PharMolix/UniProtQA huggingface dataset:
Protein: ARMD2_ARMGA
Sequence: MGSSSRVGDENSLLDLTEKVAVVTGANSGIGLYILFHVARAGAKVYLGARTEAKFNSAITRLKTEGLDTSKVVWLPFDLSDPRKAKESAKWLLERENRLDILINNAAKILGPYAQTSDGLSDSMVINHMSPYLFTKTLLPLLESTARQPGSDVRIVNVSSVAHRWVPNPRYDSLEAFNNNFADTWKPKTNLYGYTKLANVLWTKELQRSFDRANIPILAMTVHPGNVMSEGNVKLFTSLMFGTIINWVFSLFFISPFDGGYTPAFAAASRVIAEDRRKYAGAYIVPFGVIEEASEDARREDLAKDLLATTDAVLKQYDYA
What is the function of this protein?
Short-chain dehydrogenase/reductase, part of the gene cluster that mediates the biosynthesis of melleolides, a range of antifungal and phytotoxic polyketide derivatives composed of an orsellinic acid (OA) moiety esterified to various sesquiterpene alcohols (Probable).  The first step in melleolides biosynthesis is performed by the delta(6)-protoilludene synthase PRO1 which catalyzes the cyclization of farnesyl diphosphate to protoilludene (PubMed:21148562).  The orsellinic acid synthase armB produces OA by condensing acetyl-CoA with 3 malonyl-CoA units in a three-round chain elongation reaction folowed by a C2-C7 ring closure (By similarity).  ArmB further catalyzes the trans-esterification of OA to the various sesquiterpene alcohols resulting from the hydroxylation of protoilludene (By similarity).  The melleolides cluster also includes 5 cytochrome P450 monooxygenases, 4 NAD(+)-dependent oxidoreductases, one flavin-dependent oxidoreductase, and one O-methyltransferase (By similarity).  The cytochrome P450 monooxygenases may be involved in protoilludene hydroxylation to elaborate melleolides with multiple alcohol groups, such as melleolide D, which carries alcohol functionalities at C-4, C-5, C-10, and C-13 (By similarity).  The role of the NAD(+)-dependent enzymes remains unknown (By similarity).  Numerous melleolides, including arnamial, show 5'-O-methylation of the aromatic moiety which may be catalyzed by the methyltransferase encoded in the cluster (By similarity).  The flavin-dependent oxidoreductase might represent the dehydrogenase yielding the aldehyde in position 1 of arnamial and other melleolides (By similarity).  Finally, several halogenase localized outside of the cluster, are able to catalyze the transfer of a single chlorine atom to the melleolide backbone, resulting in a 6'-chloromelleolide product (By similarity).
What are the official names of this protein?
Short-chain dehydrogenase/reductase ARMGADRAFT_1169971, Melleolides biosynthesis cluster protein ARMGADRAFT_1169971.
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; Multi-pass membrane protein.
Protein: SYE1_THEP1
Sequence: MVRVRFAPSPTGHLHVGGARTALFNWMFARKEGGKFILRIEDTDTERSSREYEQQILESLRWCGLDWDEGPDIGGDFGPYRQSERLEIYREYAEKLVEDKRAYYVVYDKEDPSKELFTTYEYPHEYKEKGHPVTIKFKVLPGKTSFEDLLKGYMEFDNSTLEDFIIMKSNGFPTYNFAVVVDDHLMRISHVFRGEDHLSNTPKQLMIYEAFGWEAPVFMHIPLILGSDRTPLSKRHGATSVEHFRREGILSRALMNYLALLGWRVEGDEIFTIEEKLQSFDPKDISNKGVIFDYQKLEWVNGKHMRRIDLEDLKREFIEWAKYAGKEIPSVDERYFSETLRICREKVNTLSQLYDIMYPFMNDDYEYEKDYVEKFLKREEAERVLEEAKKAFKDLNSWNMEEIEKTLRDLSEKGLASKKVVFQLIRGAVTGKLVTPGLFETIEVLGKERTLKRLERTLQFLKKT
What is the function of this protein?
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
What are the official names of this protein?
Glutamate--tRNA ligase 1, Glutamyl-tRNA synthetase 1, GluRS 1.
