PharMolix/UniProtQA huggingface dataset:
Protein: SYH_METM7
Sequence: MIMFQKPKGTRDFLPEEMKKRKVIEKKLRKVFDSYNFSEINTPTFESFELLSKKTGDEIRTQLFVFKDHGDREMGLRPELTSSVARFYINEFKNTPKPVKLYYFTNCFRYENPQAGRYREFWQMGSELIGSNKPIADAEVINMAIEGLKEINMDFEINIGHLGVLKGVFEKYDLSDDEGNEIRRLIDKEDMDGLKSALNRIESEKNIEISEKVFEVLDLKGGREVISKLKEKLAEFESSIAALENLDSILEFVPHEYIINFGIARGLDYYTGMVFEIYGKREGARQVCGGGRYDNLIELFEGEPSPAVGFAYGFDRIMLNIDDFEVEEESIFVVPVKSSDMLLNECLKIAKTLREAGKAVELDLMGRKLNKALNYANTKGIKKVIIVGENDILEGKVALKNMETGEQSLIELKDILTI
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: PRX4_PENRO
Sequence: MIPRWQPASIPLLLHLDTLRCHHVSVQPPRATMTSLNIKEEDIPRLDGKVVVISGGASGIGLAAANIFARAGAKIFLFDCNPPDSGEAPENSTFIKADITSWAELKAAFAQAGHVDIAVANAGVSEEQPYFEDTFDEQGELKEPGFAVVDVNFKGTVMFTKLAVSYMRKQGKGGSVVITASATGYAPEQNLPVYSAIKSGLVGLVRSLRSTLPRFDISINAVAPAATITKLLPMDIAGPLMAAGLPVSSAHMVGLAVVYSAVARQPRMVETYGKENVLDLESKWNGRTILTLGEHYTELEEKLADLRPVWFGWRNTDLTKKQQATADFR
What is the function of this protein?
Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin (PubMed:24239699, PubMed:27921136).  The first step of the pathway is catalyzed by the aristolochene synthase which performs the cyclization of trans,trans-farnesyl diphosphate (FPP) to the bicyclic sesquiterpene aristolochene (PubMed:8440737, PubMed:15186158, PubMed:24239699).  Following the formation of aristolochene, the non-oxygenated aristolochene is converted to the trioxygenated intermediate eremofortin B, via 7-epi-neopetasone (PubMed:24239699, PubMed:26274339).  This conversion appears to involve three enzymes, a hydroxysterol oxidase-like enzyme, the quinone-oxidase prx3 that forms the quinone-type-structure in the bicyclic nucleus of aristolochene with the C8-oxo group and the C-3 hydroxyl group, and the P450 monooxygenase ORF6 that introduces the epoxide at the double bond between carbons 1 and 2 (PubMed:24239699, PubMed:27921136).  No monoxy or dioxy-intermediates have been reported to be released to the broth, so these three early oxidative reactions may be coupled together (PubMed:24239699).  Eremofortin B is further oxidized by another P450 monooxygenase, that introduces a second epoxide between carbons 7 and 11 prior to acetylation to eremofortin A by the acetyltransferase ORF8 (PubMed:16345540, PubMed:24239699, PubMed:27921136).  The second epoxidation may be performed by a second P450 monooxygenase (PubMed:24239699).  After the acetylation step, eremofortin A is converted to eremofortin C and then to PR-toxin (PubMed:24239699).  First the conversion of eremofortin A to eremofortin C proceeds by oxidation of the side chain of the molecule at C-12 and is catalyzed by the short-chain oxidoreductase prx1 (PubMed:16345540, PubMed:24239699).  The cytochrome P450 monooxygenase ORF6 is probably also involved in this step (PubMed:27921136).  The primary alcohol formed at C-12 is finally oxidized by the short-chain alcohol dehydrogenase prx4 that forms PR-toxin (PubMed:16345540, PubMed:24239699).
What are the official names of this protein?
Short-chain dehydrogenase/reductase prx4, PR-toxin biosynthesis cluster protein 4.
What is the protein family that this protein belongs to?
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
What are the subcellular locations of this protein?
Membrane; Single-pass membrane protein.
