accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
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|---|---|---|---|---|---|---|
Q7YT83 | TX31_CONTE | Substrate-specific endoprotease Tex31 | Cylinder | MLSTMQTVGAVLMLSIVLVAGRKRHHCDSKYYELTPAHTMCLTDKPNAVAVPLTQETEHEILEMHNKIRADVTDAANMLKMEWDERLATVAQKWAMQCILGHDSGRRGEPDLPGSVGQNVAWSSGDLTFLGAVQMWADEIVDFQYGVWTDGTGHYIQQVFAGASRIGCGQSACGNNKYFVCNYYKGTMGDEPYQLGRPCSQCRSSCQHIRGSQGRWGSLCDCTNGPDACFNGGIFNINTCQCECSGIWGGADCQEKHCPNEDFDDMCRYPDALRRPQHWCQYDNFQSDCPILCGYCPNPN | Protease responsible for cleaving the conotoxins from their propeptide precursors. The target propeptide requires minimum four residues including a leucine N-terminal of the cleavage site for efficient substrate processing (example: Xaa-Xaa-Xaa-Leu-Asn-Lys-Arg-toxin). | Q7YT83 |
C4LAP0 | MTNN_TOLAT | S-adenosylhomocysteine nucleosidase | Tolumonas | MKIGIIGAMEPEVAILREQISNMETLSIAGCEFYRGELAGHDVILTRSGIGKVAASIATTILLDRYAPDCVINTGSAGGFDPELRVGDVVISDEVRHHDVNVTAFGYEPGQLPQQPAAFISDSKLIEVATQVMHQLPELQSRIGLICTGDQFMCDPDHIEQVRQTFPAMMAAEMEAAAIAQVCHQFKVPFVVIRSLSDIAGTESPSTFEEYLEVAAKNSSAMIVAMLKQL | Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. | C4LAP0 |
Q46WE4 | RL3_CUPPJ | 50S ribosomal protein L3 | Cupriavidus | MSLGLVGRKVGMTRIFTDDGDSIPVTVVEVGDNRVTQIKTDETDGYTAVQVTFGARRASRVTKPLAGHLAKAGVEAGEIIREFRIDAAKAAELQTGGSLSVDLFEVGQKIDVQGVTIGKGYAGTIKRYHFASGRATHGNSRSHNVPGSIGMAQDPGRVFPGKRMTGHLGDVTRTVQNLEIAKIDAERKLLLVKGAIPGSKNGKVIVTPAVKAKAKA | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | Q46WE4 |
P13259 | PCY1_YEAST | Phosphorylcholine transferase | Saccharomyces | MANPTTGKSSIRAKLSNSSLSNLFKKNKNKRQREETEEQDNEDKDESKNQDENKDTQLTPRKRRRLTKEFEEKEARYTNELPKELRKYRPKGFRFNLPPTDRPIRIYADGVFDLFHLGHMKQLEQCKKAFPNVTLIVGVPSDKITHKLKGLTVLTDKQRCETLTHCRWVDEVVPNAPWCVTPEFLLEHKIDYVAHDDIPYVSADSDDIYKPIKEMGKFLTTQRTNGVSTSDIITKIIRDYDKYLMRNFARGATRQELNVSWLKKNELEFKKHINEFRSYFKKNQTNLNNASRDLYFEVREILLKKTLGKKLYSKLIGNELKKQNQRQRKQNFLDDPFTRKLIREASPATEFANEFTGENSTAKSPDDNGNLFSQEDDEDTNSNNTNTNSDSDSNTNSTPPSEDDDDNDRLTLENLTQKKKQSAN | Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis. | P13259 |
C3K256 | RS15_PSEFS | 30S ribosomal protein S15 | Pseudomonas | MALDVQEKAQIVADYQQAVGDTGSPEVQVALLTHNINKLQGHFKANGKDHHSRRGLIRMVNQRRKLLDYLKGKDLGRYQTLIGRLGLRR | Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. | C3K256 |
P05187 | PPB1_HUMAN | Placental alkaline phosphatase 1 | Homo | MLGPCMLLLLLLLGLRLQLSLGIIPVEEENPDFWNREAAEALGAAKKLQPAQTAAKNLIIFLGDGMGVSTVTAARILKGQKKDKLGPEIPLAMDRFPYVALSKTYNVDKHVPDSGATATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGTYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYPDDYSQGGTRLDGKNLVQEWLAKRQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALRLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVLKDGARPDVTESESGSPEYRQQSAVPLDEETHAGEDVAVFARGPQAHLVHGVQEQTFIAHVMAFAACLEPYTACDLAPPAGTTDAAHPGRSVVPALLPLLAGTLLLLETATAP | Alkaline phosphatase that can hydrolyze various phosphate compounds. | P05187 |
A0A140JWT2 | PTMB_PENSI | Penitrem biosynthesis cluster 1 protein B | Penicillium | MDGFDVSQAPPEYRSVEPIANLFVLGMGLGWLINYVGMIYQSFKDETYGMAIMPLCCNIAWEIVYSLIYPSKSLTEQGVFIAGLTINIGVMYAAIKFAPKEWSHAPLVMRNLSLIFFLATLGFLTGHLALAAEIGHSLAYSWGAVVCQLLLSVGGLCQLLCRGCTRGASYTLWLSRFLGSSCTVGFASLRWMYWPESFSWLNSPLVLWSLALFLTVDGSYGICYWYVRQYELSLKEAEGRKSK | Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) . Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline . Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ . Paxilline is converted to beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase ptmH which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase ptmD . A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase ptmV and ptmI leads to the production of the prenylated form of penijanthine . The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase ptmE . Five sequential oxidative transformations performed by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ yield the various penitrem compounds. PtmK, ptmU and ptmM are involved in the formation of the key bicyclic ring of penitrem C via the formation of the intermediates secopenitrem D and penitrem D. PtmL catalyzes the epoxidation of penitrem D and C to yield penitrem B and F, respectively. PtmJ catalyzes the last benzylic hydroxylation to convert penitrem B to prenitrem E and penitrem F to penitrem A . | A0A140JWT2 |
B4SLN2 | CLPX_STRM5 | ATP-dependent Clp protease ATP-binding subunit ClpX | Stenotrophomonas maltophilia group | MSEDRQGRSTDTGKILYCSFCGKSQHEVRKLIAGPSVFICDECVELCNDIIREELEEKAQSARSSLPKPREILEVLDQYVIGQNRAKRTLAVAVYNHYKRIESRQKNDEVELAKSNILLVGPTGSGKTLLAETLARLLNVPFTMADATTLTEAGYVGEDVENIIQKLLQKCDYDVEKAQQGIVYIDEIDKISRKSENPSITRDVSGEGVQQALLKLIEGTVASVPPQGGRKHPQQEFLQVDTKNILFICGGAFAGLDKVIQARSTDVGSIGFGAKVKSAERKQEVGKVLAEVEPEDLIKFGLIPEFVGRLPVVATLEELDEPALIKILTEPKNAITKQFKKLFEMENVELEFRPDALSAIARKALKRKTGARGLRTIVESVLLDTMYDLPSQENVSKVVVDESVIEHKSEPYLIYQTPAAPEQKAAGAE | ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | B4SLN2 |
Q5JDH1 | RL23_THEKO | 50S ribosomal protein L23 | Thermococcus | MDPYKVIIRPLVTEKAVSLIERENKLTFIVDRRATKQDIKRAVEEMFNVKVAKVNTLVTMKGEKKAYVKLKPEYDASEIAARLGLF | Binds to 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. | Q5JDH1 |
Q69XK5 | CESAB_ORYSJ | OsCesA11 | Oryza sativa | MDGESPEIMPVECPDPEPASSESGDDHDIPEPLSSRLSVPSGELNLYRAAVALRLVLLAAFFRYRVTRPVADAHALWVTSVACELWLAASWLIAQLPKLSPANRVTYLDRLASRYEKGGEASRLAGVDVFVAAADAAREPPLATANTVLSVLAADYPAGGVACYVHDDGADMLVFESLFEAAGFARRWIPFCRRHGVEPRAPELYFARGVDYLRDRAAPSFVKDRRAMKREYEEFKVRMNHLAARARKVPEEGWIMSDGTPWPGNNSRDHPAMIQVLLGHPGDRDVDGGELPRLFYVSREKRPGFRHHGKAGAMNALLRVSAVLTNGAYVLNLDCDHCVNNSSALREAMCFMMDPVAGNRTCFVQFALRDSGGGDSVFFDIEMKCLDGIQGPVYVGSGCCFSRKALYGFEPAAAADDGDDMDTAADWRRMCCFGRGKRMNAMRRSMSAVPLLDSEDDSDEQEEEEAAGRRRRLRAYRAALERHFGQSPAFIASAFEEQGRRRGGDGGSPDATVAPARSLLKEAIHVVSCAFEERTRWGKEIGWMYGGGVATGFRMHARGWSSAYCSPARPAFRRYARASPADVLAGASRRAVAAMGILLSRRHSPVWAGRRLGLLQRLGYVARASYPLASLPLTVYCALPAVCLLTGKSTFPSDVSYYDGVLLILLLFSVAASVALELRWSRVPLRAWWRDEKLWMVTATSASLAAVFQGILSACTGIDVAFSTETAASPPKRPAAGNDDGEEEAALASEITMRWTNLLVAPTSVVVANLAGVVAAVAYGVDHGYYQSWGALGAKLALAGWVVAHLQGFLRGLLAPRDRAPPTIAVLWSVVFVSVASLLWVHAASFSAPTAAPTTEQPIL | Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. | Q69XK5 |
G8JYC6 | PDF1_CAEEL | Pigment dispersing factor homolog pdf-1 | Caenorhabditis | MNRFIISMIALLAVFCAVSTASPLLYRAPQYQMYDDVQFVKRSNAELINGLIGMDLGKLSAVGKRSNAELINGLLSMNLNKLSGAGRR | Probable ligand of isoforms a and b of the calcitonin receptor-like protein, pdfr-1, a G-protein coupled receptor . May not signal through isoform c of pdfr-1 . Involved in locomotion; more specifically mate searching behavior of males, independent of nutritional status . Involved in regulating the male-specific expression of TGFbeta-like daf-7 in the ASJ chemosensory neurons . Plays a role in circadian rhythms of locomotor activity . Involved in mediating arousal from the sleep-like state called lethargus, which occurs during molting between larval and adult stages, in part by regulating touch sensitivity, and working in concert with neuropeptide flp-2 . In the presence of food, plays a role in initiating and extending exploratory roaming behavior, in opposition to 5-hydroxytryptamine (serotonin) signaling. | G8JYC6 |