What is the protein family that this protein belongs to?
Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: MCMBP_XENTR
Sequence: MTGGESWISDPLGVVQGLFAAQRPADGDWQKNVTDYFSAKLRDSDSAAAVPCLNDTPLHYLKPNSLVRFRCMVQDMFDPEFYMGVYETVDTNTSARVLHFGKYRDVAESLPQQEVDPDSRRNVTCERQTFYCVPVPGECPWVKDAYTSCSQAKVCASTSYAPSRQKRSYEEDEDAAPCDTRASHGLGEPKRLETEAAGAQQHLPSSCSSAPDLNFPLPGEKGPACLIKVYEGWDLFKVNDVLEVYGILSVDPALSALTEDREAVSALLDPSDDMDTLEEHRAHCPPASLVPRIHTIVTRKLQHNNPLLPPSLQGSEESKLFVSNFLSELSAVRAELLDFLSHALLGDSLAAEYLILHLISTVYARRDVLPLGKFTLNLSGCPRNGTFSELLYRVVQQLVPAAHYLPMTIENMNKLCFIPRKDYNANRLVSGLLQLSPQTSLLVDETLLEQGQLDTTGVHNVTALGNLITWQKVDYDFSYHRMEFPCNINVLVTSEGRSLLPSDCHVHLQPQMMPPNLEQYLGALLAASLPSLLNKFRTYIGLLRLLDYSISDEATKAVEDDFVEMRKNDPQSISADDLHRLLVVARLSSLSAGQTSLSREQWLRAKQLEQQRKNRLREQKHMNVNEL
What is the function of this protein?
Associated component of the mcm complex that acts as a regulator of DNA replication.  Binds to the MCM complex during late S phase and promotes the disassembly of the mcm complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA.  Can dissociate the mcm complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the mcm complex.  Required for sister chromatid cohesion (By similarity).
What are the official names of this protein?
Mini-chromosome maintenance complex-binding protein, MCM-BP, MCM-binding protein.
What is the protein family that this protein belongs to?
Belongs to the MCMBP family.
What are the subcellular locations of this protein?
Nucleus. Note=Associates with chromatin.
Protein: RS2_CLOTE
Sequence: MSVISMKQLLEAGVHFGHQTRRWNPKMAPYIFTERNGIYIIDLQKTVKKVEQAYNFIREVAAEGKDVIFVGTKKQAQEAIQEEAVRCDMHFVNNRWLGGMLTNFSTIKGRIRTLEELEQMEQDGTFEVLPKKEVIKLKLEEEKLEKNLGGIKNLNANNVGAMFVVDPRKEKNAISEAKILGIPVVAIVDTNCDPDEVDYVIPGNDDAIRAVKLITAKMADAVIEGRQGEQLAE
What are the official names of this protein?
30S ribosomal protein S2.
What is the protein family that this protein belongs to?
Belongs to the universal ribosomal protein uS2 family.
Protein: GRIA4_MACFA
Sequence: MRIISRQIVLLFSGFWGLAMGAFPSSVQIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVIKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQDVPTLGNDTAAIENRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEPEDGKEGPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLGNAVNLAVLKLNEPGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKLTFSEAIRNKARLSITGSVGENGRVLTPDCPKAVHAGTAIRQSSGLAVIASDLP
What is the function of this protein?
Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission.  L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system.  Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse.  The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist.  In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (By similarity).
What are the official names of this protein?
Glutamate receptor 4, GluR-4, GluR4, AMPA-selective glutamate receptor 4, GluR-D, Glutamate receptor ionotropic, AMPA 4, GluA4.
What is the protein family that this protein belongs to?
Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIA4 subfamily.
What are the subcellular locations of this protein?
Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. Cell projection, dendrite. Note=Interaction with CNIH2, CNIH3 and PRKCG promotes cell surface expression.
Protein: RL31B_STAAT
Sequence: MKQGIHPEYHQVIFLDTTTNFKFLSGSTKTSSEMMEWEDGKEYPVIRLDISSDSHPFYTGRQKFAAADGRVERFNKKFGLKSNN
What are the official names of this protein?
50S ribosomal protein L31 type B.
