPEWARPDHERTPGGAHLVQAMEQLRYELPEDLDLQREVYKHLKAALGSIHPVPTGPVPTNPVQGGRAA | ssDNA-binding protein that contributes to the ionizing radiation resistance of D.radiodurans. Plays a role in DNA repair and genome reconstitution, in a RecA-independent process, since DdrA is essential for recovery from severe genomic fragmentation as a result of exposure to severe levels of ionizing radiation in an environment lacking nutrients. In vitro, binds to the 3'-ends of single-stranded DNA, protecting them from nuclease degradation. Thus, DdrA is part of a DNA end-protection system that helps to preserve genome integrity following irradiation or desiccation. Does not display DNA strand annealing activity, unlike eukaryotic Rad52 protein homologs. Homooligomer composed of 8 to 10 subunits; probably arranged in a ring-structure. Induced to high levels following extreme ionizing radiation exposure. Also highly induced in response to desiccation stress. Cells lacking this gene show a normal growth rate, do not exhibit a decrease in the efficiency of natural transformation, but display a reduced capacity to survive ionizing radiation when exposed at doses superior to 2.5 kGy and exhibit increased sensitivity to mitomycin C. Belongs to the RAD52 family. |
Q9QY10 | MRIHGLILLSFLLLAAQVLSEKVRKTAKNVPDSTTEEDMSPSLGKARNKQRSRTSKSMTHGRFVTKDQATCRWAVTEEELGINLKVQCTRADQEFSCVFAGDPTGCLKYDKDQTYWKQVARTLRKQKNICENSKSVLKTRVCRKKFPESNLKVVNPRKEKAEVSPREHNKVQEAVSMEPNKVKVDITTSPAATVAVKDSECLEDPDVLTQRKTALEFCGESWSSFCTFFLNMLQATSC | Acts as a carrier protein that release fibroblast-binding factors (FGFs) from the extracellular matrix (EM) storage and thus enhance the mitogenic activity of FGFs. Enhances FGF2 signaling during tissue repair, angiogenesis and in tumor growth (By similarity). Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGF1, FGF2, FGF7, FGF10, FGF22 and HSPG2 (By similarity). Extracellular and plasma membrane-associated. Expressed in gut, eye, thymus, skin, lung, tongue, Purkinje cells and cerebral chorioid plexus (at protein level). Down-regulated by retinoids. Belongs to the fibroblast growth factor-binding protein family. |
G2TRQ2 | MNRTSESVEPQQNEKTAVHWSREWVPVVVDTYSNEDDEDNEEGDESRPQRTFLVKRWVQDNVQVEKKGDEETAAADN | Differentially expressed during meiosis. |
Q71XS4 | MAKEKIVLAYSGGLDTSVAIQWLVESGYEVIACCLDVGEGKNLDFIKEKAITVGASESYTIDAKEEFAEDFALIALQAHAYYEGKYPLISALSRPLIAKKLVEVARQEGASAIAHGCTGKGNDQVRFEVAIHALAPDLKVVSPVRDWKWSREEEINYAKEHNIPVPIDLDNPFSIDQNLWGRSNECGVLENPWTTPPEAAYDLTVSLEDAPDTPDIVEITFDAGIPISLNGENMSLANLILTLNEIAGKHGVGRIDHIENRLVGIKSREVYECPAAVTLITAHKELEDLTFVREVAHFKPIIEQKISETIYNGLWFSPLTEALVAFLKSTQKFVNGTIRVKLFKGHAIVEGRKSPNSLYDENLATYTSSDTFDQDAAVGFIKLWGLPTKVSAEVNSKVTITTEV | ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Homotetramer. Belongs to the argininosuccinate synthase family. Type 1 subfamily. |
B4JB43 | MRPLMLQGHERSITQIKYNREGDLLFSSSKDQKPNVWYSLNGERLGTYDGHQGAVWCLDVDWESRKLITGAGDMTTKLWDVEYGTVIASIATKSSVRTSNFSFSGNQAAYSTDKAMGQNCELFIIDVRNADSTLSEQEPTLRIPMVESKITSMQWGPLDETIITGHDNGNIAIWDVRKGQKVVDSGVDHAAGINDMQLSKDGTMFVTASKDNTAKLFDAESLMCLKTYKTERPVNSAAISPIFDHVVLGGGQDAMEVTTTSTKAGKFDSRFFHLIYEEEFARLKGHFGPINSLAFHPDGKSYASGGEDGFVRVQSFDSTYFENIFE | Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. Component of the eukaryotic translation initiation factor 3 (eIF-3) complex. The eIF-3 complex interacts with pix. Belongs to the eIF-3 subunit I family. |
A1KGL2 | MTQTGSARFEGDSWDLASSVGLTATMVAAARAVAGRAPGALVNDQFAEPLVRAVGVDFFVRMASGELDPDELAEDEANGLRRFADAMAIRTHYFDNFFLDATRAGIRQAVILASGLDSRAYRLRWPAGTIVFEVDQPQVIDFKTTTLAGLGAAPTTDRRTVAVDLRDDWPTALQKAGFDNAQRTAWIAEGLLGYLSAEAQDRLLDQITAQSVPGSQFATEVLRDINRLNEEELRGRMRRLAERFRRHGLDLDMSGLVYFGDRTDARTYLADHGWRTASASTTDLLAEHGLPPIDGDDAPFGEVIYVSAELKQKHQDTR | Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. Belongs to the UPF0677 family. |
Q038V3 | MTQSQQSHRKDEHVFLAEKYFQSVAHAGFDQVRLLHRALPETTMAAVDLKPDLPFNWQWPIYINAMTGGSPQTGKLNAQLGQLAQALGVAIASGSQSVALRDPQLVPTFATLRDHDPNGFILANVGAGHHATAAEAAVAMLKANALEIHLNAAQEVVMPEGDRDFMWQANIKSIIATSQVPIVVKEVGNGFIREDLQSLQQLGVQFVDVGGRGGTNFATIENARRSGHDFAYLQDWGQTTVESLLEARGLGLTMLATGGVRSPLDVVKALRLGAHAVGMSGMVLHHLIQTGYEATLAYFQNFLHQLRQLYALLGVTNWQELQEAPIVLSADLEHYRQARGLPGI | Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP). isopentenyl diphosphate = dimethylallyl diphosphate Homooctamer. Dimer of tetramers. Belongs to the IPP isomerase type 2 family. |
A6UUU3 | MDELNINFDKYKNIRRTMGRELIDLNPIQRGGELPVESKKAIYEYWDGYSVCDYCGGRLDKVETPPICEYLHDVSKFLGMDFTRPTHGARESKFIVMHSVCNEGDFVVLDGNAHYTSFVALERAKLNSEIVEHDGYPTFRVNPEKYAEVIDNLEDKNKPIGLILLTHVDGNYGNLADAEKVGKIAKQKGYPFLLNCAYSVGRLPVNGKKLNADFLAISGHKSMASASPCGLVSIKGEYADKVFRTSKTHPVKEIEMLGCTSRGAPLISLMASFSHVAERVKNWDNEVKKTRFVVDELEKIGFNQLGIKPKQHDLIKFETPILDEIAQKDKRRGYFFYEELKKRGIGGIKRGTTKEIKMSVYGLSWEQVRYVVDNIKEIVEQGNNI | Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). H(+) + hydrogen sulfide + O-phospho-L-seryl-tRNA(Cys) = L-cysteinyl-tRNA(Cys) + phosphate Homodimer. Interacts with SepRS. Belongs to the SepCysS family. |
