PharMolix/UniProtQA huggingface dataset:
Protein: DADD_METS3
Sequence: MTDNTILIKDALILNPLDFKEIKGSLLIKNDKIAEIGTDIDESNVDKVIDAKGKILLPGFVNTHTHLSMTLFRGLADDLSLDSWLNDNIWPMEANLTSEYCYIGALLGAIELIKSGTTTFSDMYFYMEDVAKAVEESGIRAVLSYGMIDFGDDEKREHEIKENIALFEKCNGMADGRIKVFFGPHSPYTASKDLLEDVRWLANEYNTGIHIHVSETQKEINDSLEAHDLRPFEYLDSIGFLGPDVVAAHSVWLSHNEIEIIKRNNVKISHNPCSNMKLASGIAPIQDLITNDICVGIGTDGASSNNNLDLIEELRTASLLQKVNLLNPKALTSNEALAMGTIKGAEVLGLEQEIGSIEVGKKADLILIDTNNANMVPDSSATSSNIIYSANGYNVDTTICDGKILMENRKLTTLDEEEIYKKARKAIEELKEASK
What is the function of this protein?
Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs.  Can also deaminate adenosine.  The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated.  Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions.  May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
What are the official names of this protein?
5'-deoxyadenosine deaminase, 5'-dA deaminase, 5'-methylthioadenosine deaminase, MTA deaminase, Adenosine deaminase, S-adenosylhomocysteine deaminase, SAH deaminase.
What is the protein family that this protein belongs to?
Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.
Protein: COXX1_PICTO
Sequence: MNKAYMYMNKLRAYFIYSKPQVWWLLVFIGLIGSILAINSFKSYLIILLLVALVANMTGSMGAEGLTNYIDRDMDSIMERTRNRPLPSGEISEKGAFLFGIILSLFSIFILLIFKRYLAALFMFLGLFDNVFIYSYLLKRRTPYSIILGGFSGAFPVLIGWYTVTDRFSWIPFILFFLVMFWIPVHVWSLAYKYRDDYYRAGVPMLPVVYSDRKTAVSISLSSMLLILFSVIPYFLGFFNYLYLLVILILSVPIVIYSVNFIKKPTKKASMRLFIYTAPYLTFVFFIVMIIHIIEIIK
What is the function of this protein?
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
What are the official names of this protein?
Protoheme IX farnesyltransferase 1, Heme B farnesyltransferase 1, Heme O synthase 1.
What is the protein family that this protein belongs to?
Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.
What are the subcellular locations of this protein?
Cell membrane; Multi-pass membrane protein.
Protein: TF3A_MOUSE
Sequence: MEPRVSVAEAVSSLTIADAFVGACEGPAPPRPALPSRFICSFPDCSASYNKAWKLDAHLCKHTGERPFVCDYEGCGKAFIRDYHLSRHVLIHTGEKPFVCADDGCNQKFNTKSNLKKHIERKHGNPQKQYVCSYEGCKKAFKKHQQLRTHQCQHTSEPLFRCTHEGCGKHFASPSRLKRHGKVHEGYLCQKGCSFMGKTWTELLKHMREAHKEDITCNVCQRMFKRRDYLKQHMKTHAPERDVYRCPRQGCGRTYTTVFNLQSHILSFHEEKRPFVCEHAGCGKTFAMKQSLMRHSVVHDPDKKRMKLKVRAPRERRSLASRLSGYFPPKRKQEPDYSLPNASAESSSSPEAQLPPPAALLTVC
What is the function of this protein?
Involved in ribosomal large subunit biogenesis.  Binds the approximately 50 base pairs internal control region (ICR) of 5S ribosomal RNA genes.  It is required for their RNA polymerase III-dependent transcription and may also maintain the transcription of other genes (By similarity).  Also binds the transcribed 5S RNA's (By similarity).
What are the official names of this protein?
Transcription factor IIIA, TFIIIA.
What are the subcellular locations of this protein?
Nucleus.