A7I1A0 | BIOB_CAMHC | Biotin synthase | Campylobacter | MDLQKIKNQILDGRNLCIEDAYELENAPLNELLEAANEVRAKFCGNYFNFCSIINVKSGKCSENCKYCAQSAHFDTKCEIYDILPFEKIMPLAKLNDDAGVARFSLVASGKGLHKKDDLQKVIEIYKKLKSHTKFHLCASFGIVSKEILAELKKSGVKTYHHNLETSRKFFPKICTTHTYDDRINTIKSALCVGLDVCSGGIFGLGESLKDRIDMAYELKNLKVSSVPINILTPIKGTPLENSAPLCVDEILRSIAIFRLILPHVFLRLAGGRNNLKNSVKTALNGGINSAITGDFLTTCGDVAQSDKNLVSECGFVYKKSFDV | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. | A7I1A0 |
Q0HRU1 | COBT_SHESR | N(1)-alpha-phosphoribosyltransferase | Shewanella | MSQSVPSFQIEPVSKAQDQFIQQKIDLKTKPPGALGLLEPLALQIARIQGPQQLQIVNPTMLVFAGDHGIAAEGVSIAPSEVTRQMVQNFAHGGAAINVFCRQLGFNLEVIDCGILTPVEGVEGIIDQRLGAGTGAIHLEPAMSLACVDKGFAMAQALIERHHQAGCNLVAFGEMGIGNTSSAAAIMAAIMQLDVADCVGRGTGISSETLERKQMLIELALLLHQSAMTGPKQVLACLGGFEIVQMTGAMLAAAERKMLVVVDGFIATAAALVAVTINAHVRDYLIFAHRSEEQGHQRMLEHLKAKPLLSLGLRLGEGTGAALALPLIQAAVNFYNQMASFSDAGIEAVV | Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). | Q0HRU1 |
B0TY95 | RECR_FRAP2 | Recombination protein RecR | Francisella | MNNQIFSPKITAVIESLRKLPTIGKKSSQRLALYLLDKSPETAITIANSLLDAAENIKKCKYCQSLTEKDVCDICGSQNRDESKLCIIESMLDLVAIEEAGFFKGKYFVLNGRISPLDGIGPNELKLDILEQIIINREINEIILAISPTVEGETTAHFISQMIGKDIKISRIGFGVPFGGELEYLDQQTLIHAFNARTNIK | May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | B0TY95 |
Q5PFK5 | YBAB_SALPA | Nucleoid-associated protein YbaB | Salmonella | MFGKGGLGNLMKQAQQMQKKMQKMQEEIAQLEVTGESGAGLVKVTINGAHNCRRVEIDPSLLEDDKEMLEDLVAAAFNDAARRIEETQKEKMASVSSGMQLPPGFKMPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q5PFK5 |
A6MW06 | RK22_RHDSA | 50S ribosomal protein L22, chloroplastic | Rhodomonas | MSTSVKQTEARAIAKYIRMSPFKVRRVLKQIRGRSYKEALMILEFMPYAACKPVLQLLQSAAANAQNNYGLQKDQMIVNYAYADPGPVLKRFRPRAQGRGFKIKKPTCHITVSLKEVL | The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | A6MW06 |
B2VFX0 | SYDP_ERWT9 | Protein Syd | Erwinia | MIDETSQALRDFSQRYCDLWQQKSGHAPASQELYGIPSPCVMATDEDEVWWQPRPFTLAPNLDAVERALDIRLQPAVTAFYTSQFAGDMTGTLDGRPLSLVQVWSEDDFIRVQENLIGHLVMKRRLKQSPTLFIATTDSELEVISVCNVSGEVILEQLGTKKRQVIASSIENLLIALQPLIINCSN | Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. | B2VFX0 |
Q1GJX4 | TTCA_RUEST | tRNA 2-thiocytidine biosynthesis protein TtcA | unclassified Ruegeria | MLDQDLDDIHPLFQGAPQTTEFKKLRKRIVRYTREAVEQYGMVERREDGSLPKWLVCLSGGKDSYTLLAVLYELKWRGLLPVDLLACNLDQGQPGFPATVLPEFLEKMQVPHRIEYQDTYSIVMDKVPQGRTYCALCSRLRRGNLYRIAREEGCSAVVLGHHRDDILETFFMNLFHGGRLATMPPKLVNEEGDLFVFRPLAHVAEADCEKFARAMNYPIIPCDLCGSQDGLQRQQVKQILDTWESNSPGRRQVMFRALMNARPSHLLDPKLFDFTGLALKNIDNSTETEEIPELR | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | Q1GJX4 |
P0C1J1 | PPIL2_RHIO9 | Rotamase | Rhizopus | MGKWTDKLYITHSEWSGEVGQHSASSGITGRNSSGGFKRLPFYCCSLSLQPFEHPVCTPDGIIFDLMNIIPYIKKYGTNPVTGEKLETKNLIKLHFHKNDKDEYFCPVTYKVFSDHTTIAAIKTTGNVFAYDTLEKLNIKAKHWKDLLTDEPFTRKDIIMLQDPHNLEKKDMSKFDYLKNNKPEELEKRKPINNINVAGMGNTKKVFDELQKKNSNEDDNKAIEKKEEIPTSFHKKRETLPYNAAHYTTGEAAESFTSTVVNAYTASTRALIDEDEFMYKKIKKKSYARIITNYGNINVELFSDKKPKTCHNFIELAKTGYYNDVIFHRNIKKFMIQGGDPTGTGKGGESIWKRYFPDEIKTTLKHDARGVLSMANRGKDTNGSQFFITYAAAPHLDGLHTVFGKVVGGLDVLSKLESIPVDEKDRPEREIKIKQIQMFVDPFEEYQRRLKNKLTHEANAERENEEMRKRREKEEKMGWFGPSVPKIQTSGGGGVGKYLQSTKRDNSEISNEGEELQKKQKITKTTFGNFDNF | May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins. May also function as a chaperone, playing a role in intracellular transport of proteins. May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on proteins. | P0C1J1 |
Q2KW44 | PYRD_BORA1 | Dihydroorotate oxidase | Bordetella | MSILFNAYPLARPALFAMDAETAHEVTLASLQRAYDCGTTRRWLHDQPQLPTTLMGMTLRNPVGLAAGLDKNGAFIDALGNLGFGFVEVGTVTPRAQSGNPKPRMFRLPKANALINRLGFNNQGLDAFLANVTRSRFRSQGGILGLNIGKNADTPIERAADDYLIGLAGVYPHADYVTVNISSPNTKNLRALQGGDELSQLLAALRDKRAELAQQHARQVPLVVKIAPDLSQEQIDIIADTLLSNGVDGVIATNTTLSREAVQGMPHAAETGGLSGAPVHELSLAVIERLRQRVGSALAIIGVGGILSGQQAREKIAAGADAVQLYTGLIYRGPALVGECVGTLKNTAR | Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. | Q2KW44 |
Q7SCW9 | RMT2_NEUCR | Type IV protein arginine N-methyltransferase | Neurospora | MADNDSISVRISEDCPPEIQRMLTAAWAHDVDTVKKLIDTPEVARGQDPKTGESPLHAAIRSCGAPSEDDTPEDHEKAKATVSELLMWGAIWNDVDNNNETPGCVAARLNRPELYELCVNAGVRAEMLFGLMDGYEALDSDDEDDEEMAEGEEAQAEDGEEAPELVAAEEATQTAEEETPAVFQPPAVNLEEQVTSDKYLRSTVAYSDGKLVDDAGNGVMMAWETDIMRRSVDALLPNKEPGKRILNIGFGMGIIDGMFAETKPAVHHIIEAHPEVLEYISTPESKFDSTWEESGPAPGAYRVWEGKWQQIGLQLLEEGHVYDAIYFDTFGEDYGQLRMFFTEYIPGLLDSNGIFGFFNGLGADRQICYDVYTKVAEMHLADAGLDVEWKEIPVDMKELAEADKDGWEGVKRRYWTLDTYRLPVCTFLG | S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins. Monomethylates ribosomal protein L12. | Q7SCW9 |
Q15PD3 | CH60_PSEA6 | Chaperonin-60 | Pseudoalteromonas | MAAKEVRFSDDARVKMLAGVNILANAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAKEIELEDKFENMGAQMVKEVASKANDEAGDGTTTATVLAQSIVTEGLKAVAAGMNPMDLKRGIDKAVIAAVEQLKTLSVPCADSKAIAQVGTISANSDTEVGDLIAEAMDKVGKEGVITVEEGQSLQNELEVVEGMQFDRGYLSPYFMNNQENGTVELDSPFILLVDKKVSNIRELLPTLEAVAKASKPLLIIAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDLATLTGGTVISEEIGLELEKVTLEDLGTAKRVVINKDNTTVVDGAGEEEAIQGRVAQIRAQIEESSSDYDKEKLQERLAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGVVAGGGVALVRAASKIVDLQGDNEDQTHGIKLLLRAMESPMRQIAANAGAEASVVTNAVKNGADNYGYNAGNDTYGDMLEMGILDPTKVTRSALQFAASIASLMITTEAMIAEAPKEDAPAMPDMGGMGGMGGMGGMM | Together with its co-chaperonin GroES, 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. | Q15PD3 |
Q6XLL6 | KAX69_OPICA | OcKTx4 | Opistophthalmus | MNAKFILLLLVVTTTTLLPDAKGAEIIRCSGTRECYAPCQKLTGCLNAKCMNKACKCYGCV | Inhibits Kv1.2/KCNA2 and Kv1.3/KCNA3 voltage-gated potassium channels . | Q6XLL6 |
C3PLX7 | TIG_RICAE | PPIase | spotted fever group | MGITILKNEGLDFHARISTPLSEIDDDIQKELLDLTKKVKIAGFRVGKVPVSIVKKKYGTSVRNDIIERRINHSVNHVIKEHNLNIIGRPTIEELQNESDKALEFTVKMELLPKITIPDLKKISLDRPKLEVNSKDVEEQLEKLAALTKNYTKESKAKIKDGDQVTIDAIGYIKEKAFEDGKLNDFKVIIGSNALIPGFEKQLIGSKTGSEVDVNVTFPENYHAKDLAGKDARFVVQIKAVHTAEPTVIDDEFAKKFQSNSLEELRTHFTKQIENESEEAINTIMKMNLFDKLEKLLDFDVPESLLEQEKNILKSGTDKNEQDESLLKDKSSKEITAYYNKLALRRVRIGLLLAEYAKSKNLQLEPDDLRKVIMQQARNFPGQENMIFDFYKNNPRAIEGLKGPALEDKAVQYIFNHEIKLKEKKYTKEELEKYLEAEEQRITLI | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | C3PLX7 |
A6VYK6 | RSMH_MARMS | rRNA (cytosine-N(4)-)-methyltransferase RsmH | Marinomonas | MTKTMAEHISVMLNESVDMLVTDTNGLYVDGTFGRGGHTRLVLDRLDKGRLLGFDKDPVAIGHGKLLEQEDARFSIVQDSFANMAEHITNVFGVDRVDGVMMDLGVSSPQIDDAERGFSFMNDGPLDMRMNPDKGQSAAEWIATVSEKDMADVMYQYGEERFSRRIAKAICEYRSHTPILTTLQLSKIIAEANPAWEKGKNPATRAFQGIRIYINNELGDLEIGLEAAAQALKVGGRLAVISFHSLEDRIVKRFMKLQAKGPELPRHLPIRNAHLDIKFKTVGKAIKPSQSEVSENVRSRSAVLRVLERVSD | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | A6VYK6 |
A2CAG3 | ACCD_PROM3 | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta | Prochlorococcus | MSLFDWFADRRKGQFVGKVSQETEESDGLWVKCPECGQVVYRKDLHANASVCSNCGYHHRIDSDERIVLIADQGSFKSLDRNLSPTDPLGFKDRRAYADRLRESQASTGMKDGVVTGLCQVEGMPMAMAVMDFRFMGGSMGSVVGEKITRLVERATAQGLPLLIVCASGGARMQEGMLSLMQMAKISGALERHREAELLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPDNFQTAEYLQEHGFVDTIVPRTQLRKTLASLLLLHGCKAKKAAGK | Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. | A2CAG3 |
