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 |
|---|---|---|---|---|---|---|
Q47NS4 | PAND_THEFY | Aspartate 1-decarboxylase alpha chain | Thermobifida | MLRTMLNGKIHRATVTHADLHYVGSITIDADLMDAANLVDGEQVHVVNITNGHRLVTYVLTGERGSGVIGINGAAARLVAPGDLVIIISYVQLTEAERATHRPHVVHVDANNRIVALGDDLAEPVPGSDQKSGALLP | Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. | Q47NS4 |
Q491V8 | UBIB_BLOPB | Ubiquinone biosynthesis protein UbiB | Candidatus Blochmannia | MLVDELCRLYSIIKTILNYGLSDFVPTHRLIFPLRIGSRFLLRVLNKHSQLTLGERFRLALQELGPIWIKFGQMLSTRRDIFPDSVADQLSILQDRVAPFDGIIAKMCIERAIGNSLETWFKDFQEIPLASASISQVHSARLKKNNKDIVIKIIRPGLLPVIKIDICLMYRLAKWICKFLPEGRKFKFSEVVSEYEKTLFNELNLLKETANTIQLRRNFKKSQILYIPKVYVDFCSENVMVMERIYGIPVYNLVALKKQKTNMKLLAERGIEIFFTQVFRDSFFHGDMHPGNIFISYKHPGNPKYISVDCGIVGSLNKKD... | Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. | Q491V8 |
A5D1B6 | RLMN_PELTS | tRNA m2A37 methyltransferase | Pelotomaculum | MVENSFCKKEGSPVVGDRINVKDLTLAGLERLLTGMGAERYRAGQVAIWVFQKGAESFREMTNLPANLREKLDAAAVISRPEILAKKVSSKKDAVKYLFGLPDGQAVESVFMKHAYGNSVCVSTQAGCRMGCRFCASALGGLTRNLSPGEIYDQVLGIRRDTGERISSVVLMGSGEPLDNYDATLTFIKNVTAPYGLHIGCRHITVSTCGLVPGIRRLAREKLALTLAVSLHAPNDRLRDILVPVNRKYPLTELMAACRDYAQETGRRVTFEYALLAGVNDRKEHAEELVRLLKGKMPCHVNLIPANPVPERGVKTPSRL... | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. | A5D1B6 |
P45482 | FTSZ_NOSS1 | Cell division protein FtsZ | Nostoc | MTLDNNQELTYRNSQSLGQPGFSLAVNSSNPFNHSGLNFGQNNDSKKISVENNRIGEIVPGRVANIKVIGVGGGGGNAVNRMIESDVSGVEFWSINTDAQALTLAGAPSRLQIGQKLTRGLGAGGNPAIGQKAAEESRDEIATALEGADLVFITAGMGGGTGTGAAPIVAEVAKEMGALTVGVVTRPFVFEGRRRTSQAEQGIEGLKSRVDTLIIIPNNKLLEVIPEQTPVQEAFRYADDVLRQGVQGISDIITIPGLVNVDFADVRAVMADAGSALMGIGVSSGKSRAREAAIAAISSPLLECSIEGARGVVFNITGGS... | Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new ce... | P45482 |
Q8IUG5 | MY18B_HUMAN | Unconventional myosin-XVIIIb | Homo | MAISSRLALWEQKIREEDKSPPPSSPPPLFSVIPGGFIKQLVRGTEKEAKEARQRKQLAVASPEREIPEISISQPNSKSSSGTRSGSQQISQDDQSSSPGSSDILGKESEGSRSPDPEQMTSINGEKAQELGSSATPTKKTVPFKRGVRRGDVLLMVAKLDPDSAKPEKTHPHDAPPCKTSPPATDTGKEKKGETSRTPCGSQASTEILAPKAEKTRTGGLGDPGQGTVALKKGEEGQSIVGKGLGTPKTTELKEAEPQGKDRQGTRPQAQGPGEGVRPGKAEKEGAEPTNTVEKGNVSKDVGSEGKHVRPQIPGRKWGG... | May be involved in intracellular trafficking of the muscle cell when in the cytoplasm, whereas entering the nucleus, may be involved in the regulation of muscle specific genes. May play a role in the control of tumor development and progression; restored MYO18B expression in lung cancer cells suppresses anchorage-indep... | Q8IUG5 |
Q3MI03 | OGFD1_BOVIN | uS12 prolyl 3-hydroxylase | Bos | MNGKRPAEPGSDRAGKKVKKEVMAKFSDAVTEETLKKQVAEAWSRRTPFRHEAIVMDMDPFLHCVIPNFIQSQNFLEGLQKELLNLDFHEKYNDLYKFQQSDDLKKRREPHICALRKILFEHFRSWISDISKIDLESTIDMSCAKYEFSDALLCHDDELEGRRIAFILYLVPPWDASLGGTLDLFSVDEHFQPKQIVKSLIPSWNTLVFFEVSPVSFHQVSEVLSEEKSRLSISGWFHGPSLTRPPTYFEPLIARSPHIPQDHEILYDWINPTYLDMEYQAQIQEEFEESSEILLKEFLQPEKFAEVCEALERGRVEWSS... | Prolyl 3-hydroxylase that catalyzes 3-hydroxylation of 'Pro-62' of small ribosomal subunit uS12 (RPS23), thereby regulating protein translation termination efficiency. Involved in stress granule formation. | Q3MI03 |