Protein: RLMKL_XANCB
Sequence: MKFFASCAKGLEYLLADELLALGASKATATISGVNVEGALRDAQRAVLWSRLASRVLWPLTEFDCPDEDALYAGVAELPWHEHLSTGHTLSVDAHVSGTAITHARYAAQRIKDAVVDTIRRQGLERPSVDVESPDLRLNLSLRKGRATISVDLGGGPLHRRGWRMAQNEAPLKENLAAAVLLRAGWPRAYADGGGLLDPMCGSGTLLIEGALMAADVAPGLQRYGSDIPSRWRGFDRDSWQQLVTEARERDSVGRAALKQVIHGSDMDPHAIRAAKENAQVAGVAEAIWFGVREVGDLQTRPQATGVVVCNPPYDERLAADAALYRKLGDTLQRVVPQWRASLLCGNAELAYATGLRAGKKYQLFNGAIECALIVCDPIAVPRRTPLAAPTALSEGAQMVANRLRKNLQKFKKWRAREGIECFRVYDADLPEYSAAIDVYQQADGDRRIFLHVQEYAAPATIPEADVRRRLGELLAAAREVFEVPAERVALKSRERGKGGSKYGRFEQRNEIVNVREHGALLRVNLFDYLDTGLFLDHRPLRGTMAQQSKGRRFLNLFCYTGVASVQAAVAGASATTSVDLSGTYLQWCADNLALNGQAGSKHKLVQADALAWLEAERAHFDVIFCDPPTFSNSARAEDFDIQREHVRLLRAAVARLAPGGVLYFSNNFRRFKLDEEAVAEFAQCEEISPRTIDPDFERHVRIHRAWRLTA
What is the function of this protein?
Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA.
What are the official names of this protein?
Ribosomal RNA large subunit methyltransferase K/L.
What is the protein family that this protein belongs to?
Belongs to the methyltransferase superfamily. RlmKL family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: TRPB1_SULTO
Sequence: MVNKDLIPKYWYNIIPDLPKPLPPPRDPPDAEFSRIELLKKILPKEVLRQQFTIERFIKIPEEVRDRYAIIGRPTPLMRAKRLEEYLDTPAKIYFKFEGATPTGSHKINTAVPQAYFAAEEGISHVVTETGAGQWGTAVALAASMYDLSSTIFMVRVSYEQKPMRKTIMELYGGKVYASPTDLTEFGRKILKENPNHPGSLGIAMSEAIEFALNHNFRYLVGSVLDVVLLHQSVIGMEAIAQLDELGEEPDILIGCVGGGSNFGGFTYPFIGAKKGKKYIAVGAAEIPKFSTGKYEYDYPDTAGLLPLVKMITLGKDYVPPPIYAGGLRYHGVAPTLSLLIKEKIVEWREYKEEEIYEAAKIFMKTQGIVPAPESAHAIKAVIDEALKAKTEKERRVIVFNLSGHGLLDLGNYESIRRRVEK
What is the function of this protein?
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
What are the official names of this protein?
Tryptophan synthase beta chain 1.
What is the protein family that this protein belongs to?
Belongs to the TrpB family.
Protein: RL4_CHRVO
Sequence: MELNVINTQGKAVGSLQVSDALFGREYNEALVHQVVTAFLANARSGNRAQLTRAEVKHSTKKPFRQKGTGNARAGMTSTPNRRGGGRAFPNKPDENFTQKVNRKMYRAGIATILSQLVRDERLIVVDDLSVASPKTKEFVGAVQPMGLEQALFITNELSENLYLSSRNLPNMLVIEAVQADPYSLLRFKKTVITRDAVKQLEEQWA
What is the function of this protein?
Forms part of the polypeptide exit tunnel.
What are the official names of this protein?
50S ribosomal protein L4.
What is the protein family that this protein belongs to?
Belongs to the universal ribosomal protein uL4 family.