Q8IZT8 | HS3S5_HUMAN | Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 5 | Homo | MLFKQQAWLRQKLLVLGSLAVGSLLYLVARVGSLDRLQPICPIEGRLGGARTQAEFPLRALQFKRGLLHEFRKGNASKEQVRLHDLVQQLPKAIIIGVRKGGTRALLEMLNLHPAVVKASQEIHFFDNDENYGKGIEWYRKKMPFSYPQQITIEKSPAYFITEEVPERIYKMNSSIKLLIIVREPTTRAISDYTQVLEGKERKNKTYYKFEKLAIDPNTCEVNTKYKAVRTSIYTKHLERWLKYFPIEQFHVVDGDRLITEPLPELQLVEKFLNLPPRISQYNLYFNATRGFYCLRFNIIFNKCLAGSKGRIHPEVDPSVITKLRKFFHPFNQKFYQITGRTLNWP | Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site. Also generates GlcUA-GlcNS or IdoUA-GlcNS and IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry. | Q8IZT8 |
B2S9N1 | ATPF2_BRUA1 | F-type ATPase subunit b 2 | Brucella | MDATFWAFIALVIFVAIVVYMKVPGMIGRTLDERADRIKKELEEARTLREEAQQLLAEYHRKRKEAEKEAGDIVASAEREAKALLEEAKRATEEYVARRNKLAEQKIATAETDAINAVRASAVDLAVAAAGSILAEKVDAKADGNLFNDALAQVKSHLN | Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). | B2S9N1 |
Q1GEU7 | ATPG_RUEST | F-ATPase gamma subunit | unclassified Ruegeria | MPSLKDLKNRISSVKNTRKITKAMQMVAAAKLRRAQEAAEDARPYAERFNAVMAGLAASVGQSDTAPKLLAGTGSDQVQLLVVMTAERGLCGGFNANIAKLARQKVLDLQAAGKTVKILTVGKKGRDVLKREFGDLFVGHVDLTEVKRVGYVDAQGIAKDILARFDAGEFDVATIFYSKFQNVVTQIPTAQQIIPAEFDAEGAEATSGVVDYEPSEEAILADLLPRGVATQIFAGLLENGASEQGARMSAMDNATRNAGEMIDKLTIEYNRSRQAVITNELIEIISGAEAL | Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | Q1GEU7 |
Q710S3 | CYB_JACJA | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Jaculus | MTNIRKTHPLMKIVNESFIDLPTPSNISAWWNFGSLLGMCLIIQIATGLFLAMHYTSDTTTAFSSVAHICRDVNYGWLIRYLHANGASMFFICLFLHVGRGLYYGSYTFIETWNIGILLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIVAALAVVHLLFLHETGSNNPIGLNSDADKNPLHPYYTIKTALGFLLMFLVLLSLVLFCPDMLGDPDNYMPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVVALVLSILILAIVPFLHNSKQRSMIFRPISQCMYWLLMADLLTLTWIGGQPVEHPFIIIGQIASILYFTIILILMPLSSMLENKILKW | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. | Q710S3 |
Q1JDC8 | YIDD_STRPB | Putative membrane protein insertion efficiency factor | Streptococcus | MMKKLLIVSVKAYQKYISPLSPPSCRYKPTCSAYMLTAIEKHGTKGILMGIARILRCHPFVAGGVDPVPEDFSLMRNKNTSKNAEKA | Could be involved in insertion of integral membrane proteins into the membrane. | Q1JDC8 |
A9ADI4 | RL7_BURM1 | 50S ribosomal protein L7/L12 | Burkholderia cepacia complex | MAIAKEDILAAVEGMTVLELNELVKAFEEKFGVSAAAVAVAGPAGGGAAAAAEEKTDFTVVLAEAGSNKVAVIKAVREITGLGLKEAKDLVDGAPKPVKEGVDKAAAEEAKKKLEDAGAKVELK | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. | A9ADI4 |
C3MB73 | AROE_SINFN | Shikimate dehydrogenase (NADP(+)) | Sinorhizobium | MRDSRETFVNHAFVTGYPIKHSRSPLIHGYWLKQFGIAGSYRAHEVTPEAFPEFMGQLRDGGTGFCGGNVTIPHKEMAFELSDRPDELSAELGAANTLWLEDGRICATNTDGRGFVANLDERASGWDRISTAVILGAGGASRAVIQAVRDRGVKTIHVVNRTAARAQELADRFGRAVHAHPIAALSEVMAGAGLFVNTTSLGMDGEPAPAIDFSPLANGAVVTDIVYVPLKTPLLRQAEEQGYRIVDGLGMLLHQAAPGFEKWFGLRPVVDETLRQIIIKDMDVHA | Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). | C3MB73 |
P0CI69 | LPMG_SALT1 | Regulatory leader peptide for mgtA | Salmonella | MDPEPTPLPRWRIFLFR | Makes mgtA transcription sensitive to intracellular proline levels. At low levels of proline this proline-rich protein cannot be fully translated, and stem loop 'C' forms in the mgtA 5' UTR which permits transcription of the downstream mgtA gene. Osmotic shock induction (0.3 M NaCl) also depends on mgtL translation. The distance between the mtgL-translating ribosome and the nucleotides which form the downstream stem loop 'C' is critical for mgtL-mediated transcription of mgtA. Cotranscribed with mgtA. | P0CI69 |
A8YZP8 | HCHA_STAAT | Maillard deglycase | Staphylococcus | MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGLNREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK | Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. | A8YZP8 |
P49019 | HCAR3_HUMAN | Nicotinic acid receptor 2 | Homo | MNRHHLQDHFLEIDKKNCCVFRDDFIAKVLPPVLGLEFIFGLLGNGLALWIFCFHLKSWKSSRIFLFNLAVADFLLIICLPFVMDYYVRRSDWKFGDIPCRLVLFMFAMNRQGSIIFLTVVAVDRYFRVVHPHHALNKISNWTAAIISCLLWGITVGLTVHLLKKKLLIQNGTANVCISFSICHTFRWHEAMFLLEFFLPLGIILFCSARIIWSLRQRQMDRHAKIKRAITFIMVVAIVFVICFLPSVVVRIHIFWLLHTSGTQNCEVYRSVDLAFFITLSFTYMNSMLDPVVYYFSSPSFPNFFSTLINRCLQRKITGEPDNNRSTSVELTGDPNKTRGAPEALIANSGEPWSPSYLGPTSNNHSKKGHCHQEPASLEKQLGCCIE | Receptor for 3-OH-octanoid acid mediates a negative feedback regulation of adipocyte lipolysis to counteract prolipolytic influences under conditions of physiological or pathological increases in beta-oxidation rates. Acts as a low affinity receptor for nicotinic acid. This pharmacological effect requires nicotinic acid doses that are much higher than those provided by a normal diet. | P49019 |
Q43433 | VATB2_GOSHI | Vacuolar proton pump subunit B 2 | Gossypium | GRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPFFSAAGLPHNEIAAQICRQAGLVKRLEKAGDLLEDGEEDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHADVSNQLYANYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERKFVTQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQYYSRDAAN | Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. | Q43433 |
Q8R0Z5 | MFRN2_MOUSE | Solute carrier family 25 member 28 | Mus | MELEGRSAGGVAGGPAAGPGRSPGESALLDGWLQRGVGRGAGGGEAGAYQPPVRLDPESGPEYEALPAGATVTTHMVAGAVAGILEHCVMYPIDCVKTRMQSLQPDPAARYRNVLEALWRIMRTEGLWRPMRGLNVTATGAGPAHALYFACYEKLKKTLSDVIHPGGNSHIANGAAGCVATLLHDAAMNPAEVVKQRMQMYNSPYHRVTDCVRAVWQNEGAGAFYRSYTTQLTMNVPFQAIHFMTYEFLQEHFNPQRRYNPSSHVLCGACAGAVAAAATTPLDVCKTLLNTQESLALNSNITGHITGMASAFRTVYQVGGVTAYFRGVQARVIYQIPSTAIAWSVYEFFKYLITKRQEEWRAGK | Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly in non-erythroid cells. | Q8R0Z5 |
Q9UJ78 | ZMYM5_HUMAN | Zinc finger protein 237 | Homo | MEKCSVGGLELTEQTPALLGNMAMATSLMDIGDSFGHPACPLVSRSRNSPVEDDDDDDDVVFIESIQPPSISAPAIADQRNFIFASSKNEKPQGNYSVIPPSSRDLASQKGNISETIVIDDEEDIETNGGAEKKSSCFIEWGLPGTKNKTNDLDFSTSSLSRSKTKTGVRPFNPGRMNVAGDLFQNGEFATHHSPDSWISQSASFPSNQKQPGVDSLSPVALLRKQNFQPTAQQQLTKPAKITCANCKKPLQKGQTAYQRKGSAHLFCSTTCLSSFSHKRTQNTRSIICKKDASTKKANVILPVESSKSFQEFYSTSCLSPCENNWNLKKGVFNKSRCTICSKLAEIRHEVSVNNVTHKLCSNHCFNKYRLANGLIMNCCEHCGEYMPSKSTGNNILVIGGQQKRFCCQSCINEYKQMMETKSKKLTASENRKRNAFREENEKQLYGSSNTLLKKIEGIPEKKEKTSQLQLSVECGTDTLLIQENVNLPPSSTSTIADTFQEQLEEKNFEDSIVPVVLSADPGTWPRILNIKQRDTLVENVPPQVRNFNFPKDNTGRKFSETYYTRILPNGEKTTRSWLLYSTSKDSVFCLYCKLFGEGKNQLKNENGCKDWQHLSHILSKHEESEMHVNNSVKYSKLKSDLKKNKAIDAAEHRLYENEKNDGVLLLYT | Functions as a transcriptional regulator. | Q9UJ78 |
Q34321 | CYB_DASHA | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Dasyurus | MINMRKTHPLMKIINHSFIDLPTPSNISAWWNFGSLLGMCLIIQILTGLFLAMHYTSDTLTAFSSVAHICRDVNHGWLLRNLHANGASMFFMCLFLHVGRGIYYGSYLYKETWNIGVILLLTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLAEWIWGGFAVDKATLTRFFAFHFILPFIIMALAVVHLLFLHETGSNNPSGINPDSDKIPFHPYYTIKDALGFMLLLLVLLLLALFSPDLLGDPDNFSPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLAVLASILILLIIPLLHTANQRSMMFRPVSQTLFWILTANLITLTWIGGHPVEQPFIIIGQLAPMPYFLLILVMMPLAGLFENYMLKPEW | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. | Q34321 |