B3QZE2 | BCHB_CHLT3 | Light-independent protochlorophyllide reductase subunit B | Chloroherpeton | MRLAYWIYEGTAHHGIGRIANSLKGVHAVFHAPLGDDYVNVIHTMLERTPNFPRATTSVVTGRDLAQGTNRLPDTLRQVEERFKPELIIVSASCSTTLLQENLQLIVGNANIDTEVFIYEVNPFRVQETEAAEGLFTALVKKYAEKQDLTEEPSINIIGPASLGFHVRSDVTSLRRMMATLGVKINVVAPYSAGLADLKKLPAAWLNVVPYQELGHGAAEHLEEKFGMSSMYDTPLGIQPTMKWLNELIEKLNAIGAKNGKSSNLKMPPLTAFSFDGMSAPSGVPWFTHSADMESFSMKRAFVFGDATRTVAMVKFLRDE... | Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex. | B3QZE2 |
Q8MJ80 | HEPC_PIG | Hepcidin | Sus | MALSVQIRAACLLLLLLVSLTAGSVLPSQTRQLTDLRTQDTAGATAGLTPVAQRLRRDTHFPICIFCCGCCRKAICGMCCKT | Has strong antimicrobial activity against E.coli ML35P N.cinerea and weaker against S.epidermidis, S.aureus and group b streptococcus bacteria. Active against the fungus C.albicans. No activity against P.aeruginosa. | Q8MJ80 |
Q5M5S1 | FABH_STRT2 | 3-oxoacyl-[acyl-carrier-protein] synthase III | Streptococcus | MAFAKISQVAHYAPAQVVTDDDLSKIMDTSDEWIRSRTGIQERRISLNENTSDLATNVAYQLLEKSGLSPEELDFVLVATISPDNSMPSVAARVQGTIGAVNAFAFDITAACSGFVFALATAEKLIKSGAYKKGLVIGAEVLSKTLDWSDRATAVLFGDGAGGVLLEESEEEHFFGESLNTDGSKGGLESGASAVISPYSDGTEQPNPYMQMDGKAIFDFAVKTVSKSIKALVEEKGEPDYFLLHQANIRILDTMAKKIDVSRDKFLANMMSYGNTSAASIPILLSENVANETLKLGSDQTILLSGFGGGLTWGSLIVKI | Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-A... | Q5M5S1 |
B9E5P2 | SYD_CLOK1 | Aspartyl-tRNA synthetase | Clostridium | MGEELKTLKRTCMCGGLTEANIGDKITVMGWVQRKRNLGGLVFVDLRDRTGILQIVFGEAINKEAFEKSDSVKSEYCIAAVGTIVKRESPNMEIPTGMVELKGEYIKIFSESETPPIYIKENLDAAENIRLKYRYLDLRRPDMQRIFMLRHKTAKVIRDFLDEQGFLEIETPILGKSTPEGARDYLVPSRNYKGKYYALPQSPQLFKQLLMVSGYDRYFQIAKCFRDEDLRANRQPEFTQVDMEISFVDQEEVMDLNERLIQRVFKQILDVDVKLPIERMTYKTAMDKYGSDKPDLRFGMEINDISEVVKGVDFKVFQNA... | Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). | B9E5P2 |
B3PYQ2 | LPXA_RHIE6 | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase | Rhizobium | MSTIAESARIHPMAVVEDGATVGEGVKIGPFCHVGPHVVLQENVELLSHAIVTGRTVIGKGTRIFPMAVVGGDPQSVHHAGEETTLSVGANCTIREGVTMNTGTADFGGQTIVGDNNLFLANSHVAHDCRVGNHVIMSNNVMLAGHVVIEDRVILGGGSAVHQFTRVGRQAFVGGLSAVSYDVIPYGMLNGNPGLLSGLNVVGMTRAGIDRAVIHRVRRAYKAIFEGTASVRENAAAIREEYADCPEVVQILDFIAADSDRALSSPTRGQKG | Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | B3PYQ2 |
Q68VU8 | ATPB_RICTY | F-ATPase subunit beta | typhus group | MTQNIGKITQVISAVVDVKFTNNSKLPEILNALECYNAKQRIVLEVAQHIGDDTVRCISMGSTEGLIRGLEVIDTGNPIHIPVGIATLGRIMNVVGEPIDGKGEIKSSTISSIYKPAPDFINQSTERDILVTGIKVVDLLAPYTKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYTVFAGVGERTREGNDLYHEMIASGVINLEAPEKSKVALVYGQMNEPPGARARVALSGLTIAESFRDMNAGQDVLFFVDNIFRFTQAGAEVSALLGRIPSAVGYQPTLATDMGELQERITSTKHGSITSVQAIYVPADDLTDPA... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | Q68VU8 |
C3PM36 | LPXA_RICAE | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase | spotted fever group | MSNSNIHTTAVIAEGAKLGKNVKIGPYCIIGPEVVLHDNVELKSHVVIEGITEIGENTVIYPFASIGQPPQILKYANERSSTIIGSNNTIREYVTVQAGSQGGGMMTRVGNNNLFMVGVHIGHDCKIGNNVVFANYVSLAGHIGVGDYAIIGGLSAVHQYARIGEYSMIGGLSPVGADVIPFGLVSSKRAVLEGLNLIGMNRKGFDKVKSLSALKAIEEIFSGEGNFAERIKQVAEKYNNNSIVIQIIDFLNQDSSRAFCRFEK | Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | C3PM36 |
A1U390 | RL9_MARN8 | 50S ribosomal protein L9 | Marinobacter | MEVILLEKVANLGSLGDKVKVKAGYGRNFLLPYGKAVPATEANVKAFEERRAELEKAAAEKLAAAQARAEALEGASFTITSKAGEEGKLFGSIGVRDIADAVSTGGTEVEKSEVRLPEGPIRVTGEYDIELQLHTDVEVTIKLAVVAE | Binds to the 23S rRNA. | A1U390 |
Q8DBV9 | RBFA_VIBVU | Ribosome-binding factor A | Vibrio | MSKDFSRTQRVSQQLQKELAMILQREVRDSRLGMVTISDVEVSRDLAYAKVFVTFLCVGEQTPESCLAALREHEVHIRMMLGKRIRLRLTPEVRFYYDNTLVEGMRMSNLVTEVVNKDKIKQKDAGREDEE | One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal heli... | Q8DBV9 |
