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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C3K6H2 | ACCA_PSEFS | Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha | Pseudomonas | MNPNFLDFEQPIADLQAKIEELRLVGNDNSLNIGDEIARLQDKSSTLTEDIFGKLTSWQIARLARHPRRPYTLDYIQHIFTEFDELHGDRHFSDDAAIVGGIARLDDQPVMVIGHQKGREVREKVRRNFGMPRPEGYRKACRLMEMAERFKMPILTFIDTPGAYPGIDAEERNQSEAIAWNLRVMSRLKTPIIATVIGEGGSGGALAIGVCDQLNMLQYSTYAVISPEGCASILWKTAEKAPDAAEAMGITADRLKGLGIVDKVIAEPLGGAHRDPAAAAATIRGELASQLAMLKKLDNEALLARRYERLMSYGL | Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. | C3K6H2 |
Q957B9 | CYB_MYOBE | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Myotis | MTNIRKSHPLMKIINNSFIDLPTPSNISSWWNFGSLLGICLTLQITTGLFLAMHYTSDTATAFNSVTHICRDVNYGWILRYLHANGASMFFICLYLHVGRGLYYGSYMYTETWNIGVILLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVEWIWGGFSVDKATLTRFFAFHFLLPFIITAMVMVHLLFLHETGSNNPMGIPSNADMIPFHPYYTIKDILGLLAMITTLLTLVLFSPDMLGDPDNYTPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILILIIIPLLHTSKQRSMAFRPL... | 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... | Q957B9 |
B0D4J6 | URM1_LACBS | Ubiquitin-related modifier 1 | Laccaria | MSTDSNTMFLKIEFGGGLELLFSNQRSHRITIPSTVPADNNTSVTTKDAASPATRPADVTYLLHHLRDHLLKEREELFMENGTVRPGILVLINDTDWELEGEGEYLLKDGDEIVLISTLHGG | Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by the MOCS3 homolog UBA4. The sulfur is then transferred to tRNA to form 2... | B0D4J6 |
A4YJG9 | FPG_BRASO | DNA-(apurinic or apyrimidinic site) lyase MutM | unclassified Bradyrhizobium | MPELPEVETVRRGLQPVMEGAKIVTAEARRGDLRFPFQPDFVKRLQGQTVRGLGRRAKYLLADLGSGDVLLMHLGMSGSFRVIKPEHEETPGEFHYPRGKDSVHDHVVFHMSSGADIVFNDPRRFGFMKIIGRGEIETEPHLKDLGPEPLGNEFDAAMLARACAGKKTSLKAALLDQRVVAGLGNIYVCEALFRAHLSPRRLAATLATRKGEPTDHAKRLVEAIHTVLNEAIRAGGSSLRDHRQTTGELGYFQHSFQVYDREGEPCRTDGCEGVVKRFVQNGRSTFWCPKCQR | 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. ... | A4YJG9 |
A2T195 | LEP4_AERS4 | N-methyltransferase | Aeromonas | MTLLLELAHGLPWLYFSLVFLFSLMIGSFLNVVIHRLPIMLEREWQAEYRSYFSSDTPQPEDDERYNLMVPRSCCPRCNHPITALENIPLLSWLWLKGRCRGCQAAISARYPLVELLTALLSVVVAMTLTPGWGTLAALLLTWVLVALTFIDLDKMLLPDQLTLPLLWGGLLFNLLGGYVPLGDAVIGAMAGYLVLWSLYWAFKLLTGKEGMGYGDFKLLAALGAWLGWQALPIVLLLSSLVGAIFGIGLILLRNHHQSKPIPFGPYLAIAGWIALLWGDSITRWYLSTIL | Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine. | A2T195 |
P00458 | NIFH_KLEPN | Nitrogenase reductase | Klebsiella | MTMRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDPKADSTRLILHAKAQNTIMEMAAEVGSVEDLELEDVLQIGYGDVRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAANNISKGIVKYAKSGKVRLGGLICNSRQTDREDELIIALAEKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPACKQANEYRTLAQKIVNNTMKVVPTPCTMDELESLLMEFGIMEEEDTSIIGKTAAEENAA | The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein. | P00458 |
Q8YMZ0 | PURA_NOSS1 | IMP--aspartate ligase | Nostoc | MANVIVIGAQWGDEGKGKITDLLSRSADVVVRYQGGVNAGHTIVVKGQTFKLHLIPSGILYPDTECMIGCGTVIDPQVLIKELDQLESLNISTKNLLISETAHVTMPYHRLIDKASEERRGSHKIGTTGRGIGPTYADKSERTGIRVLDLMDPAALRDQLEWTINNKNVILEKLYNLPPLDTEEVIQEYIGYAERLRPHVVDTSLKIYDAIQRRRNILFEGAQGTLLDLDHGTYPYVTSSNPVAGGACVGTGLGPTMIDRVIGVSKAYTTRVGEGPFPTELHGELGELLCDRGAEFGTTTGRKRRCGWFDAVIGRYAVRI... | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. | Q8YMZ0 |
P10898 | PSBC_CHLRE | Protein P6 | Chlamydomonas | METLFNGTLTVGGRDQETTGFAWWSGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVSHFVPEKPMYEQGLILLPHIATLGYGVGPGGEIIDTFPYFVSGVLHLISSAVLGFGGVYHSLIGPETLEESYPFFGYVWKDKNKMTNILGYHLIMLGLGAWLLVWKAMYFGGVYDTWAPGGGDVRVITNPTTNAAVIFGYLVKSPFGGDGWICSVDNMEDIIGGHIWIGTLEILGGIWHIYTTPWPWARRAFVWSGEAYLSYSLGAIGVMGFIACCMSWFNNTAYPSEFYGPTGPEASQSQAFTFLVRDQRLGANVASAQ... | One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient sub... | P10898 |
Q5IW40 | HEPD_STRVT | Phosphinothricin tripeptide biosynthesis protein D | Streptomyces | MRIDPFKLAHWMNARKYTAAQTADLAGLPLDDLRRLLGDEANEPDPAAATALAEALSVEPSQLAADAHRNLTVVHKSAEEMHASRRPIQRDGIHFYNYYTLAAPEGRVAPVVLDILCPSDRLPALNNGHLEPAITVNLGPGDINGRWGEEITPQTWRVLHANHGGDRWITGDSYVEPSYCPHSYSLAGDAPARIVSYTAQSNISPLMTEANNWSTGAFEEALKALSGKVSAGSVLDLFLARRAHTRTSAAEAAGVPPADLEAALRSPASETGLTVLRTLGRALGFDYRVLLPADDQHDGVGKTWTTIEDSRRSRRTFGTY... | Non-heme-dependent dioxygenase that catalyzes the conversion of 2-hydroxyethylphosphonate (HEP) to hydroxymethylphosphonate (HMP) in the biosynthesis of phosphinothricin tripeptide (PTT). PTT contains the unusual amino acid phosphinothricin attached to 2 alanine residues. Synthetic phosphinothricin (glufosinate) is a k... | Q5IW40 |
Q59702 | PCHA_PSEPU | 4-hydroxybenzaldehyde dehydrogenase (NADP(+)) | Pseudomonas | MSQRLAAYENMSLQLIAGEWRVGKAGRDLDVLDPFTQEKLLQIPLANREDLDEAYRSARQAQVAWAACGPSERAQVMLNAVRIFDERRDEIIDWIIRESGSTRIKAQIEWGAARAITQESASLPSRVHGRILASDVPGKESRVYREPLGVIGIISPWNFPLHLTARSLAPALALGNACVIKPASDTPVTGGLLLAHIFEEAGLPKGVLSVVVGSGSEIGDAFVEHEVPGFISFTGSTQVGRNIGRIAAGGEHLKHVALELGGNSPFVVLADADLDQAVNAAVVGKFLHQGQICMAINRIIVEDSVYDEFVNRYAERVKSL... | Involved in p-cresol and 2,4-xylenol catabolism. Catalyzes the oxidation of 4-hydroxybenzaldehyde and 4-hydroxy-3-methylbenzaldehyde to yield 4-hydroxybenzoic acid and 4-hydroxy-3-methylbenzoic acid, respectively. | Q59702 |
