PharMolix/UniProtQA huggingface dataset:
Protein: LV537_HUMAN
Sequence: MAWTPLLLLLLSHCTGSLSQPVLTQPPSSSASPGESARLTCTLPSDINVGSYNIYWYQQKPGSPPRYLLYYYSDSDKGQGSGVPSRFSGSKDASANTGILLISGLQSEDEADYYCMIWPSNAS
What is the function of this protein?
V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447).  Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes.  In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells.  Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414).  The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain.  Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen.  The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
What are the official names of this protein?
Immunoglobulin lambda variable 5-37.
What are the subcellular locations of this protein?
Secreted. Cell membrane.
Protein: SOTB_ECOK1
Sequence: MTTNTVSRKVAWLRVVTLAVAAFIFNTTEFVPVGLLSDIAHSFHMQTAQVGIMLTIYAWVVALMSLPFMLMTSQVERRKLLICLFVVFIASHVLSFLSWSFTVLVISRIGVAFAHAIFWSITASLAIRMAPAGKRAQALSLIATGTALAMVLGLPLGRIVGQYFGWRMTFFAIGIGALITLLCLIKLLPLLPSEHSGSLKSLPLLFRRPALMSIYLLTVVVVTAHYTAYSYIEPFVQNIAGFSANFATALLLLLGGAGIIGSVIFGKLGNQYASALVSTAIALLLVCLALLLPAANSEIHLGVLSIFWGIAMMIIGLGMQVKVLALAPDATDVAMALFSGIFNIGIGAGALVGNQVSLHWSMSMIGYVGAVPAFAALIWSIIIFRRWPVTLEEQTQ
What is the function of this protein?
Involved in the efflux of sugars.  The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites.
What are the official names of this protein?
Probable sugar efflux transporter.
What is the protein family that this protein belongs to?
Belongs to the major facilitator superfamily. SotB (TC 2.A.1.2) family.
What are the subcellular locations of this protein?
Cell inner membrane; Multi-pass membrane protein.
Protein: SYA_SULIM
Sequence: MKASEEEYRLNFFIKNDFKRKICKSCKTPFWTRDEKKEYCSDIPCTDYYFFDINIKSQPLTVKEAREKFLSFFEKRGHTRISPKPVLARWRDDLYLTIASIVDFQPHVTSGLVPPPANPLVVSQPSIRLEDIDNVGITFGRHLTTFEMAAHHAFNYPDHYVYWKDETTAYATEFFTKELGIPEEELNFKESWWEGGGNAGPCLEVTVGGLELATLVFMQYKITDNGNYTPLKLKIVDTGYGVERIAWITQKTPSAFHAIYGNLVYKFFNKIGVAYIDETLLKVASRFAGKIDPDNPDTIKIHRQMVSKELGIDIKAVEEELDRAAKVFQILDHTKTIMLMLADGLVPSNSGEGYLGRLVIRRALKVLRLLKSDVRLYELVKEQIDFWKEDFPQVLKNKDYILDAVELEQQRFEKILEKVPSIASTLARKSEITTEDLIQVYDSNGIPPDLLEEELKKKSVKFELPRNFYALVAKRHQTSTIKSVYDKVKLPKDMLEYITALQPTEKLYYKDQYMRSFEGKVLGVYKNYLILDKTTFYPEGGGQLGDTGLIIDEKSSKRYEVIDTQKVNDVIVHILKEEPSTIKVGDNVRGEINWERRYRLMRHHTVTHVILAAAKKVLGEHVWQAGAEKTPEKGRLDITHHKTLTEEEVKLIENYANSVISDRRPVKPLEMNRMEAEMKYGVSIYEGGVPNSATIRLLEIKDWDIESCGGTHVSNTSEIGAVKIINVERIQDGVIRLEYVAGPALVDYIRETEAKIVEASKIIGSSPDQLTSRLRRLLNEIEEKNNLIIQYRRIIETELLNNLKPYEINGNKIYIIEGLGDEEENKEILRKLTSTDNTIAISISDNRLQIATSKNMRVDKIVEELLKGGGKGGGKGTFANVILNSKKSKEEIIEIVRKSL
What is the function of this protein?
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala).  Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
What are the official names of this protein?
Alanine--tRNA ligase, Alanyl-tRNA synthetase, AlaRS.