Protein: HIS2_HALHL
Sequence: MSNAASERTAADTLRALAETIEQRRGASADTSYVARLHDKGLDAILKKVGEEATEAVIAAKGGEREQVVYETADLWFHTLVMLSASGVSVDEVLAELERRVGRSGLDEKAARGE
What are the official names of this protein?
Phosphoribosyl-ATP pyrophosphatase, PRA-PH.
What is the protein family that this protein belongs to?
Belongs to the PRA-PH family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: DBH_RHIME
Sequence: MNKNELVAAVADKAGLSKADASSAVDAVFETIQGELKNGGDIRLVGFGNFSVSRREASKGRNPSTGAEVDIPARNVPKFTAGKGLKDAVN
What is the function of this protein?
Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
What are the official names of this protein?
DNA-binding protein HRm.
What is the protein family that this protein belongs to?
Belongs to the bacterial histone-like protein family.
Protein: OXLAB_CERCE
Sequence: ADDKNPLEECFREADYEEFLEIAKVTVLEASERNDKEDWYANLGPMRLPEKLNEFVQETENGWYFIKYPVKPSEEGKSAGQLYEESLRKSAGQLYQESLGKAHDDIFAYEKRFDEIVDGMDKLPTSMYQAIQERINFKPPLPPKKYAMGAITTFTPYQFQHFSEALTAPVGR
What is the function of this protein?
Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:30647580).  Shows high specificity for L-Arg, L-Met, L-Phe, L-Leu, L-Tyr, L-Ile and L-Trp, low specificity for L-Val, L-Ala, L-Asn, L-Gln, and no specificity for L-Pro, L-Ser, L-Thr, L-Cys, L-Gly and L-Asp (PubMed:30647580).  Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation.  Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation.  These different effects are probably due to different experimental conditions.
What are the official names of this protein?
L-amino acid oxidase, CC-LAAO, LAO.
What is the protein family that this protein belongs to?
Belongs to the flavin monoamine oxidase family. FIG1 subfamily.
What are the subcellular locations of this protein?
Secreted.
Protein: METK_ALBFT
Sequence: MANDFLFTSESVSEGHPDKVADQISDAILDAIFKQDPKSRVAAETLCNTGLVVLAGEITTNAHVDYIQVARDTLKRIGYDNTEYGIDYKGCAVLVAYDKQSNDIAQGVDHASDDHLNTGAGDQGLMFGYACNETPELMPAPIYYAHRLVERQAQLRKDGRLPFLRPDAKSQITMHYVDGKPHSIDTVVLSSQHSPEMSNGLTMKPAFIEAVMEDIIKPVCPKEWLTADTKYLINPTGRFVVGGPQGDCGLTGRKIIVDTYGGACPHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLARQCQIQVAYAIGVAKPMNVTVYTEGTGVIPDDKIAELVHELFDLRPKGIIQMLDLLRPIYEKTAAYGHFGREEPEFTWERTDKAQALRAAAGL
What is the function of this protein?
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP.  The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
What are the official names of this protein?
S-adenosylmethionine synthase, AdoMet synthase, MAT, Methionine adenosyltransferase.
What is the protein family that this protein belongs to?
Belongs to the AdoMet synthase family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: LPL_ECOL6
Sequence: MTHIVRFIGLLLLNASSLRGRRVSGIQH
What is the function of this protein?
Involved in control of the biosynthesis of leucine.
What are the official names of this protein?
leu operon leader peptide, leu operon attenuator peptide.
Protein: LIPA_ALKMQ
Sequence: MNIKRKPEWLRIKLGEGRNLNYVKGLLKKFSLNTVCEEANCPNQIECFSKKTATFMILGSDCSRSCGFCNVSHGALQPIDPNEPENVANAVAELGLKHVVITSVTRDDLADGGAQHFADVVNQIKSKNKETMIEVLIPDFQGNKEALQKVVQSKPDIINHNMETIPRLYPEIRPKAEYVQSLELLKNVKEMDPEILTKSGVMVGLGEGEEELIEVFKDLRGSGCDFLTVGQYLPPSTKHYPLKAYISPEVFERYKEEALKIGFSFVASSPLVRSSYNAAEALEKHEEMKS
What is the function of this protein?
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
What are the official names of this protein?