P45958 | MAKEKIIGIDLGTTNSVVSVIEGGQPIILENPEGQRTTPSVVAFKNSDIIVGGAAKRQAVTNPNVVQSIKSKMGTTSKVNLEGKDYSPEQISAEILRYMKNYAEAKLGQKVTKAVITVPAYFNDAQRKATKDAGTIAGLQVERIINEPTAAALAYGLDKQDKEETILVYDLGGGTFDVSILAIGGGSFDVIATSGNNKLGGDNFDEEIIKWLLGKIKAEYNIDLSKEKMALQRLKDEAEKAKINLSSQLEVEINLPFIAMNESGPISFATTLTRSEFNKITKHLVDLTIQPVKDALSAAKKTPSEINEVLLVGGSTRIPAVQELVKSLLNKEPNRSINPDEVVAMGAAVQGGVLAGEVTDILLLDVTPLSLGIETMGGVMTKLIERNTTIPAKRTQIFSTATDNQPAVDINVLQGERAMAADNKSLGQFQLTGIQPAPRGIPQIEVTFEIDANGIVSVSAKDKNTNEEKTITISNSGNLSEAEVERMIKEAQENAANDEAKKKNIELKNKAENYINIIETSLLQAGDKISAEQKEQSQKMIDEIKELVKNENYEALEQKMAELEQAMAAAAEFANKHNDSDSNNNSSEQNN | Acts as a chaperone. By stress conditions e.g. heat shock (By similarity). Belongs to the heat shock protein 70 family. |
Q2NKP9 | MSSEESYRAILRYLTNEREPYAPGTEGNVKRKIRKAAACYVVRGGTLYYQRRQRHRKTFAELEVVLQPERRRDLIEAAHLGPGGTHHTRHQTWHYLSKTYWWRGILKQVKDYIKQCSKCQEKLDRSRPISDVSEMLEELGLDLESGEESNESEDDLSNFTSSPTTASKPAKKKPVSKHELVFVDTKGVVKRSSPKHCQAVLKQLNEQRLSNQFCDVTLLIEGEEYKAHKSVLSANSEYFRDLFIEKGAVSSHEAVVDLSGFCKASFLPLLEFAYTSVLSFDFCSMADVAILARHLFMSEVLEICESVHKLMEEKQLTVYKKGEVQTVASTQDLRVQNGGTAPPVASSEGTTTSLPTELGDCEIVLLVNGELPEAEQNGEVGRQPEPQVSSEAESALSSVGCIADSHPEMESVDLITKNNQTELETSNNRENNTVSNIHPKLSKENVISSSPEDSGMGNDISAEDICAEDIPKHRQKVDQPLKDQENLVASTAKTDFGPDDDTYRSRLRQRSVNEGAYIRLHKGMEKKLQKRKAVPKSAVQQVAQKLVQRGKKMKQPKRDAKENTEEASHKCGECGMVFQRRYALIMHKLKHERARDYKCPLCKKQFQYSASLRAHLIRHTRKDAPSSSSSNSTSNEASGTSSEKGRTKREFICSICGRTLPKLYSLRIHMLKHTGVKPHACQVCGKTFIYKHGLKLHQSLHQSQKQFQCELCVKSFVTKRSLQEHMSIHTGESKYLCSVCGKSFHRGSGLSKHFKKHQPKPEVRGYHCTQCEKSFFEARDLRQHMNKHLGVKPFQCQFCDKCYSWKKDWYSHVKSHSVTEPYRCNICGKEFYEKALFRRHVKKATHGKKGRAKQNLERVCEKCGRKFTQLREYRRHMNNHEGVKPFECLTCGVAWADARSLKRHVRTHTGERPYVCPVCSEAYIDARTLRKHMTKFHRDYVPCKIMLEKDTLQFHNQGTQVAHAVSILTAGMQEQESSGPQELETVVVTGETMEALEAVAATEEYPSVSTLSDQSIMQVVNYVLAQQQGQKLSEVAEAIQTVKVEVAHISGGE | May be involved in transcriptional regulation. The disease is caused by variants affecting the gene represented in this entry. |
A3PVL5 | MARLVGVDLPRDKRMEIALTYIYGVGRTRSQEILEATGIDRDLRTKDLTDDQVTQLRDYIEANLKVEGDLRREVQADIRRKIEIGCYQGLRHRRGLPVRGQRTKTNARTRKGPKRTIAGKKKAR | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. Part of the 30S ribosomal subunit. Forms a loose heterodimer with protein S19. Forms two bridges to the 50S subunit in the 70S ribosome. Belongs to the universal ribosomal protein uS13 family. |
F1SY66 | MFLQIVTSVLATGLLYALISVLQQNRTLSASLPPGPPGHWLFGNAPPRAFPYRHFAELTETYGPVFTLRFGRRIVCVIGRYQAAVDILMKHSAETSDRPRSVAANEIMSKGHRVLMTPAGERLKKYRRALHAFLQPSSSATYKPMQYKNAKNYVLDCLHDGRHHLYHGRKYAASVVMSVAYGKTTPTSYSDPEVLQINKSLARLGAALKPGAYLVDTYPILKYCPGYASHLRRYREEELALITKQANAVRELLAKGEAPPSFTAYLIENQERLGISDDELAYLSGAIFGAGSDTTAAALGIMTMAAACYPEAQARVQAQLDEVVGRDRAPTFEDEDLLPEVTAFVLEAYRWRPVSAGGFSHRATKDVVWNGYVIPAGAEIIGNHWAISRDPEVYPNPEDFKPARWLNEHGRIRNDLKFINFGFGRRVCVGQHVADQSLFINTALVLWAFRISQDAQCPIDTYAFTDTANVHPLPFSLHFEPRVKDMEAMLGAQAE | Cytochrome P450 monooxygenase that is able to use 4-ethoxybenzoic acid as a substrate for oxidation. Secondary metabolite biosynthesis. Belongs to the cytochrome P450 family. |
B5EXY0 | MANFPASLLILNGKSADNQPLREAITLLRDEGIQIHVRVTWEKGDAQRYVDEARRLGVETVIAGGGDGTINEVSTALIQIRDGVAPALGLLPLGTANDFATSAGIPEALDKALKLAIAGNAMEIDMARVNDKTCFINMATGGFGTRITTETPEKLKAALGGVSYLIHGLMRMDTLTPDRCEIRGENFHWQGDALVIGIGNGRQAGGGQQLCPTALINDGLLQLRIFTGEELLPALFSTLTQSDDNPNIIDGASAWFDIHAPHEITFNLDGEPLSGQEFHIEVLPGALRCRLPPDCPLLR | Probably phosphorylates lipids; the in vivo substrate is unknown. Binds 1 Mg(2+) ion per subunit. Ca(2+) may be able to substitute. Belongs to the diacylglycerol/lipid kinase family. YegS lipid kinase subfamily. |
P46642 | MNWRSEHIWIELLKGSRKRGNFFWACILFLGSLGFLAVGASSYLGKNMISVLPSQQILFFPQGVVMSFYGIAGLFISSYLWCTILWNVGSGYDRFDRKEGIVCIFRWGFPGIKRRIFLQFLVRDIQSIRIQVKEGLYPRRILYMEIRGQGVIPLTRTDEKFFTPREIEQKAAELAYFLRVPIEVF | Seems to be required for the assembly of the photosystem I complex. Belongs to the Ycf4 family. |
Q2P907 | MHIDVIGHGPALVLLHGWALHGGVFAPLVERLAPHYQLHLVDLPGHGFSRDDSTPLALPYVVAEIAAATPPAVWLGWSLGGLFALHAAATLPQVRGLAMIAATPRFVRGSDWPDAVQRELFVQFGTELSRDYRGTLERFLALDTLGSAHARSELRSLRETLTARGEPAPEALQQGLSLLERTDLRRALPQLARPSLWIAGQRDRLVPAAGMHAAAALSPHAQALTIAGGGHAPFLGHADQVSEALQRFVASVP | The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. 6-carboxyhexanoyl-[ACP] methyl ester + H2O = 6-carboxyhexanoyl-[ACP] + H(+) + methanol Cofactor biosynthesis; biotin biosynthesis. Monomer. Belongs to the AB hydrolase superfamily. Carboxylesterase BioH family. |
Q1XDK9 | MQTTINNGQTSSKETLLTPRFYTTDFEEMANMDISGNQEDFLAILEEFRADYNSEHFIRDEEFNQSWSNLEHKTKSLFIEFLERSCTAEFSGFLLYKELSRKLKDRNPVIAECFLLMSRDEARHAGFLNKAIGDFNLSLDLGFLTKSRKYTFFSPKFIFYATYLSEKIGYWRYITIYRHLEQHPEHRIYPIFRFFENWCQDENRHGDFFAALLKSQPHFLNDWKAKMWCRFFLLSVFATMYLNDFQRIDFYNAIGLDSRQYDMQVIRKTNESAARVFPVALDVDNPKFFKYLDTCACDNRALIDIDNNNSPLFIKSIVKIPLYFSLFANLLKIYLIKPIDSKTVWNTVR | Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME). 2 H(+) + Mg-protoporphyrin IX 13-monomethyl ester + 3 NADPH + 3 O2 = 3,8-divinyl protochlorophyllide a + 5 H2O + 3 NADP(+) Porphyrin-containing compound metabolism; chlorophyll biosynthesis (light-independent). Belongs to the AcsF family. |