Q47C25 | PSD_DECAR | Phosphatidylserine decarboxylase beta chain | Dechloromonas | MSDRLAVLPQYLIPKQALTVLAGKLASAKAGGLTTSVIRWFVRRYNVNMTEAANPDIASYKSFNEFFTRPLKDGARPAADADFLCPVDGAISQYGTIDRDQIFQAKGHSYSTTALVGGDRKLAEQFENGSFATLYLSPRDYHRIHMPCDGKLTRMIYVPGALFSVNPTTARGVPGLFARNERVICVFESEFGSFVLTLVGATIVGSMATVWHGTINPPRPGVIREWRYDEQNIRLKKGQEMGRFLLGSTVVMLFPKNTLAFNPDWSPSRAIRMGEQMGSNAN | Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). | Q47C25 |
A8H7T1 | GCST_SHEPA | Glycine cleavage system T protein | Shewanella | MANKTVLFNKHLESNGKMVDFHGWDMPLNYGSQIEEHHAVRQDAGMFDVSHMTVVDVIGDDACAFLRKLLANDVAKLKVPGKALYGGMLDHNGGVIDDLITYYLSDTEYRIVVNSATREKDLAWINEQVKGFSVEVTERPELAMIAVQGPNAKAKAATVFNDAQNAAIEGMKPFFGVQAGSLFIATTGYTGETGYEVIVPNDEAEALWQAFLDAGIKPCGLGARDTLRLEAGMNLYGLDMDESVNPLAANMGWTVAWEPAERDFNGRQALEKIKAEGTDKLVGLIMDAKGVIRHGMSVFFTDSDGVEQQGTITSGTFSPT... | The glycine cleavage system catalyzes the degradation of glycine. | A8H7T1 |
A0K438 | HEM1_BURCH | Glutamyl-tRNA reductase | Burkholderia cepacia complex | MQLLTIGINHHTAPVALRERVAFPLEQIKPALVTFKNVFLGPQAPNTPEAAILSTCNRTELYCATDDRAAREGAVRWLSEYHRIPVDELAPHVYALPQSEAVRHAFRVASGLDSMVLGETQILGQMKDAVRTATEAGALGTYLNQLFQRTFAVAKEVRGTTEIGTQSVSMAAAAVRLAQRIFEKVSDQRVLFIGAGEMIELCATHFAAQGPRELVVANRTAERGQRLAERFNGRAMPLADLPTRMHEFDIIVSCTASTLPIIGLGAVERAVKARRHRPIFMVDLAVPRDIEPEVGKLKDVFLYTVDDLGAIVREGNASRQ... | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | A0K438 |
Q9SKD6 | CNG11_ARATH | Cyclic nucleotide- and calmodulin-regulated ion channel 11 | Arabidopsis | MNLQRRKFVRLDSTGVDGKLKSVRGRLKKVYGKMKTLENWRKTVLLACVVALAIDPLFLFIPLIDSQRFCFTFDKTLVAVVCVIRTFIDTFYVIHIIYYLITETIAPRSQASLRGEIVVHSKATLKTRLLFHFIVDIISVLPIPQVVVLTLIPLSASLVSERILKWIILSQYVPRIIRMYPLYKEVTRAFGTVAESKRVGAALNFFLYMLHSYVCGAFWYLSSIERKSTCWRAACARTSDCNLTVTDLLCKRAGSDNIRFLNTSCPLIDPAQITNSTDFDFGMYIDALKSGVLEVKPKDFPRKFVYCFWWGLRNISALGQ... | Putative cyclic nucleotide-gated ion channel. | Q9SKD6 |
Q6GHE0 | MUTS_STAAR | DNA mismatch repair protein MutS | Staphylococcus | MSNVTPMMQQYLKIKSEYQDCLLFFRLGDFYEMFYEDAKEASRVLEITLTKRDAKKENPIPMCGVPYHSADSYIDTLVNNGYKVAICEQMEDPKQTKGMVRREVVRIVTPGTVMEQGGVDDKQNNYILSFVMNQPEIALSYCDVSTGELKVTHFNDEATLLNEITTINPNEVVINDNISDHLKRQINMVTETITVRETLSSEIYSVNQTEHKLMYQATQLLLDYIHHTQKRDLSHIEDAVQYAAIDYMKMDFYAKRNLELTESIRLKSKKGTLLWLMDETKTPMGARRLKQWIDRPLISKEQIEARLDIVDEFSAHFIER... | This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | Q6GHE0 |
Q6N1G8 | METXA_RHOPA | Homoserine transacetylase | Rhodopseudomonas | MMNIHSVKGQKIAAGERTQEVDHPHSLVAQFGADQPLPLDCGIELSPFQIAYQTYGTLNADKSNAILVCHALTMDQHIANVHPITGKPGGWLTLVGPGKPIDTDRYFVICSNVIGGCMGSTGPASINPATGKAWGLDFPVITIPDMVRAQAMLIDRFGIDKLFCVVGGSMGGMQVLQWSVAFPERVFSALAIACATRHSAQNIAFHELGRQAVMADPDWQHGRYFEHGCFPHRGLAVARMAAHITYLSDAALHRKFGRKMQDRELPTFSFDADFQVESYLRYQGSSFVERFDANSYLYLTRAMDYFDIAADHDGVLAAAF... | Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. | Q6N1G8 |
A1WQY3 | ALR_VEREI | Alanine racemase | Verminephrobacter | MPRPIQARIHSSALQANLRRVRQSVPDAKVWAVVKANAYGHGIARVFESLRGADGFALLDLAEAQGLRGLGWRGPILLLEGVFEPRDLELCSRLGLWHVVHCDEQIDMLAAHRSQAPQHVFLKLNAGMNRLGFAPQRYRSAWARLGALAQVDEISLMAHFSDADGPRGIAPQLAAFVRATQDLPGARSLCNSAATLRHAADASVRADWVRAGIVLYGSAPDFPGHDAGHWGLQPAMTLATRLIGVQQLQAGDTVGYGARFVAPGPMAIGVAACGYADGYPLHCGTGTPVLVDGIRTRVVGRVSMDMLTVDLTPLQRAGLQ... | Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. | A1WQY3 |