What is the protein family that this protein belongs to?
Belongs to the bacterial ribosomal protein bL31 family. Type B subfamily.
Protein: RPP40_BOVIN
Sequence: MGFGPYYFVKGLPLYELITHEFINTFVKKGSCYALTYNTNIDEDNTVALLPNGKLILSLDKDTYEETGLQGCPSQYSGRKTMRFIVSIDLMDLSSNLDSKKYKRVSWAFKEKKPLKFDFLLAWHQTGAEGSTMMSYFSGYGIQEHQPKIALSTTPDLRCPVLRSGLLGGEPEAACSAHELFDWLGAVFSHADLNNEPYNFVSTYCCPQPSSVVAQASLCSVTGFLLPERICVLLEQLCRYFDEPKLAPWVTLSVQGFADSPVSWRESEHGFQKGGEHLYNFVIFNNRDYWLQMAVGADDDCPP
What is the function of this protein?
Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends.  Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences.
What are the official names of this protein?
Ribonuclease P protein subunit p40, RNaseP protein p40.
What are the subcellular locations of this protein?
Nucleus, nucleolus.
Protein: TUSA_ECOBW
Sequence: MTDLFSSPDHTLDALGLRCPEPVMMVRKTVRNMQPGETLLIIADDPATTRDIPGFCTFMEHELVAKETDGLPYRYLIRKGG
What is the function of this protein?
Sulfur carrier protein involved in sulfur trafficking in the cell.  Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA.  Interacts with IscS and stimulates its cysteine desulfurase activity.  Accepts an activated sulfur from IscS, which is then transferred to TusD, and thus determines the direction of sulfur flow from IscS to 2-thiouridine formation.  Also appears to be involved in sulfur transfer for the biosynthesis of molybdopterin.
What are the official names of this protein?
Sulfur carrier protein TusA, Sulfur mediator TusA, Sulfur transfer protein TusA, tRNA 2-thiouridine synthesizing protein A.
What is the protein family that this protein belongs to?
Belongs to the sulfur carrier protein TusA family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: DTD_XANC5
Sequence: MLALIQRVTRAAVTVDDQIVGQIGPGLLALIGVEPGDSDAQIRRLAERLLSYRVFGDDAGKMNRSLTDTGGGLLLVSQFTLAADTSSGNRPGFSTAAPPLEAEPAFNQLVAICREKHRGGVEAGRFGAHMVVDLVNDGPVTFLLRP
What is the function of this protein?
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs.  Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS.  Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site.  By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
What are the official names of this protein?
D-aminoacyl-tRNA deacylase, DTD, Gly-tRNA(Ala) deacylase.
What is the protein family that this protein belongs to?
Belongs to the DTD family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: FIXX_RHIME
Sequence: MKTAIAERIEDKLYQNRYLVDAGRPHITVRPHRSPSLNLLALTRVCPAKCYELNETGQVEVTADGCMECGTCRVLCEANGDVEWSYPRGGFGVLFKFG
What is the function of this protein?
Could be a 3Fe-4S cluster-containing protein.
What are the official names of this protein?
Ferredoxin-like protein.
What is the protein family that this protein belongs to?
To ferredoxins from P.putida and C.tartarivorum, ferredoxin I from A.vinelandii, ferredoxin II from D.desulfuricans.
Protein: VMH4A_VIPAA
Sequence: MIQPLLVVTCLVVFPYQVSSIILESGNVNDYEVVYPQKVTSLPKGAVQQPEQKYEDTMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTNPPVEDHCYYHGHIQNEADSTASISACNGLKGHFKLQGETYLIEPLKIPESEAHAVYKYENIEKEDEAPKMCGVTETNWESDEPIRKASQLVATSEQRRNIQKYIELVIVVDNVMFRKYTGNSTAIRTRIYEIVNTLNVVFRNVHIFVALVGIEIWNKKDQIKVKSAESVTLDLFGDWREKDLLRRKRHDNAQLLTGIDLNEQTLGIAPMSGMCKPKSSVGLIQDYCKSYLLVAIVMAHELGHNLGMDHDDGNCICREMPCIMSPEAGSKPAFYFSDCSWNQYQKFRNDIKSKCIDNKPLKTDIVSPAFCGNYFVEEGEECDCGFPGNCRNPCCNATTCKLTPGSECGDGECCDQCRIQTAGTECRPAWDECDVPEYCTGQSAECPTDVLQRNGQPCKNNNGYCYNGVCPILTNQCISLFGSSVTVAPDRCFNNNLQGTENFHCGMENGRYIKCKPQDKKCGRLFCVEPPTGGGINCKSIRSEGDPDHGMVDLGTKCADGKVCNSNRQCVDVNTAY
What is the function of this protein?