Q4QK64 | MMSHTETSLGAENTRTHNFITQIIDEDLASGKHKSVHTRFPPEPNGYLHIGHAKSICLNFGLAKEYQGLCNLRFDDTNPVKEDVEYVDSIKADVEWLGFKWEGEPRYASDYFDALYGYAAELIKKGLAYVDELSPDEMREYRGTLTEPGKNSPYRDRTIEENLALFEKMKNGEFAEGKASLRAKIDMASPFMVMRDPVIYRIKFASHHQTGDKWCIYPMYDFTHCISDAIERITHSICTLEFQDNRRLYDWVLENISIERPLPHQYEFSRLNLEGTLTSKRKLLKLVNDEIVDGWNDPRMPTISGLRRRGYTPASLREFCRRIGVTKQDNVVEYSALEACIREDLNENAPRAMAVIDPVRVVIENFESEAVLTAPNHPNRPELGERQLPFTKELYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAERVEKDANGEITTIFCTYDPETLGKNPADGRKVKGVIHWVSAVNNHPAEFRLYDRLFTVPNPGAEDDIESVLNPNSLVIKQGFVEQSLANAEAEKGYQFEREGYFCADSKDSRPEHLVFNLTVSLKEGF | ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln) Monomer. Belongs to the class-I aminoacyl-tRNA synthetase family. |
Q28PE4 | MTQFDPATLRYDVNGLIPCIAQQEGTGEVLMMAWMNADSVARTLESGRVTYWSRSRQAFWVKGETSGHVQELVDLRVDCDRDCLLAVVRQTGPACHTNRRVCFYTSVTSGEEVELMAPE | Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP. 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide Binds 1 Mg(2+) ion per subunit. Binds 1 zinc ion per subunit. Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. Homodimer. Belongs to the PRA-CH family. |
B0U281 | MPEYRSKTSTYGRNMAGARALWRATGMKDDDFQKPIIAIANSFTQFVPGHVHLKDLGQLVAREIERLGGVAKEFNTIAVDDGIAMGHDGMLYSLPSREIIADSVEYMANAHCADALVCISNCDKITPGMLMASLRLNIPTVFVSGGPMEAGKTTLADHKLDLVDAMVLAADPHASDEEVATVERSACPTCGSCSGMFTANSMNCLTEALGLSLPGNGTVVATHSDRKQLFLNAGRTVIELCHRWYGAEDATALPRGIATFAAFENAITLDIAMGGSTNTILHLLAAAQEAQVSFTMQDIDRLSRNVPQLCKVAPNTQKYHIEDVHRAGGIFGILAELARGNLLHTDVATVHSKTLGEAIATWDIIGTQDEAVHTFYKAGSAGIPTQVAFSQSTRWPSLDTDRTEGCIRDMEHAFSKEGGLAVLYGNIAQDGCVVKTAGVDASIHVFEGSALVYESQEAAVKGILSDEVQPGMIVVIRYEGPKGGPGMQEMLYPTSYLKSKGLGKQCALFTDGRFSGGTSGLSIGHASPEAAAGGAIGLIRDGDRIRIDIPQRAINVLISEEELASRRLEQHAIGWKPAQSRTRKVSSALKAYSLLATSADKGAVRNKTLL | Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively. (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O (2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2-oxopentanoate + H2O Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor. Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 3/4. Homodimer. Belongs to the IlvD/Edd family. |
A6QQS3 | MSPLECSECFGDQLLHRTYTWHLTLHSRPNFTRKRDTRSESLEIPINVVLPQRGTAEPFLRLHNLYPTPRCARQAALPRLSRRVVSQHSYPLNRFSSVPLDPMERPTSQADLELDYNPPRVQLSDEMFVFQDGRWVSENCRLQSPYFSPSSSFHHKLHHKRLAKECLLQENKTLREENRALREENRMLRKENKILQVFWEEHQAALGRDDSRASSPLLHKDNASSLEAMKKETALQAHRGRENSTLQLLREENRALQQLLEQRKAYWAQPDEKAASTEEIKPISSPHEEPHGLLPDPGPGLPSPFEEPKGLPAPPDDSKTLRALREMVSTLSAQPGEEVGKGGPGLPDGSQSLELLREMNQALQALREENQSLQVLRDENRLLQEENRALHALREEHRLFQEENKALWENNKLKLQQKLVIDTVTEVTARMEMLIEELYAFMPAKSKDPKKPSRV | Homodimer. Binds to NEK1 (By similarity). Belongs to the chibby family. SPERT subfamily. |
Q6KHL2 | MQIEVKNISKVFEPKSPIEFTALKGVSLSFEQGEFISIIGPTGSGKTTFIEHLNALNLPSIGSIVIKGKFKDQKDKKNPVLIESEVILQKTKRKIKQIKEIRRQIGIVFQFAEYQLFESTIEKDIAFGPISLGISKEEAYKRAKKYISIVGLPENYLQRSPFELSGGQKRRVALAGILAMDPDFLIFDEPTAGLDPQGSKEILEIFGKLNSEGKTVIIVTHNLDHALEWTNRTIFFNDGFVIKDGKTYDVLEDVDFLRENEMEPPKLLVLKKLLQDKGINLSKVRSIEDFAREINQYLETKNKTKENN | ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. Forms a stable energy-coupling factor (ECF) transporter complex composed of 2 membrane-embedded substrate-binding proteins (S component), 2 ATP-binding proteins (A component) and 2 transmembrane proteins (T component). Belongs to the ABC transporter superfamily. Energy-coupling factor EcfA family. |
Q9CRB3 | MATESSPLTTHVLDTASGLPAQGLCLRLSRLEAPCQQWMELRTSYTNLDGRCPGLLTPSQIKPGTYKLFFDTERYWKERGQESFYPYVEVVFTITKETQKFHVPLLLSPWSYTTYRGS | Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+) Purine metabolism; urate degradation; (S)-allantoin from urate: step 2/3. Homotetramer. HIU hydrolysis also occurs spontaneously, but more slowly. Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily. |
Q7M732 | MIEPSEDSFETMMELKNPSSKQMESSEGSSNTVEETPGSSGAQAGAQAGAQAEAQAETQVEAQAEAQAEAQVEAQVEAQAGSDSGPAQEEKEPPSGPLKEMQELPTNLLQEVEEPSSGPHQEMQELPTDLLQEVEEPSSGPHQEMQELPTDLLREVEEPSSGPYQEMQELPTDLLREVEEPSSGPYQEMQELPTDLLREVEEPSSGPYQEMQELPTDLLREVEEPSSGPYQEMQELPTDLLREVEEPSSDPCEASSNDLPQDMEESSDDGSNQESSDGSNHELSNGSNHESSFGSNPESSDVSNLESSGGSNQESSDGSQKESSYDSNPELSDNSNQELSDNSNQESSDSSNQSSDISNQEGSEPLSEASDYSMDETINSSETQSDQDDTDLGDDEEEEEEEGGEEEGQPKNSPEEVVATMGNVISLFLRMQDLKEQQRVAERLMMQAINEGRLPSLRPFSGDRRDYHEFVVLCQMTMQNYPSMLYNDELRVKFVIRHLTDLALEWANDLVEQNSPVINNFSAFLEAMSEKFEYRQTLRVAEDAMFNIRQGNRCAADYINEFRGLIPTLGWPDEVLQAHLCQGLNEEIRHYLFRIPQPNSLDNLIVLVLQLEEKLAERRALLRLPPESRPRSVAWMDAPAPEKWRVSSWLPNEFHPDIDRDHLFLLLLVRVDPYHSVAVRALVDSGAEGNYMDERFAQEHYVELYEKPYPQIIQGVDGIPIGNEPVWLCTEPLVCVHQKHYEYIEFDILPSPNFSIVLGMKWLRTHAPEVDWMRGRCTFHSPYCLRNCFTPPPPCIALETYSISLLPGLPHTYSDLADVFNPREADDETSDQPSSDGSDDLSESEPSELQQAGDSDQSGVFYESGARETLEPVSARMQEKARQQEKAREQEEYWILYDMLTDRQDYTQMVPELFDQLHGAAWFTKLELLGIKESEMRHTVTHTEDTWRASFGFGLHQMRCYRPFTMNSYSDEGNNIVHFILKDILGLFVICHGREVLVYSMSQEEHSQHVRQVLVRFRYHNIYCSLDKTQFHRQTAEILGFNISPKGVKLNKNLMNLIVGCPVPGSRRCLQSVIDLVYPYRHFVENFAVIAAPLVRQLLSSEPYYWGEEEQEALESLKRAFRKSPVLYHPKPQNPFYLETDITGSFLSASLVQTDDETGKKSTCAFYSRPLSTMEVEYPRVEMRILPIRAAFMVWCRYLENTEEPIMILLNTEDLASLNNDRLTVLLPGHWVFFFSHFNFGVMEMPAEGDTQALFRRCWNQRGFRARFLRPLLLMSIRANLRYFDRSSETEDKEDDEEEEEEDGEEEEGEEEEDGEEEEGEEEEDGEEEEEEEEDDEEEEGEEEEDGEEEEGEEEEDGEEEEGEEEEDGEEEEGEEEGEEEEEGEEEEEEEEDEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEDEEEEDEEEEDEEVPSMVRELLAAIPMDHILNGLLAHFSVAQIRAVVLNFFRGLLYWKSLLGVAAVLVMLRARQPLSPVPAPNLEVARPQHRHTLRLILDSTLIASSGMATAIAQLLSQMPPLVGANTLPARELAELFLGPRCWHRNALHSQPPRGMRFTPGFWLTLCEFFGVRVNPEDDVFPDPYQHRYLELHVVGDEDVVLREALQDDLQRYRQCGLHDGLQDTSQDAQDNDVQEDLFGDQEAVTFRPRNLLDPEVLDFLNNRLLYTLGTDGRLTLLSRDQVAQALTRFLAMASRMALPSPAREQARLEELSDSDDELD | Plays an essential role in capillaries endothelial cells for the maintenance of feto-maternal interface and for development of the placenta. Expressed in placenta and in various tissues in late-fetal stage. Increased expression throughout development from 9.5 dpc to 18.5 dpc in placenta and, from 12.5 dpc to 15.5 dpc in embryo. Barely detectable in adult brain and midbrains of 14.5 dpc, but abundant at 8.5 dpc. Down-regulated during time-course of induced adipogenesis in 3T3L1 cells; Lipid accumulation is unchanged during adipocyte differentiation when Rtl1 is overexpressed. Mice suffer from late fetal or neonatal lethality. Mice overexpressing Rtl1 show notable overgrowth and morphological abnormalities of the placenta. Rtl1 is one of at least 11 genes called Mar or Mart related to long terminal repeat retrotransposons. They do not correspond to functional retrotransposons, but rather to neofunctionalized retrotransposons genes. Rtl1 is an imprinted gene located in a cluster of imprinted genes on distal chromosome 12. It is expressed from the paternal chromosome and has an antisense transcript expressed from the maternal chromosome containing 2 microRNAs, mir-136 and mir-127, with full complementarity to Rtl1; mir-136 and mir-127 are processed from an antisense transcript, Rtl1as, and may function as small interfering RNAs to silence Rtl1. |
Q5TJF4 | MTTPANAQNASKTWELSLYELHRTPQEAIMDGTEIAVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCSDCIVTALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSREEYEAHQDRVLIRLSRLHNQQALSSSIEEGLRMQAMHRAQRVRRPMPGSDQTTTMSGGEGEPGEGEGDGEDVSSDSAPDSAPGPAPKRPRGGGAGGSSVGTGGGGAGGVGGGAGSEDSGDRGGTLGGGTLGPPSPPGAPSPPEPGGEIELVFRPHPLLVEKGEYCQTRYVKTTGNATVDHLSKYLALRIALERRQQQEAGEPGGPGGGASDAGGPDGGGGEGGGTRGGDGPEEPALPSLEGVSEKQYTIYIAPGGGAFTTLNGSLTLELVNEKFWKVSRPLELCYAPTKDPK | Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity (By similarity). S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. Protein modification; protein ubiquitination. Component of chromatin-associated Polycomb (PcG) complexes. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2/RING2 MBLR, L3MBTL2 and YAF2. Interacts with CBX2 and PCGF6. Component of a PRC1-like complex. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RNF2/RING2. Interacts with BMI1, PHC2, PCGF2, RNF2; CBX6, CBX7 and CBX8 (By similarity). Interacts with MN1 (By similarity). |
Q9DG39 | MGRFIFLSFGLLVVFLSLSGTGADCPSGWSSYEGHCYNIFHLFKTWAEAERFCRKQVKGAHLVSIESSEEADFVAQLVSENMKRYGIYIWIGLRVRGKKKQCSSQWSDGSSVSYQNWIEAESKTCLGLQKETEFRKWFNIYCGERNPFVCEA | Anticoagulant protein which binds to the gamma-carboxyglutamic acid-domain regions of factors IX (F9) and factor X (F10) in the presence of calcium with a 1 to 1 stoichiometry. Heterodimer of subunits A and B; disulfide-linked. Expressed by the venom gland. Calcium is required for ligand binding. Belongs to the snaclec family. |
Q3ZX06 | MKIGVLALQGAFREHLNMLGTLGAEAVEVRKAEGLPELSGLIIPGGESTTITKLLDIFGMAEPIKALAKKGMPIWGTCAGMICLAKELPGDISGVKPLGLMDITVRRNAFGRQVNSFEAMLKVKGLDEADFPAVFIRAPLVEKTGKGVEILSKLPDGTIVAVRENNLLAISFHPELSGDNRFHRYFVQMAKTYKA | Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate H2O + L-glutamine = L-glutamate + NH4(+) Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis. In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer. Belongs to the glutaminase PdxT/SNO family. |
O76472 | MSDSMLYQTLQTCLPKSRLITLWLAFTLAMLIQEPRRHAATVNAATAGGSMLGDVNISAILDSFSVSYDKRVRPNYGGPPVEVGVTMYVLSISSLSEVKMDFTLDFYFRQFWTDPRLAYRKRPGVETLSVGSEFIKNIWVPDTFFVNEKQSYFHIATTSNEFIRVHHSGSITRSIRLTITASCPMNLQYFPMDRQLCHIEIESFGYTMRDIRYKWNEGPNSVGVSSEVSLPQFKVLGHRQRAVEISLTTGNYSRLACEIQFVRSMGYYLIQIYIPSGLIVVISWVSFWLNRNATPARVALGVTTVLTMTTLMSSTNAALPKISYVKSIDVYLGTCFVMVFASLLEYATVGYMAKRIQMRKQRFMTIQKMAEQKKQQQLDGVQPPPNPNPNTMVDHGGHGHGHGHHSHGHPHVPKQTVSNRPIGFQTMQQQNIGGRGCSIVGPLFQEVRFKVHDPKAHSKGGTLENTVNGGRGGPPVGPHGPGPQGPPGGPPAGGGGGGAPPEGGDAEAAVPAHLLHPGKVKKDINKLLGITPSDIDKYSRIVFPVCFVCFNLMYWIIYLHVSDVVADDLVLLGEEK | GABA, an inhibitory neurotransmitter, mediates neuronal inhibition by binding to the GABA receptor and opening an integral chloride channel. Homomultimer. Flies carrying the Rdl-S mutation are resistant to dieldrin. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. |
P34950 | MASVAESSGVVEVIELISDGGNDLPRKIMSGRHGGICPRILMPCKTDDDCMLDCRCLSNGYCG | Inhibits trypsin. The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin. Belongs to the protease inhibitor I7 (squash-type serine protease inhibitor) family. |