Q1C0N0 | ACSA_YERPA | Acyl-activating enzyme | Yersinia | MSQIHKHPIPAAIAEHALITPEKYQHYYQQSVQNPDEFWGEQGKIIDWIKPYKTVKNTSFDPGHVSIRWFEDGTLNLAANCLDRHLAERGDQTAIIWEGDDPNQSKTVTYKQLHHDVCQFANVLKSLGVKKGDVVAIYMPMVPEAAVAMLACARIGAVHSVIFGGFSPDAVAGRIIDSHSKLVITADEGIRAGRAIPLKKNVDEALKNPAITSIKNVVVFQRTGNASYWEDGRDVWWHDLIKEASADCPPEEMNAEDPLFILYTSGSTGKPKGVVHTTGGYLVYAALTFKYVFDYHPGDIYWCTADVGWVTGHSYLLYGP... | Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis. | Q1C0N0 |
Q59337 | CATA_DEIRA | Catalase | Deinococcus | MSDENNKGVGTAVQGVGGPRDGRTAPGEQGTTLTTRQGHPVHDNQNSRTVGSRGPMTLENYQFIEKLSHFDRERIPERVVHARGVGAHGVFRATGKVGDEPVSKYTRAKLFQEDGKETPVFVRFSTVGHGTHSPETLRDPRGFAVKFYTEDGNWDLVGNNLKIFFIRDALKFPDLIHSQKPSPTTNIQSQERIFDFFAGSPEATHMITLLYSPWGIPASYRFMQGSGVNTYKWVNDQGEGVLVKYHWEPVQGVRNLTQMQADEVQATNFNHATQDLHDAIERGDFPQWDLFVQIMEDGEHPELDFDPLDDTKIWPREQFP... | Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. | Q59337 |
A7TKF2 | EIF3B_VANPO | Translation initiation factor eIF3 p90 subunit homolog | Vanderwaltozyma | MSAALEDIKLEDIPVDDIDFSDLEKQYSVNDTVSFDQYIVVCGAPVIPEGKVAVLKKALTGLFSKAGKVVDIEFPIEDGKTKGFLFVECASPADGNKIIKAFHTKRLDLKHRLFIYTMRDVEKYNDKNFPTEFVEPEIPDFFPTSTLKSWLSDEDGRDQFVLQANEMTTVLWNSAIEDEESVVESRKNWSTNYIRFSPKGTYLFSYHPQGVVMWGGPHFDRLRRFYHPNVRTSSVSPSEKFLVTYSPDPIVVDEEDADCPFTKKNEGHQLCIWDIDSGLLQSTFPVVKSSYLQWPLVRWSYNDQYCARMVGETLVVHDVK... | RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and... | A7TKF2 |
A6VRW7 | MTGA_MARMS | Peptidoglycan glycosyltransferase MtgA | Marinomonas | MAKRKQGIFGRIWFVAWRFLLLFVIVLFLFRFVPLPTTSFMLQSQYPVKHTWISIDKLPTYMPLAVVASEDQRFPDHFGVDFTAISKALDQYDDGDGLRGASTITQQTAKNLFLWSGRSFIRKGLEAGLAIGLETLWGKKRILEVYLNIAEFGKGIYGVEAASQHYFGRSASKLTMNQAARLAVLLPSPRTRNPNDLTFYLRERVDWVERQMQQLGPDYLKPIIE | Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors. | A6VRW7 |
Q74H92 | RNPA_LACJO | Protein C5 | Lactobacillus | MRKSYRVKTERDFQKVFKEGQSMANRGFVVYTLPKENQKHFRVGISVGKKVGHTAVARNRLKRFIRATLTELKPEIRPDLDFLVIARPYARDFDMGRTKKNLIHVLRLAKVLSSEETEIEEK | RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the riboz... | Q74H92 |
Q8DUK7 | QUEC_STRMU | Queuosine biosynthesis protein QueC | Streptococcus | MKRQSALVVFSGGQDSTTCLFWAMKHYEYVETVTFSYGQRHSQELEVAKEIAAEQGVKHHILDMSLLGQITENALTSDIAIETKDGEVPNTFVDGRNHLFLSFAAVLAKQRKIRDIVTGVCQTDFSGYPDCRDVFVKSLNVTLNLAMDYEFVIQTPLMWLDKAETWELADQLGKFDYVRQKTLTCYNGIRGTGCRQCPACHLRQAGLEKYLSQKGKN | Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). | Q8DUK7 |
C1A8L2 | MUTL_GEMAT | DNA mismatch repair protein MutL | Gemmatimonas | MSRIAILPSAVADQIAAGEVVERPASVVKELVENALDAGATSVDITIEDGGRTLIRIADNGSGMDGADAVLALSRHATSKITSAEQLVGVRSFGFRGEALPAIASVSELQIETASEDGSGTLVRVQAGTLTETGQVARRQGTTVSVHRLFHNTPARLKFMRSARSEWRAIVDAMQAIGVLRRDVHFTVRHDGRVALDWPAVSTLRARLAALWGAADVERFVDVDDVQGVVHVSGLAERPADVGTATRRVLLIVNGRVVRDHGLIRAAEAAYRSTIPAGMRPSLVLQVHVPGGDVDVNVHPAKAEVRFRDRWPLERAVEEA... | 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 ... | C1A8L2 |
Q98QZ1 | RRF_MYCPU | Ribosome-releasing factor | Mycoplasmopsis | MDISIINEVFSTLEEKSMNVVSNFEFNLSKISTGRANPQLIKNIKVSYYEELIPLEQISNISVPEPQQLLIKPFDHNITKEIHKSLLLANLDVAIVNEGNQIRLNFPALNTQRRKELVKSLNKFTEQARVSIRLLRQESNKKIKSFKSEISEDDIKKYETKIQTINDSYIEQIDEITKRKERELMEI | Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another. | Q98QZ1 |