Heterodimer (A and B subunits): Zinc metalloprotease that has fibrinogenolytic and hemorrhagic activities.  Cleaves insulin B chain preferably at '40-Tyr-|-Leu-41' bond, but also at '28-Gln-|-His-29' and '34-His-|-Leu-35' bonds.  Hydrolyzes effectively isolated extracellular matrix (ECM) bovine fibronectin, and only slightly, basal membrane (BM) proteins human collagen IV and murine laminin, in vitro.  Cleaves nidogen-1 (at '350-Ser-|-Phe-351' and '380-Tyr-|-Asn-381' bonds), but not laminin, in a solubilized BM preparation.  Hydrolyzes plasma proteins involved in blood coagulation in vitro.  It slightly shortens prothrombin time and significantly prolongs thrombin time.  Has potent alpha-fibrinogenase activity cleaving human fibrinogen alpha chain at '441-Glu-|-Leu-442' and '539-Glu-|-Phe-540' bonds, and to a lesser extent, beta chain at '52-Lys-|-Arg-53' and '48-Pro-|-Leu-49' bonds, but does not cleave gamma chain.  Hydrolyzes bovine prothrombin at '200-Ser-|-Gly-201' bond, but does not activate it, however, it cleaves fragment 1 and prethrombin 1 from it.  Hydrolyzes bovine factor X heavy chain, but the cleavage does not produce an activated factor Xa heavy chain.  No hydrolysis or activation of plasminogen.  The ability to degrade some of the ECM, BM and plasma proteins is likely the main contributor to its hemorrhagic activity.  Inhibits platelet aggregation induced by collagen in vitro.  Its binding to glycosaminoglycans (GAGs) may assist in concentrating it in the proximity of blood vessel walls enabling in vivo degradation of BM protein components.  Cytotoxic to cultured HeLa cancer cells in a concentration- and time-dependent manner.  In the solubilized BM preparation (Matrigel), it induces morphological changes in the HeLa cells and inhibits their adhesion, however, the viability of the cells is not reduced.
What are the official names of this protein?
Zinc metalloproteinase-disintegrin-like protein H4 subunit A, Hemorrhagin 4 subunit A, Metalloproteinase H4-A, P-III metalloproteinase H4 subunit A, Snake venom metalloproteinase, SVMP, VaH4-A.
What is the protein family that this protein belongs to?
Belongs to the venom metalloproteinase (M12B) family. P-III subfamily.
Protein: MTNA_PSE14
Sequence: MRDRLLAAEKVKAIDWRDDALYLLDQRVLPFEEVWHRYTTAEGVAEAIRTMVVRGAPAIGISAAYGAVLGARARIAEGGDWYPALEEDMQLLADSRPTAVNLFWALNRMRDRLMRVKDGDDPLVALEAESVAIHLSDREANLTMAQLGADLIRRHQGNLQTVLTHCNTGALATGGFGTALGVIRAAHLEGMIERVYADETRPWLQGSRLTAWELANEGIPVTLNADSAAAHLMRTKGITWVIVGADRITANGDVANKIGTYQLAVAAMHHGVRFMVVAPSSTIDMEMASGDDIIIEERDGRELLEVGGQRVGAQVEAFNPVFDVTPADLIDAIVTEKGIVERPDTARMAQLMSRKHLH
What is the function of this protein?
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
What are the official names of this protein?
Methylthioribose-1-phosphate isomerase, M1Pi, MTR-1-P isomerase, S-methyl-5-thioribose-1-phosphate isomerase.
What is the protein family that this protein belongs to?
Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.