A6U8E5 | MTAIIDIIGREILDSRGNPTVEVDVHLEDGSFGRAAVPSGASTGAHEAVELRDGGTRYLGKGVERAVDAVNGEIFEAIGGLDAENQIQIDRTMFELDGTPNKSRLGANAILGVSLAVAKAAAEAAGLPLYRYVGGPNAHLLPVPMMNIINGGAHADNPIDFQEFMIMPVGAETLKDAVRMGSEVFHTLKKQLAADGHNTNVGDEGGFAPGLASAPAALDFIMKSIEKAGYRPGEDMYVALDCASTEFFKDGKYVLEGEGRTLEPGAMAEYLAELAGKYPIVSIEDGMAEDDWDGWKALTDLIGNKCQLVGDDLFVTNSARLRDGIKMGVANSILVKVNQIGSLSETLDAVETAHKARYTAVMSHRSGETEDSTIADLAVATNCGQIKTGSLARSDRLAKYNQLIRIEEQLGPQAQYAGRSILRG | Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein. Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface. Belongs to the enolase family. |
Q7A215 | MKWLKQLQSLHTKLVIVYVLLIIIGMQIIGLYFTNNLEKELLDNFKKNITQYAKQLEISIEKVYDEKGSVNAQKDIQNLLSEYANRQEIGEIRFIDKDQIIIATTKQSNRSLINQKANDSSVQKALSLGQSNDHLILKDYGGGKDRVWVYNIPVKVDKKVIGNIYIESKINDVYNQLNNINQIFIVGTAISLLITVILGFFIARTITKPITDMRNQTVEMSRGNYTQRVKIYGNDEIGELALAFNNLSKRVQEAQANTESEKRRLDSVITHMSDGIIATDRRGRIRIVNDMALKMLGMAKEDIIGYYMLSVLSLEDEFKLEEIQENNDSFLLDLNEEEGLIARVNFSTIVQETGFVTGYIAVLHDVTEQQQVERERREFVANVSHELRTPLTSMNSYIEALEEGAWKDEELAPQFLSVTREETERMIRLVNDLLQLSKMDNESDQINKEIIDFNMFINKIINRHEMSAKDTTFIRDIPKKTIFTEFDPDKMTQVFDNVITNAMKYSRGDKRVEFHVKQNPLYNRMTIRIKDNGIGIPINKVDKIFDRFYRVDKARTRKMGGTGLGLAISKEIVEAHNGRIWANSVEGQGTSIFITLPCEVIEDGDWDE | Member of the two-component regulatory system WalK/WalR that regulates genes involved in cell wall metabolism, virulence regulation, biofilm production, oxidative stress resistance and antibiotic resistance via direct or indirect regulation of autolysins. Functions as a sensor protein kinase which is autophosphorylated at a histidine residue in the dimerization domain and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of WalR. In turn, WalR binds to the upstream promoter regions of the target genes to positively and negatively regulate their expression. ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. By zinc. Zinc-binding negatively regulates WalK kinase activity and thus autophosphorylation. Forms homodimers. Forms homooligomers. Autophosphorylated. |
P27954 | RNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSSGLYHVTNDCPNSSIVYEAADAILHTPGCVPCVHEGNVSRCWVAMTPTVATRDGKLPTTQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRRHWTTQGCNCSI | Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Homooligomer (By similarity). Interacts with E1 (via C-terminus) (By similarity). Interacts with the non-structural protein 5A (By similarity). Interacts (via N-terminus) with host STAT1 (via SH2 domain); this interaction results in decreased STAT1 phosphorylation and ubiquitin-mediated proteasome-dependent STAT1 degradation, leading to decreased IFN-stimulated gene transcription (By similarity). Interacts with host STAT3; this interaction constitutively activates STAT3 (By similarity). Interacts with host LTBR receptor (By similarity). Interacts with host TNFRSF1A receptor and possibly induces apoptosis (By similarity). Interacts with host HNRPK (By similarity). Interacts with host YWHAE (By similarity). Interacts with host UBE3A/E6AP (By similarity). Interacts with host DDX3X (By similarity). Interacts with host APOA2 (By similarity). Interacts with host RXRA protein (By similarity). Interacts with host SP110 isoform 3/Sp110b; this interaction sequesters the transcriptional corepressor SP110 away from the nucleus (By similarity). Interacts with host CREB3 nuclear transcription protein; this interaction triggers cell transformation (By similarity). Interacts with host ACY3 (By similarity). Interacts with host C1QR1 (By similarity). Interacts with host RBM24; this interaction, which enhances the interaction of the mature core protein with 5'-UTR, may inhibit viral translation and favor replication (By similarity). Interacts with host EIF2AK2/PKR; this interaction induces the autophosphorylation of EIF2AK2 (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity). Forms a heterodimer with envelope glycoprotein E2 (By similarity). Interacts with mature core protein (By similarity). Interacts with protease NS2 (By similarity). The heterodimer E1/E2 interacts with host CLDN1; this interaction plays a role in viral entry into host cell (By similarity). Interacts with host SPSB2 (via C-terminus) (By similarity). Part of the viral assembly initiation complex composed of NS2, E1, E2, NS3, NS4A, NS5A and the mature core protein (By similarity). The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). The transmembrane regions of envelope E1 and E2 glycoproteins are involved in heterodimer formation, ER localization, and assembly of these proteins. Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The structural proteins, core, E1, E2 and p7 are produced by proteolytic processing by host signal peptidases (By similarity). The core protein precursor is synthesized as a 23 kDa, which is retained in the ER membrane through the hydrophobic signal peptide (By similarity). Cleavage by the signal peptidase releases the 21 kDa mature core protein (By similarity). The cleavage of the core protein precursor occurs between aminoacids 176 and 188 but the exact cleavage site is not known (By similarity). Some degraded forms of the core protein appear as well during the course of infection (By similarity). The other proteins (p7, NS2, NS3, NS4A, NS4B, NS5A and NS5B) are cleaved by the viral proteases (By similarity). Autoprocessing between NS2 and NS3 is mediated by the NS2 cysteine protease catalytic domain and regulated by the NS3 N-terminal domain (By similarity). Phosphorylated by host PKC and PKA. Ubiquitinated; mediated by UBE3A and leading to core protein subsequent proteasomal degradation. Highly N-glycosylated. Viral particle assembly takes place at the surface of ER-derived membranes in close proximity to lipid droplets. NS2 associates with E1/E2 glycoproteins, NS3 and NS5A, which interacts with the viral RNA and core protein to promote genome encapsidation. The nucleocapsid buds at the ER membrane where E1/E2 glycoproteins are anchored and afterward associate with nascent lipid droplet to acquire APOE and APOC. Secretion of viral particles is probably regulated by viroporin p7. Exerts viral interference on hepatitis B virus when HCV and HBV coinfect the same cell, by suppressing HBV gene expression, RNA encapsidation and budding. Belongs to the hepacivirus polyprotein family. The core gene probably also codes for alternative reading frame proteins (ARFPs). Many functions depicted for the core protein might belong to the ARFPs. |
A1ST25 | MKKNRLTHLKALEAESIQIMREVAAEFDNPVMLYSVGKDSSVLLHLARKAFYPGKIPFPLLHVDTNWKFKEMIAFRDNIAKKYDFDLLVHKNPRGMEMGISPFEHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERVYSFRDKKHRWDPKNQRPELWNIYNAKVDRGESIRVFPLSNWTELDIWQYIYQEDIEMVPLYFAKKRPVVERDGALIMVDDERMPLKEGEVPEMKMVRFRTLGCYPLTGAIESQATTLPEIIQEMLLTTTSERQGRVIDNDSAGSMEKKKMEGYF | With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD. ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3. Heterodimer composed of CysD, the smaller subunit, and CysN. Belongs to the PAPS reductase family. CysD subfamily. |
A1TTE9 | MASNFLTKLFGSRNDRLLKQYRKTVARINAMEPEYEKLSDDALRAKTVEFQGRVARGESLDDLLPEAFAVGREASKRVMKMRHFDVQLLGGMALHHGKISEMRTGEGKTLTATLPVYLNALGGKGVHVVTVNDYLANRDARWMGRLYNFLGLTVGINLPQMPREEKQAAYAADITYGTNNEYGFDYLRDNMVYEARDRVQRALNFAIVDEVDSILIDEARTPLIISGQAEDHTAMYIAMNKVVPLLVRQEGEADPRTGEGVTKPGDFTIDEKSHQVFLTEQGHETAERVLAAQGLIPEGASLYDPSHITLMHHLYAALRANHLYHRDQHYVVQNGEIVIVDEFTGRLMSGRRWSEGLHQAVEAKEGVEIQAENQTLASITFQNYFRLYSKLSGMTGTADTEAYEFQEIYGLETVVIPPNRPSKRDDQLDRVYKTTREKYEAAIQDIRECHERGQPVLVGTTSIENSEIIDDLLNKAGLPHQVLNAKQHAREADIVAQAGRAGMITIATNMAGRGTDIVLGGNIEKEVAAIEDDESLDEATKQARIAALREQWAADNEKVKALGGLRIIATERHESRRIDNQLRGRSGRQGDPGSSRFYLSLDDSLMRIFAGERVRAIMERLKMPDGEAIEAGIVTRSIESAQRKVEARNFDIRKQLLEYDDVANDQRKVIYQQRNEILDAADLSGVIAGMRESCLTDIVRQYVPEESVEEQWDLAGLEKALADEWQIRLPLQQEVESAQAITDGEILEKVVAAGNAAFQAKVDMVGPENFHQFQRAVLLQSFDSNWRDHLSALDYLRQGIHLRGYAQKQPKQEYKREAFELFRQLIDQVKNEVTRILLTVQVQSPSELDQAAEALESRAEQIANVTYTAPTETGEPETLPDPRTAGAGGDGLNLPEGVRIGRNDPCPCGSGKKYKQCHGKLA | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2. May bind 1 zinc ion per subunit. Monomer and homodimer. Part of the essential Sec protein translocation apparatus which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC. Distribution is 50-50. Belongs to the SecA family. |
B8H4E2 | MKIAEIRGMTPDQLADTLISLKKEQFNLRFQAATGQVEKTHRVNEIRKDIARIKTVLRAKAAA | Belongs to the universal ribosomal protein uL29 family. |
A3D475 | MNVSQDTIYAQASEHISDFQFDNRVAGVFSDMIRRSVPGYTQIINTIGDFADRFVMPNTQIYDLGCSLGAATLSIRRQIQGRQCRIIAVDNSESMVARCQENLNAYVSDTDVDLVCGDIRDIDIQNASLVVLNFTLQFLPPEDRETLIAKIYQGLNPGGILVLSEKIRFEDAPIQTLLEEQHLDFKRANGYSELEISQKRSALENVMKPDTLTTHQQRLTSQGFSHFSLWFQCFNFASMVAIK | Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM). prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O Homodimer. Belongs to the class I-like SAM-binding methyltransferase superfamily. Cx-SAM synthase family. |
Q6NWL2 | MNEPEGLRFRRLNRPHIITDETHEPQYKATSTYSGKVFRVTLLTMVAFLLLPLLVVVFVLESPIQPEVFSLNEPPLMTGCYEPNLKLRQAERLFEERLVGPESLANIGDVFYTGTADGKIVKIEGRNIHVLATIGKPPCGSREHEHTCGRPLGIRVGPNGTLFVADAYLGLFEVNPVTGEVKSLVSTEKRIAGRRLGFVNDLDVTQDGKKVYFTDSSSRWQRRDFMHLIMEATADGRVLEYDTETKEVNVMMENLRFPNGIQLFPDEESVLVAETTMARIKRVHVSGLNKGGMDTFIENLPGFPDNIRRSSSGGYWVAMSAVRPNPGFSMLDFLSQRPWLKKLIFKLFSQDTLLKFVPRYSLVVELQSDGTCVRSFHDPQGLVSAYSSEAHEYSGHLYLGSFRSPYLCKLDLSKV | Belongs to the strictosidine synthase family. |
P33161 | MSLSNKLPVTDVDLKGKRVLIRVDFNVPLDENKNVTNPQRIVGALPTIKYAIDNGAKAVVLMSHLGRPDGKVNPKYSLKPVVPVLEKLLGKSVTFAEDCVGPQTEETVNKASDGQVILLENLRFHAEEEGSSKDAEGKKVKADKADVDAFRKGLTALGDVYVNDAFGTAHRAHSSMVGVDLPQKAAGFLVKKELEYFAKALESPARPFLAILGGAKVSDKIQLIDNLLPKVNSLIITGGMAFTFKKTLENVKIGNSLFDEAGSKIVGEIVEKAKKYNVEIVLPVDYVTADKFSADATVGAATDATGIPDGYMGLDVGPESVKLYQKTIAEAKTILWNGPPGVFELKPFASATEATLDAAVKAAESGSIVIIGGGDTATVAAKYKVEDKISHVSTGGGASLELLEGKELPGVAALSSK | (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. Monomer. Belongs to the phosphoglycerate kinase family. |