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: RISB_SALPC
Sequence: MNIIKANVAAPDARVAITIARFNQFINDSLLDGAVDALTRIGQVKDDNITVVWVPGAYELPLATEALAKSGKYDAVVALGTVIRGGTAHFEYVAGGASNGLASVAQDSGVPVAFGVLTTESIEQAIERAGTKAGNKGAEAALTALEMINVLKAIKA
What is the function of this protein?
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate.  This is the penultimate step in the biosynthesis of riboflavin.
What are the official names of this protein?
6,7-dimethyl-8-ribityllumazine synthase, DMRL synthase, LS, Lumazine synthase.
What is the protein family that this protein belongs to?
Belongs to the DMRL synthase family.
Protein: SEY1_BLAGS
Sequence: MVANGHFASNGEGQDSGSYEHGVQVIDEDKEFNPNVSRYLTYENVTPAGFNYHLISVFGSQSTGKSTLLNHLFGTHFSVMSETERRQTTKGIWLSKNKRVESSKDRDPQMKMADNILVMDVEGTDGRERGEDQDFERKSALFALATSEVLIVNIWEHQVGLYQGANMGLLKTVFEVNLELFLKDNKSTPRSLLFFVIRDFVGTTPLQNLQNTLLQDLNRIWSSLSKPAGLENSTINDYFDFAFAGLPHKNFQPEKFVDEVQKLSTRFRNAHRDPNNVDSRGTGSIEGGIFLPEYHRRIPADGFAVYAEGVWDQIVNNKDLDLPTQQELLAQFRCDEISREALVAFDEAISPFESKQAEAVQAGSPQVLGGLGPVMRNARMNAVKNFDAEASRYHKRVYQMKKSELEEKIDTRLKALFLGQLNAAHRSGVQDFSESVSAAVKAGQKRGASYDFAEIVSRERQLAIEKFEKEARSTLVEDAPWSNYQQELSLYQKDLERISGQLRRDEMRRLATRVERWVRSRLGESVDLEFNALGSGRGGSGAPEFGDKPSENTIWDRVWTIFVDTVLDAERRFTERASSFDASLDEVDVGLWRLRRKSWGVLRAKIEEEVMEGNLLLKLRENFEDKFRYDDAGVPRIWRPTDDIESVYTQARESTLTLIPLLARFRLAETNAPPPLDKWIGHTPSSATPADEEDLTPIGGVDEDEGKSLEEEMTMIGEAKKQDLIVRFKKTADGVYVEAKRSAIGGITQVPLYFYGLLLALGWNEIMAVLRNPAYFFLLFVCAIGAYVTYQLNLWGPIIKMTEAASHQALEEGKRRLRDFLEASDTGRQAMAMSGARNATEEHEMSNLNRKSGERGGQKYRGEDVADDDDVDDDF
What is the function of this protein?
Cooperates with the reticulon proteins and tubule-shaping DP1 family proteins to generate and maintain the structure of the tubular endoplasmic reticulum network.  Has GTPase activity, which is required for its function in ER organization.
What are the official names of this protein?
Protein SEY1.
What is the protein family that this protein belongs to?
Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
What are the subcellular locations of this protein?
Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Enriched in the cortical ER. Concentrated in punctae along the ER tubules.
Protein: VP35_NPVBM
Sequence: MCVIFPVEIDVSQTVIRDCHVDEQTRELVYINKIMNTQLTKPVLMMFNISGPIRSVTRKNNDLRDRIKSKVDEQFDQLEREYSDKIDGFHDNIQYFKDEHYSVSCQNGSVLKSKFAKILKSHDYTDKKSIETYEKYCLPQLVDKHNDCYVAVCVLKPGFENGSNQVLSFEYNPIGNKVIVPFAHEINDTGLYEYDVLAYVDSVEFDGKQFEEFVQKLILPSSFNDSEKVLYYNEASKNKNMIYKALEFTTESSWVKSNKFNWKIFCNGFIYDKKSKALYVKLHNVTSTLNKNVILDMIK
What is the function of this protein?
Blocks the insect or worm host cells apoptotic response initiated by the viral infection.  Confers protection from cell death in mammalian cells.  Acts by blocking the activity of members of the caspase family of proteases.
What are the official names of this protein?
Early 35 kDa protein, Apoptosis-preventing protein, p35.
What is the protein family that this protein belongs to?
Belongs to the protease inhibitor I50 (p35) family.