B8GN14 | GCSPB_THISH | Glycine dehydrogenase (aminomethyl-transferring) subunit 2 | Thioalkalivibrio | MLIFERSRPGRGATAQAPLREATVSGLPERFRRGTRAPLPELSELDVVRHYTRLSQKNFSIDTQFYPLGSCTMKYNPRACNSLAMLPGFLGRHPHAPDTHSQGFLACMFELQEMLRDVTGMKGGVSLTPMAGAQGEFAGVAMIRAYHDARKDTARTEILVPDAAHGTNPATATMCGYTVKEIPTDDSGDVDMEALKAALGPHTAGIMLTNPSTLGVFERRIKEIADLVHQAGGLLYYDGANLNAILGKVRPGDMGFDVIHMNLHKTFSTPHGGGGPGAGAVGVSERLRPFMPIPVVAKEGERYRFMTEKDLPQSIGRLSA... | 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. | B8GN14 |
Q3BUF7 | HISX_XANC5 | Histidinol dehydrogenase | Xanthomonas | MKILDWSQLDGAARTDALTRPVQTVATQTRDAVAALIADVRARGDAALREITARFDGVSLESFAVSEADFAAAEAAVAPELRQAMQDAVARIDAFHRAGMSEGYAVETAPGVVCEKIVRPIGRVGLYVPAGSAPLPSTALMLGVPARLAGCREVVLCTPPRKDGSVDPAVLVAAQLTGVRRVFKLGGAQAIAAMAYGTESVPSCDKLFGPGNSYVTEAKQQVAQSGAAAIDMPAGPSEVLVIADAGAQPAFVAADLLSQAEHGPDSQVLLLSDSDGLIDAVQVQLEVQLAQLSRADIARQALAQSRMIKVQALDEAFAIS... | Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. | Q3BUF7 |
Q64524 | H2B2E_MOUSE | H2b 613 | Mus | MPELAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIANEASRLAHYNKRSTITSREIQTSVRLLLPGELAKHAVSEGTKAVTKYTSAK | Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated v... | Q64524 |
Q6MAK1 | ATP6_PARUW | F-ATPase subunit 6 | Candidatus Protochlamydia | MIMGQYLFWLANAHEPIENRIPELPNFISVLYHRFQHTTWAQFLHRWENIIFAILVASLISLVAYLGARKKEIIPSKFQNLLEIAVEKFSHLILEVLGPEGKAYIPFLGTLFIYIFTMNIFGMVPLMKAPSSSLNITAALAICVFCLVQFLNIRNMGIFGFLYHLAGSPKSMLEWLLAPLMFSLEIISQLSRPLTLALRLFGNVLGEDILIGTFALMGVVMISSVETFVGIPLQLPFMFLGLLTSFMQALVFTLLSTVYILLSMHKEGEKN | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | Q6MAK1 |
Q74AT2 | LOLD_GEOSL | Lipoprotein-releasing system ATP-binding protein LolD | Geobacter | MSNLIEVVDLCKTYGAGDTRVDVLRGVNLAVAEGETIALVGASGAGKSTLLHLMGTLDRPSSGSVLFGGEDVFRKSDMDLAAFRNRSIGFVFQFHHLLPEFTAEENVMMPALIGGMKRSAALGPARELLSEVGLAHRLTHKPGELSGGEQQRVAIARALVLSPRLLLADEPTGNLDMKTSDEVHETLSEINRKRGLTLVVVTHNERLASRMGRTVRLVDGRIEV | Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. | Q74AT2 |
P18187 | PHNS_SOLFR | NiFe hydrogenlyase small chain | Solidesulfovibrio | MNFSVGLGRDDAEKRLVQNGVSRRDFMKFCATVAAAMGMGPAFAPKVAEALTAKHRPSVVWLHNAECTGCTEAAIRTIKPYIDALILDTISLDYQETIMAAAGEAAEAALHQALEGKDGYYLVVEGGLPTIDGGQWGMVAGHPMIETTKKAAAKAKGIICIGTCSAYGGVQKAKPNPSQAKGVSEALGVKTINIPGCPPNPINFVGAVVHVLTKGIPDLDENGRPKLFYGELVHDNCPRLPHFEASEFAPSFDSEEAKKGFCLYELGCKGPVTYNNCPKVLFNQVNWPVQAGHPCLGCSEPDFWDTMTPFYEQG | Involved in hydrogen uptake for the anaerobic reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is the physiological electron acceptor. | P18187 |
Q82N59 | RLMG_STRAW | rRNA (guanine-N(2)-)-methyltransferase RlmG | Streptomyces | MNDPMTTPWGAYALARFPEDPRDRLRAWDASDAYLLRHLAASGTPLSGSVVVLGDRWGALTTALAAHRPTQITDSFLAREATRENLGRAGVDPSSVRLLTTRDTPPERIDVLLVRVPKSLALLEDQLHRLAPGVHEGTVVVGAGMVKEIHTSTLKLFERILGPTRTSLAEQKARLIFCTPDPGLVRDPNPWPYRYRLPDGVGPLSGRPVTNHAGVFCADRLDIGTRFFLRHLPRVSGAERVVDLGCGNGVVGTAVALTEPEAEVLFVDESYQAVASARETFRANADGTAEFLVGDGLSGVPAASVDVVLNNPPFHSHQAT... | Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA. | Q82N59 |
Q1RI52 | MURD_RICBR | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase | belli group | MTIHKKQNIGVFGFGKTGISVYEELQSKCNIIAYDDLEVNRNKFEELFSKNYIIPISDIKWQNLDKIVLSPGIPLTHEIVKIAKNFNIPITSDIDLFFEKSKGLNLLAVTGTNGKSTTTALISHILSDNGLDYPVAGNIGVPVLQAKASKGGYVLELSSFQLDLVKTFAAKIAVLLNITPDHLDRHENMEGYITAKSKIFDRMDKDSYGIINIDNDYCHEIFTNLQQKHHIKLIPFSVTKILEKGISIVNDIITDNFFEHISFKLISNKSLQGIHNSENIAASYAVARIIGLEPVKIIESISSFQGLPHRMQYLGNIDDI... | Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). | Q1RI52 |