Protein: LEXA_RUEPO
Sequence: MLTKKQLDLLEFIHKRLQADGVPPSFDEMKLALDLRSKSGIHRLITALEERGFIRRLAHRARAIEIVKLPESLGGEPTVGFQPRVIDGDRPDRPRPANAEPVTIHAVELPVMGRIAAGVPIEAISQVSHQVAVPGSMVGKGEHYALEVKGDSMIEAGINDGDVVVIRETSTADNGDIVVALVDDSEATLKRFFRRGASIALEAANPAYETRVLPSDRVRVQGRLVGLIRTY
What is the function of this protein?
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA.  In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
What are the official names of this protein?
LexA repressor.
What is the protein family that this protein belongs to?
Belongs to the peptidase S24 family.
Protein: PUR5_LEPIN
Sequence: MEEKITYKNAGVDTEKGREFIQKIKRNVESTHGPRVIGGLGGFAGAYDVSVLKKYKHPILLSGTDGVGTKIELARLLKIYNTIGIDLVAMCVNDILVCGGEPLFFLDYIACGKLDPEKMDQIVSGIVQGCKMSNASLLGGETAEHPGTMKEDEFDLAGFVVGAVEKDSMIDGSTIRSGDKILGLESSGPHSNGFSLIRKLLLKEGKYLPTDPQQVKFLKDYALKPTRIYVSSILKLLQQVSVKGMVHITGGGYQENVPRILPQGTQSKFFKEKIPSGYFFEKIKKDHKIEELELFATFNMGIGYMVIVSEENAELAKKIMESSGEVVHEIGEIVSGNKEEVQFV
What are the official names of this protein?
Phosphoribosylformylglycinamidine cyclo-ligase, AIR synthase, AIRS, Phosphoribosyl-aminoimidazole synthetase.
What is the protein family that this protein belongs to?
Belongs to the AIR synthase family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: DXS_BURL3
Sequence: MYDLLKTIDDPADLRRLDRRQLQPLADELRAFVLDSVSKTGGHLSSNLGTVELTIALHYVFNTPNDRIVWDVGHQTYPHKILTGRRDQMHSLRQQDGISGFPRRSESEYDTFGTAHSSTSISAALGMAIGSQLNGDDRFSIAVIGDGAMTAGMAFEAMNNAGVSEDAKVLVILNDNDMSISPPVGALNRHLARLMSGRFYAAARAGVERVLSVAPPVLELARKLEEHAKGMVVPATLFEEFGFNYIGPIDGHDLDSLIPTLQNIRELRGPQFLHVVTKKGQGYKLAEADPVLYHGPGKFNPAEGIKPSTTPAKKTYTQVFGEWLCDEAERDTRVVGITPAMREGSGMVEFEKRFKDRYYDVGIAEQHAVTFAGGMATEGLKPVVAIYSTFLQRAYDQLIHDVALQNLPVVFAIDRAGLVGADGATHAGAYDLAFMRCIPNMTIMAASDENECRQMLHTALQQPNPTAVRYPRGAGTGVPTVKEFTEIPLGKGEVRRQTSQPEGKRVAILAFGTMVAPSLAAAEELDATVANMRFVKPVDAALVRELAETHDYLVTVEEGCVMGGAGSACVEALMESGVIRPVLQLGLPDLFIDHGDPAKLLSQCGLDGAGIAKSIRERFLNPAADVAGQAKRVA
What is the function of this protein?
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
What are the official names of this protein?
1-deoxy-D-xylulose-5-phosphate synthase, 1-deoxyxylulose-5-phosphate synthase, DXP synthase, DXPS.
What is the protein family that this protein belongs to?
Belongs to the transketolase family. DXPS subfamily.
Protein: VA712_ARATH
Sequence: MSILYALVARGTVVLAELSTTSTNASTIAKQILEKIPGNGDSHVSYSQDRYVFHVKRTDGLTVLCMADEDAGRRIPFSFLEDIHQRFVRTYGRAIHSAQAYAMNDEFSRVLNQQIEYYSNDPNADTISRIKGEMNQVRDVMIENIDNILDRGERLELLVDKTANMQGNTFRFRKQTRRFNNTVWWRNCKLTLLLILVLLVIIYIGVAFACHGPTLPSCV
What is the function of this protein?