B3R6G6 | DNAJ_CUPTR | Chaperone protein DnaJ | Cupriavidus | MAKRDYYEVLGVGKNASDDEIKKAYRKLAMKFHPDRNPDSKDAEEKFKEAKEAYEMLSDPEKKAAYDQYGHAGVDPNMAGGFGGAQGYGGFAEAFGDIFGDIFGQGGGGRRGGGPQAYRGADLRYSMEISLEQAAHGHEAQIRVPHWDDCDHCHGNGAEPGSSVETCPTCHGAGQVRVSQGFFTMQQTCPKCHGSGKFIPKPCTKCHGQGKLKSQKTLEVKIPAGIDEGMRIRSSGNGEPGINGGPPGDLYVEVHIKPHAVFERDGDDLHCQMPISFATAALGGDLEVPTLSGKATFPVPEATQSGKTFRLRGKGIKGVRSGYPGDLYVHVNVETPVKLTEAQKEMLRQFDRSVHEGGSRHSPQETSWLDKVKSFFS | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins. | B3R6G6 |
B4NYT3 | DRE2_DROYA | Fe-S cluster assembly protein DRE2 homolog | Sophophora | MENFKGLQKSLYIWTDSADLDKRVQQLKSATGGDVALENVHRLSFSSYANSSFDLIVIECAQLTDSYVKLLHMLKPSGKLHLVSFIGPAASLLQEIKLSGFINCREDSPDALTAEKPGYETGSSARLSFAKKNASAVNVWKISGDDEELIDEEELLDEEDKQKPDPAGLRVCSTTGKRKACKNCSCGLAEELETEKQSQKANETAKSSCGNCYLGDAFRCSTCPYLGMPAFKPGEKVQLGDNLLKSDI | Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit. | B4NYT3 |
A1AXD1 | RL19_RUTMC | 50S ribosomal protein L19 | Candidatus Ruthia | MNLIDQIESEQLKLDLPSFSSGDTIVVQVKVREGERERLQAFEGVVIAKKNRGIGSAFTVRKISHGEGIERVFQTHSKMIDSIEVKRHGKVRQAKLYYLRSLTGKKARIKEKLQLKK | This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. | A1AXD1 |
B8CH33 | HSLO_SHEPW | Heat shock protein 33 homolog | Shewanella | MTKDNLYRYLFDNASVRGELVQLEKSYQEVIAAHDYPVAIQHLLGELMAATSLLTATLKFSGDISIQLQGDGPVSLAVINGNNLQQLRGVSRWDGDIAADAQLQSLFGKGHMVITLTPDDGERYQGVVALDKETLSECLEAYFEQSEQLPTKIKLFADAKQAAGMFLQVLPTDGNHNEEFEHLSVLTETVKQEELFTLEAEEVLHRLYHEEEVRLFEPVAITFNCTCSKERSAQAIRTVAKEEIDSIIAEQGKIEMGCEYCNSKYVFDAIDVEAIYAVAPNSGTTQ | Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | B8CH33 |
A3PGM1 | RL14_CERS1 | 50S ribosomal protein L14 | Cereibacter | MIQMQTNLDVADNSGARRVQCIKVLGGSHRRYASVGDIIVVSVKEAIPRGRVKKGDVRKAVVVRTAKEVRREDGTTIRFDRNAAVILNNQGEPVGTRIFGPVVRELRAKNFMKIISLAPEVL | Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. | A3PGM1 |
Q88BX8 | GLMS_PSEPK | L-glutamine--D-fructose-6-phosphate amidotransferase | Pseudomonas | MCGIVGAVAERNITAILIEGLKRLEYRGYDSAGLAVLTQNGELQRRRRIGKVSELEVAVADDPLAGQLGIAHTRWATHGAPTEGNAHPHFSGNDVAVVHNGIIENHEELREELKGLGYVFTSQTDTEVIVHLIHHTLKSIPDLTDALKAAVKRLHGAYGLALISAKQPDRLVAARSGSPLVIGLGLGENFLASDQLALRQVTDRFMYLEEGDIAEIRRDQVSIWDQQGNKVQRETVQYHEGAEAADKGAYRHFMLKEIHEQPSVVQRTLEGRLGKDNVLVQAFGPQAADLFAKVRNVQIVACGTSYHAGMVARYWLESLAGIPCQVEVASEFRYRKVVVQPDTLFVSISQSGETADTLAALRNAKELGFLGSLAICNVGISSLVRESDLTLLTLAGPEIGVASTKAFTTQLVSLMLLTLALGQVRGTLEAGVEAELVEELRRLPTRLGEALAMDATVEKIAELFADKHHTLFLGRGAQYPVAMEGALKLKEISYIHAEAYPAGELKHGPLALVDNDMPVVTVAPNNELLEKLKSNLQEVRARGGELVVFADEHAGMTNGEGTHVIKVPHIADALAPILYTIPLQLLSYYVAVLKGTDVDQPRNLAKSVTVE | Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. | Q88BX8 |
Q9K0K4 | TRMD_NEIMB | tRNA [GM37] methyltransferase | Neisseria | MLIQAVTIFPEMFDSITRYGVTGRANRQGIWQFEAVNPRKFADNRLGYIDDRPFGGGPGMIMMAPPLHAAIEHAKTQSSQAAKVIYLSPQGKPLTHQKAVELAELPHLILLCGRYEGIDERLLQSSVDEEISIGDFVVSGGELPAMMLMDAVLRLVPGVLGDMQSAEQDSFSSGILDCPHYTKPLEFQGMAVPEVLRSGNHGLIAEWRLEQSLRRTLERRPDLLEKRVLIPKESRLLETIRQEQREIQS | Specifically methylates guanosine-37 in various tRNAs. | Q9K0K4 |
C1IC47 | 3S13_WALAE | Three-finger toxin W-III | Walterinnesia | MKTLLLTLVVVTIVCLDLGHTFVCHNQQSSQPPTTTNCSGGENKCYKKQWSDHRGSITERGCGCPTVKKGIKLHCCTTEKCNN | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. | C1IC47 |
P0CL74 | DNLI_PYRAY | Polydeoxyribonucleotide synthase [ATP] | Pyrococcus | MRYIELAQLYQKLEKTTMKLIKTRLVADFLKKVPEDHLEFIPYLILGDVFPEWDERELGVGEKLLIKAVSMATGIDSKEIENSVKDTGDLGESIALAVKRRKQKSFFSQPLTIKRVYQTLVKVAETTGEGSQDKKMKYLANLFMDAEPIEAKYIARTVLGTMRTGVAEGLLRDAISLAFNVKVELVERAYMLTSDFGFVAKIAKTEGNDGLAKVTIQIGKPIKPMLAQQAANIKEALLEMGGEAEFEIKYDGARVQVHKDGEKVTIYSRRLENVTRAIPEIVEAIKEALKPAKAIVEGELVAIGEDGRPLPFQYVLRRFRRKYNIEEMMEKIPLELNLFDVLYVDGVSLIDTKFMERRKKLEEIVEANGKVKIAENLITKNVEEAEQFYKRALEMGHEGLMAKRLDAIYEPGNRGKKWLKIKPTMENLDLVIIGAEWGEGRRAHLLGSFILGAYDPETGEFLEVGKVGSGFTDDDLVEFTKMLRPLIIKEEGKRVWIQPKVVIEVTYQEIQKSPKYRSGFALRFPRYVALREDKGPEDADTIERIAQLYELQERMKGKV | DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. | P0CL74 |
Q9PFB8 | MUTL_XYLFA | DNA mismatch repair protein MutL | Xylella | MPIRQLPEILINQIAAGEVVQRPASVVKELVENAIDAGATRVDIELEAAGGRLIRIRDNGHGMAAQELPLAVLRHATSKIASLDDLEAVATLGFRGEALPSIVSVSRFTLMSRRAMDEHGAVLQIEGGTLGEVIPHAHAPGTTVEVRDLFYNVPARRKFLRAERTELGHIEEWARSLALAHPDLELRLSHNGKLSRRYKPGDWYSDARLIEILGEDFAHQALRVDHSGAGLRLHGCIVQPHYSRSNTDQQYLYVNGRAVRDRSVAHAVKQAYSDVLYQGRHPAYVLFLELDPARVDVNVHPAKQEVRFRDARLIHDFVYRTVQGTLAQTRAGTPPLAVGAGDVGGEGARPPVRHAVSFSGRRGGASHVLGSYSASTAPLMQSAPSVSVADAPAAYAALYAAPPTQVIDAVPQMQTGLPLAAGAGDVPPLGYAIAQLHGIYILAECADGLIVVDMHAAHERIGYERLKRAHDGIGLRTQPLLVPMTLMVAEREADVAECEAETLASLGFEVTRSGPGSLQVRSIPALLAQAEPEILLRDVLSDLSEHGHTRRVAEARDTLLATMACHGAVRAQRRLSISEMNALLRDMEATERSGQCNHGRPTWARFSLAEIDRWFLRGR | This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex. | Q9PFB8 |
B7MDB8 | COBS_ECO45 | Cobalamin-5'-phosphate synthase | Escherichia | MSKLFWAMLSFITRLPVPRRWSQGLDFEHYSRGIITFPLIGLLLGAISGLVFMVLQAWCGAPLAALFSVLVLVLMTGGFHLDGLADTCDGVFSARSRDRMLEIMRDSRLGTHGGLALIFVVLAKILVLSELALRGEPILASLAAACAISRGTAALLMYRHRYAREEGLGNVFIGKIDGRQTCVTLGLAAIFAAVLLPGMHGVAAMVVTMVAIFILGQLLKRTLGGQTGDTLGAAIELGELVFLLALL | Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate. | B7MDB8 |
A4IYP1 | SYI_FRATW | Isoleucyl-tRNA synthetase | Francisella | MSDYKDTLNLPKTSFSMKGNLANKEPMILNKWEKQGIYKKIREHFAGREKFVLHDGPPYANGSIHVGHAVNKILKDIIIKSKTLSGYDAPFTPTWDCHGLPIELQVEKKHGKAGQSISEDDFRKECRKYAKKQVEIQKKDFKRLGVLGDWEQPYLTINFDYEANMIRTLAKIIENGHLSKGFKPVHWCTDCGSALAEAEVEYADKVSPAIDVKFKIKDKDKLAQAFGLDSLNHDAFAIIWTTTPWTLPANQAIAVNNQLNYSLIKIEDFYIILAENLVEQTLKRYAIENAQIIATTTGNKLTGIIAEHPFYSRHVPILHGDHVTDDSGTGLVHTAPTHGVDDFTLGKEHNLSMEIFVKGNGCYSENTKLFAGEFIFKANDRIIELLGEKKRLMNSDKIKHSYPHCWRHKTPLMFRATPQWFISMEKQGLRDKALQAIKETSWAPSWGQARIEGMVKDRPDWCISRQRTWGVPLPLFIHKETEELHPNTIEILHKVAEKIEKDGIEAWFNADDCEFITETAQYKSVKDTLDVWFDSGSSSMCILDLDKRLSYPADLYLEGSDQHRGWFQTSLLVAMSAKGSQPYKEVFTHGFVVDEHGRKMSKSLGNVTSPQDIYNTLGADILRLWTASTDYKSEMAVSDQILKRTADTYRRLRNTARFLLSNLDGFNPVTDIIEFDKLVKLDQWAIAKTKEFQDKIIEAYDKYQTHTVAQLIHHFCSIEMGSFYLDIIKDRQYTAKTDGHPRKSAQTAIYHIVHALVRWMAPILSFTANEIWDATPKTTDLPIQLCEWYTGLKSFDQDAELDLEYWAKIQEIRSEVNRVLEIKRNEDVIKASLEAEITIYADKYNYKLLEKLGNELRFLLISSKADLKVIEESTSSSIAANIPGLLIEITKIEEPKCERCWHRSSTVGDNPQYKDICSRCVENITTEAGESREFA | Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). | A4IYP1 |
A8FQ83 | LEU1_SHESH | Alpha-isopropylmalate synthase | Shewanella | MSNRVIIFDTTLRDGEQALAASLTVKEKLQIALSLERLGVDVMEVGFPVSSPGDFNSVQTIANTVKNSRVCALARALEKDIDAAAQSLSVADQFRIHTFISTSTIHVESKLKRSFDQVLEMAVGAVKYARRFTDDVEFSCEDAGRTPIDNLCRMVEEAIKAGARTINIPDTVGYTIPSEFGGIIETLFNRVPNIDQAIISVHCHDDLGLSVANSITAVQQGARQIECTVNGIGERAGNCSLEEIAMILSTRKDSLGLETGINAKEIHRTSNLVSQLCNMPVQANKAIVGANAFTHSSGIHQDGMLKSQNTYEIMTPESIGLHRNNLNMTSRSGRHVIKHRMEEMGYGNKDYDMDTLYEAFLQLADKKGQVFDYDLEALAFMEAQVDEEADYKLAQLVVHSDSTEGNATATVKLEIDGKTVTEAATGNGPVDAAYNAIARASQCEVNITSYKLSAKGEGQNALGQVDIEANYNEQSFHGVGLATDVVEASVQALVHVMNLTSRADKVADCKEKIQKDRSELGGV | Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). | A8FQ83 |
Q7NM37 | GLGA_GLOVI | Starch [bacterial glycogen] synthase | Gloeobacter | MKVLFAAAECAPLAKVGGMADVVGSLPLALAEMGLDVRIILPYYGFLGELPKSEQPVWTGGAMFQQVEIYEARLPGSDIPLYLVGHPAFANERIYGFEDEAWRFTLFSRTVAEFLWRGGWDPQVLHCHDWHTGLLPLWMRSMPVMTVFTIHNLAYQGPPLPYFRAFVDVPYDTGAWNPMVAGIIHSDAITAVSPTYAREICTPEYGERLDGLLRGQGNRLTGILNGINTKALDPATDKHLTVNYDTTSLDRRVENKLALQREFGFEVSADRLLVGIVSRLVDQKGFDLLAPLWDNWMHTSGAQLVVLGSGDPFYEFLFRSAAERYPDRIKAVLSYNVPIAQRIYGGADLFLMPSRFEPCGIGQMIALRYGAVPLVRKTGGLADTVFFHNPLDEKGNGFLFDRYDPANLLAMLYRAEEAFRYKDYWRRLQLRGMEADLSWRASAHQYADLYKSLIARLG | Synthesizes alpha-1,4-glucan chains using ADP-glucose. | Q7NM37 |