Protein: DEL2A_HOTJU
Sequence: GRDAYIADDKNCVYTCAKNSYCNNECTKNGAESGYCQWLGKYGNGCWCKNLPDKVPIRIPGPCR
What is the function of this protein?
This non-amidated recombinant toxin slows fast inactivation on Nav1. 1/SCN1A (EC(50)=52. 8 nM), Nav1. 4/SN4A (EC(50)=32 nM), Nav1. 5/SCN5A (EC(50)=116. 7 nM), Nav1. 6/SCN8A (EC(50)=46. 3 nM), and Nav1. 7/SCN9A (EC(50)=147. 4 nM) voltage-gated sodium channels (PubMed:32259093).  On Nav1. 1/SCN1A channel, acts as an agonist by inducing a shift in both the voltage dependence of channel inactivation (alpha-toxin activity) and activation (beta-toxin activity) (PubMed:32259093).
What are the official names of this protein?
Delta-buthitoxin-Hj2a, Delta-BUTX-Hj2a.
What is the protein family that this protein belongs to?
Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily.
What are the subcellular locations of this protein?
Secreted.
Protein: CCSA_CHLVU
Sequence: MMVNIPVIENFLSNSCFLILFLTTVYYWLKIGFGGKSSFSFTGLTGYGSALCCLTLQLILRWVDSGHFPLSNLYESLIFLAWCLLLLYIYIEVSTKTLFLGVLTSPAILCLVAFTDFSLPTELQQSTPLVPALQSNWLVMHVTVMIASYAALLLGCFIAIAYLVLSKFFIKTTFVTAPLSSQNTVLRQESFLEEKQKTDIVFEKNDKNLKFLFFLDNLSYRTIGIGFCFLTLGILSGAIWANETWGNYWSWDPKETWAFITWLTFACYLHSRLVGGWTGSKPALVASFGFLVVWVCYLGVNLLGQGLHSYGFLNV
What is the function of this protein?
Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
What are the official names of this protein?
Cytochrome c biogenesis protein CcsA.
What is the protein family that this protein belongs to?
Belongs to the CcmF/CycK/Ccl1/NrfE/CcsA family.
What are the subcellular locations of this protein?
Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Protein: FPG_BURL3
Sequence: MPELPEVEVTRRGIEPFVAGRRVERVDVRTEMLRWPVPAGLAEQLRAREVLAVERRGKYLLFEVDAGWFIVHLGMTGTLRVLPADGLPVAAKHDHIDWIFDEFVLRFRDPRRFGAVLWHPREAGDVHAHPLLASLGVEPFSPAFTGALLHARTRGRTVSVKQALLAGDMVVGVGNIYASESLFRAGIRPTTAAGKVSLPRYERLADAVRATLADAIERGGSTLRDFVGSNGESGYFQLDCFVYDRAGQPCRVCNTPIRQIVQGQRSTYFCPTCQR
What is the function of this protein?
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents.  Acts as DNA glycosylase that recognizes and removes damaged bases.  Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG).  Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand.  Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
What are the official names of this protein?
Formamidopyrimidine-DNA glycosylase, Fapy-DNA glycosylase, DNA-(apurinic or apyrimidinic site) lyase MutM, AP lyase MutM.
What is the protein family that this protein belongs to?
Belongs to the FPG family.