Involved in the targeting and/or fusion of transport vesicles to their target membrane.
What are the official names of this protein?
Vesicle-associated membrane protein 712, AtVAMP712.
What is the protein family that this protein belongs to?
Belongs to the synaptobrevin family.
What are the subcellular locations of this protein?
Vacuole membrane; Single-pass type IV membrane protein. Prevacuolar compartment membrane; Single- pass type IV membrane protein.
Protein: NUSB_SALTI
Sequence: MKPAARHRARECAVQALYSWQLSQNDIADVEYQFLAEQDVKDVDVLYFRELLSGVATNSAYLDGLMKPYLSRLLEELGQVEKAVLRIALFELSKRSDVPYKVAINEAIELAKTFGAEDSHKFVNGVLDKAAPVIRPNKK
What is the function of this protein?
Involved in transcription antitermination.  Required for transcription of ribosomal RNA (rRNA) genes.  Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
What are the official names of this protein?
Transcription antitermination protein NusB, Antitermination factor NusB.
What is the protein family that this protein belongs to?
Belongs to the NusB family.
Protein: KTHY_ECOLI
Sequence: MRSKYIVIEGLEGAGKTTARNVVVETLEQLGIRDMVFTREPGGTQLAEKLRSLVLDIKSVGDEVITDKAEVLMFYAARVQLVETVIKPALANGTWVIGDRHDLSTQAYQGGGRGIDQHMLATLRDAVLGDFRPDLTLYLDVTPEVGLKRARARGELDRIEQESFDFFNRTRARYLELAAQDKSIHTIDATQPLEAVMDAIRTTVTHWVKELDA
What is the function of this protein?
Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor (PubMed:8631667).  Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth.
What are the official names of this protein?
Thymidylate kinase, Thymidine monophosphate kinase, dTMP kinase, TMPK.
What is the protein family that this protein belongs to?
Belongs to the thymidylate kinase family.
Protein: Z_LASSJ
Sequence: MGNKQAKAPESKDSPRASLIPDATHLGPQFCKSCWFENKGLVECNNHYLCLNCLTLLLSVSNRCPICKMPLPTKLRPSAAPTAPPTGAADSIRPPPYSP
What is the function of this protein?
Plays a crucial role in virion assembly and budding.  Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L.  Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP.  Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway.  The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z.  Also selectively represses protein production by associating with host eIF4E.
What are the official names of this protein?
RING finger protein Z, Protein Z, Zinc-binding protein.
What is the protein family that this protein belongs to?
Belongs to the arenaviridae Z protein family.
What are the subcellular locations of this protein?
Virion. Host cytoplasm, host perinuclear region. Host cell membrane; Lipid-anchor; Cytoplasmic side. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells.
Protein: COX7_NEUCR
Sequence: MPGLVNAPNHVPEKQRYYQQAFKNHTRLWKIGPRSGIIMTTFNIAMWGTFGASMYAMSRKVLGYNTWFSED
What is the function of this protein?
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation.  The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase.  Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water.  Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of Cox2 and heme A of Cox1 to the active site in Cox1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)).  The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
What are the official names of this protein?
Cytochrome c oxidase subunit 7, mitochondrial, Cytochrome c oxidase polypeptide VII, Cytochrome c oxidase subunit Cox7.
What is the protein family that this protein belongs to?
Belongs to the cytochrome c oxidase VIIa family.
What are the subcellular locations of this protein?
Mitochondrion inner membrane; Single-pass membrane protein.
Protein: EFP_MYCS5
Sequence: MIEVNKFKPGITFQDSGNIYVVLEATHSKQGRGQANVKAKAKNLRTGATTILSFTGGDKVEPAHIEKRKMNFLYSDDSNIYLMDSSDYSQIEIDLLKVEWEMNFLKENSEVQVRMFQDEILDIELPANVDLKVTYAPDAVKGNTTTNPQKKVTLETNFELETPMFIKENDVIIVSTETGKYVGKSK
What is the function of this protein?
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.
What are the official names of this protein?
Elongation factor P, EF-P.
What is the protein family that this protein belongs to?
Belongs to the elongation factor P family.
What are the subcellular locations of this protein?
Cytoplasm.