Protein: PSBB_GNEPA
Sequence: MGLPWYRVHTVVLNDPGRLIAVHIMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFILPFMTRLGIKESWGGWSITGESAVNPGLWSYEGVAGAHIVFSGLCFLSAIWHWVYWDLEIFSDPRTGKPSLDLPKIFGIHLFLSGVACFGFGAFHVTGLYGPGIWVSDPFGLTGRIQPVSPAWGAEGFDPFVPGGIASHHIAAGLLGIIAGLFHLSVRPPQRLYRGLRMGNIETVLSSSIAAVFFAAFIVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIDRRVRAGLTEKLSLSEAWSRIPEKLAFYDYIGNNPAKGGLFRAGAMDNGDGIAVGWLGHPIFRDKEGNELFVRRMPTFFETFPVVLVNKEGIVKADVPFRRSESKYSVEQVGVTVEFYGGELNGVSFSDPAIVKKYARRAQLGEIFELDRATLKSDGVFRSSPRGWFTFGHATFALLFFFGHIWHGARTLFRDIFAGIDPELDAQVEFGAFQKLGDPTTKRQVV
What is the function of this protein?
One of the components of the core complex of photosystem II (PSII).  It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII.  PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
What are the official names of this protein?
Photosystem II CP47 reaction center protein, PSII 47 kDa protein, Protein CP-47.
What is the protein family that this protein belongs to?
Belongs to the PsbB/PsbC family. PsbB subfamily.
What are the subcellular locations of this protein?
Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Protein: GREA_CERS5
Sequence: MEKIPMTRAGFAALDDELKLLKTVERPAVIRAIAEAREHGDLSENAEYHAAREKQSFIEGRIKELEALLSLAEVIDPARLSGSIKFGATVTILDEETEEEKTYQIVGEAEADIENGLLNIKSPLARALIGKDEGDSIEVKTPGGERGYEVVSVRFV
What is the function of this protein?
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites.  The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes.  Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus.  GreA releases sequences of 2 to 3 nucleotides.
What are the official names of this protein?
Transcription elongation factor GreA, Transcript cleavage factor GreA.
What is the protein family that this protein belongs to?
Belongs to the GreA/GreB family.
Protein: INS_CHLAE
Sequence: MALWMRLLPLLALLALWGPDPVPAFVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDPQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYCN
What is the function of this protein?
Insulin decreases blood glucose concentration.  It increases cell permeability to monosaccharides, amino acids and fatty acids.  It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
What are the official names of this protein?
Insulin.
What is the protein family that this protein belongs to?
Belongs to the insulin family.
What are the subcellular locations of this protein?
Secreted.
Protein: BACE1_HUMAN
Sequence: MAQALPWLLLWMGAGVLPAHGTQHGIRLPLRSGLGGAPLGLRLPRETDEEPEEPGRRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYNIPQTDESTLMTIAYVMAAICALFMLPLCLMVCQWRCLRCLRQQHDDFADDISLLK
What is the function of this protein?
Responsible for the proteolytic processing of the amyloid precursor protein (APP).  Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase (PubMed:10656250, PubMed:10677483, PubMed:20354142).  Cleaves CHL1 (By similarity).
What are the official names of this protein?
Beta-secretase 1, Aspartyl protease 2, ASP2, Asp 2, Beta-site amyloid precursor protein cleaving enzyme 1, Beta-site APP cleaving enzyme 1, Memapsin-2, Membrane-associated aspartic protease 2.
What is the protein family that this protein belongs to?
Belongs to the peptidase A1 family.
What are the subcellular locations of this protein?
Cell membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network. Endoplasmic reticulum. Endosome. Cell surface. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane raft. Lysosome. Late endosome. Early endosome. Recycling endosome. Cell projection, axon. Cell projection, dendrite. Note=Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (PubMed:17425515, PubMed:11466313). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (PubMed:15886016).
Protein: IFNT_CEREL
Sequence: MAFVLSLLMALVLASYSPGGSLGCDLSQNHVLLGRQNLKLLGQMTRLSPRFCLQDRKDFGLPQEMVEGGQLQKDQAISVLHEMLQQCFNLFHTERSSAAWDTTLLEQLRTGLHQQLDDLDACLGQVMGKEDSDLRRMGPTLTVKKYFQGIHVYLQEKEYSDCAWEIVQVEMMRALSSISRLQKRLRKMGGDLNSP
What is the function of this protein?