O14040 | DI3L2_SCHPO | DIS3-like exonuclease 2 | Schizosaccharomyces | MDLKPNIRRKEKRNLLKGEAALEKKGSIDRKTKNKAYPSTTHDPHQNDDSNIPGLGSGLLERIKDIVQRPTDTQLKGQDSNHKKASLTETKTEKAKVKPKAKKKNSKEKISKSSKQDEHKTDVHKESVSKLSKNLESRNNRDENSAKREKNNSHQVEADTNNATEMVSSNAKKSVYPLYYDSATVKKGLKSGTLFKGTLRILENHRSAFACMEDIPDFYVDGPIARNRAFHNDVVIVEPVMNNDSPTEKSNFLQNGVEKVKIKDHDDELGGAMEHLERLEIKSVASFKGDSRTRARVVAIEKRAEISKIVGILRAPGWSLKNVEYVSKKSSYAIFIPKDKRLPFITIHKNDLSDLSGENWIENILKHHDQLFSVEITRWSIYSRYPMGVLGEKLGNITDVEAYTNALLLENGISSSPFSDEVLNCLPPDDWIISHEEIKKRRDLRNELIITIDPETARDLDDAVSCRALDNGTYEVGVHIADVTHFVKPDSALDKEAASRATTVYLVQKAIPMLPPLLCERLCSLNPNVERLAFSVFWKLDSNGKEIGKRWFGKTVIKTCARLAYSEAQGVIEGKSWDDAVGKPIGGTHTPKDVETSILTLCEISRKLRKDRFAKGAVEINSTELKFQLDEYGMPNKCEVYEQTDANHLIEEFMLLANRSVAEHISKNFSNNSLLRRHASPKEKQINEFCHFLKSMNFDFDASSSAAFNASMVRLRSTFNEELVELFENMAVRSLNRAEYFCTGDFGEKTDWHHYALSFNHYTHFTSPIRRYPDIIVHRLLERSLKNTSPGIDKKNCSLVAAHCNEKKEKSTTVQEDSQQLFLSVYIAEYCKKHDKKSMPVQAFATRISGNSIDVYISEYGISNRVDLSSDDRIKSFIVAPDDSSVKITLFDDSQKTIALTDRFQVYLYSDYSRTFFSIRCSLVSLN | 3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'. | O14040 |
Q16AZ3 | DUT_ROSDO | dUTP pyrophosphatase | Roseobacter | MALVSLKLQWADGADTSVPLPAYETSGAAGADIRANCPDGPVTLAPGARALVPTGLRMAIPQGYEVQIRPRSGLALRHGITLVNSPGTIDSDYRGAVGVIMQNLGDAAFEITHGMRIAQMVVAPVVQASFELSDSLSETDRGSGGFGSTGGD | This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. | Q16AZ3 |
Q8RNT4 | LOX_PSEAI | Oleate 10S-lipoxygenase | Pseudomonas | MKRRSVLLSGVALSGTALANDSIFFSPLKYLGAEQQRSIDASRSLLDNLIPPSLPQYDNLAGKLARRAVLTSKKLVYVWTENFANVKGVPMARSVPLGELPNVDWLLKTAGVIVELIVNFVASLPASAAAQFERIAAGLSGDLEAARQVHEALLEEAKNDPAAAGSLLLRFTELQTRVIALLTRVGLLVDDILKSASNLVTQGGQGDGLNRFRAVFGTLRLPEVADSFRDDEAFAYWRVAGPNPLLIRRVDALPANFPLGEEQFRRVMGADDSLLEAAASRRLYLLDYAELGKLAPSGAVDKLLTGTGFAYAPIALFALGKDRAGLLPVAIQCGQDPATHPMFVRPAESESDLYWGWQMAKTVVQVAEENYHEMFVHLAQTHLVSEAFCLATQRTLAPSHPLHVLLAPHFEGTLFINEGAARILLPSAGFIDVMFAAPIQDTQATAGGNRLGFDFYRGMLPESLKARNVDDPAALPDYPYRDDGLLVWNAIRQWAADYVAVYYASDGDVTADVELAAWVGEVIGSGKVAGFRPITGRSQLVEVLTMVIFTASAQHAAVNFPQPSMMTYAPAICAMSAAPAPDSPSGKSEADWLKMMPPTLVALEKVNIYHLLGSVYHGRLGDYRQTGFPYAPVFSDRRVTASGGPLERFQARLKEVEATIRTRNQARRKPYEYLLPSRIPASTNI | In presence of oxygen, converts linoleate into (9S)-hydroperoxy-10,12-octadecenoate (9HPOD), which spontaneously decomposes to the corresponding 9-hydroxy-10,12-octadecenoate (9HOD), and into 13-hydroperoxy-9,11-octadecenoate (13HPOD) which spontaneously decomposes to the corresponding 13-hydroxy-9,11-octadecenoate (13HOD). Also active on linolenate. To a lesser extent, is also able to convert oleate into (10S)-hydroperoxy-8E-octadecenoate, which spontaneously decomposes to the corresponding 10-hydroxy-8E-octadecenoate. Is almost not active on arachidonate. | Q8RNT4 |
C0RLN1 | GCSP_BRUMB | Glycine dehydrogenase (aminomethyl-transferring) | Brucella | MTEFLPFVARHIGPRHEDERAMLAALGLPSMETLITQAVPASIRLNRALNLPAALSEADALAELGTIMGRNVVKKSFIGAGYHGVHTPPVIQRNLFENPAWYTAYTPYQSEISQGRLELLFHFQTLVAELTGLPVACASLLDEATAVAEAIGVACRHHRDKRSRILLAGELHPQTVDVVNTRAEPLGWEIATGSDVDDNTAAIVVPWPDTRGVYGDFAKVIADAKAKGALVIAVADPLALTIMEAPARWGADMAVGSMQRYGVPMGFGGPHAAYLAVSEALTRIIPGRIVGQSVDAHGRAAYRLALQTREQHIRRDKATSNICTAQALLANMAAAFAIWHGPAGLQAIATRVAALAARFAAALKAAGVEIAGESLFDTVTAKVPGKAAAIAAEADKGGRLIRIIDADTVGVTFDETSTEEDLTALASLFGAKPVGGDTVLVPGKERGEGFLTQEVFHSHRSETEMMRFLRRLADKDLALDRAMIPLGSCTMKLNAAAEMMPVSWNTVANLHPFAPAEQVQGYAKMTSDLEAWLCEITGFAGVSLQPNAGSQGEYAGLMAIRHYHQARGQGHRNICLIPSSAHGTNPASASMAGMSVVVVNCRPDGDIDIDDLKAKAEKHRDNLAAFMITYPSTYGVFEEGIKAFCEIVHDNGGQVYFDGANLNALVGLARPADIGADVCHMNLHKTFCIPHGGGGPGVGPIGVAKHLVPYLPGHVEAGSEHAVAAAQFGSASILVITWMYIRMMGGAGLKKATEAAILNANYIAHRLKGVYPILYTGAHDRVAHECIVDTRVLKDSAGITVEDVAKRLIDYGFHAPTMSWPVAGTLMIEPTESEPKLEIDRLCDAMIAIAGEAKKVADGVWPADDNPLANAPHTASDTLATEWKHPYTREEAVFPGGAFDPTAKYWPPVSRVDNVGGDRNLICSCPPVAAYG | The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. | C0RLN1 |
Q8DCA3 | METK_VIBVU | Methionine adenosyltransferase | Vibrio | MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVMVGGEITTSAWVDIEELTRETVREIGYVHSDMGFDANSCAVLNTIGKQSPDINQGVDKADPKEQGAGDQGIMFGYACNETEVLMPAPITYAHRLMERQAKVRKDGTLPWLRPDAKSQVTFQYEQGKIVGIDAVVLSTQHCDSISTPDLREAVMEEIIKPVLPSEWLNKETKYFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGAARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGMADRCEIQLSYAIGVADPTSIMVETFGTEKVSHDIIIEAVRQFFDLRPYGLQEMLNLLQPIYKKTAAYGHFGREEFPWEATDKAALLREFAGIK | 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. | Q8DCA3 |
O47675 | COX2_NYCPR | Cytochrome c oxidase polypeptide II | Nyctereutes | MAYPFQLGLQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAIILILIALLSLRILYMMDEINNPFLTMKTMGHQWYWSYEYTDYEDLNFDSYMIPTQELKPGELRLLEVDNRVILPMEMTVRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMAMRPGLYYGQCSEICGSNHSFMPIVLEMVPLSYFETWSALMV | 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 subunit 2 and heme A of subunit 1 to the active site in subunit 1, 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. | O47675 |
A1W8D4 | RECR_ACISJ | Recombination protein RecR | unclassified Acidovorax | MSDTSSLDALIQALRRLPGVGVKSAQRMAFHLLQHDRAGAQVLSQALAQAATQVRHCERCHTFTEGAVCETCLDPARDATRLCVVETPADQAAMERTAAFKGLYFVLMGRLSPLDGVGPRDIGVHNLLERASDGVVQEVILATSFTAEGEATAHAIGEALKRRGVHVTRLARGVPVGSELEYVDLGTIAHALADRR | May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | A1W8D4 |
Q5E968 | CATK_BOVIN | Cathepsin K | Bos | MWGLTVLLLPVVSFALYPEEILDTQWELWKKTYRKQYNSKGDEISRRLIWEKNLKHISIHNLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLKVPASRSRSNDTLYIPDWEGRAPDSVDYRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGCGGGYMTNAFQYVQKNRGIDSEDAYPYVGQDENCMYNPTGKAAKCRGYREIPEGNEKALKRAVARVGPISVAIDASLTSFQFYRKGVYYDENCNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGENWGNKGYILMARNKNNACGIANLASFPKM | Thiol protease involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen. | Q5E968 |
Q9JU79 | LEU3_NEIMA | Beta-IPM dehydrogenase | Neisseria | MTKHIAILRGDGIGPEIVAETVRVLDKLIAQGLDVGYEYAPLGGEAYDEYGHPYPEFTQNLCRKADAVLLGAVGSPQYDNLDRPLRPERGLLAIRKDLNLFANLRPAILYPELANASTLKSEIVAGLDILIVRELTGDIYFGEPRGIRVLENGEREGYNTMKYSESEIRRIAHVAFQSAQKRSKKVCSVGKANVLETTELWREIFEEIGKEYPDVELSHMYVDNAAMQLVRAPKQFDVIATGNIFGDILSDEASMLTGSIGMLPSASLDENGKGLYEPSHGSAPDIAGQNKANPLATVLSLAMLLRYSLNDEARAQQVENAVQKVLQQGLRTGDIYEEGTKLVSCSEMGDAVLATL | Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. | Q9JU79 |
Q9KRP7 | ALDC_VIBCH | Alpha-acetolactate decarboxylase | Vibrio | MNPLLSAHCSCSQEIAQQFAHYQHISGEGEIYQTSLMSALIAGVYEGATTIAQLLEHGDFGLGTFNELDGELIAFDRQVFQLRADGSAQPAHPEQQTPFAVFTFFKADIELPITERMTREQVHQLIDRLVPSDNLFCAIRIDGTFPSVQTRTVPKQQRPYRPMLEVVKQQPVFRFQQQHGVIAGFRSPQYTTGINVPGYHEHFITQQRTGGGHIQDYIIRSGFLQIGRVSRLVVDTPVSRDFLEANLTPNNIRTAIEAAEK | Converts acetolactate into acetoin. | Q9KRP7 |