A8AKT0 | THIE_CITK8 | Thiamine-phosphate pyrophosphorylase | Citrobacter | MYQPDFPAVPFRLGLYPVVDSVQWIERLLEAGVRTLQLRIKDKRDEEVEDDVSAAIALGRRYNARLFINDYWRLAIKHNAYGVHLGQEDLETTDLKAIQAAGLRLGVSTHDDMEIDIALAARPSYIALGHVFPTQTKQMPSAPQGLEQLARHIERLGDYPTVAIGGISLERASPVLKTGVGSIAVVSAITRAEDWREATAQLLAIAGAGDE | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | A8AKT0 |
Q8RIE2 | SYP_FUSNN | Prolyl-tRNA synthetase | Fusobacterium | MRFSKAYIKTLKETPKEAEIASHKLMLRAGMIKKLASGIYAYLPLGYRTIKKIENIVREEMDRAGALELLMPVVQPAELWQESGRWDVMGPEMLRLKDRHERDFVLSPTQEEMITAIIRSDISSYKSLPINLYHIQTKFRDERRPRFGLMRGREFTMKDAYSFHTSQESLDEEFLNMRDTYTRIFTRCGLKFRPVDADSGNIGGSGSQEFQVLAESGEDEIIYSDGSEYAANIEKAVSELINPPKEELKEVELVHTPDCPTIESLAKYLDVPLERTVKALTYKDMGTDEIYMVLIRGDFEVNEVKLKNILNAVEVEMATD... | Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two addit... | Q8RIE2 |
A5FJ06 | RLMN_FLAJ1 | tRNA m2A37 methyltransferase | Flavobacterium | MQIEKKDIRALSKDQLRDFFVANNDKAFRGNQVYEWLWSKGAHSFEDMTNVAKTTRSMLEENFVINHIKVDTMQRSNDGTVKNAVRLHDGLVVESVLIPTETRTTACVSSQVGCSLDCNFCATARLKRMRNLEPGEIYDQIMAIDKESRLYHNHPLSNIVFMGMGEPLMNYNNVIKAIDMVTSEEGLGMSPKRITLSTSGIPKMIKKMADDDVKFRLAVSLHSAIDETRAKIMPFSKNFPLKDLREALEYWYRKTKSKVSYEYVVWKGINDDKASVDALVKFCKYVPCKVNLIEYNPIDDGEFQQASEESILAYIKALEN... | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. | A5FJ06 |
A6VPE8 | NUSB_ACTSZ | Antitermination factor NusB | Actinobacillus | MAEQKKKVSPRRRARECAVQALYSWAVSNNDATEIELSFITEQDMKGVDTPYFRKLFRNTVTYLESVDVTIAPFLDRTSEELTPIEKAVLRLATYELKYEPDVPYKVAINEAIELAKTFGAEDSHKYINGVLDKIAPALGRK | Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons. | A6VPE8 |
A0B7K2 | SYM_METTP | Methionyl-tRNA synthetase | Methanothrix | MPTDNDPILVTCGLPYANGPAHIGHLRTYVPADIFVRALRRMGHDVLFICGSDAHGTPIVVNAESRGMSPRELVEFYHKHFEDVFRSINVRFDYFGCTDDPSNHHRTQEIVRALMERGHVYPKEIELAYCPRCERFLPDRYVEGICPYCGVPARGDECDQGCGRHLEPGEIKDAVCKVCGTRAEYRKQTHYFFRLSAFREFLLDYLQRLGGTASARNYALEWVRQELKDWCITRNMSWGVKFPGSEDLVVYVWVDAPIGYISFTEEWCKAHGVPWERYWRGKSRIIHFIGGDIVYHHCIFWPAMLEGAGYTLPSDVVASG... | Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | A0B7K2 |
Q1QSU1 | NUOK_CHRSD | NDH-1 subunit K | Chromohalobacter | MNGIPMEHGLILASILFALGLVGLMMRRNMLFVLMSLEIMMNSAGLAFIVAGTRWGQPDGQVMFLLVITLAAAEASVGLALLLQLYRRFKTLDIDAASRLRG | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are t... | Q1QSU1 |
B3CL69 | DUT_WOLPP | dUTP pyrophosphatase | unclassified Wolbachia | MQRDKIKVEIKKLSHGKSLPLPCYATMQSAGMDLYAALDDSVILNPLERLLIPTGIVIAIPNGFEGQVRPRSGLAAKHGITVLNSPGTIDSDYRGEVKVCLINLSNQPYEIKRGDRIAQILITPVPEIIWNNIEEFYAKETARNEGGFGSSGR | 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. | B3CL69 |
Q27415 | NLP_DROME | dNLP | Sophophora | MAEESFYGVTLTAESDSVTWDVDEDYARGQKLVIKQILLGAEAKENEFNVVEVNTPKDSVQIPIAVLKAGETRAVNPDVEFYESKVTFKLIKGSGPVYIHGHNIKDDVEVVDMEEDDEEDDVAEDEEDEHPKKRAKIENAADGKNAKNNKKK | Inactive for chromatin assembly. In vitro it appears to form a high molecular mass aggregate with the core histones. | Q27415 |
P15818 | 3NO4H_BUNMU | BM10-1 | Bungarus | MKTLLLTLVVVTIVCLDLGYTMKCKICHFDTCRAGELKVCASGEKYCFKESWREARGTRIERGCAATCPKGSVYGLYVLCCTTDDCN | Inhibits carbachol-induced muscle contraction in a reversible manner. | P15818 |
P23557 | XYN4_CALSA | ORF4 | Caldicellulosiruptor | MKQQYLLDYEATKASKNGMPVCKFDSCIPALQFCKENGIKMRGHVLVWHNQTPEWFFHKDYDVSKPLVDAATMERRLESYIKQVIEFCQKNYPGVVYCWDVVNEAILDDGSWREINNNWYTIMKEKYVEKAFYYARKYAKKDVALFYNDYNVFLPAKREAIYNLAQKLKEKGLIDGLGLQPTVGLNYPELDSDDIDSFKTTLETFAKLGLQIHITELNFEIKGDESNRTPENLKKQADRYYEMMKLLLKEDTDNGGPCNITCVTVFGICDDYPLYKNFKQCMYLWDKNCNPKPCFYSFLQAGLDWKASLLSK | Could be a xylanase. | P23557 |
P96740 | PGDS_BACSU | Poly-gamma-glutamate depolymerase | Bacillus | MNTLANWKKFLLVAVIICFLVPIMTKAEIAEADTSSELIVSEAKNLLGYQYKYGGETPKEGFDPSGLIQYVFSKADIHLPRSVNDQYKIGTAVKPENLKPGDILFFKKEGSTGTVPTHDALYIGDGQMVHSTQSKGVIITNYKKSSYWSGTYIGARRIAADPATADVPVVQEAEKYIGVPYVFGGSTPSEGFDCSGLVQYVFQQALGIYLPRSAEQQWAVGEKVAPQNIKPGDVVYFSNTYKTGISHAGIYAGAGRFIQASRSEKVTISYLSEDYWKSKMTGIRRFDNLTIPKENPIVSEATLYVGEVPYKQGGVTPETG... | Cleaves, in an endo-type manner, the gamma-glutamyl bond between D-glutamate and L-glutamate of poly-gamma-glutamate (PGA). | P96740 |
Q9UL59 | ZN214_HUMAN | BWSCR2-associated zinc finger protein 1 | Homo | MAVTFEDVTIIFTWEEWKFLDSSQKRLYREVMWENYTNVMSVENWNESYKSQEEKFRYLEYENFSYWQGWWNAGAQMYENQNYGETVQGTDSKDLTQQDRSQCQEWLILSTQVPGYGNYELTFESKSLRNLKYKNFMPWQSLETKTTQDYGREIYMSGSHGFQGGRYRLGISRKNLSMEKEQKLIVQHSYIPVEEALPQYVGVICQEDLLRDSMEEKYCGCNKCKGIYYWNSRCVFHKRNQPGENLCQCSICKACFSQRSDLYRHPRNHIGKKLYGCDEVDGNFHQSSGVHFHQRVHIGEVPYSCNACGKSFSQISSLHN... | May be involved in transcriptional regulation. | Q9UL59 |
Q8CPG9 | CODY_STAES | GTP-sensing transcriptional pleiotropic repressor CodY | Staphylococcus | MSLLSKTRELNTLLQKHKGIAVDFKDVAQTISNVTVTNVFIVSRRGKILGSCLNELLKSERIKDMLEDRHIPREYTEELMNVKQTESNIDIDNELTVFPPENREVFLNSRTTIFPILGGGERLGTLVLGRVQDDFNENDLVLGEYAATVIGMEILREKHNEVEKEARDKAAITMAINSLSYSEKEAIEHIFEELGGTEGLLIASKVADRVGITRSVIVNALRKLESAGVIESRSLGMKGTFIKVKKDKFLDELEKNK | DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer b... | Q8CPG9 |
P47921 | NDK_SOLLC | Nucleoside diphosphate kinase | Solanum subgen. Lycopersicon | FIMIKPDGVQRGLVGEIISRFEKKGFSLKGLKLITVDRAFAEKHYADLSAKPFFNGLVEYIVSGPVVAMVWEGKGVVATGRKIIGATNPLESAAGTIRGDFAIDIGRNVIHGSDAVESARKEIALWFPEGIAEWQSSLHSCIYE | Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. | P47921 |