Q8Z397 | WECG_SALTI | UDP-N-acetyl-D-mannosaminuronic acid transferase | Salmonella | MTNNAAAPLYSLRGLPLIGWRDMSHALNYLFADGQLKQGTLVAINAEKLLTAEDNPEVRALIAAAEFKYADGISVVRSIRKKFPQAQVSRVAGADLWEALMARAGKEGTPVFFVGGKPEVLAQTEAKLRTQWNVNIVGSQDGYFTPEQRQALFARIHASGAKIVTVAMGSPKQELLMRDCREVHPHALYMGVGGTYDVFTGHVKRAPKIWQNLGLEWLYRLLSQPKRITRQMRLLRYLRWHYTGDL | Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA (Lipid II), the second lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis. | Q8Z397 |
Q1WUA0 | RNC_LIGS1 | Ribonuclease III | Ligilactobacillus | MIEGLQEMLKRDFNITFKDVDLLDAAFTHASYVNETPERKKKLKYYERIEFLGDAVMQLCVSEYIYEHYPEMPEGKMSRLRAAMVRADSFSKFAIECHFNEYIRLGKGEEKGNARQRPSLLCDIFESFIGALYLDQGKDEVVRFISKVIFPKLELGWFDHMMDNKTELQEVLQQNGECKIKYNEVNVTGPDNERVYTMNVVVNNEVMGEGTGRTKKAAEQMAAYQALKKLRK | 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. | Q1WUA0 |
P0DL22 | NDBX_TITPA | Toxin Tpa3 | Tityus | ADDDLEGFSEEDLKAIKEHRAGLAA | Unknown. Is not toxic to mammals. | P0DL22 |
A0B913 | RLMH_METTP | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Methanothrix | MHMRIIAVGRIRERFWQDAASYYLRRLSPYTRLDVVEVREEDPIKEGRGILAHLCGGVTVALDEHGESMSSQELALWLQNRIVEGCGSINWIIGGPEGLSQDVLNRSDLQLSLSKMTFPYQMARILLLEQLYRAFKIIKNEPYHR | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | A0B913 |
Q51948 | NAHD_PSEPU | 2-hydroxychromene-2-carboxylate isomerase | Pseudomonas | MIVDFYFDFLSPFSYLANQRLSKLAQDYGLTIRYNAIDLARVKIAIGNVGPSNRDLKVKLDYLKVDLQRWAQLYGIPLVFPANYNSRRMNIGFYYSGAEAQAAAYVNVVFNAVWGEGIAPDLESLPALVSEKLGWDRSAFEHFLSSNAATERYDEQTHAAIERKVFGVPTMFLGDEMWWGNDRLFMLESAMGRLCRQNADLSS | Involved in the naphthalene catabolic pathway. Catalyzes the reversible glutathione-dependent isomerization of 2-hydroxychromene-2-carboxylate (HCCA) to trans-O-hydroxybenzylidenepyruvate (THBPA). | Q51948 |
B9LA97 | TRMA_NAUPA | tmRNA (uracil(341)-C(5))-methyltransferase | Nautilia | MTCSSFGKCGSCVLWEMPYDEQLKMKSEKLKEMFSEFDMPEIEVVHGSDEHFRARAEFRVWHEGDKSYYAMRKRKEDGRGVIPIEECKIVDKAIYDIMTPLLKEIEKNDNLRFKLYEIDFLSNSKGELIITLIYHKKVDESIAEDIKKLKEKFKNADFIVRKKGRKYVFDKNYLIEELNINSKTYKYKIIENTFSQPNRQMNQKMIEWAMRNSEDLKGDLVELYCGNGNFTIPLSERFNKVIATEISKESIEAATYNAEINARDNITFLAMSAAEFSKLYKDRSPLITKYDLKNILIDPPRAGLDDKSREFVNEFDNIIY... | Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA). | B9LA97 |
Q5PPI9 | TTLL1_RAT | Tubulin--tyrosine ligase-like protein 1 | Rattus | MAGRVKWVTDIEKSVLINNFEKRGWVQVTENEDWNFYWMSVQTIRNVFSVETGYRLSDDQIVNHFPNHYELTRKDLMVKNIKRYRKELEKEGSPLAEKDENGKYLYLDFVPVTYMLPADYNLFVEEFRKSPSSTWIMKPCGKAQGKGIFLINKLSQIKKWSRDSKTSSFVSQSTKEAYVISLYINNPLLIGGRKFDLRLYVLVSTYRPLRCYMYKLGFCRFCTVKYTPSTSELDNMFVHLTNVAIQKHGEDYNHIHGGKWTVNNLRLYLESTRGREVTSKLFDEIHWIIVQSLKAVAPVMNNDKHCFECYGYDIIIDDKL... | Catalytic subunit of a polyglutamylase complex which modifies tubulin, generating side chains of glutamate on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Probably involved in the side-chain elongation step of the polyglutamylation reaction rather than the initiation st... | Q5PPI9 |
Q1Q889 | ZNUC_PSYCK | Zinc import ATP-binding protein ZnuC | Psychrobacter | MNNTSKLLNLSNVSYYIGQQRLLSNINIDIAVNETVSVIGPNGAGKSTLVKLILGLIVPTSGQVTPSEPLQIGYVPQRFSVPPILPLRVSDLLAQACKKRLTAEQRQFIFDKLSLTHLLSRQMLHLSGGETQRVLLARALLDKPNLLILDEPMQGLDPETEVWLYQFIDELPEFLRCAMLVVSHDLHWVMKGSRRVICLNKHICCEGQPSELAISSEFQKLFGHHYEQPYVHQPHACEHHAPS | Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. | Q1Q889 |