Paracrine hormone primarily responsible for maternal recognition of pregnancy.  Interacts with endometrial receptors, probably type I interferon receptors, and blocks estrogen receptor expression, preventing the estrogen-induced increase in oxytocin receptor expression in the endometrium.  This results in the suppression of the pulsatile endometrial release of the luteolytic hormone prostaglandin F2-alpha, hindering the regression of the corpus luteum (luteolysis) and therefore a return to ovarian cyclicity.  This, and a possible direct effect of IFN-tau on prostaglandin synthesis, leads in turn to continued ovarian progesterone secretion, which stimulates the secretion by the endometrium of the nutrients required for the growth of the conceptus.  In summary, displays particularly high antiviral and antiproliferative potency concurrently with particular weak cytotoxicity, high antiluteolytic activity and immunomodulatory properties.  In contrast with other IFNs, IFN-tau is not virally inducible.
What are the official names of this protein?
Interferon tau, IFN-tau, Antiluteolysin, Trophoblast antiluteolytic protein, Trophoblast protein 1, TP-1, Trophoblastin.
What is the protein family that this protein belongs to?
Belongs to the alpha/beta interferon family. IFN-alphaII subfamily.
What are the subcellular locations of this protein?
Secreted. Note=Secreted into the uterine lumen.
Protein: SYH_WOLSU
Sequence: MKEQALITPRTLSGFKDRLPQEAMAKSRLLRTVSEVFEGFGFVPIETPHLEYAEILVKQGSDEIQKELYRFFDHGGRDVALRFDQTVPLARFISQHRNALGLPFKRYAIGNVFRGERAQRGRYREFTQCDFDFIGSESIGSDAEIIQVIYASLKALGIERFTISMNNRKILNGICDYFGVKEQTSDVLRIIDKLDKIGEESVIKELVEELGLSQESARGILGFTSLKQERSSEEFFAKVASYEGLSDSLREGMGEMRALYAILDTLEMDRACYKINFSIARGLGYYTGIVYETTLDALPSIGSVCSGGRYDNLTQSFSKERMSGVGASIGVDRLLAALEELGLLEGRGTSAQVLVACMEESQLAYSYKVAERLRTLGIKSEVYPEAVKPKRSLAYANSKGHPYVAVIGEDELKQGVVTLKDMQWGDQKPCISIEAAAEILLG
What are the official names of this protein?
Histidine--tRNA ligase, Histidyl-tRNA synthetase, HisRS.
What is the protein family that this protein belongs to?
Belongs to the class-II aminoacyl-tRNA synthetase family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: CSPA_MYCTU
Sequence: MPQGTVKWFNAEKGFGFIAPEDGSADVFVHYTEIQGTGFRTLEENQKVEFEIGHSPKGPQATGVRSL
What are the official names of this protein?
Probable cold shock protein A.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: NCAP_I73A3
Sequence: MASQGTKRSYEQMETDGERQNATEIRASVGKMIDGIGRFYIQMCTELKLSDYEGRLIQNSLTIERMVLSAFDERRNRYLEEHPSAGKDPKKTGGPIYKRVDGKWMRELVLYDKEEIRRIWRQANNGDDATRGLTHMMIWHSNLNDTTYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELIRMIKRGINDRNFWRGENGRKTRGAYERMCNILKGKFQTAAQRAMMDQVRESRNPGNAEIEDLIFLARSALILRGSVAHKSCLPACVYGPAVASGYNFEKEGYSLVGIDPFKLLQNSQVYSLIRPNENPAHKSQLVWMACNSAAFEDLRLLSFIRGTKVSPRGKLSTRGVQIASNENMDTMESSTLELRSRYWAIRTRSGGNTNQQRASAGQISVQPAFSVQRNLPFDKSTIMAAFTGNTEGRTSDMRAEIIRMMEGAKPEEVSFRGRGVFELSDEKATNPIVPSFDMSNEGSYFFGDNAEEYDN
What is the function of this protein?
Encapsidates the negative strand viral RNA, protecting it from nucleases.  The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication.  The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex.  NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway.  Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins.  It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export.  M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals.  Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein.  Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.
What are the official names of this protein?