B4U8V5 | ATPL_HYDS0 | Lipid-binding protein | unclassified Hydrogenobaculum | MKLKTLMLLTLASSIAMADTASSSSSDAHARALFYGLMAVAAGVSIGLGALGAGVGAGSAIRGAEEGMARNPNMAGKLQTIMFIGLAFIETFALYAMLFSIIFVFTGIFSGKAGF | Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. | B4U8V5 |
A1S4E2 | SURE_SHEAM | Nucleoside 5'-monophosphate phosphohydrolase | Shewanella | MRLLVSNDDGVYAPGIKALAEALKTIAHVDVVAPDRNCSAASNSLTLTNPLRINRLDNGYIAVNGTPSDCVHIAIREICTEEPELVVSGINAGANMGDDTLYSGTVAAAMEGRFQGLPAIAVSLSARTPVHYDAAAQIALRIVEGLKAHPLPADQILNVNVPDLPLEEIKGIKVTRLGARHRAEGVVRTTDPAGREIFWLGPPGEELDASEGTDFGAVAEGYVSITPLTVDLTAHSQLNALANWIEKI | Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates. | A1S4E2 |
Q3MA59 | PSBD_TRIV2 | Photosystem Q(A) protein | Trichormus | MTIAVGRAPSRGWFDVLDDWLKRDRFVFVGWSGILLFPCAFLALGGWLTGTTFVTSWYTHGLASSYLEGANFLTVAVSSPADSMGHSLLLLWGPEAQGDFTRWCQLGGLWPFVALHGAFGLIGFMLRQFEIARLVGIRPYNALAFSAPIAVFVSVFLMYPLGQSSWFFAPSFGVAAIFRFLLFLQGFHNWTLNPFHMMGVAGVLGGALLCAIHGATVENTLFEDGEGANTFRAFNPTQSEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVTGLWMSAVGIVGLALNLRAYDFVSQELRAAEDPEFETFYTKNILL... | Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photoni... | Q3MA59 |
Q5LGL5 | SECA_BACFN | Protein translocase subunit SecA | Bacteroides | MGFNEFLSSIFGNKSTRDMKEIQPWVDKIKAAYPEVAKLDNDGLRAKTEELKEYIRNSASKERAKADELRAGIENVELEDREEVFAQIDKIEKEILEIYEKALDEVLPVAFSIVKESAKRFSENEEIVVTATDFDRKLAATKDFVRIEGDKAIWQNHWNAGGNDTVWNMVHYDVQLFGGVVLHKGKIAEMATGEGKTLVATLPVFLNALTGNGVHVVTVNDYLAKRDSEWMGPLYMFHGLSVDCIDRHQPNSDARRQAYLADITFGTNNEFGFDYLRDNMAISPKDLVQRQHNYAIVDEVDSVLIDDARTPLIISGPVPK... | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains acro... | Q5LGL5 |
Q753V6 | DLT1_ASHGO | Defect at low temperature protein 1 | Eremothecium | MGAVNIPTWARHSFATVLILLLLAFSLILPVDVIRRVSQMPHEILNTAIIVGAAITLLITFTSLSFGRLLVHRSCMQDIPKRYVPITERDLPNTRIRGEIYHKLEHCKQLAHDFSTPETRVVHAGLEPPAHVDHCGDDMLPPLLDYQACVKIIADRFKFQGILLNKYMLEPKLGMTFAAQLRRTVSENDCVDRNQLEEFITLYETIRYSGHPVTRGKFIRFMELCLLLVDFSLLTHRVDTPPSGEPSSTTDSATNFNAHVLYSRTEESISQSSA | Required for growth under high-pressure and low-temperature conditions. | Q753V6 |
Q0I9G1 | ACCD_SYNS3 | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta | unclassified Synechococcus | MSLFDWFADRRKGQYVGKVNQEPDEGDGLWSKCPECGQVVYRKDLLSNASVCGNCGYHHRIDSTERIAVLVDPNSFVPMDQELQPTDPLGFKDRRAYADRLRETQASTGLRDGVITGLCEVEGIPMALAVMDFRFMGGSMGSVVGEKITRLVEVATAKKLPLLIVCASGGARMQEGMLSLMQMAKISGALERHREAGVLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPDNFQTAEYLQEHGFVDSIVPRTQLRSTLASLLRLHGCESRVASS | 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. | Q0I9G1 |
P29660 | COX2_MEGAT | Cytochrome c oxidase polypeptide II | Megalops | MAHPSQLGLQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTDKYTIDSQEIEIVWTVLPAVILI | 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, CII... | P29660 |
C4ZUJ8 | TUSB_ECOBW | tRNA 2-thiouridine synthesizing protein B | Escherichia | MLHTLHRSPWLTDFAALLRLLSEGDELLLLQDGVTAAVDGNRYLESLRNAPIKVYALNEDLIARGLTGQISNDIILIDYTDFVRLTVKHPSQMAW | Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. | C4ZUJ8 |
B5XIM6 | DTD_STRPZ | Gly-tRNA(Ala) deacylase | Streptococcus | MKLVLQRVKEASVSIDGKIAGAINQGLLLLVGVGPDDNAEDLAYAVRKIVNMRIFSDADGKMNQSIQDIKGSILSVSQFTLYADTKKGNRPAFTGAAKPDLARQLYDSFNEQLAEFVPVERGVFGADMQVSLINDGPVTIILDTKCH | An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By rec... | B5XIM6 |
Q2YXY9 | NIKD_STAAB | Nickel import system ATP-binding protein NikD | Staphylococcus | MSLIDIQNLTIKNTSEKSLIKGIDLKIFSQQINALIGESGAGKSLIAKALLEYLPFDLTCTYYSYQFDGENVSRLSKYYGHTIGYISQNYAESFNDHTKLGKQLTAIYRKHYKSSKEEALSKIDKALSWVNLQSKDILNKYSFQLSGGQLERVYIASVLMLEPKLIIADEPVASLDALNGNQVMDLLQHIVLEHGQTLFIITHNLSHVLKYCQYINVLKEGQIIEQGNIDHFKYEHLHPYTEQLIKYRTQLKRDYYD | Part of the ABC transporter complex NikABCDE (Opp2) involved in nickel import. Probably responsible for energy coupling to the transport system. | Q2YXY9 |
A0A3B7TNW2 | BLC01_BRELC | Crinkler effector protein BLC01 | Bremia | MMVKLICAIVDIAGAAFPIDIDTNELVGDFKKVIKAENSRTIACDANDLRLFLAKTDGRWLTEFEVQNGVADISVFEELDVVGAPLNMIGLSEETVSSVAITKELVKAKKTPLHVLVVPSEPVQLQRKLWLVTGTVVNALGSKGIRRHLHLMASLHIGFYDPTRRVDNKNVAFWYEAKNLCFHVLFKSSTCFFYVSPF | Secreted effector that elicits necrosis in host plants, a characteristic of plant innate immunity. | A0A3B7TNW2 |
Q02H37 | SECA_PSEAB | Protein translocase subunit SecA | Pseudomonas | MFAPLLKKLFGSKNERDVKRMAKAVQAINALEPQMVALSDEQLKAKTAEFQQRYAKGETLDQLLPEAFAVVREAGKRVMGMRHFDVQLIGGMTLHDGKIAEMRTGEGKTLVGTLPVYLNALSGKGVHVVTVNDYLARRDANWMRPLYEFLGLSVGVVTPFQPPEDKRAAYAADITYGTNNEFGFDYLRDNMAFSLDDKFQRELNFAVVDEVDSILIDEARTPLIISGQAEDSSELYIKINKLIPRLNRQVEEVEGKPTEEGHYSIDEKTRQVELNEQGHQFIEDLLSQNGLLGEGESLYSAHNLSLLTHVYAALRAHTLF... | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor drivin... | Q02H37 |
Q75FW5 | RNC_LEPIC | Ribonuclease III | Leptospira | MSFKKAQSHFFLKNPERVRSLQKLSKKIGIKFSKVEYYNTAFIHSSYKNENQEILEDNERLEFLGDSVLGLVAARSLFRKYPKANEGELSRIKSRIVSTPILNSISEKLELSEYLLLGKGEKNSLGKGRRKLSANLFESLVGAIYLDQGFEIAEKFILRHLSEFVENPEKEESVRDYKTQLQEYSQKHFKILPIYRTKSESGPDHAKTFQVVVRIRDQWEASGSGVSKKSAEQNAAKELYNRIRKKT | Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. | Q75FW5 |
B6EGJ0 | CMOA_ALISL | Carboxy-S-adenosyl-L-methionine synthase | Aliivibrio | MANPDTIFSAPIDKIGDFTFDERVAEVFPDMIQRSIPGYSNIISAIGMLAERYAKPHSSVYDLGCSLGAATLSMRRHINQEGCQIIGVDNSSAMVERCRLLINAYRSDTPVTIVEADIRDVNIQDASVVVLNFTLQFLVPADRRALLEKIYSGLRPGGILILSEKYIFEDGVVNELLIDLHHDFKRANGYSELEISQKRSAIENVMLPDPIDVHKQRFQEIGFKSSEVWFQCFNFGSMFAIK | Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM). | B6EGJ0 |