Protein: GLNE_COREF
Sequence: MTDPLIHTRKVMGFVRDPLPTTGALSLKSTNARADLEWLGWRNVESIPLMWALSGAGDPDVALNQLVRMYQTLESQSPQAREELDQRIRADEAFRVRLLALLGGSSAMGDHLVANTHLWELLTEEAPTRAEMFTAMLESVGATPAEVVPVDDEGEERQVANTATEDLTTPGTYRATLTGVDAERALRFTYRTLMMRLAALDLAGTYPNDARRRSQPRVEFTTVTRRLSNLADAALTAALAVAVTGVYGQKPVDARLSVMAMGKCGAQELNYISDVDVIFIAEPAHSRSTRLAAEFIRTGCSSFFEVDAALRPEGKSGALVRTLESHIAYYKRWAETWEFQALLKARPMTGDMDLGQAYLDAIGPMVWTASQRDSFVDDIQAMRRRVLENVPEELRDRELKLGRGGLRDVEFAVQLLQMVHGRYDETLRVRSTVEALQVLVDQGYIGREDGHNLIESYEFLRLLEHRLQLERVKRTHTMPKVEDRMNMRWLARASGFTGSGGQSSARAMEHHLRRVRLQIQSLHSQLFYRPLLNSVVNLSVDAMKLSQEAAKLQLGALGYQHPVRAYEHLTALASGTSRKAKIQAMLLPTLMEWLSQTADPDAGLLNYRKLSDAAYDRSWFLRMLRDEGVVGQRLMRILGTSPYTSELIIATPDFVSELGDGTTGPKLLETAPDRVCKALKATVARHDDPDRAIQAARSLRRQELARVASADLLNLLTVQEVCHSLSLVWDAVLDAALEAEIRAATADPAKPDEPLAAISVIGMGRLGGAELGYGSDADVMFVAEPAPGVDENEAIAWAISVCESMRSRLAKPSGDPPLEVDLGLRPEGRSGAVVRTIESYENYYAKWGETWEVQALLRASWVAGDRELGTRFLETIDKFRYPAGGASDAQIREVRRMKARVDNERLPRGADRNTHTKLGRGALADIEWTVQLLTMLHAHEHPELHNTSTLEVLEVVEEKGIINPLQAQTLREAWLTATAARNALVLVKGKRADQLPPPGRHLAQVAGAAGWDPDEYQEYLDHYLKVTRKSRQVVEEVFWGLDSVEARREL
What is the function of this protein?
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia.  When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity.  Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity.  The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
What are the official names of this protein?
Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme, ATP:glutamine synthetase adenylyltransferase, ATase.
What is the protein family that this protein belongs to?
Belongs to the GlnE family.
Protein: FTSW_BACSU
Sequence: MLKKMLKSYDYSLIFAIVLLCGFGLVMVYSSSMITAVSRYGVSSNFFFMRQLFALIAGGALFILMALFPYKALAHQKFQKGILLVSVLALISLFVFGHVAGNAQSWFKIGGMSIQPGEFVKLVVILYLAAVYAKKQSYIDHLLTGVAPPVVMTLIICGLIAMQPDFGTAMIIGLIATCMILCSGFSGKTLVRLVILGGIVFILVSPIIYLNQDKILTEGRLARFESLEDPFKYANSSGLQVINSYYAISSGGIFGLGLGESIQKYGYLPESHTDFIMAVIAEELGIFGVLFVIFLLGFVVIKGFYIARKCEDPFGSLLAIGISSMIAIQSFINLGGVSGLIPITGVTLPFISYGGSSLVLLLGSMGILANISMFVKYSENKKKKEPLAPKGMKKKQLKKTVYL
What is the function of this protein?
Peptidoglycan polymerase that is essential for cell division.
What are the official names of this protein?
Probable peptidoglycan glycosyltransferase FtsW, PGT, Cell division protein FtsW, Cell wall polymerase, Peptidoglycan polymerase, PG polymerase.
What is the protein family that this protein belongs to?
Belongs to the SEDS family. FtsW subfamily.
What are the subcellular locations of this protein?
Cell membrane; Multi-pass membrane protein. Note=Localizes to the division septum.
Protein: RSBW_STAAM
Sequence: MQSKEDFIEMRVPASAEYVSLIRLTLSGVFSRAGATYDDIEDAKIAVSEAVTNAVKHAYKENNNVGIINIYFEILEDKIKIVISDKGDSFDYETTKSKIGPYDKDENIDFLREGGLGLFLIESLMDEVTVYKESGVTISMTKYIKKEQVRNNGERVEIS
What is the function of this protein?
Negative regulator of sigma-B activity.  Phosphorylates and inactivates its specific antagonist protein, RsbV.  Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B).
What are the official names of this protein?
Serine-protein kinase RsbW, Anti-sigma-B factor, Sigma-B negative effector RsbW.
What is the protein family that this protein belongs to?
Belongs to the anti-sigma-factor family.
Protein: SGK3_RAT
Sequence: MQRDCTMDYKESCPSVSIPSSDEHREKKKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNSLKKQFPAMALKIPAKRIFGDNFDPDFIKQRRAGLNEFIQNLVRYPELYNHPDVRAFLQMDSPRHQSDPSEDEDERSTPKPHSTSRNINLGPTGNPHAKPSDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSMGHVVLTDFGLCKEGIAISDTTTTFCGTPEYLAPEVIRKQPYDRTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLNLRPGVSLTAWSILEELLEKNRQNRLGAKEDFLEIQNHPFFESLSWTDLVQKKIPPPFNPNVAGPDDIRNFDAVFTEETVPYSVCVSSDYSIVNASVLEADDAFVGFSYAPPSEDLFL
What is the function of this protein?
Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cell growth, proliferation, survival and migration.  Up-regulates Na(+) channels: SCNN1A/ENAC and SCN5A, K(+) channels: KCNA3/KV1. 3, KCNE1, KCNQ1 and KCNH2/HERG, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channel: BSND, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, amino acid transporters: SLC1A5/ASCT2 and SLC6A19, glutamate transporters: SLC1A3/EAAT1, SLC1A6/EAAT4 and SLC1A7/EAAT5, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na(+)/H(+) exchanger: SLC9A3/NHE3, and the Na(+)/K(+) ATPase.  Plays a role in the regulation of renal tubular phosphate transport and bone density.  Phosphorylates NEDD4L and GSK3B.  Positively regulates ER transcription activity through phosphorylation of FLII.  Negatively regulates the function of ITCH/AIP4 via its phosphorylation and thereby prevents CXCR4 from being efficiently sorted to lysosomes (By similarity).
What are the official names of this protein?
Serine/threonine-protein kinase Sgk3, Cytokine-independent survival kinase, Serum/glucocorticoid-regulated kinase 3, Serum/glucocorticoid-regulated kinase-like.
What is the protein family that this protein belongs to?
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.
What are the subcellular locations of this protein?
Cytoplasmic vesicle. Early endosome. Recycling endosome. Note=Endosomal localization is a prerequisite for complete kinase activity. It is essential for its colocalization with the kinase responsible for phosphorylating Ser-486 thus allowing PDPK1 phosphorylation of Thr-320 resulting in complete activation of SGK3. Localized in vesicle-like structures and in the early endosome. Colocalizes with SLC9A3/NHE3 in the recycling endosomes (By similarity).
Protein: TPIS_BACCR
Sequence: MRKPIIAGNWKMNKTLSEAVSFVEEVKGQIPAASAVDAVVCSPALFLERLVAATEGTDLQVGAQNMHFEKNGAFTGEISPVALSDLKVGYVVLGHSERREMFAETDESVNKKTIAAFEHGLTPIVCCGETLEERESGKTFDLVAGQVTKALAGLTEEQVKATVIAYEPIWAIGTGKSSSSADANEVCAHIRKVVAEAVSPEAAEAVRIQYGGSVKPENIKEYMAQSDIDGALVGGASLEPASFLGLLGAVK
What is the function of this protein?
Involved in the gluconeogenesis.  Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
What are the official names of this protein?
Triosephosphate isomerase, TIM, TPI, Triose-phosphate isomerase.
What is the protein family that this protein belongs to?
Belongs to the triosephosphate isomerase family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: ISPH_NEIMA
Sequence: MNEKTIILANPRGFCAGVDRAISIVERALEEFGAPIYVRHEVVHNKFVVDNLREKGAVFIEDLAEVPPGATLVYSAHGVSKAVRQEAAERGFRVFDATCPLVTKVHKEVARLDAQDCEIIMIGHKGHVEVEGTMGQLAPGKMLLVETVGDVAKLEVRNPDKLAYVSQTTLSVDETKDIIAALNARFPNIRNPHKEDICYATTNRQTAVKELAEQCDIVIVVGSPNSSNSNRLREVAASRGIDAYMVDNAGYLQRAWFEGKNKVGVTAGASAPEVLVREVLATIRGWGHETVREGEGAEESIVFVLPKELRREGETKPDLCKR
What is the function of this protein?
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).  Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
What are the official names of this protein?
4-hydroxy-3-methylbut-2-enyl diphosphate reductase, HMBPP reductase.
What is the protein family that this protein belongs to?
Belongs to the IspH family.
Protein: MURR_ECO5T
Sequence: MLYLTKIRNAESEFTENEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTELRMALIGEYSASREKTNATAQHLHSSITSDDSLEVIARKLNREKELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGCDLSFKLMKIGYRVACEADTHVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSGETEWRSSSMSTRTAQNSVTDLLFVGLVQLNDVESLKMIQRSSELTQRLK
What is the function of this protein?