A7FKN1 | MKQAVYVASPDSQQIHVWQLDSAGELTLLQTVDVPGQVQPMAISPNQRHLYVGVRPDFGIVSYHIADDGTLTAAGMAPLPGSPTHIDTDRQGRFLFSASYSFNCVSISPIDTHGVVQAPIQQLDDLPAPHSANIDPTNQILLVPCLKEDKVRLFDLSAEGQLTPHAQADITVAAGAGPRHMAFHPNHQVAYCVNELNSSVDVYQISNNGQEYHLVQSLDAMPADFTGTRWAADIHITPNGRYLYISDRTANLLGIFTVSEDGRVISLVGHHLTEAQPRGFNIDHSGNFLIASGQKSDHIEVYRIDQNTGELTTLKRYPVGKGPMWVSIRGAQNS | Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. |
P20850 | PGQLGNSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGPLGSPGLPGLPGPPGLPGMKGDRGVFGEPGPKGEQGASGEEGEAGVRGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGLPGVEGPRGPPGPRGVQGEQGATGLPGIQGPPGRAPTDQHIKQVCMRVVQEHFAEMAASLKRPDTGASGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPPGRGPKGLPGAIGLPGDPGPASYGKNGRDGEQGPPGVAGIPGVPGPPGPPGPPGFCEPASCTLQAGQRAFSKGPDK | Structural component of hyaline cartilage and vitreous of the eye. Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha 3(IX) chain. Each subunit is composed of three triple-helical domains interspersed with non-collagenous domains. The globular domain at the N-terminus of type IX collagen molecules represents the NC4 domain which may participate in electrostatic interactions with polyanionic glycosaminoglycans in cartilage. Covalently linked to the telopeptides of type II collagen by lysine-derived cross-links. Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Belongs to the fibril-associated collagens with interrupted helices (FACIT) family. |
A5GN71 | MTLSHGELLYEGKAKRIYASADDQQVLVEFKNDATAFNAQKKAQLEHKGRLNCQISACLFELLERHGIPTHYVGVADATWMVVQRVEVIPIEVVLRNTATGSLCRETPIPQGTALDPALLDLYYKDDALGDPLLTDARIALLGVVSAELRQRMEALARQVNAVLQPFFKDLGLQLVDFKLELGLNQAGELLVADEISPDTCRLWDLSSTDANERILDKDRFRKDLGGVIEAYGEVCKRVQGACPQPRNCG | 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2. Belongs to the SAICAR synthetase family. |
Q66L58 | MNTEKDFSPLTPNIVRALNDKLYEKRKVAALEIEKLVREFVAQNNSAQIRHVIQILATEFALSQHPHSRKGGLIGLAACSIALGKDSGLYLKELIDPVLTCFNDSDSRLRYYACEALYNIVKVARGAVLPHFNVLFDGLSKLAADPDPNVKSGSELLDRLLKDIVTESNKFDLVAFVPLLRERIYSNNQYARQFIISWIHVLESVPDINLLDYLPEILDGLFQILGDSSKEIRRMCELVLGEFLKEIKKNPSSVKFAEMANILVIHCQVSDESKSTNDLIQLTSMTWMREFIQLAGRVVLPYSSGILTAVLPCLSYDDRKKSTKEAASACNHSLMKLVTPEDDEDDEESQTKSSPPSDEAPSKKEGDLNDSLNESQESVGFSNISFFTPASSDRSAVTLDLDGIVQVLDRHLHDSSTGMMTRIAVLKWLYHLYIKTPRKMFKHTDSLFPMLLKTLSDESDEVILKDLEVLAEIASSPAGQTDTSGSCDISDSKTELHIPGSKMTDLSPSTPSMNSYFYKFMINLLKRFSLERKLLEMRGAFIIRQLCLLLHAENIFHSMADILLKEEDLKFASTMVQTLNTILLTSAELFQLRNQLKDLRTQESCALFCCLYRSWCHNPVATVSLCFLTQNYRHAYDLIQKFGDLEVTVDFLMEVDKLVQLIESPIFTYLRLQLLDVEHNPYLIKALYGLLMLLPQSQAFQLLSHRLSCVPNPELMRTLEDQKVAVKDKHLAQPHIDYSELLQHFDRVQSKHLEVRHQRTGRSEHPDRKLM | Scaffold protein component of the PI(3,5)P2 regulatory complex which regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Pentamerizes into a star-shaped structure and nucleates the assembly of the complex. The pentamer binds a single copy each of PIKFYVE and FIG4 and coordinates both PIKfyve kinase activity and FIG4 phosphatase activity, being required to maintain normal levels of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P). Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes. Forms pentamers. Component of the PI(3,5)P2 regulatory complex/PAS complex, at least composed of PIKFYVE, FIG4 and VAC14. VAC14 nucleates the assembly of the complex and serves as a scaffold by pentamerizing into a star-shaped structure, which can bind a single copy each of PIKFYVE and FIG4 and coordinates their activities. Interacts with NOS1. Mainly associated with membranes of the late endocytic pathway. The C-terminal domain (residues 523-782) mediates pentameric interactions and is necessary for the formation and maintenance of the PI(3,5)P2 regulatory complex. Belongs to the VAC14 family. |
Q66JN8 | MSVPPGSIIVSDWHRCPDSREFFSKILHKKRRRKFGLLEAPMMPPQMNVDLVRYKVFLSGKTGVGKSALAARLAGLDLPKMHYETTGIETTVVFWPVRLKESGRVLFFRFELWDCGESAMRRFDHMLLSCKEKVDAILFLFSFTDRGSFDDLTNQISRITEPSDRVVKLVVGTKFDLFMHTDVTESDVTHFQEVWGLPVFRVGGDVSAGLGEVAPLLNALAENLWHQDCMAASSVSISPQAALRETSSEIIV | Potential effector of the planar cell polarity signaling pathway. Plays a role in targeted membrane trafficking most probably at the level of vesicle fusion with membranes. Involved in cilium biogenesis by regulating the transport of cargo proteins to the basal body and to the apical tips of cilia. More generally involved in exocytosis in secretory cells (By similarity). Belongs to the small GTPase superfamily. Rab family. |
C3NH88 | MVELLGIIRIRGWAKAPWYINETLEMLRLRYNFNTMMYPKTSQILGMLNKVSPYVTWGEIDPDTLKLLIIKRLETAKGDKVSDSYVKEVLKIENIDTMVKQLYEGKIYLHKLDQYFKLPIRLHPPKGGFKGSVKRPYKNKGEFGYRGDKINELMRRMM | Part of the 50S ribosomal subunit. Belongs to the universal ribosomal protein uL30 family. |
Q57S29 | MLKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVAFDVVARYLRFLGYKLKYVRNITDIDDKIIKRANENGESFVALVDRMIAEMHQDFDALNILRPDSEPRATHHIQEIIELTRTLIEKGHAYVADNGDVMFDVPTDPTYGQLSRQDLEQLQAGARVDVVDVKRNPMDFVLWKMSKEGEPSWPSPWGEGRPGWHIECSAMNCKQLGNHFDIHGGGSDLMFPHHENEIAQSTCAHDGEYVNYWMHSGMVMVDREKMSKSLGNFFTVRDVLKYYDAETVRYFLMSGHYRSQLNYSEENLKQARASLERLYTALRGTDKSAAPAGGEAFEARFVEAMNDDFNTPEAYSVLFDMAREVNRLKGEDMTAANAMASHLRKISGVLGLLEQEPDVFLQSGAQADDGEVAEIEALIQQRLDARKAKDWAAADAARDRLAEMGIILEDGPQGTTWRRK | ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys) Binds 1 zinc ion per subunit. Monomer. Belongs to the class-I aminoacyl-tRNA synthetase family. |