Lipoyl synthase, Lip-syn, LS, Lipoate synthase, Lipoic acid synthase, Sulfur insertion protein LipA.
What is the protein family that this protein belongs to?
Belongs to the radical SAM superfamily. Lipoyl synthase family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: APOE_SHEEP
Sequence: MKVLWVALVVALLAGCQADMEGELGSEEPLPPEQPRGQDSQPWEQVLGRLWDYLRWVQTLSDQVQEELLNTQVIQELTVLMEETMKEVKAYREELEGQLAPMAQETQARVSKELQAAQARLGSDMEDLRNRLAQYRSEVQAMLGQSTEELRARMASHLRKLRKRLLRDADDLKKRLAVYQAGASEGAERSVSAIRERLRPLVEQSQSRAATLSTQVGQPLLDRAEAWRQKLHGRLEEVGVRAQDRLDKMRQQLEEVRSKVEEQGSQIRLQAEAFQARLRSWFEPLVEDMQRQWAGLVEKVQLALHLSPTSPPSENH
What is the function of this protein?
APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids.  APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance.  Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma.  As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL).  It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles.  Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells.
What are the official names of this protein?
Apolipoprotein E, Apo-E.
What is the protein family that this protein belongs to?
Belongs to the apolipoprotein A1/A4/E family.
What are the subcellular locations of this protein?
Secreted. Secreted, extracellular space. Secreted, extracellular space, extracellular matrix. Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans- dependent manner. Lipidation induces the release from the extracellular matrix.
Protein: NUP62_DROME
Sequence: MVFQLPTTTAAPTGGATSSFSFGLSTGTPAAAPASGAATTAPATKTTFSFGTPAPTAGIGGGDADNSKAQAPPAFGFGLGSGTASAPLTLGTQAAANPASTTSATATGTSAAPPAFGGFTAQPAASVVPTIATSAPNTAATTTGLLGGSGLGAPKTTAAASTTLTAAPSAIASTQGAAPAPTLSTGGAFANLTTETKTTDSSAVSTASQLSYHQLEEHINKWTLEFEEQEKVFTEQATQINAWDKLLISNNGKIVELNDAVKKVKTDQQVLDQELEFIATQQKELEDSLGPLEKEFVNLPRVDMERSQTYLMVENLDTQLKQMSEDLKEIIDNLNEANKGQDTTDPIIQIGKILNAHMNSLQWIESQSTNISKKLEDIGKIQDSQKRDIFRAPF
What is the function of this protein?
Essential component of the nuclear pore complex (By similarity).  The N-terminal is probably involved in nucleocytoplasmic transport (By similarity).  The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of Nup62 to the pore complex (By similarity).  Binds to transcriptionally active genes (PubMed:20144760).  Negatively regulates chromatin attachment to the nuclear envelope, probably by preventing chromatin tethering by Nup154 (PubMed:26341556).
What are the official names of this protein?
Nuclear pore glycoprotein p62, 62 kDa nucleoporin.
What is the protein family that this protein belongs to?
Belongs to the nucleoporin NSP1/NUP62 family.
What are the subcellular locations of this protein?
Nucleus. Chromosome. Nucleus envelope. Nucleus, nuclear pore complex. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Central region of the nuclear pore, within the transporter (By similarity). Associates with chromatin (PubMed:20144760).
Protein: REX_GEOSW
Sequence: MNNEQPKIPQATAKRLPLYYRFLKNLHASGKQRVSSAELSEAVKVDPATIRRDFSYFGALGKKGYGYNVNYLLSFFRKTLDQDEITEVALFGVGNLGTAFLNYNFTKNNNTKIVMAFDVDQKKVGKEVGGVPVYHLDELENRLHEGIPVAILTVPAPAAQWITDRLVQKGIKGILNFTPARLNVPKHIRVHHIDLAVELQSLVYFLTVDEHFSLQ
What is the function of this protein?
Modulates transcription in response to changes in cellular NADH/NAD(+) redox state.
What are the official names of this protein?
Redox-sensing transcriptional repressor Rex.
What is the protein family that this protein belongs to?