Nucleoprotein, Nucleocapsid protein, Protein N.
What is the protein family that this protein belongs to?
Belongs to the influenza viruses nucleoprotein family.
What are the subcellular locations of this protein?
Virion. Host nucleus.
Protein: PHF23_RAT
Sequence: MLEAMAEPSPEDPPPTLKPETQPPEKRRRTIEDFNKFCSFVLAYAGYIPPSKGAPDSATLLEKMKLKDSLFDLDGPKVASPLSPTSLTSRPPAALTPVPLSQGDLSQPRKKDRKNRKLGPGGGAGFGVLRRPRPAPGDGEKRSRIKKSKKRKLKKADRGDRLPPPGPPRAPPSDTDSEEEEEEEEEEDDEEETTVVGGGGVPAPVLPTPPEAPRPPVTVHPEGAPPTDSEGKDAGSTETSQDGDGSSSEGEMRVMDEDIMVESGDDSWDLITCYCRKPFAGRPMIECSLCGTWIHLSCAKIKKTNVPDFFYCQKCKELRPEARRLGGLPKSGEP
What is the function of this protein?
Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria.
What are the official names of this protein?
PHD finger protein 23, PDH-containing protein JUNE-1.
What is the protein family that this protein belongs to?
Belongs to the PHF23 family.
What are the subcellular locations of this protein?
Nucleus. Cytoplasm. Note=Mainly present in the nucleus and part in the cytoplasm.
Protein: MOT9_HUMAN
Sequence: MELKKSPDGGWGWVIVFVSFLTQFLCYGSPLAVGVLYIEWLDAFGEGKGKTAWVGSLASGVGLLASPVCSLCVSSFGARPVTIFSGFMVAGGLMLSSFAPNIYFLFFSYGIVVGLGCGLLYTATVTITCQYFDDRRGLALGLISTGSSVGLFIYAALQRMLVEFYGLDGCLLIVGALALNILACGSLMRPLQSSDCPLPKKIAPEDLPDKYSIYNEKGKNLEENINILDKSYSSEEKCRITLANGDWKQDSLLHKNPTVTHTKEPETYKKKVAEQTYFCKQLAKRKWQLYKNYCGETVALFKNKVFSALFIAILLFDIGGFPPSLLMEDVARSSNVKEEEFIMPLISIIGIMTAVGKLLLGILADFKWINTLYLYVATLIIMGLALCAIPFAKSYVTLALLSGILGFLTGNWSIFPYVTTKTVGIEKLAHAYGILMFFAGLGNSLGPPIVGWFYDWTQTYDIAFYFSGFCVLLGGFILLLAALPSWDTCNKQLPKPAPTTFLYKVASNV
What is the function of this protein?
Extracellular pH-and Na(+)-sensitive low-affinity creatine transporter (PubMed:31784090).  Functions also as a pH-independent carnitine efflux transporter (PubMed:21886157).
What are the official names of this protein?
Monocarboxylate transporter 9, MCT 9, Solute carrier family 16 member 9.
What is the protein family that this protein belongs to?
Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family.
What are the subcellular locations of this protein?
Cell membrane; Multi-pass membrane protein.
Protein: MURA_METRJ
Sequence: MDRIHITGGAPLNGVIPISGAKNAALPLMIASLLTGETLELINVPRLADIAALTRILGNHGVDHMVVGKRPGQTTETGQTIRLTASNVIDTTAPYELVSTMRASFWVVAPLLARFGEAKVSLPGGCAIGTRPVDLLIMALERLGAEIEIDAGYVVARTKNGLRGAEIAFPKVTVGGTHVALMAAALAYGTTVLENAAREPEVVDLAECLNKMGAKIRGAGTPRIEIEGVARLNGARHEVLPDRIETGTYAMAVAMAGGDVVLKDTRADLLHSALDVLSTTGAEITQVEGGIRVRRNGGGIAAVDITTDPFPGFPTDLQAQFMALMTLAKGQSHIRETIFENRFMHVQELARLGAKIRLEGDLAIVEGVDRLKGAPVMATDLRASVSLVIAGLAAEGETQINRVYHLDRGFEALEAKLGRCGAQIERVRA
What is the function of this protein?