B6S1P8 | MVKSHIGSWILVLFVAMWSDVGLCKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGTHGQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMHRYPNQVYYRPVDQYSNQNNFVHDCVNITVKEHTVTTTTKGENFTETDIKMMERVVEQMCITQYQRESQAYYQRGASVILFSSPPVILLISFLIFLIVG | Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity). Monomer and homodimer. Has a tendency to aggregate into amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Soluble oligomers may represent an intermediate stage on the path to fibril formation. Copper binding may promote oligomerization. Interacts with GRB2, APP, ERI3/PRNPIP and SYN1 (By similarity). Mislocalized cytosolically exposed PrP interacts with MGRN1; this interaction alters MGRN1 subcellular location and causes lysosomal enlargement (By similarity). Interacts with APP. Interacts with KIAA1191 (By similarity). Interacts with ADGRG6 (By similarity). Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. The normal, monomeric form has a mainly alpha-helical structure. The disease-associated, protease-resistant form forms amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Disease mutations may favor intermolecular contacts via short beta strands, and may thereby trigger oligomerization. Contains an N-terminal region composed of octamer repeats. At low copper concentrations, the sidechains of His residues from three or four repeats contribute to the binding of a single copper ion. Alternatively, a copper ion can be bound by interaction with the sidechain and backbone amide nitrogen of a single His residue. The observed copper binding stoichiometry suggests that two repeat regions cooperate to stabilize the binding of a single copper ion. At higher copper concentrations, each octamer can bind one copper ion by interactions with the His sidechain and Gly backbone atoms. A mixture of binding types may occur, especially in the case of octamer repeat expansion. Copper binding may stabilize the conformation of this region and may promote oligomerization. Variations in PRNP are responsible of transmissible bovine spongiform encephalopathies (BSE), a class of neurodegenerative diseases that affect various mammals. These diseases are caused by abnormally folded prion proteins. BSE can be subdivided into at least three groups: classical, H-type and L-type, with the latter 2 collectively referred to as atypical BSE. Susceptibility or resistance to a BSE disease can be influenced by at least 3 factors related to the host prion protein: protein expression levels, number of octapeptide repeats, and specific polymorphisms. In cattle, as in humans, BSEs can occur as infectious, spontaneous and genetic diseases. The heritable variant Lys-211 can be the cause of genetic late onset H-type BSE. Belongs to the prion family. |
A9AZL0 | MIASVRGVVQLIGQDQVVIDVHGVGLAIAVPRTVLATIGAIGDTAQLYTHLHVREDMLALFGFSSPAQRALFELLLGVSGIGPKVALALLSAATPEELQHAIAREDITMLSKVPGIGKKTAARLVLELKGKFGVATISPQLSTNPGLLALNTELIDILTSLGYSTTEAQAALNALPADAPADTEERLRLALQYFGGV | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. ATP + H2O = ADP + H(+) + phosphate Forms a complex with RuvB. Belongs to the RuvA family. |
Q0HN86 | MPWIQLRINTNSDDAETISDLLMEEGAVSITFEDGKDTPIFEPKLGETPLWQDTVVVALFEADTDLAPTIEMLKTLPFLGEHFSHKIEQIEDKDWVREWMDNYHPIQFGKRLWICPSWREVPDPSAVNVILDPGLAFGTGTHPTTALCLEWLDSLDLSNEEVIDFGCGSGILAVAALKLGAKKVTGIDIDYQAIEASKANAERNDVADQLALYLPEDQPADLKADVLVANILAGPLRELAPLIAERVKSGGKLALSGLLKEQAQEISDFYSQWFDMDEAAHKEDWSRLTGKRK | Methylates ribosomal protein L11. L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine Belongs to the methyltransferase superfamily. PrmA family. |
Q25381 | AEREIVRNIKEKLCYVALDFEQEMATPAASSSLEKSYELPDGQVITIGNERFRCPETLFQPAFIGMESAGIHETTYNSIMKCDIDIRKDLYANTVLSGGTSMYPGIADRMQKEITALAPSSMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Belongs to the actin family. |
Q1B6C7 | MRLYRDRAVVLRQHKLGEADRIVTLLTRDHGLVRAVAKGVRRTRSKFGARLEPFAHIDVQLHPGRNLDIVTQVQAIDAFASDIVSDYGRYTSACAVLETAERLAGEERAPMPALHRLTVGALRAVADGSRPRELVLDAYLLRAMGIAGWAPALTECARCATPGPHRAFHVAAGGSVCVHCRPSGSVTPPQAVLDLMSALHDGDWPAAEASTPSHRSQASGLVAAHLQWHLERQLRTLPLVERVYRVDHAVADHRISLLRQDVHRGDEPGDQLAAGS | Involved in DNA repair and RecF pathway recombination. Belongs to the RecO family. |
C4GPR7 | MDEKRLTHLRQLEAESIHIIREVAAEFGNPVMLYSIGKDSSVMLHLARKAFFPGHLPFPLLHVDTGWKFREMYEFRDHTVKEFGCELLVHRNPEGVAMGINPFVHGSAKHTDIMKTEGLKQALNKYGFDAAFGGARRDEEKSRAKERIYSFRDRFHRWDPKNQRPELWHNYNGQINKGESIRVFPLSNWTELDIWQYIFLEKIEIVPLYLAKPRPVVERDGMLLMVDDDRIDLQPGEVIVQKKVRFRTLGCWPLTGAVESEAETLPAIIEEMLISTTSERQGRMIDRDQSGSMELKKRQGYF | With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD. ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3. Heterodimer composed of CysD, the smaller subunit, and CysN. Belongs to the PAPS reductase family. CysD subfamily. |