Q122H7 | SUCC_POLSJ | Succinyl-CoA synthetase subunit beta | unclassified Polaromonas | MKIHEYQGKEILRNFGVPVPRGIPAFTVQEAVEAAQKLGGPVWVVKAQIHAGGRGKGGGVKVAKTIDDVKRIAGEILGMQLKTHQTGPEGQKVRRLYIEDGADIQKEYYVSAVTDRESQKVAFIASSEGGMDIEEVAHSNPEKIIKVFVDPLVGMTDAQAKEVAAGIGMPADSVAQTVDVLQKLYKCYMETDASLVEINPLNRNSKGEIMALDAKFNFDANALFRHPEIVAYRDLDEEDPAEVEASKFDLAYISLDGNIGCLVNGAGLAMATMDTIKLFGGEPANFLDVGGGATAEKVTEAFKIMLKNPEVKGILVNIFGGIMKCDTIADGVITACKAVNLSVPLVVRMKGTNEDLGKKMLADSGLPIIAADTMAEAATKIVAAVK | Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. | Q122H7 |
B3E4H5 | LPXA_TRIL1 | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase | Trichlorobacter | MSIHASAIVHPSAQLAEGVEVGPYAIIEEHAIIGKGTSIGAHAVIGKWTELGENNQIYHMASVGAAPQDLKYKGEECWTRLGNGNVIREFATIHRGTVTGHAETVMGNNNLMMAYSHVAHDCTVGNGVVMANAATLAGHVTVQDNVILGGLVAIHQFVTIGAYAMLGGGTLVGMDIPPYMIATSGGKREAQLRGLNLIGLKRRGFSDEAISGLKKAYKTLFMAHLKQADAIAKIRSEIVGCAEVDTLLAFIEASQRGICRG | Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | B3E4H5 |
Q8LB17 | RBL15_ARATH | Rhomboid-like protein 15 | Arabidopsis | MRPNIVTEAGVQTRVGQWWNAIPFLTSSVVVVCGVIYLICLLTGYDTFYEVCFLPSAIISRFQVYRFYTAIIFHGSLLHVLFNMMALVPMGSELERIMGSVRLLYLTVLLATTNAVLHLLIASLAGYNPFYQYDHLMNECAIGFSGILFSMIVIETSLSGVTSRSVFGLFNVPAKLYPWILLIVFQLLMTNVSLLGHLCGILSGFSYSYGLFNFLMPGSSFFTTIESASWMSSFIRRPKFIMCTGGNPSSYIPTYSAQNTTSSGFSTGNAWRSLSSWLPQREASNQSSEDSRFPGRGRTLSTARDPTAPAGETDPNLHARLLEDSSSPDRLSDATVNTVADSRQAPIANAAVLPQSQGRVAASEEQIQKLVAMGFDRTQVEVALAAADDDLTVAVEILMSQQA | Probable rhomboid-type serine protease that catalyzes intramembrane proteolysis. May function in senescence. | Q8LB17 |
Q9XSM2 | TRYT_SHEEP | Tryptase-2 | Ovis | MLHLLALALLLSLVSAAPAPGQALQRSGIIGGKEAPGSRWPWQVSLRVRDQYWRHQCGGSLIHPQWVLTAAHCIGPELQEPSDFRVQLREQHLYYQDRLLPISRVIPHPHYYMVENGADIALLQLEEPVSISRHVQPVTLPPASETFPPESQCWVTGWGDVDNGRPLPPPYPLKQVKVPIVENSVCDWKYHSGLSTDYSVPIVQEDNLCAGDGGRDSCQGDSGGPLVCKVNGTWLQAGVVSWGDGCAKPNRPGIYTRITSYLDWIHQYVPQEP | Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. | Q9XSM2 |
A8ZV62 | RL22_DESOH | 50S ribosomal protein L22 | Desulfosudis | MEQVSATARYLRIGPQKVRMLVDGIKGKSVEKGLNTLRFMPNKGAGLVEKALRSAVANAEEKNMDVDGLVILNVLVDQGPTLKRFRPRARGRATRILKRTSHITVVLAEKAAKN | The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | A8ZV62 |
B7GW24 | RS13_ACIB3 | 30S ribosomal protein S13 | Acinetobacter calcoaceticus/baumannii complex | MARIAGVNIPDNKHAVISLTYIFGIGRHTAKNILAAVGITETTKIRELDDAQLDAIRAEVAKVPTEGDLRREISMNIKRLMDLGCYRGLRHRRSLPVRGQRTKTNARTRKGPRKPIKK | Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. | B7GW24 |
A1U1R0 | LPXH_MARN8 | UDP-2,3-diacylglucosamine diphosphatase | Marinobacter | MTTLFISDLHLEESRPDITGAFLTFLRDKALGVERLYILGDFFEAWIGDDERTPLQEQVAAALREVRDTGTDIYLMHGNRDFLIGEDFCARAGAILLDDPTVVDLYGTPALLMHGDSLCTADVEYQKFRANMRNPQTVKMLLSRPLKDRQLMARQLREISMAKNQGKAETIMDVTPEEVVKELEAHNVQLMIHGHTHRPAIHELEANGRPARRIVLGDWDENVWWLEASKNQPVALRHQPLADF | Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | A1U1R0 |
Q5T8A7 | PPR26_HUMAN | Protein phosphatase 1 regulatory subunit 26 | Homo | MFLMNASPVVALQSKWEAFGPPGSCRFPRCFSEADEGVESASVSARVQMLISTLQRDGAARGTSDERAAQRGHRAEGCHDARPAAKPTVHKEPPALAVCGLVADFDPMGEEETTDFGPLVLDSDSDDSVDRDIEEAIQEYLKAKSGAAQPGAGGAQPGAAQPSRAAGGGSRCKPEPAHGSAPTALCPPKLVPGSGGGPGSQVGSSKDQGSASPVSVSSDDSFEQSIRAEIEQFLNEKRQHETQKCDGSVEKKPDTNENSAKSLLKSHQEPPTKVVHRQGLLGVQKEFAFRKPPRLAKMNVQPRSLRSKVTTTQENEGSTKPATPCRPSEAAQNKGGIKRSASAARRGKRVMSAAQASEASDSSSDDGIEEAIQLYQLQKTRKEADGDLPQRVQLREERAPDPPAHSTSSATKSALPETHRKTPSKKKLVATKTMDPGPGGLDTDHAPKLLKETKAPPPASPASRSEFVERSSCRADTSAELMCAEAILDISKTILPAPVEGSDGSLSASPLFYSPNVPSRSDGDSSSVDSDDSIEQEIRTFLALKAQSGSLLARGESCPQAAQGPLLPPGLNSQTGGHKTPLSKTPDPLLGCKRKRRGGGHVRPSTPKKMQEVVKDGSQDADHSQGRAEPGHERRDLPIQGKASEALGGEGTARGPGDTRMSQGQGKTDEARRLDEKESSEDKSSSLDSDEDLDTAIKDLLRSKRKLKKRCREPRAACRKKVRFSTAQTHFLEQLGGLRRDWKDRGPPVLKSCLSKSKRDSGEGPGKKPPSVFGSTAERMRQEGAASQDAALAFRVRRPASASASEGNPFPRESQGPAPSPGSLSDDSSSVDSNDSIELEIRKFLAEKAKESVSSSEVQAEGPTALGTGGPARPEVLCRKEPAPPPGVCTRSQRARGVPHLAEGLRGTESAGAQGTAGLFSQGGKGLPAAPARGDPVPPRSTSGGVSAKGLSVSRRNVYVHKDQSPRGAEPAAKSAFGQLPSCATAGTEAGGARGTFHMGCGSPSFLTPSPGAERDAGAQADRTPPWSDFAHQSRLPSPWVLRSEGRDAVWRGGVGSERDKGSEGPARGLPSLPLAGFSPLLSTQLFHFGKGVSWGGRQAGLFSPHLGLPLQGPSFSAFREAQAGPSPVFGSPHLLAKKDGGPWPTRKAQAGLSLHDRRSSGSEESILDLRYRRRVNRDDQEQDALGSDASDFSDTSTEDSGGSSVVKV | Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. May positively regulate cell proliferation. | Q5T8A7 |
A7ZM51 | CLCB_ECO24 | Voltage-gated ClC-type chloride channel ClcB | Escherichia | MFRRLLIATVVGILAAFAVAGFRHAMLLLEWLFLNNDSGSLVNAATNLSPWRRLLTPALGGLAAGLLLMGWQKFTQQRPHAPTDYMEALQTDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTPRQEWKLWIACGAAAGMAAAYRAPLAGSLFIAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALLYNVQLSVTVQARDYALIISTGVLAGLCGPLLLTLMNACHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAPGGVFTPTLFIGLAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVISRTLHRDSIYRQHTAQHS | Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response. | A7ZM51 |
Q09FZ7 | CCSA_PLAOC | Cytochrome c biogenesis protein CcsA | Platanus | MIFLTLEHIFTHISFSIVSIVITIHLMTLLVDGIVGLYDSSEKGMIATFLCITGFLVTRWIYSRHFPLSDLYESLIFLSWSFSIIHMVPKIRNHKNHLSAITAPSAIFTQGFATSGLLTEMHQSAILVPALQSQWLMMHVSMMVLSYAALLCGSLLSIALLVIRFRKNIEIFGKDNYLLIGSFSFGESQYVNERSNILRNTSFLSFRNYYRYQLIQQLDHWSYRVISLGFIFLTIGILSGAVWANEAWGAYWNWDPKETWAFITWTIFAIYLHTRTNKDLQGANSAIVASIGFLIIWICYFGVNLLGIGLHSYGSFTLTSN | Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. | Q09FZ7 |
Q9FFZ6 | RBP11_ARATH | Small RNA-binding protein 11, chloroplastic | Arabidopsis | MAALARIGGRHLKSVCLINSSASCFFTQRRGVASKLFIGGLSFCTTEQGLSEAFSKCGQVVEAQIVMDRVSDRSKGFGFVTFASADEAQKALMEFNGQQLNGRTIFVDYAKAKQSLGGGGGYPIARGPPDPAVIAATRTTETSKSD | Probable RNA-binding protein that may be involved in salt and oxidative stress tolerance. | Q9FFZ6 |
B5XZS9 | CRCB_KLEP3 | Putative fluoride ion transporter CrcB | Klebsiella | MFQLLCAVFIGGGTGSVLRWWLGMKLNPVHHAIPIGTLTANLVGAFVIGAGLAWFNRLTDIDPMWKLLITTGFCGGLTTFSTFSAEVVFLLQQGRVSWALLNVMVNLLGSFAMTAVAFWLFSQAASR | Important for reducing fluoride concentration in the cell, thus reducing its toxicity. | B5XZS9 |
C8Z7U0 | YFH7_YEAS8 | Altered inheritance of mitochondria protein 12 | Saccharomyces | MVDTHKLADDVLHLLDNRIEDNYRVCVILVGSPGSGKSTIAEELCQIINEKYHTFLSEHPNVIEVNDRLKPMVNLVDSLKTLQPNEVAEMIENQGLFKDHVEDVNFQPIKYSALTSNNEECTAVVARGGTANAIRIATVDNPVNVNKLAQDSINIAQIVPMDGFHLSRRCLDLFKDPQTAHKRRGSPSTFDSNNFLQLCKILAKTSLCKVSSHHKFYSTSSVFEKLSKTFSQTIPDIFVPGFNHALKDPTPDQYCISKFTRIVILEGLYLLYDQENWKKIYKTLADTGALLVYKIDIDYEATEERVAKRHLQSGLVTTIAEGREKFRSNDLLNGRDIDNHLIKVDNIVHIRND | ATP-dependent kinase that could be involved in endoplasmic reticulum membrane assembly. | C8Z7U0 |
Q1MJ02 | KGUA_RHIL3 | GMP kinase | Rhizobium | MKPAKSSPVQIARRGLMLVISSPSGAGKSTIARTLLETDRQIGLSVSVTTRQRRPSEVEDVHYHFKSVREFERLRDSDALLEWAEVHGNFYGTPREPVEQAMGEGRDMLFDIDWQGAQQLQEKMSADVVSIFVLPPTMTELQSRLHRRAEDSEEVIQTRLANSRAEIAHWREYDYVIVNDDLNAALDAVQSIVKAERLRRDRRHGMFDFVRELLEETPSL | Essential for recycling GMP and indirectly, cGMP. | Q1MJ02 |
A0QIQ3 | LEXA_MYCA1 | LexA repressor | Mycobacterium avium complex (MAC) | MDDSNDSSSAGPDGRLHAVDPSLTERQRTILNVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRGVDDDVAAPATEVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGDGTLFLLKVVGDSMVEAAICDGDWVVVRQQHVADNGDIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV | 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. | A0QIQ3 |