A4YPM4 | APT_BRASO | Adenine phosphoribosyltransferase | unclassified Bradyrhizobium | MTFDLDIKNTVRTIPDYPKPGILFRDITTLLADARAFRRAVDELVHPWAGSKIDKVAGIEARGFILGGAVAHQLSAGFVPIRKKGKLPHKTVSMSYALEYGTDEMEMHVDAVQPGERVILVDDLIATGGTAEGAVKLLRQIGATVVAACFIIDLPDLGGAAKLRALDVPVRSLIAFDGH | Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | A4YPM4 |
Q0P3M1 | PSBZ_OSTTA | Photosystem II reaction center protein Z | Ostreococcus | MLFIFQLTLLAFIGLSLALVIGVPVLLASPEGWAQSKGLVFSGSALWMLLVFVVGALNSFVS | Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. | Q0P3M1 |
P14551 | TCR_STRRM | TET347 | Streptomyces | MDVLGAAALALFLVPLLIVAEQGRTWGWGSPAALALFALGAAGLAVFIPVELRRGDEAILPLGLFRRGSIALCSAVNFTIGVGIFGTVTTLPLFLQMVQGRTPTQAGLVVIPFMLGTIASQMVSGKLIASSGRFKKLAIVGLGSMAGALLAMATTGATTPMWGIVLIVLWLGVGIGLSQTVITSPMQNSAPKSQLGVANGASACAGQIGGSTGIAVLFSVMFAVALGRLADLLHTPRYERLLTDPAITGDPANHRFLDMAESGQGAGINLDDTSLLNGIDARLMQPVTDSFAHGFHIMFLPGGVVLLAGFVMTWFLRELQ... | Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter. | P14551 |
Q7VJ35 | UREH_HELHP | Urease accessory protein UreH | Helicobacter | MSSFAQKSILKLKTKRGLNGKNIIEEMFFTPPLKIISPLEDEDIAEIMLISVSAGLLKDDCQDIQIHIGKESKIRLISQSYEKIHDTQDGYASKHTQITIEENAFLDYAPLPILPFKDSSFKNTTDIYLSKNARLHYSEIICAGRVAMGEIFDFSELSSRLRIYKENHLVFFENMNLKPAQMAMQNICLFDKYTHALSMVIFDDLIEVQALEQKIKNSSLNVGISTNNGGIIIKALDNQSERLLQFKKDLAL | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | Q7VJ35 |
Q2SZG9 | ZAPD_BURTA | Z ring-associated protein D | pseudomallei group | MILYEYPFNERIRTLLRLEDLFERFTFFVAQEDAREHHVALTTLFEISEVAGRADLKSDLMKELERQRQTLAPFRGNPGIEQNALEAVLGEIEQTLANLAQMQGKTGQHLIDNEWLASIRSRAVIPGGTCKFDLPSYYAWQQWPAEQRRQDIAKWSMPLLPLRDAAMIVLRLARESGQASKVMAMQGSYQQMLSGRTYQLMQVRVPPELRVIPEASANKYMLWVRFTAQDGDVRPRAVDIDVPFQLTLCNL | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. | Q2SZG9 |
Q8ZZP3 | VAPC3_PYRAE | Putative toxin VapC3 | Pyrobaculum | MKLVVDASAIAALYVPEERSEQAERAVSQAQELHTLDLAAYEVANDLWKHARRGLLREDEASNMLEELWEFFKALKVHSYAEVLKDAFALALKHGVTVYDAAYVALAEKIGGKLLTLDRQLAEKFPALVTP | Toxic component of a type II toxin-antitoxin (TA) system. Has ribonuclease activity. | Q8ZZP3 |
Q8RIJ5 | PTH_FUSNN | Peptidyl-tRNA hydrolase | Fusobacterium | MKVVIGLGNPGKKYEKTRHNIGFIAVDNLRKKFNISDEREKFQALVSEKNIDGEKVIFFKPQTFMNLSGNSVIEIINFYKLDPKKDIIVIYDDMDLSFGDIRIREKGSSGGHNGIKSIISHIGEEFIRIKCGIGAKERDAVEHVLGEFNQTEQKDLDEILEKINNCVIEMLSVQNLDRIMQKYNKKKEISK | The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. | Q8RIJ5 |
A1TLE0 | ACP_ACIAC | Acyl carrier protein | Acidovorax | MSDIEARVKKIIAEQLGVEESQVTNEKAFVADLGADSLDTVELVMALEDEFGIEIPDEDAEKITTVQNAIDYANTHQKA | Carrier of the growing fatty acid chain in fatty acid biosynthesis. | A1TLE0 |
Q2KI51 | PR15A_BOVIN | Growth arrest and DNA damage-inducible protein GADD34 | Bos | MAPGQMPHQPAPWRGTHPLFLLSPLMGLLSRAWSLLRAPGPPEPWLVEAVTEADQGGAGLEDEAKASLATYHALWGRHPQEETKDSGAAEEDREASPGACPNLEAKHSLPEAWGLSDDDDEKYGGEEATGVPREQKEFMDGQPAPLPLSLLIRSLPDLPGEEESKEEAVTGGGGNEVTAFSFPLSHWECCPGEEEEEEEENGEAVRVCRPVNGATEERTQTEAATKTSMSPSSVGSHLRAWECCSGKESEEEEKDKQAEKGDADPGPHFTSLAQRPSLRTWQHPSSAITEEEEDRDSEEMGASSSVPLTSAFLSDWVYQP... | Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signali... | Q2KI51 |
Q3BUQ9 | RECA_XANC5 | Recombinase A | Xanthomonas | MDENKKRALSAALSQIEKQFGKGSVMRMGDRVIEAVEVIPTGSLMLDIALGIGGLPKGRVVEIYGPESSGKTTLTLQAIAQCQKNGGTAAFIDAEHALDPIYAAKLGVNVDDLLLSQPDTGEQALEIADMLVRSGSVDIVVVDSVAALTPKAEIEGEMGDQLPGLQARLMSQALRKLTGNIKRSNTLVVFINQLRMKIGVMMPGQSPEVTTGGNALKFYASVRLDIRRIGAIKKGDEIIGNQTKIKVVKNKLAPPFKQVVTEILYGEGISREGELIDMGVEAKLVDKAGAWYSYGDERIGQGKDNARTYLRDNPQVATRL... | Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. | Q3BUQ9 |
A4WCV2 | TRUA_ENT38 | tRNA-uridine isomerase I | Enterobacter | MSEVELKPVHRIALGIEYDGSKYYGWQRQNEVRSVQEKLEKALSQVANQPIAVCCAGRTDAGVHGTGQVVHFETTSVRKDAAWTLGVNANLPGDIAVRWVKDVPDDFHARFSATARRYRYIIYNQRLRPAVLGQGVTHFYEPLDAERMQRAAQSLIGENDFTSFRAVQCQSRTPWRNVMHINVSRYGAYVVVDIKANAFVHHMVRNIVGSLMEVGAGHQPESWIAELLAAKDRTLAAATAKAEGLYLVSVDYPERFDLPKPPMGPLFLAD | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | A4WCV2 |
B8DYT2 | ATPA_DICTD | F-ATPase subunit alpha | Dictyoglomus | MKEEVLGLPIDKIEKKIKEYDFSPRISNIGYVKHVGDGVAEVSLLNSAFIGEMVVFESGIQGMVLSLKEDSVGVILFGKDEYVKEGDVVYSTSKILQVPTGNGFLGRVIDPLGNPIDGGGLIFPEAYVPIDNEAPSIFDREPVKEPLYTGIRTIDALIPIGHGQRELILGDRQTGKTTIALDTIISQKNYGTICIYVAIAQKRTNIARIVQTLREYGALSNTIVIATFPDEPPALRYIAPMAGCAMGEYFMRQGERVLIVYDDLTKHANTYREVALLLRRVPGREAYPGDIFYLHAHLLERAAKLNKRLGGGALTALPIA... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | B8DYT2 |
B2VIQ7 | GMHA_ERWT9 | Sedoheptulose 7-phosphate isomerase | Erwinia | MYQDIIRSELNEAADTLNKFLSDEANIAAIQRAAVLLADAFKAGGKVLSCGNGGSHCDAMHFAEELTGRYRENRPGYPAIAISDVSHLSCVSNDFGYDYVFSRYVEAVGKAGDVLLGLSTSGNSANIIKAVEAARAQGMKVIALTGKDGGKMDGLADVEIRVPHFGYADRIQEIHIKVIHILMLLIEKEMVK | Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. | B2VIQ7 |
B7V8H0 | YCIB_PSEA8 | Inner membrane-spanning protein YciB | Pseudomonas | MKQFIDFIPLILFFIVYKIDPQNVEFAGFNLSGIYGATATLILASVIVYGALWLKHRHLEKSQWFTLGACLVLGGLTLAFHEDTFLKWKAPLVNWLFALAFAGSHFIGDKPMIQRIMGHAIQLPQGLWVRLNIAWVVFFLVCGFANLYVVFTYPNFWVDFKVFGSLGMTLLFLIGQGLFLARHLHDADTGEKPKD | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | B7V8H0 |