Cell wall formation.  Adds enolpyruvyl to UDP-N-acetylglucosamine.
What are the official names of this protein?
UDP-N-acetylglucosamine 1-carboxyvinyltransferase, Enoylpyruvate transferase, UDP-N-acetylglucosamine enolpyruvyl transferase, EPT.
What is the protein family that this protein belongs to?
Belongs to the EPSP synthase family. MurA subfamily.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: TRT3_ASPTN
Sequence: MTIPFSPNPEQINVSSVPATQAEVQVEYTLRTKSDAIEHTSQSNRLKDLAKDPWLRTTGNRHASSGTEIPSSEQTKSARILVVGAGYGGLLFAVRLLQSGFSLGDILLVDAAGGFGGTWYWNRYPGLMCDIESYIYMPLLEETGHIPSRKYVPGEELRGHAERIAEKWKLHTQTLFRTTISCLTWDENKTQWIATASQSNSESQESNSFVISADFAILANGTLSKPKIPDLPGVDDFAGHVFHTARWDYDYTGGSPSIPVMDRLKTKRVGVIGTGSTAVQVIPQLARWAGELTVFQRTPVAVGLQENQETDRIWWSEEIDKVGPGWQRKRCENFNAFITDTRQEKLEEVMKEDKVQDGWTRFPSFSAAIGGAHNLQPDFLQLVVKVDEERQKTARQHIKSTVHDPATAEALLNSTYSWCKRPCFHQGYYETYNLPHVKLVNTAGEGVTELTRGGVLLDGKEYELDLIVLATGYDIGSLCPADRAQISVRGRKGHLMNQKWAAGPATFHGVMTRDFPNLFFPGTSQAGVTANQSYMFDRAAEHVSYIIRQAYNHVAAGFANPKVCVEPSQEAEDWWTMETVARAKAFAATKICSSGSYTISARSGGSGNVEKTARHMPWGEGMASYVKILEEWRKKGHMDGLEIAWKGT
What is the function of this protein?
FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of terretonin, a fungal meroterpenoid that acts as a mycotoxin (PubMed:22549923, PubMed:23116177, PubMed:25671343).  The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase trt4 (PubMed:22549923, PubMed:23116177).  DMOA is then prenylated into farnesyl-DMOA by the polyprenyl transferase trt2 (PubMed:22549923, PubMed:22782788, PubMed:23116177).  Methylation by the methyltransferase trt5 then leads to farnesyl-DMOA methyl ester which is further subject to epoxidation by the FAD-dependent monooxygenase trt8 to yield epoxyfarnesyl-DMOA methyl ester (PubMed:22549923, PubMed:22782788, PubMed:23116177).  Cyclization of epoxyfarnesyl-DMOA methyl ester by the terpene cyclase trt1 leads to a tetracycle intermediate which is in turn converted to preterretonin (PubMed:22549923, PubMed:22782788, PubMed:23116177).  Dehydrogenase trt9 comes next to transform preterretonin to preterrenoid (PubMed:22549923, PubMed:23116177).  The FAD-dependent monooxygenase trt3 is then required for the C-hydroxylation at C16 of preterrenoid to yield terrenoid (PubMed:22549923, PubMed:23116177).  The cytochrome P450 trt6 catalyzes three successive oxidations to transform terrenoid into an unstable intermediate, which then undergoes the D-ring expansion and unusual rearrangement of the methoxy group to afford the core skeleton of terretonin (PubMed:25671343, PubMed:28759016).  Trt14 catalyzes the D-ring expansion of terretonin involving intramolecular methoxy rearrangement as well as the hydrolysis of the expanded D-ring and the methyl ester moiety (PubMed:25671343, PubMed:28759016).  Finally, the nonheme iron-dependent dioxygenase trt7 accomplishes the last two oxidation reactions steps to complete the biosynthesis of terretonin (PubMed:25671343).  Terretonin C is produced via spontaneous decarboxylation of the terretonin precursor (PubMed:23116177).  Another shunt product of the terretonin biosynthesis is dihydrofarnesyl-DMOA, derived from epoxyfarnesyl-DMOA through hydrolysis of the epoxide (PubMed:22549923, PubMed:22782788, PubMed:23116177).