P83299 | CAH1_CHIHA | Ice-CA | Chionodraco | AHAWGYGPTDGPDKWVSNFPIADGPRQSPIDILPGGASYDSGLKPLSLKYDPSNCLEILNNGHSFQVTFADDSDSSTLKEGPISGVYRLKQFHFHWGASNDKGSEHTVAGTKYPAELHLVHWNTKYPSFGEAASKPDGLAVVGVFLKIGDANASLQKVLDAFNDIRAKGKQTSFADFDPSTLLPGCLDYWTYDGSLTTPPLLESVTWIVCKEPISVSCEQMAKFRSLLFSAEGEPECCMVDNYRPPQPLKGRHVRASFQ | Catalyzes the reversible hydration of carbon dioxide. | P83299 |
Q65TP2 | EX7S_MANSM | Exodeoxyribonuclease VII small subunit | Basfia | MARKPKESSTVDFETTLNQLETIVTRLEAGDLPLEEALKEFENGIKLAKLGQERLQQAEQRIQILLQKSDTAELTDYQPTDE | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | Q65TP2 |
Q9JXI5 | GMHBB_NEIMB | D,D-heptose 1,7-bisphosphate phosphatase | Neisseria | MKLIILDRDGVINQDRDDFVKSVDEWIPVEGSMDAVAFLTQAGYTVAVATNQSGIGRKYFTVQNLTEMHAKMHRLVRQAGGEINGIWFCPHTDADNCNCRKPKPGMIEDIIGRFNAQASETWLVGDSLRDLQAIDAVGGKPALVLTGKGKKTLSQHGHELPEHTQVFDTLLDFSQYIMQENTAPQAD | Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position. | Q9JXI5 |
Q8YEA6 | LNT_BRUME | Apolipoprotein N-acyltransferase | Brucella | MIARLAGRIILLNGWRRALAAFLSGAFATLTQPPFDIFVAGFVSFPVLVWLIDGAIARTDAGPLRRLLLAAKVGWWFGFGYFVSGLWWIGTALLVDADQFAWALPLAVLGLPAFLALFYAFAAMIARLLWSDGLGRILAFAFGFALAEWLRTFIFTGFPWNLIGYAAMPVPLLMQSVAVIGLVGMSALAVFVFAAPALLTGGHFARTGIGLAIFLALAHVGFGAWTLSRAPAIVDENGPLAVRIVQPSIAQAMKWDNAERRAIFDKLVGLTEEAPAEGKPRPDVIVWPETAIPYILESTPQALAHIGDALQEGQVLLAGAVREEKGADGGEPRYYNSIYTIDDRGRIVSTADKVHLVPFGEYLPFESFLRGLGLQEVVEMPGGFTAGTTRHALAVKDGRSFLPLICYEAIFPDELGYEGAGASAIINVTNDAWYGDTPGPYQHFRQAQVRAVEQGLPLIRAANNGLSAIVDTYGRITGSLALDAVGVVDSYLPSPRDPFWGRPPGWIQTVLILLTLLAASVGLILYSRRRFH | Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. | Q8YEA6 |
Q11QA9 | RS7_CYTH3 | 30S ribosomal protein S7 | Cytophaga | MRKAKPKKRYLLPDPKFSDTMVTKFVNSLMYDGKKSTAYSIFYDAVALVEKKTSESGLEVWKKALNNVSPQVEVRSRRVGGSTFQVPTEVRPDRKMALGMKWLINYARSRGEKTMTDKLAGEIISASKGEGAAVKKRDDVHRMAEANKAFSHFRF | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. | Q11QA9 |
F4JZT3 | ARR24_ARATH | Arabidopsis response regulator 24 | Arabidopsis | MTRDQVAEELPNLAESKLTALVVDDSFVNQTIHQKLLNRLGIKNDVVTNGKEAVDVYCSGGNYDLILMDMDMPIMNGIQATKRLREMGIESKIAGVTTRANEGEKKEFMEAGLNDFQEKPLTISKLLSILHKLNFYVQT | Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling. | F4JZT3 |
Q9CAU4 | SCP4_ARATH | Serine carboxypeptidase-like 4 | Arabidopsis | MANNNVYSVLKSLLLLLHLVFLSKQHVDSASIVKFLPGFEGPLPFELETGYIGVGEEEEVQLFYYFIKSERNPKEDPLLLWLTGGPGCSAISGLLYQNGPLAMKLDVYNGTLPSLVSTTYSWTKTSSMIFLDQPVGTGFSYSRTQLFNKPSDTGEAKRIHEFLQKWLGKHQEFSSNPFYVGGDSYSGLVVPATVQEISKGNCQCCNRPINLQGYVLGNPLTDCVYDCNYRVPFAHKMALISDELYESLKRTCRGEYVNVHPHDTECLKFVEEFNKLTNRVCERHILHSCCETETPSCYSYRFMLTTYWANDETVRKALQINKESIGEWTRCYRGIPYNHDIKSSVPYHMNNSIDGYRSLIYSGDHDIQVPFLGTQAWIRSLNYSIIDDWRPWMIKDQIAGYTTSYVNKMTFATVTGGGHTAEFTPKETFMMFQRWINGQPL | Probable carboxypeptidase. | Q9CAU4 |
Q3SZX2 | IPP2_BOVIN | Protein phosphatase inhibitor 2 | Bos | MAASTASHRPIKGILKNKSSTTSSVVSTAEQPGKSVDEELSKKSQKWDEMSILATYHPADKDYGLMKIDEPSTPYHSMVADDEDALSDSETTEALTPDILARKLTAAAAESLEPKYRVREQESSGDEDSDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLNDEEEDEEMSETAAGESMNMEESSQGSATSDQLQNKSQSS | Inhibitor of protein-phosphatase 1. | Q3SZX2 |
Q8IQ56 | TMM11_DROME | Protein PMI | Sophophora | MVSRNIESTSKVPTFHVIREVYDSSNAHERFEAELDKALEAKLDFIVIEPPRLGDETGRWIWVGNCLHKTAVATGVVSLVASLLWRDRPIIAAPACALSIFCTGLYTVSWNYDPCCQYQVENNDTVLEKLPLTDVSSPVILGYSPNSKTKYLHRSVSLLSAALCAWQIWRSYNRFVHSAGSG | Plays a role in mitochondrial morphogenesis. | Q8IQ56 |
Q3EBQ3 | FRS2_ARATH | Protein FAR1-RELATED SEQUENCE 2 | Arabidopsis | MDDEDVEIDLLTKSSNVDVFCEASTSGNVAQCATVSELRNGMDFESKEAAYYFYREYARSVGFGITIKASRRSKRSGKFIDVKIACSRFGTKREKATAINPRSCPKTGCKAGLHMKRKEDEKWVIYNFVKEHNHEICPDDFYVSVRGKNKPAGALAIKKGLQLALEEEDLKLLLEHFMEMQDKQPGFFYAVDFDSDKRVRNVFWLDAKAKHDYCSFSDVVLFDTFYVRNGYRIPFAPFIGVSHHRQYVLLGCALIGEVSESTYSWLFRTWLKAVGGQAPGVMITDQDKLLSDIVVEVFPDVRHIFCLWSVLSKISEMLNPFVSQDDGFMESFGNCVASSWTDEHFERRWSNMIGKFELNENEWVQLLFRDRKKWVPHYFHGICLAGLSGPERSGSIASHFDKYMNSEATFKDFFELYMKFLQYRCDVEAKDDLEYQSKQPTLRSSLAFEKQLSLIYTDAAFKKFQAEVPGVVSCQLQKEREDGTTAIFRIEDFEERQNFFVALNNELLDACCSCHLFEYQGFLCKHAILVLQSADVSRVPSQYILKRWSKKGNNKEDKNDKCATIDNRMARFDDLCRRFVKLGVVASLSDEACKTALKLLEETVKHCVSMDNSSKFPSEPDKLMTGGSIGLENEGVLDCASKVSKKKKIQKKRKVYCGPEDATNRSEELRQETEQVSSRAPTFENCYIPQANMEEPELGSRATTLGVYYSTQQTNQGFPSISSIQNGYYGHPPTIQAMGNLHSIHERMSQYETQPSMQGAFQGQTGFRGSAIRGCYDIEETLHDMTMGSSQFQGSDSSHPSDHRLSN | Putative transcription activator involved in regulating light control of development. | Q3EBQ3 |
Q0CG34 | TPZA_ASPTN | Terreazepine biosynthesis cluster protein A | Aspergillus subgen. Circumdati | MRLTIPPSSMEEPKGKLSEEENVCLFPKLTQVGLPAPASVAIETVGLGLEISRAMNERFSYDRLLELQVMLSTVWAIVIHRFVEANPVFFAMVIDDEVSASTESCRNLWKTLIDPTTSVGVLNDIKRWEICPLAEHHQGSFNTGLFILSKNLETAQMLDVNLVAQPKGSEFTLELVYQPKHLSPFHAQHLMSAVSSAIHGVASAEPNRSLCDISLCTSSQQKQILYWQNSRLKEGPSLAMYQIVAELATRQPGAQAVQSSKSALTYLELDDLSSRLAIHLQARYNLAPGAMIMLCATKDVWAVVAMLAINKTGACFVPCDASHPVSRRQTMAGKCQSELALVSPEHETLFQGIIKESFIISEATVTKLPQETRDSWTVGERFPVAPSTPAYCFFTSGSLGEPKGCLGTHSALAAVAHQVPALRMDTKSRVLQFAKFGFGISFIEIFCTLAAGGTVCIASEHERLNALDAAIRRMEVNWALITPTLAQSLSPEEIPTLRKLFLGGEAPNDDLISRWQSKASLFQVFGTTEMAGVTMVSSEITSTAQRKIVGFPANSRIWLVESTGKDSNDTRLAPIGAVAELLIEGPSLAEGYLGDPVRTQASFLSLPSWLPDGYSGSTRLYKTGDLVRYNGDGSLSYIGRMGTQVKLRGQRIELEEVECHLVRLLPGTHSFSEARLVIALVVEPRGDAEKRTLAAFVLVPPKVNSPRSSDTGRLEFVKPDTPHLYEELEDIRQRLQGTLPSFMVPQLLFVLTDVPRTVTGKIDRSGLQRQINALPYDELRRISGRRVDMQVPGSEVEHLIHAIVCEILAIRSDQVSMRDDFFHLGGNSMSAIKLAAAAKRRSLKLVVADIFKHSVLADMATVALKTSNGVHAHTTIHGTTIHGAPTKTTLERFKLLSEYSVTREDINEAVATQCGISYSSLTVDAYPCSPLQEGMMSMTEKSATMYRAQVVCKLHSGIQIDRFQAAWEGVVENNDILRTRLISVSSKGMWQIVISEPFEWDRDASRAVSDSMGLGTRLVRAAIETSKDGAVFILTIHHVLCDLWTIRLLLDQLWSSYDSITDGVAGPNYYRPFIEYVLERSRDPASASYWKARFSGLEAEAFPRLPQPDLSPSPDEKTTCHINLPPLVTGGITVATYLRLAWAMVVSHHTAVDDVVFGETLNGRSGRLQEQSDESLEKIVGPAIVTVPQRILLDPERSVAETLSLIQEQQTQMISFEQVGLQHIRRLSPEADCACMFQSHLVFQPAWKPPGQLFKSVEAGASEVGGFSSYALGLECGLSEDENEVDITAYFDSRVVSRAQAARLLNHLEMVLQSLVQEPYQTIRSVPHITPEDLDQIHAWNVTLPDGLKECAHEAIRKQSQETPSAPAIRAWDGDLTYEELEHYSNQIAVAIVDRGIRQGSLIPLLFEKSMWMTVAMIGVNKAGGAFVPMDSAQPLQRLRVIAELTECTVILCSKSNTELAKQISPNAIILPVPGCREGGSIMQDSGQGLVDLQCLPKVQPHDLMYAVFTSGSTGTPKGVLIEHGSYCTAARECSSAHEIDRQSRMLQFASYSFDAFLAESLNTLVVGGCVCVPSEKDRQNGLAKAMREMQVTHAMLTPAISRLFRHEDVPSLRSLILMGEAMRSADFDYWGSHIQLFNGYGPTECTIALSCREYQAGVHVNDIGWPRAAAAWIIDPRNPNRLMPIGAVGELVVEGPPVARGYLKSPDQTSKAFISPPSWRPQTHQSHRMYRTGDLVSYTEDRSLRIVGRMNDQIKLRSQRLERGEVESRLRQFWQPPGVEVAVDVIVPAGDADRVSLAAFIVQEGSEQNNSDKNADHGTDCRSLCRNPTAEFSRVATQVEAQLQQELPRFMVPSIFVPVSRMPHMPSGKIDRPRLKRELEASPWEELRRYLPSAAPSRLATTNEERTLQEIWAQVLHLPSSKVGIDDNFFHLGGDSVNGMQAVVQARARNIPHTLEEIFRWKTIAAILSHLTGRKHQERPPRHHDSNLTKTNNHLESFRGTLARSRLPFEGVEDIYPCGPIQQNILLVHSRRPAFYHVAFTWEIHDATVDMVVRAVKQLIARHAIFRTRFLEPDIVDGSFLQIVLRQGQQDIPIRSVSEGLIDFPGDFQPTARCPSQFTIYHRDWSSVHVRLDITHALWDGGPATVVERELGLASHSKPLPPDPPLYRDYISYVQSQDLAAGEAFWSSHIKDTSPCHFPSLRATRMYEPDVPQDLHFELDQHAEVGPFCRRHNVTAPNMFCLAWGLVLRAVTSMDEVCFGNVVSGRDLPLTGALEMVGPLINLLPCRINLREGTVIETLQRIYHDYAACLSHQAFPIANLPHSSGRSALTLFNTQLSIRRATTASQPGEEAPKACLRAIQSWDPHECRINVYVIMEESRTRVEMRYWKSAMSPAQAALIEKCFSAAVSQILAHGDQPLTELGILPPEEQKRVWEPSLSAAVVRLRELWAKVLDIPHHLIGGEDDFFRLGGNSVRALQVTGLAREAGMDLRVADVFTASTLHAMARRSLVVSQSG | Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of terreazepine, . The first step of terreazepine biosynthesis is catalyzed by the indoleamine 2,3-dioxygenase tpzB which produces N-formyl-kynurenine through the catabolism of tryptophan . The two-module NRPS tpzA then utilizes anthranilate and kynurenine to assemble terreazepine . The first adenylation domain of tpzA (A1) loads anthranilate onto the T1 domain, while A2 loads kynurenine, generated through spontaneous nonenzymatic deformylation of the tzpB-supplied N-formyl-kynurenine . TpzA produces a 2:1 mixture of S-R enantiomers, which suggests that the A2 domain accepts both D- and L-kynurenine . The peptide bond formation between the tethered amino acids is catalyzed by the first condensation domain (C1) between anthranilate's carbonyl carbon and kynurenine's aliphatic primary amine . The second C domain (C2) catalyzes the final cyclization event between the aromatic amine of kynurenine and the tethered carbonyl carbon, yielding the final terreazepine product . The T3 domain may facilitate the interaction with downstream tailoring enzymes . | Q0CG34 |