B5Y110 | PPNP_KLEP3 | Xanthosine phosphorylase | Klebsiella | MLQSNEYFDGKVKSIGFTSSSTGRASVGVMAEGEYTFGTAQPEEMTVVSGALNVLLPGETEWKVYAAGEVFNVPGNSEFHLQVAEPTSYLCRYL | Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions. | B5Y110 |
Q9CAK4 | ROH1_ARATH | Protein ROH1 | Arabidopsis | MRPAQDNQGSFLGRISIRRNQFVDVNNEQEQEDLELFQKHIADRFTELLSPPQPPPSDEINTVASVAATEQIMSVTWLRKLMDVFLCCEAEFKAILLMGRDPTQISKPPFDRLVPEMLDRSIKALDICTAVVNGIDSVRHYQRLAEIAVTALEQRPLGDGNVRRAKRALANLVVALSLEDKENVSGGGGGGGGGNKTTERSWSFGRRSGGSSAASKGGATIGQLKSSSWAVGRNWSAAKQIHAMTANLTPPRGNEAAGLPQPMFIMSTVMVFVMWVLTAAVPCQERSGLANHLPVPPKHLNWAQSLIGIHEKIGDEWKKK... | Required for seed coat mucilage deposition. | Q9CAK4 |
B5ZMJ6 | GATB_RHILW | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B | Rhizobium | MTLVDVRTPDPKRFIPGATGDWEVIVGMEVHAQVLSNSKLFSGASTEFGKPQNSNVSLVDAAMPGMLPVINEECVRQAVRTGLGLKAQINKRSLFDRKNYFYPDLPQGYQISQFKDPIVGEGKIVISLGPDRQGQFEDIEIGIERLHLEQDAGKSLHDQHATMSYVDLNRSGVALMEIVSKPDMRSSDEAKAYMTKLRSIVRYLGTCDGNMDEGSMRADVNVSVRRPGEGFGTRCEIKNVNSIRFIGQAIEYEARRQIGILEDGGTIEQETRLFDPNKGETRSMRSKEDAHDYRYFPDPDLLPLEFDDAFVSALAVDLPE... | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated ... | B5ZMJ6 |
Q88FH0 | NUOI_PSEPK | NDH-1 subunit I | Pseudomonas | MFKYIGDIVKGTGTQLRSLAMVFSHGFRKRDTLQYPEEPVYLPPRYRGRIVLTRDPDGEERCVACNLCAVACPVGCISLQKAETEDGRWYPEFFRINFSRCIFCGLCEEACPTTAIQLTPDFEMAEFKRQDLVYEKEDLLISGPGKNPDYNFYRVAGMAIAGKPKGSAQNEAEPINVKSLLP | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are t... | Q88FH0 |
G1FSB5 | AV238_PHYSO | Avirulence homolog protein 238 | Phytophthora | MRGVFFVAVAVAIFARSSAEAKLLSEAAPGLAADAVISGESRERFLRVADSEDDDLAAPADDGKTEERAPKFKSLSEINKKLDEEVMVHVSKILGNMGAIHADNIAKARAALEAAHKSGDITDKQLAAGLAKLV | Effector that, due to the lack of a histidine residue at position 79, is not able to induce cell death in tomato, tobacco, eggplant, potato, or in A.thaliana. | G1FSB5 |
Q73F11 | METN1_BACC1 | Methionine import ATP-binding protein MetN 1 | Bacillus cereus group | MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNSQDLTTLSAKELAKARQKIGMIFQGFNLLKTVTVYENIALPLRLAGISKVEIEKRVEKYLRIVDLFTRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKFVNSAFAAKIPEDVQKELQTTGEIVTLSFIGNSSGEPALAVATKRFQVYPNILSGNITQLKHEAYGKLIIHMQGEQNEINR... | Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. | Q73F11 |
B4TUC3 | ASTD_SALSV | Succinylglutamic semialdehyde dehydrogenase | Salmonella | MTLWINGDWITGQGERRRKTNPVSAEILWQGNDANAAQVAEACQAARAAFPRWAREPFAARQAIVEKFAALLEAHKAELTEVIARETGKPRWEAATEVTAMINKIAISIKAYHARTGEQKSELVDGAATLRHRPHGVLAVFGPYNFPGHLPNGHIVPALLAGNTLIFKPSELTPWTGETVIKLWERAGLPAGVLNLVQGGRETGQALSSLDDLDGLLFTGSASTGYQLHRQLSGQPEKILALEMGGNNPLIIEDAANMDAAVHLTLQSAFITAGQRCTCARRLLVKQGAQGDAFLARLVDVAGRLQPGRWDDDPQPFIGG... | Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. | B4TUC3 |
P11509 | CP2A6_HUMAN | Cytochrome P450(I) | Homo | MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMKISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSNGERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVSNVISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQLLQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFIGGTETVSTTLRYGFLLLMKH... | Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Acts as a 1,4-cineole 2-exo-monooxygenase. Possesses low phenacetin O-deethylation act... | P11509 |
A5V3L9 | DAPA_RHIWR | 4-hydroxy-tetrahydrodipicolinate synthase | Rhizorhabdus | MFSGSIPALVTPFRDGAFDEKLFRGFVDWQIAEGSSALVPCGTTGESATMSIEEHNHVVRVCIEQAQGRVPVIAGCGSNDTAVALEHMKAAQAAGADAALVVLPYYNRPNQDGLIAHFRHLTDNCTLPIIVYNVPARTVTDILPETLGALAGIKTIVGIKDASGKVERVSAQRQHCGPDFCQLSGNDDMALGFMAMGGVGCISVTANVAPGLCAEFQTACADGRWADALALQDKLFPLHAALFSDASPGPVKYALTRTYRDFPADLRLPMTWPSEASRAAVDAALAHAGIA | Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). | A5V3L9 |
Q9ZCX7 | SECA_RICPR | Protein translocase subunit SecA | typhus group | MLSILKKLFGTANDRTVKKLFSEITKINSFEPAIKILSDAALKNKTVEFKEKLKNGATLDDILYEAFAVVREAASRVCGMRHFDVQLIGGIILHRGMIAEMRTGEGKTLVATLPAYLNALTEKGVHVVTVNDYLALRDSASMGKIYNFLGLSVGCIVAGMTDEAKRIAYNSDITHATNNELGFDYLRDNMKYSMQERVLRPFNFAIIDEVDSILIDEARTPIVISGPVNDNSALYGKIDKIVRLLNVSDFEKDEKLKTINLTEAGITHIESLLIKDGIIKPDTGLYDFENLNLVHYVNQALRAHHMFTIDVDYLVREGKV... | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor drivin... | Q9ZCX7 |
A0RHL9 | Y3477_BACAH | UPF0122 protein BALH_3477 | Bacillus cereus group | MLEKTTRMNYLFDFYQSLLTQKQRSYMSLYYLDDLSLGEIAEEFDVSRQAVYDNIKRTEAMLEEYEDKLVLLQKFQERQRLVAKLKQLISEEEHVNEEMKQVVEAIEKLD | Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. | A0RHL9 |
Q73JJ4 | RL1_TREDE | 50S ribosomal protein L1 | Treponema | MKHGKNYKNALAKYDSAASYELPKAVDIVKELKYAKFDETVEVHVSLTLGKGQSVRDTLVLPHQFRGEKKVLVFCTDDRVKEALDAGAAYAGSTEYIEKVKGGWLDFDIAVATPDMMKDVGRLGMVLGRRGLMPNPKTGTVTTDIASAINELKKGRVEFRADKGGVVHLPVGKVSMDSSKIVENVQALINETMRKKPADAKGDYIRSVSISSTMGPGVWVDYKVGE | Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. | Q73JJ4 |
C1L2D9 | UVRC_LISMC | Excinuclease ABC subunit C | Listeria | MSSEHIQNKLALLPDQPGCYLMKDRQGTIIYVGKAKILKNRVRSYFSGTHDSKTQRLVQEIVDFEYIVTSSNVEALLLEINLIKKHDPRFNIRLKDDKTYPFIKITNERHPRLIITRQVKKDKGKYFGPYPNVYAANEVKRILDRLYPLRKCSTLPNKVCLYYHLGQCLAPCVFDVEASKYKEMQDEIVAFLNGGYKTVKNDLMKKMQEAAENMEFEKAGEFRDQINAIETTMEKQKMTMNDFVDRDVFGYAIDKGWMCVQVFFIRQGKLIERDVSQFPFYNDADEDFLTFIGQFYQKANHIPPKEIYLPDDVDSEAVQA... | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | C1L2D9 |