What are the official names of this protein?
FAD-binding monooxygenase trt3, Terretonin synthesis protein 3.
What is the protein family that this protein belongs to?
Belongs to the FAD-binding monooxygenase family.
Protein: BIOD_CHRSD
Sequence: MTTYFVTGTDTDAGKTLVASGLLALARRRGLTTLGLKPVASGCESTTEGLRNIDALTLQAQSMPTPPYATLNPYAYAPAIAPHLAARRAGRIPTLDALVAHVADPLAEKRDLTLIEGAGGWRVPLNDDEDLAGLAVRLELPVILVVGLELGCLNHARLSAEAIRADGLPLAGWVGNLIDPGLSFDEVADEACYRDNLATLERTLEAPCLGIVPRLAAATPDARAHAAADYLTLPGDA
What is the function of this protein?
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
What are the official names of this protein?
ATP-dependent dethiobiotin synthetase BioD, DTB synthetase, DTBS, Dethiobiotin synthase.
What is the protein family that this protein belongs to?
Belongs to the dethiobiotin synthetase family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: ENO_HALWD
Sequence: MTQITNVSLRRILDSRGNPTVEADVLTQSGGFGRAAAPSGASTGEYEAIELDPAEAIASARDHVAPRLIDTVHAGNQREVDAALHAADGTDNFSQIGANSAVAISMAAAKAGADVLGAPVYQHLGGTFRGESFPTPLGNVVGGGEHAKEATHIQEFLSAPIGAPNVSEAVFANAAVHARVSEILDERGIPAAKGDEGAWAPPISDAEAFSLVNDAVADVEDDLGFEIRFGLDMAAAELYDDDVGGYVYGDEVKSTTEQVEYVAEMIAEYNLVYVEDPLDENDYDGFATLTERVGDQTLICGDDLFVTSVERLQTGIDADAANSILIKPNQIGTLTDAFDAIELAREHGYETVVSHRSGETEDVTIAHLAVATDAGFIKTGTVQGERTAKLNELIRIAEDAV
What is the function of this protein?
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate.  It is essential for the degradation of carbohydrates via glycolysis.
What are the official names of this protein?
Enolase, 2-phospho-D-glycerate hydro-lyase, 2-phosphoglycerate dehydratase.
What is the protein family that this protein belongs to?
Belongs to the enolase family.
What are the subcellular locations of this protein?
Cytoplasm. Secreted. Cell surface. Note=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.
Protein: SYK_MANSM
Sequence: MSEQQNAELDFHGEMAVRREKLAALRAKGNAFPNTFRRDALAQDLHNQYDETDGEQLKEKDLHVAVAGRIMTRRTMGKATFITIQDMSGKIQLYVARDNLPEGVYGEDVKSWDLGDIVGIKGTLFKTKTNELTVKAHEVQLLTKALRPLPDKFHGLSDQETRYRQRYLDLISNEESRRTFVIRSKVIAGIREYFIGKGFIEVETPMLQVIPGGAAARPFVTHHNALDIDMYLRIAPELYLKRLVVGGFERVFELNRNFRNEGVSVRHNPEFTMIEYYQAYADYHDLMDNTEELLRKLALDILGTTIVPYGEYEFDFGKPFERITMHDAVIKYGAEKGIVKEDLYDLDRAKAAAAKLGIEIQKSWGLGSIVNAIFEEVAEHHLIQPTFLMAHPAEISPLARRNDENPEVTDRFELFIGGREIGNGFSELNDAEDQAERFDAQVAAKDAGDDEAMFKDDDFVTALEHGLPPTAGEGLGIDRLAMLFANAPSIRDVILFPAMKHKG
What are the official names of this protein?
Lysine--tRNA ligase, Lysyl-tRNA synthetase, LysRS.
What is the protein family that this protein belongs to?
Belongs to the class-II aminoacyl-tRNA synthetase family.
What are the subcellular locations of this protein?
Cytoplasm.