Q5DRA9 | PCDGE_PANTR | Protocadherin gamma-B2 | Pan | MKASSGRCGLVRWLQVLLPFLLSLFPGALPVQIRYSIPEELAKNSVVGNLAKDLGLSVRDLPARKLRVSAEKEYFTVNPESGDLLVSDRIDREQICGKQPLCVLDFDTVAENPLNIFYIAVIVQDINDNTPLFKQTKINLKIGESTKPGTTFPLDPALDSDVGPNSLQRYHLNDNEYFDLAEKQTPDGRKYPELILQHSLDREEHSLHQLVLTAVDGGDPPQSGTTQIRVKVTDANDNPPVFSQDVYRVTLREDVPPGFFVLQVTATDRDEGVNAEITYSFHNVDEQVKHFFNLNEKTGEITTKDDLDFEIASSYTLSIEAKDPGDLAAHCSIQVEILDDNDCAPEVIVTSVFTPLPEDSPPGTVIALIKTRDRDSGENGEVYCQVLGNAKFILKSSSKNYYKLVTDGALDREEIPEYNLTITATDGGKPPLSSSIIVTLHISDVNDNAPVFQQTSYMVHVAENNPPGASIAQISASDPDLGPNGQVSYSIVASDLKPREILSYVSVSAQSGVVFAQRAFDHEQLRAFELTLQARDQGSPALSANVSLRVLVGDLNDNAPRVLYPALGSDGSALFDMVPRAAEPGYLVTKVVAVDADSGHNAWLSYHVLQASEPGLFSLGLRTGEVRTARALGDRDAARQRLLVAVRDGGQPPLSATATLHLIFADSLQEVLPDLSDRPEPSDPQAELQFYLVVALALISVLFFLAVILAISLRLRRSSRSDAWDCFQPGLSSKPGPGVLPSYSEGTLPYSYNLCVASQSAKTEFNFLNITPELIPAQDLLCDNASWEQNTNHGAAGVPFASDTILKQAPPNTDWRFSQAQRPGTSGSQNGDDTGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK | Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain. | Q5DRA9 |
C6E9F3 | ATPA_GEOSM | F-ATPase subunit alpha | unclassified Geobacter | MEIKAEEISEIIRKQIKEYGTEVAVAETGTIISIGDGIARIHGLDKAMAGELLEFPGGITGMVLNLEEDNVGAAILGEFSEIKEGDSVKLTGKIVEVPVGPALIGRVVDAIGNPIDGLGPINTDTFGKVEVKAPGIVKRKSVHQPMQTGLKAIDSMVPIGRGQRELIIGDRQTGKTAVAIDTIINQKGGDVVCIYVAIGQKRSTVAQVVSKLKEHGAMDYTIVVAATASEPAPLQFIAPYTGVTMGEFFRDSGKHALIIYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERACKVSDDCGAGSLTALPVIETQAGDVSAYIPTNVISITDGQIYLESDLFYSGVRPAINVGLSVSRVGGSAQVKAMKQVAGTLRLALAQYREMAAFAQFGSDLDKATQMQLARGARLVEILKQPQYRPIPNEKQVLIIFAANNGFVDEYPIGSLGRYETELYAFFDSRKATLLGELRDKKAIDDAMKGEIIASLEEFKKEFTA | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | C6E9F3 |
A4JCM8 | PNCB_BURVG | Nicotinate phosphoribosyltransferase | Burkholderia cepacia complex | MIITSLLDTDLYKFTMMQVVLHHFPAATVEYRFRCRTRGVDLVPYIDEIRDEVRGLCALRFTDVELDYLRRMRFIKSDFVDFLALFHLNEKYISIMPSPKGNGEIDIVIEGPWLHTILFEIPVLAIVNEVYFRNTQREPDYREGRERLRDKIKLLGAKPEFADCKIADYGTRRRFSKVWHEEVALTLRDGLGPQFAGTSNVFYAMKHDLTPLGTMAHEYLQACQALGPRLRDSQTYGFEMWAKEYRGDLGIALSDVYGMDAFLNDFDMYFCKLFDGARHDSGDPFDWGERMLRHYEANRCDPRTKVLVFSDALDIPKVMQLYERFRGRCKLAFGVGTNLTNDLGYVPLQIVIKMVRCNGQPVAKLSDSPGKSMCDDKAYLAYLRQVFGIAQPVGDDASQ | Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP. | A4JCM8 |
A9ILI4 | ARGB_BART1 | NAG kinase | Bartonella | MDDAKNSAVDVLEKQAAFLSSALPYMQKYENETVVVKYGGHAMGDPALGRAFARDIALLKQSGINPVVVHGGGPQIAEILMKMGIESRFENGLRVTDERIVEVVEMVLAGSINKEIVALINAEGEWAIGLCGKDGNMVFAEKAYRTVIDPDSHIERVLDLGFVGEPIEVDRTLLDLLACSEMIPVLAPVAPGRDGKTYNINADIFAGAIAGALEAKRLLFLTDVPGVLDKQGKLLKELTVSEAEKLIKNGTISGGMIPKVETCVKALQNGVEGVVILNGKTPHSVLLELFTEQGVGTLIVS | Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. | A9ILI4 |
Q0VL18 | PSTB_ALCBS | Phosphate-transporting ATPase | Alcanivorax | METAQQLDKPALDTNDAARDKAINEQVTMTQDTPYPDQTVGNPFVDDPKMRLRDVEVFYDDNQAIHGVSLDIGKNEVVSLIGPSGCGKSTFLRCLNRMNDTIDICKVKGSLHLESQDLYDPKLDVVELRARVGMVFQKPNPFPKSIYDNVAYGPRIHGLANKKYDLDEIVETSLRKAGLWEEVKDRLHAPGTGLSGGQQQRLCIARTIAVSPEVVLMDEPCSALDPIATAKIEELISELSESYTIAIVTHSMQQAARVSSRTAYFHLGRLVEMNDTETVFTKPEHDLTEAYITGRFG | Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. | Q0VL18 |
P32236 | GNRHR_BOVIN | Gonadotropin-releasing hormone receptor | Bos | MANSDSPEQNENHCSAINSSIPLTPGSLPTLTLSGKIRVTVTFFLFLLSTIFNTSFLLKLQNWTQRKEKRKKLSRMKLLLKHLTLANLLETLIVMPLDGMWNITVQWYAGELLCKVLSYLKLFSMYAPAFMMVVISLDRSLAITKPLAVKSNSKLGQFMIGLAWLLSSIFAGPQLYIFGMIHLADDSGQTEGFSQCVTHCSFPQWWHQAFYNFFTFSCLFIIPLLIMVICNAKIIFTLTRVLHQDPHKLQLNQSKNNIPRARLRTLKMTVAFATSFTVCWTPYYVLGIWYWFDPDMVNRVSDPVNHFFFLFAFLNPCFDPLIYGYFSL | Receptor for gonadotropin releasing hormone (GnRH) that mediates the action of GnRH to stimulate the secretion of the gonadotropic hormones luteinizing hormone (LH) and follicle-stimulating hormone (FSH). This receptor mediates its action by association with G-proteins that activate a phosphatidylinositol-calcium second messenger system. | P32236 |
P29428 | SODC2_PICAB | Superoxide dismutase [Cu-Zn] II | Picea | MSPLKAVAVLTGADVKGVVQFT | Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | P29428 |
Q46244 | ANFG_CLOPA | Nitrogenase component I | Clostridium | MEDPSKVQLNQLTDYIMKNCLWQFHSRKWDRERQNEGILTKTKQILLGEEVDLSTPADRCYYADALCLADAYKTEYPWINDMSKDELIQLMQQLKDRIDYVTITGSLNAELTDPRY | The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein (component 2) and a component 1 which is either a molybdenum-iron protein, a vanadium-iron, or an iron-iron protein. | Q46244 |
A4VK43 | TAL_PSEU5 | Transaldolase | Pseudomonas | MTSKLEQLKQFTTVVADTGDIDAIARLKPVDATTNPSLLLKAAAMPRYAEHLGNAMKQCQGDIGLACDLFAVAVGKQILELIPGRISTEVDARLSFDTQAMVQRGERLIGLYEQAGISRERVLIKIASTWEGIRAAEQLEKAGIQTNLTLLFSFTQAVACAEAGVFLISPFVGRIYDWYKKHEGRDYQGAEDPGVQSVSRIYDYYKTHGYKTVVMGASFRNVGQIESLAGCDRLTISPELLGQLAEASGTLERKLEPGRASEPRISLDEKSFRWGLNEDAMATEKLAEGIRQFARDQEKLEALLTELA | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | A4VK43 |
Q8BG67 | EFR3A_MOUSE | Protein EFR3-like | Mus | MPTRVCCCCSALRPRYKRLVDNIFPEDPKDGLVKADMEKLTFYAVSAPEKLDRIGAYLAERLSRDVVRHRSGYVLIAMEALDQLLMACHSQSIKPFVESFLHMVAKLLESGEPKLQVLGTNSFVKFANIEEDTPSYHRRYDFFVSRFSAMCHSCHSDPEIRTEIRIAGIRGIQGVVRKTVNDELRATIWEPQHMDKIVPSLLFNMQKIEEVDSRLGPPSSPSAADKEENPAVLAESCFRELLGRATFGNMNNAVRPVFAHLDHHKLWDPNEFAVHCFKIIMYSIQAQYSHHVIQEILGHLDARRKDSPRVRAGIIQVLLEAVAIAAKGSIGPTVLEVFNTLLKHLRLSVELEANDSQKGSVGSVTVSSKDNDEKIVQNAVIQTIGFFGSNLPDYQRSEIMMFIMGKVPVFGTSTHTLDISQLGDLGTRRIQIMLLRSLLMVTSGYKAKTIVTALPGSFLDPLLSPSLMEDYELRQLVLEVMHNLMDRHDNRAKLRGIRIIPDVADLKIKREKICRQDTSFMKKNGQQLYRHIYLGCKEEDNVQKNYELLYTSLALITIELANEEVVIDLIRLAIALQDSAIINEDNLSMFHRCGIMALVAAYLNFVSQMIAVPAFCQHVSKVIETRTMEAPYFLPEHIFRDKCMLPKSLEKHDKNLYFLTNKIAESLGGSGYSVERLTVPYVPQVTDEDRLSRRKSIVDTVSIQVDILSNSVPSDDVVSNTEEITFEALKKAIDTNGMEEQEKEKRRLVIEKFQKAPFEEIAAQCESKANLLHDRLAQILELTIRPPPSPSGTLTVTSGHTQYQSVPVYEMKFPDLCVY | Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, EFR3A probably acts as the membrane-anchoring component. Also involved in responsiveness to G-protein-coupled receptors; it is however unclear whether this role is direct or indirect. | Q8BG67 |
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