Q2NW08 | RF3_SODGM | Peptide chain release factor 3 | Sodalis | MKNELYADEIAARRTFAIISHPDAGKTTITEKVLLFGQAIQTAGTVKGRGSNQHAKSDWMEMEKQRGISITTSVMQFPYRQALVNLLDTPGHEDFSEDTYRTLTAVDCCLMVIDAAKGVEDRTRKLMEVTRLRDTPILTFMNKVDRDIRDPMELLDEVESELRIACAPITWPIGCGKLFKGIYHLAKDETYLYQSGQGHTIQAVRVVKGLDNPELDQAVGEDLAAQLREELELVQGASHPFDEQAFLAGELTPIFFGTALGNFGIDHMLDGLVAWAPPPMPRQTDVRVVSAREEKFTGFVFKIQANMDPRHRDRVAFLRV... | Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. | Q2NW08 |
A5D5I7 | EFG_PELTS | Elongation factor G | Pelotomaculum | MARQFPLEKTRNIGIMAHIDAGKTTTTERILFYTGRVHKIGEVHEGTATMDWMAQEQERGITITSAATSCRWRDCQINIIDTPGHVDFTVEVERSLRVLDGAVAVFCSVGGVEPQSETVWRQADKYGVPRIAYINKMDRVGADFHRGIQMIRERLGANPVAIQLPIGVEDGFCGVVDLVRNRAIIYTDDLGTTSEETEIPPELAGEAAAFRERLIEAVAEFDESLMEKYLENGELTEEEIKEGLRRATLAVKIVPVLCGSSFKNKGVQPLLDAIVDYLPAPTDIPAIRGVNPVSGAGEVREARDDEPFSALAFKIMTDPY... | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respective... | A5D5I7 |
Q6GLU8 | PHAR1_XENLA | Phosphatase and actin regulator 1 | Xenopus | MAASSEEETDRRPIRRVRSKSDTPYLAEVRISLNLETAEEVERLAAMRSDSLVPGTHTPPIRRRSKFATLGRLFKPWKWRKKKSEKFKQTSAALERKISMRQSREELIKRGVLKEMYDKDGDLHNEEGLMENGQAVSSGSSSLPIITELELTSMAGDTCAYEVLPTSELMDGTVSEDLSSEPGSLSQDPSYKPAMLLPPKKTVGFPVDQEDTPVKQITLLKQPPALPPKPISRIANHIADSGAPVKLPCMPGKMSPPLPPKKVMICMPLGGTDFPYGPYSNQKSSQHHHTVLPSQLAAHQLQYGSQHFSTGSSSISIHPS... | Binds actin monomers (G actin) and plays a role in the reorganization of the actin cytoskeleton and in formation of actin stress fibers. | Q6GLU8 |
Q8UH56 | BETB_AGRFC | Betaine aldehyde dehydrogenase | Agrobacterium tumefaciens complex | MTIATPLKAQPKASHFIDGDYVEDNTGTPFESIFPATGEMIAKLHAATPAIVERAIASAKRAQKEWAAMSPMARGRILKRAADIMRERNDALSTLETLDTGKPIQETIVADPTSGADAFEFFGGIAPSALNGDYIPLGGDFAYTKRVPLGVCVGIGAWNYPQQIACWKAAPALVAGNAMVFKPSENTPLGALKIAEILIEAGLPKGLFNVIQGDRDTGPLLVNHPDVAKVSLTGSVPTGRKVAAAAAGHLKHVTMELGGKSPMIVFDDADIESAVGGAMLGNFYSSGQVCSNGTRVFVQKKAKARFLENLKRRTEAMILG... | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. | Q8UH56 |
C1F3B8 | KDSB_ACIC5 | CMP-2-keto-3-deoxyoctulosonic acid synthase | Acidobacterium | MSSLNVLGVIPARIGSTRLPRKVLREIAGEPMLAWVYRAARASGQLRQVLIATDAEEVMEFARQKGLPAIFTPEDCASGTDRVFVVAQSIDADIYVNIQGDEPMLTPAHFTALLAPFEQPHVQVTTLSVPCSEDEIANPNAVKVVTAADGRALYFSRATIPYDRDAAGFIGYRKHLGLYAYRKAALRRFATLPPSRLEEIERLEQLRLLENGIDIHVAEAPGSTIGVDTEEDLRAVEQLLLERKK | Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. | C1F3B8 |
P52067 | FSR_ECOLI | Fosmidomycin resistance protein | Escherichia | MAMSEQPQPVAGAAASTTKARTSFGILGAISLSHLLNDMIQSLILAIYPLLQSEFSLTFMQIGMITLTFQLASSLLQPVVGYWTDKYPMPWSLPIGMCFTLSGLVLLALAGSFGAVLLAAALVGTGSSVFHPESSRVARMASGGRHGLAQSIFQVGGNFGSSLGPLLAAVIIAPYGKGNVAWFVLAALLAIVVLAQISRWYSAQHRMNKGKPKATIINPLPRNKVVLAVSILLILIFSKYFYMASISSYYTFYLMQKFGLSIQNAQLHLFAFLFAVAAGTVIGGPVGDKIGRKYVIWGSILGVAPFTLILPYASLHWTGV... | Confers the resistance against fosmidomycin. | P52067 |
A1RK78 | GLO2_SHESW | Glyoxalase II | Shewanella | MLTITAIKAFNDNYIWVLQQTPHSQVYVVDPGDAKVVIAYLVSHQLALAGILLTHHHQDHTGGVGELKRYVEQTSSQTLQVYGPQKENIAHVNVPLNPEMRTELTLPFLNAQIQVLNVPGHTAGHIAYVIEDALFCGDTLFSAGCGRLFEGTAEQMLSSLTLLAKLPANTRVFCAHEYTLSNLKFALTVEPNNLNLQAYMQKATEMRAQNSATIPSSIALERAINPFLRVGEQSIIDSIKQHFDDPDPIKLDELTCFTRLRQWKDIF | Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. | A1RK78 |
A5VT37 | HSLU_BRUO2 | Unfoldase HslU | Brucella | MSNFSPREIVSELDRFIIGQKDAKRAVAIALRNRWRRQQLEGQMREEVMPKNILMIGPTGVGKTEISRRPAKLAGAPFVKVEATKFTEVGYVGRDVEQIIRDLVEIAITLVREKRREDVKAKAHLNAEERVLDALVGKTASPATRDSFRKKLRNGEMDDKEIEIEVSDSGASPNFEIPGMPGANIGVLNISDMLGKAMGGRTKTRKTTVKDSYPILINDESDKLLDQDQIVQEALRVSEDEGIVFIDEIDKIAAREGGSGAGVSREGVQRDLLPLVEDTTVATKYGPVKTDHILFITSGAFHVSKPSDLLPELQGRLPIR... | ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before... | A5VT37 |
B4S5P3 | GATB_PROA2 | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B | Prosthecochloris | MSYELVVGLEVHCQLNTNSKAFCGCSTEFGKPANTNVCPVCLALPGALPVLNQRVVDDAIKLGMSTGCSIAPHSVLARKNYFYPDLPKGYQISQFEEPICLEGCLSIDAGEGQRDIRLIRIHIEEDAGKSIHDIGDDTFIDANRSGVPLLEIVSYPDIRSSKEASAYLQKLRQIVKYLGISDGNMEEGSLRCDANVSMRPRGESEYGTRTEIKNMNSFKSVEKAIEYEAQRHIDVLEAGGTIVQETRLWDADKLETRSMRGKEFSHDYRYFPDPDLVPIAVDDAMLDRLRKELPEFPEARAARFVEEYDIPPYDAGVLTA... | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated ... | B4S5P3 |
Q8YDV4 | LIVB4_BRUME | Leu/Ile/Val-binding protein homolog 4 | Brucella | MSLKVFLQAGVACAALSLAGAAGASAEPLKIALVETLSGPQASTGLLYRAAVLYQLGKINEAGGFNGEKIQILEYDNQGGPVGAADRVKAAIADGAQIIVQGSSSAVAGQITEDVRKYNLRNKGKEVLYLNLGAEALELTGSKCHFYHFRFSPNAAIRFKTVAQGMKDKGILGERAYSINQNYSWGVDVENTVVANAKEIGYEVVDKTLHEVNKIQDFSPYVAKIQAANVDTVFTGNWSNDLLLLMKAASGAGLKAKFATSFLDQPGNIGNAGAIAEGHIVSTPFNPEANGEASMAFAEDYKKVTGHYPSYAEPAAVFGL... | Component of an amino-acid transport system. | Q8YDV4 |
A1Z6L1 | TO402_DROME | Translocase of outer membrane 40 kDa subunit homolog 2 | Sophophora | MGNVMASTADAESSRGRGHLSAGLRLPEAPQYSGGVPPQMVEALKAEAKKPELTNPGTLEELHSRCRDIQANTFEGAKIMVNKGLSNHFQVTHTINMNSAGPSGYRFGATYVGTKQYGPTEAFPVLLGEIDPMGNLNANVIHQLTSRLRCKFASQFQDSKLVGTQLTGDYRGRDYTLTLTMGNPGFFTSSGVFVCQYLQSVTKRLALGSEFAYHYGPNVPGRQVAVLSAVGRYAFGDTVWSCTLGPAGFHLSYYQKASDQLQIGVEVETNIRQQESTATVAYQIDLPKADLVFRGSLDSNWLISGVLEKRLQPLPFSLAI... | Channel-forming protein essential for import of protein precursors into mitochondria. | A1Z6L1 |