Belongs to the transcriptional regulatory Rex family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: GTF_ACTP7
Sequence: MENNIDLNVYFCFVNRPCTGGDFVNLDHVRTLRKLGINASILLAGNQSEEIVNSFGSLPVVILNEEIEFSSQDIFIVPEVMQVLYDLASKMTVFPRMIMHNQNPFYTGYGFLSAQHINEHRLERIIVPSSYTKYKLQEIGVTKPIDIIHPYIPDYFKPAEKQREVIQIAFSRRKRSAEFDIFKFYFLSLYSHKHSVNFVNIQGLTREEVAKVMSEAAIFISFAERESLGLMTLEAMASGCHVIGFSGYTDIYNNEVIDDSVGDWIGEGEYTLFAQKVCQAIDDFVNGKMNPKIENGLRLIEQRFRIRHFEQEVKRVYGNIFDYDLENSRS
What is the function of this protein?
Catalyzes the transfer of a glucose moiety from UDP-glucose to another glucose that is N-linked to an asparagine within a peptide or protein.  Can act in a repetitive manner, and this way it elongates the N-linked glucose by a glycan chain consisting of several alpha-1->6 linked glucose residues.  Is able to add up to six glucose units in vitro.  Cannot use UDP-Gal, UDP-GlcNAc or UDP-GalNAc as a substrate donor.
What are the official names of this protein?
Alpha-1,6-glucosyltransferase, alpha6GlcT, Polymerizing glucosyltransferase.
What is the protein family that this protein belongs to?
Belongs to the glycosyltransferase group 1 family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: ASIP_MACSY
Sequence: MDVTRLLLATLLVFLCFFTAYSHLPPEEKLRDDRSLRSNSSVNLLDFPSVSIVALNKKSKQISRKEAEKKRSSKKEASMKKVARPRTPLSAPCVATRDSCKPPAPACCDPCASCQCRFFRSACSCRVLSLNC
What is the function of this protein?
Involved in the regulation of melanogenesis.  The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment) (By similarity).
What are the official names of this protein?
Agouti-signaling protein, ASP, Agouti switch protein.
What are the subcellular locations of this protein?
Secreted.
Protein: CYCB_GEOSL
Sequence: MSRKVTKYSAVLAVSLFAAALAGCGSENKEGTVGTGPGGVATVGDSACVQCHSAVTEALTGESLIAQYQKSSPHNTAGLGCESCHGGGAQHNGVGPIPFAQPDASRCADCHDGTTAVATNSDTAFAESRHNIQTIRSGATCRRCHTHEGAVLSNIAGYTGDLATLEDTVNQNKVPLVSSYSQISCATCHEHGGGLRTIKATNGAAGPVVNWDPNNNRTVDQFDLCTSCHNMYSYNGSTLLTNGVPVNGVATGTVGHHETTWYRIIATTHFDNYSTGPQAGAGASGTNAKVEGYVLRRTGANPCFDCHGHEAKTNTRPGRDATIHTDWAKSAHAGGLLTAKYNAVGALTGAAAVNAAMNAYVDDTTAIAWTHYNWDASSRGSCQRCHTATGAANFMSNPAGYDPTGAGNSFSHLQGWSAANGSKQNELLYCWGCHTNAGTGELRNPGAITENYAGVNSTSTGTTGTAVTISYPDIAGSNVCMTCHLGREAGENIKAITDADGILGFVNSHYLAAGGQLFGKTGYEYATRSYAKPTFFAHDKIGTAAAPGTGTNGPCAGCHMTTPNSHSFLPVTKDGTGAVTAITSTACATCHAGAYALTPEALTAEEEEYVASLEALKAALAGKGILFFNAHPYFYRDTNANGIGDPGELVSSNAFTNWAGVYGLALWKDVMGAAFNANLLIHDPGGYAHNRFYVKRLIWDSIDFIYDGVLNNDVTAAIDAQVTATRLDSATATAAKAYLGTTRP
What is the function of this protein?
Involved in anaerobic respiration with Fe(3+) as terminal electron acceptor.  Acts as an electron-transport mediator in the dissimilatory reduction of Fe(3+).
What are the official names of this protein?
C-type polyheme cytochrome OmcB, Outer membrane c-type cytochrome B.
What are the subcellular locations of this protein?
Cell outer membrane; Lipid-anchor.