O68946 | ANFG_AZOMA | Nitrogenase component I | Azomonas | MDDKVEEPIDFIMKHCLWQSHSRNWDRERQNEEILKKTKQLLCGEPVDLSTPSDRCYWVDAVSLVDAYRERYTWINAMSKDELAQLIDTLKARLDYLTISGSLNEELSDKNY | 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. | O68946 |
P53966 | KTR5_YEAST | Probable mannosyltransferase KTR5 | Saccharomyces | MLLIRRTINAFLGCIHCNLTATCILIAFVITMYVVLVSEPASVDGTMGNFLPFSKMDLATKRDRPFYSNCVNTQDYLLNPSYIKQNASFVMLTRNGELEDVIKTINSIEEHFNQWFHYPYVFLNDQPFEEDFKAKVRDVTVGALVEFGTIDEISWNFPSDVKDTFEFYNAIEDQGDRSILYGNLESYHKMCRFYSGLFYKHPLVQKYEWYWRLEPDVEFFCDITYDPFLEMLRTNKKYGFTIIIPELYWTVPNLFRHTKSFISQKGVTLGSLWKLFTKDYDIFESDDPELRDWINYDFQAKAKISEKIAIEQLLKKGDDF... | Possible glycosyltransferase that transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. | P53966 |
A0T0L7 | PSBZ_PHATC | Photosystem II reaction center protein Z | Phaeodactylum | MITALTALLVLISLGLIVTVPVALATPGEWENSKSDFTKGFQAWVALVLVIAAADGVASSL | Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. | A0T0L7 |
Q3SFS3 | YQGF_THIDA | Putative pre-16S rRNA nuclease | Thiobacillus | MSDAQTHGTVLAFDLGLKRTGVASGELAIGIAHPLTVIQAESTDARMAAIEKLAAEWQPALFVLGLPTRADGSENEMTRVARNFARRLESRFERPVFLIDERLTSATAESELHARGIHGKKNKALTDAVAAQLILQGFFDARLTA | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | Q3SFS3 |
F7DRV9 | BRDT_XENTR | Bromodomain testis-specific protein | Silurana | MSMSSRHLHSSIVNPPPPEYINRKKTGRLTNQLQYLEKVVLKALWRHHFSWPFQQPVDAAKLNLPDYYQIIKNPMDLSTIRKRLEYNYYSKALDCIQDFNTMFTNCYIYNKPGDDIVVMSQELEKVFMEKIAEMPHEEIELSVVGNRGVKSRIKISAVAAEVCKKKMVSQKMHRRTFPCPVIAMMPKRTTLVPLSVIRSSTSSHSASSVSKVNKGIKRKADTTTPAVSLIATSCESSPTLSEPKPNKILSGTEKTRSAETSAVDLPDSQHHIHFIKSNQICEQLKHCNNILNEMMSKKHAEYAWPFYKTVIPTSLLDCSD... | Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the promoter of ... | F7DRV9 |
Q92BF6 | ENGB_LISIN | Probable GTP-binding protein EngB | Listeria | MDVNNVELVISAVRPEQYPETDLPEYALAGRSNVGKSSFINTMIRRKSMARISQKPGKTQTLNFYKIEEALFFVDVPGYGFAKVSKTEREKWGVMIETYITSREQLRGVIQIVDLRHKPTEDDRMMYEFLKYYDIPVIVVATKADKIPRSKWQKNAKIVRETLDFDPDDKFVLFSSETKMGKDEAWQFIKEGME | Necessary for normal cell division and for the maintenance of normal septation. | Q92BF6 |
P13609 | SRGN_MOUSE | gp600 | Mus | MQVPVGSRLVLALAFVLVWGSSVQGYPARRARYQWVRCKPNGFFANCIEEKGPQFDLIDESNNIGPPMNNPVLMEGPSKDFISNYDDYGSGSGSGSGSGSGSGSGSGSGFLGDMEWEYQPTDESNIVYFNYKPFDRILTEQNQDQPEDDFII | Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in azurophil g... | P13609 |
P60043 | PA2B1_NAJSG | Phosphatidylcholine 2-acylhydrolase | Naja | SNRPMPLNTYQFKNMIQCTVPKRSWWDFADYGCYCGRGGSGTPIDDLDRCCQVHDNCYNSAREQGGCRPKQKTYSYECKAGTLSCSGSNNSCAATVCDCDRLAAICFAGAPYNDNNYNIDLKARCQ | PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | P60043 |
Q5P081 | NAGZ_AROAE | N-acetyl-beta-glucosaminidase | Aromatoleum | MTLQSDLPATVRPLGPVMLDVAGFALTEEERERLLDPLVGGVILFARNFRDSEQLQALTAEIHALRSPALIIAVDHEGGRVQRFRTDGFTRIPSMRCLGRLWERDHVAALESARCAGYVLAAELLAHGVDLSFTPVLDLDYGCSRVVGDRAFHRDPLVVAALAQSLVSGMADAGMGCVGKHFPGHGYAEADSHVEIPVDEREFDAIWTEDIAPYRHRLGRQLAGVMPAHVIYPRVDPNPAGFSRFWLQDILRGRVGFGGVIFSDDLTMEGATVVGDILARARAAFGAGCDVVLVCNRPDLAVDLLDRWAPDIAPESRARI... | Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. | Q5P081 |
Q9ABF9 | Y268_CAUVC | Nucleoid-associated protein CC_0268 | Caulobacter | MKDLGGLMKQAQAMQQKLADAQARLAETTVDGTSGGGMVTVTLMGNGELVRVLMDESLVQPGEGEVIADLIIAAHADAKKKLDAKQAQMMQDAAGPMAGLMGGLPGMKF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q9ABF9 |