Represses the expression of the murPQ operon involved in the uptake and degradation of N-acetylmuramic acid (MurNAc).  Binds to two adjacent inverted repeats within the operator region.  MurNAc 6-phosphate, the substrate of MurQ, is the specific inducer that weakens binding of MurR to the operator.
What are the official names of this protein?
HTH-type transcriptional regulator MurR, MurPQ operon repressor.
Protein: HIS3_METBF
Sequence: MFCNLSPMIDFDALKSEKGLILAVVQDQLSREVLMCAYMNREALEKTVETGITHFWSRSRQQLWKKGETSGHVQKVKEIRVDCDMDSLLLLVEQVGGACHMGYRSCFYRNLEGEVVGEKVFEPDEVYKS
What is the function of this protein?
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
What are the official names of this protein?
Phosphoribosyl-AMP cyclohydrolase, PRA-CH.
What is the protein family that this protein belongs to?
Belongs to the PRA-CH family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: CA12_CONGE
Sequence: ECCHPACGKHFSC
What is the function of this protein?
Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
What are the official names of this protein?
Alpha-conotoxin GII.
What is the protein family that this protein belongs to?
Belongs to the conotoxin A superfamily.
What are the subcellular locations of this protein?
Secreted.
Protein: LEUC_MYCMM
Sequence: MALQTREARTLAEKVWDDHVVVSGRNEAPDLIYIDLHLVHEVTSPQAFDGLRLAGRPVRRPDLTIATEDHNVPTVDIDKPIADPVSRTQVETLRRNCAEFGIRLHPMGDVEQGIVHVVGPQLGLTQPGMTIVCGDSHTSTHGAFGALAMGIGTSEVEHVLATQTLPLRPFKTMAVNVDGRLPAGVSAKDIILALIAKIGTGGGQGHVIEYRGSAIESLSMEGRMTICNMSIEAGARAGMVAPDETTYEYLRNRPHAPTGAQWDAALGYWQQLRTDPGAVFDTEVHLDAAELSPFVTWGTNPGQGVPLCATVPDPELIGDDGERQAAEKALAYMDLEPGKAMRDIAVDAVFVGSCTNGRIEDLRVVAEVLRGRKVAPGVRMLIVPGSMRVRAQAEKEGLGEVFTVAGAEWRQAGCSMCLGMNPDQLAPGERCAATSNRNFEGRQGKGGRTHLVSPAVAAATAVRGTLSAPADLN
What is the function of this protein?
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
What are the official names of this protein?
3-isopropylmalate dehydratase large subunit, Alpha-IPM isomerase, IPMI, Isopropylmalate isomerase.
What is the protein family that this protein belongs to?
Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.
Protein: DAPF_SYNE7
Sequence: MSLQFAKYHGLGNDFILVDNRESGEPRLTPEQAVQVCDRNFGVGADGVIFALPGSGDSDYVMRIFNSDGSEPEMCGNGIRCLAKFLSELDGGAQSRYRIATGAGLIVPTLTETGLVTVDMGPAYLKPVEIPTTLTGTGDRVVEADLEVGDRPWKVTTVSMGNPHCITFVEDVAAVPLAEIGPLFEHHPVFPQRTNTEFVEVVRPDYLKMRVWERGAGATLACGTGACATLVAAVLTGRSDRQATVELPGGPLQIEWREDGHLFMTGPAVKVFSGSMELAA
What is the function of this protein?
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
What are the official names of this protein?
Diaminopimelate epimerase, DAP epimerase, PLP-independent amino acid racemase.
What is the protein family that this protein belongs to?
Belongs to the diaminopimelate epimerase family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: CH10_HELPY
Sequence: MKFQPLGERVLVERLEEENKTSSGIIIPDNAKEKPLMGVVKAVSHKISEGCKCVKEGDVIAFGKYKGAEIVLDGTEYMVLELEDILGIVGSGSCCHTGNHDHKHAKEHEACCHDHKKH
What is the function of this protein?
Together with the chaperonin GroEL, plays an essential role in assisting protein folding.  The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.  GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
What are the official names of this protein?
Co-chaperonin GroES, 10 kDa chaperonin, Chaperonin-10, Cpn10.
What is the protein family that this protein belongs to?
Belongs to the GroES chaperonin family.
What are the subcellular locations of this protein?
Cytoplasm.