C6DZK7 | MURC_GEOSM | UDP-N-acetylmuramoyl-L-alanine synthetase | unclassified Geobacter | MYGKIERIHFVGIGGIGMSGIAEVLLNLGYKVSGSDLRGSEITQRLESLGGEIFFGHAAENVANADVVVISSAVHEDNPEVVEAHLRLIPVIPRAEMLAELMRMKYGIAVAGTHGKTTTTSMVATILSKGGIDPTIVIGGRLNSLGTNARLGQGQFLVAEADESDGSFLLLSPTIAVVTNIDADHLDFYSGIEEIKDTFVEFINKIPFYGLAVLCLDNGNVADVLPRVKKRFTSYGLSAQADFRATDVRLSGFSTSFVAHHKGVRLGEITFSMPGAHNVLNALAAIAVAMELDIPFETIQEGFAGFGGVGRRFHLKGEAN... | Cell wall formation. | C6DZK7 |
O24386 | CPI6_SOLTU | PCPI-6 | Solanum | LNSPNAVLQHMSIPQFLGKGTPVVFVRKSESDYGDVVRVMTGVYIKFFFKTSKLCVDETVWKVNDEELVVTGGNVGNENDIFKIKKTDLVIRGMKNVYKLLHCRSHLGCKNIGGNFKNGYPRLAAVDDDKDFIPFVFIKA | Inhibitor of cysteine proteases. May protect the plant by inhibiting proteases of invading organisms. | O24386 |
Q8PER4 | PYRF_XANAC | OMP decarboxylase | Xanthomonas | MSRAPLPLAAHERLIFALDVPSHDQAIAWVDRLGDSVSFYKIGMELLASGEYFHVLDALAKRDKRVFVDLKFFDIPATVAGTIRRLAQWPVSYCTVHGWHAGMLQAAAEANHGDMRLLAVTVLTSMGRPDLVAMGIDREPVDVVVERALAARAAGIDGVIASGQEAGPIRRATGPDFSIVCPGIRPGGPVGDDQQRTVGVAQAFIDGADAIVVGRPIRLASDPAAAADAIQAEIRAALMQNGD | Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). | Q8PER4 |
O49079 | PSBO_FRIAG | OEC 33 kDa subunit | Fritillaria | MASSLQAAATLIPAKVGAPARTHLRSNSHLSKAFGFDNSTAGRLTCSINSDLRDIAQKCTDAAKLAGFALATSALVISGASAEGVPKRLTFDEIQSKTYMEVKGSGTANQCPTIEGGTESFGYKTGKYTLKKLCLEPTSFTVKAEGINKNAPPEFQKTKLMTRLTYTLDEIEGPFEVAPDGTVKFEEKDGIDYAAVTVQLPGGERVPFLFTVKQLVATGKPESFSGSYLVPSYRGSSFLDPKGRGGSAGYDNAVALPAGGRGDEEELVKENIKDVSSSTGKITLSVTKSKPETGEVIGVFESIQPSDTDLGSKAPKDVKI... | Stabilizes the manganese cluster which is the primary site of water splitting. | O49079 |
A9I7R5 | DCD_BORPD | Deoxycytidine triphosphate deaminase | Bordetella | MSIKSDRWIRRAAEAGMIEPFEAGQVRTANGGRIVSYGTSSYGYDVRCADEFKIFTNINSTIVDPKQFDEKSFVDFKGDVCIIPPNSFALARTVEYFRIPRSVLTICLGKSTYARCGIIVNVTPLEPEWEGHVTLEFSNTTPLPAKIYAGEGCAQMLFLESDEVCETSYRDRGGKYQGQRGVTLPRT | Catalyzes the deamination of dCTP to dUTP. | A9I7R5 |
P0CE45 | UIDB2_ECOLI | Glucuronide permease | Escherichia | MNQQLSWRTIVGYSLGDVANNFAFAMGALFLLSYYTDVAGVGAAAAGTMLLLVRVFDAFADVFAGRVVDSVNTRWGKFRPFLLFGTAPLMIFSVLVFWVPTDWSHGSKVVYAYLTYMGLGLCYSLVNIPYGSLATAMTQQPQSRARLGAARGIAASLTFVCLAFLIGPSIKNSSPEEMVSVYHFWTIVLAIAGMVLYFICFKSTRENVVRIVAQPSLNISLQTLKRNRPLFMLCIGALCVLISTFAVSASSLFYVRYVLNDTGLFTVLVLVQNLVGTVASAPLVPGMVARIGKKNTFLIGALLGTCGYLLFFWVSVWSLP... | Responsible for the transport of glucuronide into the cell energized by the proton motive force (probably by symport). Import is enhanced by UidC (GusC, AC Q47706). | P0CE45 |
P03926 | NU6M_RAT | NADH dehydrogenase subunit 6 | Rattus | MTNYMFILSLLFLTGCLGLALKPSPIYGGLGLIVSGCIGCLMVLGFGGSFLGLMVFLIYLGGMLVVFGYTTAMATEEYPETWGSNWFIFSFFVLGLFMELVVFYLFSLNNKVELVDFDSLGDWLMYEIDDVGVMLEGGIGVAAIYSCATWMMVVAGWSLFAGIFIIIEITRD | Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. | P03926 |
Q9RW24 | RPIA_DEIRA | Phosphoriboisomerase A | Deinococcus | MDLEALKKEAALRSVALVQSGQRVGLGTGSTAKYAIEELGRKLAAGELSGIVGVSTSEASEKLAREVGIPTEPLDPRPLDIAIDGADEIAPNLDLVKGLGGALVREKMTEVQAKRLIIIADHTKLVTRLGEKAPLPIEIVPFGFLSTIERLREFLPGGRLRQPGAQPYVTDNGNYIFDAQLPAEFDARELERRIKGTLGVVDTGLFLGMAERAFVAAPDGVQELTR | Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. | Q9RW24 |
O46607 | GPX5_CANLF | Glutathione peroxidase 5 | Canis | MTAWLGASYVLPILLVSFVQTNAKPEKTKMDCYKDVKGTIYEYEALTLNGNERIQFKQYPRKHVLFVNVATYCGLTAQYPELNSLQEELKPLGLVVLGFPCNQFGKQGPGENSEILPGLKYVRPGRGYVPNFQLFEKGDVNGEKEQKVFTFLKLSCPHPSEVLGSFRHISWDPVKVHDIRWNFEKFLVGPDGVPVLRWFHRTPISTVKEDILVYLKQLKMK | Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids. | O46607 |
A1JJF5 | PDXA_YERE8 | 4-(phosphohydroxy)-L-threonine dehydrogenase | Yersinia | MQNHNNRIVITPGEPAGVGPDLVIALAQQDWPVELVVCADPALLLTRASQLNLPLQLREYQQDKPALAQLAGTLTILPVKIAAEVIPGQLDVKNSHYVVETLAKACDGAISGEFAALVTGPVQKSIINDAGIPFIGHTEFFADRSHCSRVVMMLATEELRVALATTHLPLLAVPGAITQTSLHEVISILDNDLKTKFGISQPQIYVCGLNPHAGEGGHMGHEEIETIIPALATLRQQGINLIGPLPADTLFQPKYLQHADAVLAMYHDQGLPVLKYQGFGRAVNITLGLPFIRTSVDHGTALELAATGTADVGSFITALN... | Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). | A1JJF5 |
Q72S34 | FMT_LEPIC | Methionyl-tRNA formyltransferase | Leptospira | MKIGYFGTPEHSAKLLEALIDSQLTEVLFVVTNPDRPKGRSKIPEPGPVKKKALEYNIPVFQYESIKKEKEKALSDFGLFSADLYVVFAYGSILPKEVYAHSTLTSINLHGSLLPDLRGASPVQTALWKGYTKTGITIQYIGEKMDEGDILLTKEVEIAPEDNTGTLMDKITDAGIESILQLLKTYDGKPFPSVPQAHDKATYCGKIKSEDRILDWSLKSEELHNRIRALYPDMIATTTFRDKRMNILKTKPSSLSLEINPTPGKLKRLDKKRLLTQCGDGRFLEILELQPENKNRMTASDFLNGFRIQEGETFG | Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. | Q72S34 |
A8LKA2 | PANC_DINSH | Pantoate-activating enzyme | Dinoroseobacter | MTDVMRDVASLRMLQGMWRRAGETVGLVPTMGALHDGHMALARAAREECGKVIATIFVNPTQFGPTEDLDAYPNTFDSDLHMLREVGVDVVFAPTRDVMYPAGFGTTVKVAGLTAPLCGAARPGHFDGVTQVVAKLLNLGQADRAYFGQKDWQQLAVVRQMVRDLNFPTEIVGIPTVRAEDGLALSSRNAYLTEAEREIAPILYRTIRDAAARVAAGHGATGVCEAAARGLLGKGFTRIDYLECRDATTLAPAETPDPGTARIFVAAQLGGARLIDNVSVG | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | A8LKA2 |
A5UHR5 | MLTC_HAEIG | Murein lyase C | Haemophilus | MKKYLLLALLPFLYACSNSSNQGINYDEAFAKDTQGLDILTGQFSHNIDRIWGVNELLVASRKDYVKYTDSFYTRSHVSFDEGNIVIETQQDLNRLHNAIVHTLLMGADAKGIDLFASGDVPISSRPFLLGQVVDHQGQQIANQVIASNFATYLIQNKLQTRRLQNGHTVQFVSVPMIANHVEVRARKYLPLIRKAAQRYGIDESLILGIMQTESSFNPYAISYANAIGLMQVVPHTAGRDVFAMKGKGGQPSTRYLYDPANNIDAGVSYLWILQNQYLDGITNPTSKRFAMISAYNSGAGAVLRVFDNDKDTAIYKINQ... | Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. | A5UHR5 |