Protein: UP23_BOMMO
Sequence: ESKDPEDSXT
What are the official names of this protein?
Unknown protein 23 from 2D-PAGE.
Protein: FDH1_YEAST
Sequence: MSKGKVLLVLYEGGKHAEEQEKLLGCIENELGIRNFIEEQGYELVTTIDKDPEPTSTVDRELKDAEIVITTPFFPAYISRNRIAEAPNLKLCVTAGVGSDHVDLEAANERKITVTEVTGSNVVSVAEHVMATILVLIRNYNGGHQQAINGEWDIAGVAKNEYDLEDKIISTVGAGRIGYRVLERLVAFNPKKLLYYDYQELPAEAINRLNEASKLFNGRGDIVQRVEKLEDMVAQSDVVTINCPLHKDSRGLFNKKLISHMKDGAYLVNTARGAICVAEDVAEAVKSGKLAGYGGDVWDKQPAPKDHPWRTMDNKDHVGNAMTVHISGTSLDAQKRYAQGVKNILNSYFSKKFDYRPQDIIVQNGSYATRAYGQKK
What is the function of this protein?
Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide.  Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms (PubMed:9178506, PubMed:12144528, PubMed:11921099).  Has a role in the detoxification of exogenous formate in non-methylotrophic organisms (PubMed:11921099).
What are the official names of this protein?
Formate dehydrogenase 1, FDH, NAD-dependent formate dehydrogenase.
What is the protein family that this protein belongs to?
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: ASCH_ACREG
Sequence: MGLSLGYSPDRGSIGSWICAAPLILALFVISYRLFQSVIDYRLSHRNGCKPPPTYPHKDWYLGLHHVFGLLKAKKENRLPTAFSELFDASGPDVHTLGHYVLGKKSYWTRDPENIKAVLSSKFNDWGLPSARKATFRTCLGGGIFGVDGKEWEHSRAMLKPSFTRTQIGDTATLSKHADNLIARIPEGETVDLAELFPLLTMDVGTEMLFGESVGSLDPAEIKQATRFTTSFDYIVQTMSKHMALPILTKLRDKTLQGCVEFVDDFAADVVNRTIANESKTEKPSSLGKYIFPTELAKMGLPEKQIRIEVINIMVAGRDTTAALLSLIWWYLAKRPDAVMKLHQELEPLGGRPPTGEEVKKMKYLRNFVNEILRLHPINPLNSRTAAKDTTLPRGGGPDGKSPVFIRKGTQLMFSSAALQRRKDLYGEDALDLRPERWERIRPSAFEYIPFGGGPRICPGQQLALTEASYFTARLLQEFQGVTSESSGPFQEAFAILVTSGDGVKVKFHKKH
What is the function of this protein?
Cytochrome P450 monooxygenase; part of the asc-2 gene cluster that mediates the biosynthesis of ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis (PubMed:30952781, PubMed:35418536).  The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:30952781, PubMed:35418536).  Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B (PubMed:30952781, PubMed:35418536).  Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB (PubMed:30952781, PubMed:35418536).  The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group (PubMed:30952781, PubMed:35418536).  Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin (PubMed:30952781, PubMed:35418536).  The terpene cyclase ascF produces a monocyclic terpene, and the cyclization reaction is proposed to be initiated by protonation of the terminal epoxide of ilicicolin A epoxide to generate a monocyclic tertiarycation, which is followed by a series of hydride and methyl shifts with abstraction of proton, leading to the formation of the (14S,15R,19R)-trimethylcyclohexanone ring structure of ilicicolin C, which is finally reduced to ascochlorin by the dehydrogenase ascG (PubMed:30952781).  On the other hand, ilicicolin A epoxide is hydroxylated by the cytochrome P450 monooxygenase ascH, and the resultant product is cyclized by the terpene cyclase ascI to ascofuranol via protonation-initiated epoxide ring opening, which facilitates the 6-endo-tet cyclization to form the tetrahy-drofuran ring (PubMed:30952781, PubMed:35418536).  Finally, ascofuranol is oxidized into ascofuranone by ascJ (PubMed:30952781, PubMed:35418536).
What are the official names of this protein?
Cytochrome P450 monooxygenase ascH, Ascofuranone/ascochlorin biosynthesis clusters protein H.