C1DND6 | ATPD_AZOVD | F-type ATPase subunit delta | Azotobacter | MINNQTLARPYAKAAFEYASAANGSDAWSGMLGLAAAVVEAPEVAELLRNPRLTRESKVEAVLRLFADDVDEAFRNFIANLGEHDRLFVLPTVREQFEAYKAEAEKTIDVELETAYELSAEQLETLAAALSKRLDRSVNPRQVVNPALIGGLVIRAGDLVVDGSVRGKLSQLAESLKS | This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. | C1DND6 |
Q8NP40 | IF2_CORGL | Translation initiation factor IF-2 | Corynebacterium | MPGKLRVHELAKQLGITSKELLATLKDKGEFVKTASSTIEPPVVKRMQEHYGSSGSDKSDTAAKPAAAKPAAPKPAASAAPKPGAPAKPAAPAAKPAPAAPSAASAAKPGAAPKPGVQAKPAAAAKPGAPAKPAAPAAPSAAKSGSAPKPAAAAKPAFSGPTPGDAAKKAEPAAKPGAEAPRPGGMPRPMGKPAPKPGARAPRVANNPFSTGGGERPAPRPGGGPRPGGGPRPGGGPRPQGQGRPGGQRDGQRDGQRDGQGNRGGQRQGAGAGGPRPQGGPRPQGGSRPQGGSAQGAQGAPSQERQGGGRRPSPAMMPPT... | One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. | Q8NP40 |
A0T0U0 | PSBL_THAPS | Photosystem II reaction center protein L | Thalassiosira | MTGPNPNKQAVELNRTSLYWGLLLIFVLAVLFSSYFFN | One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, a... | A0T0U0 |
Q72MG4 | IPYR_LEPIC | Pyrophosphate phospho-hydrolase | Leptospira | MVHPWHDISPGDQNPEIVNGVIEIKRGSRAKYEVDKEYGILKLDRVLYSSFYYPANYGFIPQSYCGDQDPLDILVLSQVELEPLCLVKAKVIGVMRMLDSGEEDDKIIAVAANDMSVNHINDISELPPHFTLELKHFFEDYKKLENKTVVIEEFQNAILARKIVLDSLELYKKTFPKK | Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. | Q72MG4 |
Q3AVW5 | ENO_SYNS9 | 2-phosphoglycerate dehydratase | unclassified Synechococcus | MIDSLDLVIDTIVAREVLDSRGNPTVEAEVLLEGGAMGRAIVPSGASTGAHEAHELRDGGKRYMGKGVSQAVTHIEERIAPALCGLSALDQAAVDAAMLELDGSDNKSNLGANSILAVSMATARAAANGLGLPLYRYLGGPLANLLPVPLMNVINGGAHAANSLDFQEFMLVPHGAPSFREALRMGTEVFHTLKDLLNAKGMSTSVGDEGGFAPNLGNVEAGEILVEAIQKAGYKPGEQISLALDVASTEFFENGRYAFDGGSYTSAEMVGQLEQLVNQFPIVSIEDGLAEDDWEGWKLLTERLGSKVQLVGDDLFVTNT... | Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. | Q3AVW5 |
A9BAR3 | HEM1_PROM4 | Glutamyl-tRNA reductase | Prochlorococcus | MNIAVVGLSHRTAPVEVREKLSISDDNIPSAFNTLNTNDQIIEVSILSTCNRLEIYSFVKNSDNGVKAIKDFLCKHSGLGIDELDPHLFSYDQAEAVKHVMRVAGGLDSLVLGEGQILSQVKKMVRLGQENHSMGPILNRLLTQAVSTGKRVRSETNLGTGAVSISSAAVELAQLKLGQSEGKDELMSLEREKVSIVGAGRMSRLLIQHLQSKGCSKLKLINRTFQRAEALALDFPDVDIHCQLLDDLDESLRNSTLIFTSTAAENPIIDAARLKEVVRDETLRLIDIGVPRNISSDVKGLTGFEAHDVDDLQEVVSRNQ... | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | A9BAR3 |
Q642B6 | THAP4_RAT | THAP domain-containing protein 4 | Rattus | MVICCAAVNCSNRQGKGEKRAVSFHRFPLKDSKRLIQWLKAVQRDNWTPTKYSFLCSEHFTKDSFSKRLEDQHRLLKPTAVPSIFHLSEKKRGAGGHGPARRKTTGAMRGHTSAATGKGTIGSSLSSSDNLMAKPESRKLKRASPQDDTAPKATPGAVSQEPGQSLERTPGDQAAPLARGQEEAQVSATEADHQKASSSAADAGGADKSGISMDDFTPPGSGACKFIGSLHSYSFSSKHTRERPSVPREPMDRKRLKRDIEPRCSGNSVAQSPPSSSLTATPQKASQSPSAPPTDVTPKPAAEAVQSEHSDANPMSINEV... | Heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate. Therefore, this protein likely plays a role in peroxynitrite sensing and in the detoxification of reactive nitrogen ... | Q642B6 |
Q1D6P1 | CYSC_MYXXD | Adenosine-5'-phosphosulfate kinase | Myxococcus | MGRSAGFILWLTGLSGAGKSTLSRALRAHLASSMPVEVLDGDEVRTWLSRGLGFTREDREENVRRIGHVARLLAKHGVGVIAAAISPYASSRAEVRRLAEEAGIPFVEIYVQAPLDVLIARDVKGLYKKALAGELAHFTGVSDPYEAPDAPDVTVHSDVDTVEAGLWRVLETLRKRGLLDAAAAA | Catalyzes the synthesis of activated sulfate. | Q1D6P1 |
A4IFU8 | AUNIP_BOVIN | Aurora kinase A and ninein-interacting protein | Bos | MRRRGPEKEEEACGVWLDAAALKRRKTQTQLIKSSTKMLTLLPGERKAKISFTQRSCPSAGTRQTSIASFLTSQQGKTNGADQRSVSSHTESQTNKESKEDATQLEHLTQGLRADFMAPPLATSTPADIQEARLSPQSLKASCQHGIGTPYLTVPCLFRPDTSVCAGASKASLACSFAHDLESSCLLDQKEGEDSSCEREWLQGSKKNNYQSVERHSKTTGHKGHQLLDKTNLENVSAKRSRQAPVLQTYKDSRRGANMKAVKQSSCPIPGFSWDSERNDKDSWSQLFTEDSQGQRVIAHNSRAPFRDVTNDQNQGYGRV... | DNA-binding protein that accumulates at DNA double-strand breaks (DSBs) following DNA damage and promotes DNA resection and homologous recombination. Serves as a sensor of DNA damage: binds DNA with a strong preference for DNA substrates that mimic structures generated at stalled replication forks, and anchors RBBP8/Ct... | A4IFU8 |
E2IUA8 | FRIES_KALDA | Friedelin synthase | Kalanchoe | MWKLKIAEGGSDPYIYTTNNFVGRQIWEFDPQATDPQQLAKVEAARLNFYNHRHKIKPSSDLLWRLQFLEEKDFRQNIAQVKVEDGEEVSYEAATAALKRGVHFYSALQASDGHWPAENAGPMFFMSPLVMCLYITGHLNTIFTEEHRRETLRYIYYHQNEDGGWGFHIEGQSTMFGTVLNYICMRLLGEGPEGGQDNAVSRGRKWILDHGGATAIPSWGKTWLSIMGLCDWSGCNPMPPEFWLLPSYLPMHPAKMWCYCRMVYMPMSYLYGKRFTTHITPLILQLREELHTQPYDQINWKKVRHVCCKEDTYYPHPILQ... | Oxidosqualene cyclase that generates friedelin, a triterpenoid product with the maximum number of rearrangements possible. Friedelin is probably required to coat the leaf exterior as defense compound against pathogens or herbivores. | E2IUA8 |
Q5WDZ7 | PCKA_ALKCK | Phosphoenolpyruvate carboxykinase (ATP) | Alkalihalobacillus | MKMLHRSALLEQLLSSPKTLHQLPASTLVEHALQRNEGILTDSGALAVKTGLYTGRSPQDKFIVDEPMSRDSIHWGATNKPISSEVFTRLKDKVLHYLQQKEVRYASVGFAGADPSFQLPITYLNEFAWHHLFARQLFIREQAPSNNGLEPFTIISAPTFKADPSVDGTRSEAFVIISFEQRIILIGGTEYAGEMKKAIFSVMNYLLPEAGVLPMHCSANTTDEGETALFFGLSGTGKTTLSASEHRRLIGDDEHGWSEKGIFNIEGGCYAKCIGLSKESEPQIWDAIAFGAVLENVVVDPNTGKPDFKSGELTENTRAA... | Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. | Q5WDZ7 |
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