What is the protein family that this protein belongs to?
Belongs to the cytochrome P450 family.
What are the subcellular locations of this protein?
Membrane; Single-pass membrane protein.
Protein: GRPE_STRZJ
Sequence: MAQDIKNEEVEEVQEEEVVETAEETTPEKSELDLANERADEFENKYLRAHAEMQNIQRRANEERQNLQRYRSQDLAKAILPSLDNLERALAVEGLTDDVKKGLGMVQESLIHALKEEGIEEIAADGEFDHNYHMAIQTLPADDEHPVDTIAQVFQKGYKLHDRILRPAMVVVYN
What is the function of this protein?
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE.  It is the nucleotide exchange factor for DnaK and may function as a thermosensor.  Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex.  GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle.  Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
What are the official names of this protein?
Protein GrpE, HSP-70 cofactor.
What is the protein family that this protein belongs to?
Belongs to the GrpE family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: NFUA_ACIB3
Sequence: MSTENTNTAVAEEIPNLLITPSAQEYLHELLAKQNTPGIGVRIFVEHPGTPRAECCMAYSAPEEVVPTDYKQDYPDFPAYIDAPSIPYLLDAVIDYNKDRFGGQLTFRAPNSKVPRVGPDASIEERITYVLQAEINPGLAGHGGNCSLVEVQDDPEHGLTAVLKFGGGCQGCSAIDVTLKQGVETTLKEHIPELQRVVDQTDHTQAEGAYFK
What is the function of this protein?
Involved in iron-sulfur cluster biogenesis.  Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins.  Could also act as a scaffold/chaperone for damaged Fe/S proteins.
What are the official names of this protein?
Fe/S biogenesis protein NfuA.
What is the protein family that this protein belongs to?
Belongs to the NfuA family.
Protein: FABH_STRP4
Sequence: MAFAKISQVAHYVPEQVVTNHDLAQIMDTNDEWISSRTGIRQRHISRTESTSDLATEVAKKLMAKAGITGKELDFIILATITPDSMMPSTAARVQANIGANKAFAFDLTAACSGFVFALSTAEKFIASGRFQKGLVIGSETLSKAVDWSDRSTAVLFGDGAGGVLLEASEQEHFLAESLNSDGSRSECLTYGHSGLHSPFSDQESADSFLKMDGRTVFDFAIRDVAKSIKQTIDESPIEVTDLDYLLLHQANDRILDKMARKIGVDRAKLPANMMEYGNTSAASIPILLSECVEQGLIPLDGSQTVLLSGFGGGLTWGTLILTI
What is the function of this protein?
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.  Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production.  Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities.  Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
What are the official names of this protein?
Beta-ketoacyl-[acyl-carrier-protein] synthase III, Beta-ketoacyl-ACP synthase III, KAS III, 3-oxoacyl-[acyl-carrier-protein] synthase 3, 3-oxoacyl-[acyl-carrier-protein] synthase III.
What is the protein family that this protein belongs to?
Belongs to the thiolase-like superfamily. FabH family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: RECA_STRP6
Sequence: MAKKLKKNEEITKKFGDERRKALDDALKNIEKDFGKGAVMRLGERAEQKVQVMSSGSLALDIALGAGGYPKGRIIEIYGPESSGKTTVALHAVAQAQKEGGIAAFIDAEHALDPAYAAALGVNIDELLLSQPDSGEQGLEIAGKLIDSGAVDLVVVDSVAALVPRAEIDGDIGDSHVGLQARMMSQAMRKLSASINKTKTIAIFINQLREKVGVMFGNPETTPGGRALKFYASVRLDVRGTTQIKGTGDQKDSSIGKETKIKVVKNKVAPPFKVAEVEIMYGEGISRTGELVKIASDLDIIQKAGAWFSYNGEKIGQGSENAKRYLAEHPELFDEIDRKVRVKFGLLEESEEESAMAVASEETDDLALDLDNGIEIED
What is the function of this protein?
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs.  It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
What are the official names of this protein?
Protein RecA, Recombinase A.
What is the protein family that this protein belongs to?
Belongs to the RecA family.
What are the subcellular locations of this protein?
Cytoplasm.