Q56YP2 | PI5K1_ARATH | PtdIns(4)P-5-kinase 1 | Arabidopsis | MSDSEEDEEEEEASEVILSSVVQKKKKKNLRFGEEVERRDGLVLLAQSTPMVRSRSQGTTRRVTPTPLVDVEKPLPNGDLYIGSFSGGFPHGSGKYLWKDGCMYEGDWKRGKASGKGKFSWPSGATYEGEFKSGRMEGFGTFTGADGDTYRGTWVADRKHGHGQKRYANGDFYEGTWRRNLQDGRGRYVWRNGNQYTGEWRSGVISGKGLLVWPNGNRYEGLWENGIPKGNGVFTWSDGSSCVGAWNESNIMRSFFNGVEKNDLIVGNRKRSSVDSGAGSLGGEKVFPRICIWESDGEAGDITCDIIDNVEASMIYRDRI... | Catalyzes the synthesis of phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4-bisphosphate. | Q56YP2 |
B0K460 | SP5G_THEPX | Putative septation protein SpoVG | unclassified Thermoanaerobacter | MEITDVRVRKLNEEGKMKAVVSVTFDNEFVVHDIKVIEGQNGLFIAMPSRKTPEGEFKDIAHPINSDTRNKLQSAILKEYEKAKEQEAAHKE | Could be involved in septation. | B0K460 |
Q5L6G5 | NTPPA_CHLAB | Nucleotide pyrophosphatase | Chlamydia | MEPKFILGSSSPRRKLILEYFRIPFTCIPSNFEEHSVPYHGDPVAYSQELAIGKAESIVKDHNPEGLILTADTVVAYQGKIFNKPGSYDEAIEMLKTLSGQTHAVITSIALLQDRKLVTGEETTQVTFTQLPEAYLGRYIKAFSTLDKCGAYSIQEGGSLIIHNIQGCAYNVQGLPIKTLKHLLLEFNVDLWDYLV | Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. | Q5L6G5 |
Q33BY2 | RR7_NICTO | 30S ribosomal protein S7, chloroplastic | Nicotiana | MSRRGTAEKKTAKSDPIYRNRLVNMLVNRILKHGKKSLAYQIIYRAVKKIQQKTETNPLSVLRQAIRGVTPDITVKARRVGGSTHQVPIEIGSTQGKALAIRWLLAASRKRPGRNMAFKLSSELVDAAKGSGDAIRKKEETHRMAEANRAFAHFR | 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. | Q33BY2 |
A6WRS8 | RLMI_SHEB8 | rRNA (cytosine-C(5)-)-methyltransferase RlmI | Shewanella | MAIRIKLKPGREKSLERRHPWVFSNAIHNIKGKPEAGETVDVVAHDGHWLGRGAWSPESQIQVRIWTFDREEEIDREFFARRLQRAQIGRNDLIREQGLTGYRLVAAESDGLPGITIDRYANVLVCQLLSTGADLWRDTLVELLAEQYPDCAIYERSDVDSRKKEGLLPVTGLLHGTLPEMPVIIEENGIKIAVDVIKGHKTGFYLDQRDNRAIAARFVKDKSVLNCFCYTGTFGLYAAKAGAASIENVDVSSLALATARLNMQVNGLSDDNVHYNEADVFKLLRQYRDEGKTFDVIVLDPPKFADNKAQLNGACRGYKD... | Specifically methylates the cytosine at position 1962 (m5C1962) of 23S rRNA. | A6WRS8 |
Q8M9Y9 | CLPP_CHAGL | Endopeptidase Clp | Chaetosphaeridium | MPVGVPKVPYRLPGDVQVQWIDLYNRLYRERILFLGQTVNYEIANQIIGLMLYLNGDDKSKDMYLYINSPGGAVVPGIAIYDTMQFVEPEIRTICMGVAASMGSFILTGGEITKRIALPHARVMIHQPSSSYYKDQAGELIMEAEEVLKLRDCITKVYVQRTGKPISVISEDMERDVFMSAKEAKEYGIVDLVALDVDSNS | Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. | Q8M9Y9 |
Q3IRQ4 | LEUC_NATPD | Isopropylmalate isomerase | Natronomonas | MSEGTLYDKVWENHKVTTLPNGQDQLFVGLHLIHEVTSPQAFGMLRERDIEVARPDLTHATVDHIVPTADQSRPLDNEAAEEMMAELEENVREAGITLDDPTTGNQGIVHVIGPEQGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSQIRDVLATQTIAMEKKDVRKIEVTGELGEGVTAKDIILTIIRRLGTDGGVGYVYEYAGEAIENLGMEGRMSICNMSIEGGARAGYVNPDETTYEWLRETDAFADDPERFEELKPYWESVRSDPDAEYDDVVTIDGSEIEPVVTWGTTPGQGIGITEEIPAPEDLPADKQDTA... | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | Q3IRQ4 |
F8RKW1 | VM34_DRYCN | Snake venom metalloproteinase | Drysdalia | MIEVLLVTICFTVFPYQGSSIILESGNVNDYEVVYPQKVPALPKGGVQNPQPETKYEDTMQYEFHVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAAISACDGLKGHFKHRGETYFIEPLKLSNSESHAIYKDEHVEKEDEIPKICGVTQTTSESDEPIEKISQLTNTPEQDRYLQVKKYIELYVVVDNRMYRNYNSNRDAINERVYEMVNTLNVMYRPLNFFIALIGLEIWSNQDEINIEPEVAVTLRSFGEWRNTTLLPRKRNDNAQLLTGIDFNGATVGLAYVGTLCSPTQ... | Snake venom zinc metalloproteinase that may impair hemostasis in the prey. | F8RKW1 |
P86413 | OSR1_XENLA | Protein odd-skipped-related 1 | Xenopus | MGSKTLPAPVPIHPSLQLTNYSFLQAFNGLPVPAEHVPNLYGFSALHAVHLHQWTLGYPTLHLPRSSFSKVPGVSSLVDSRFQIPTFPLFPHMIHPKQESPNLSNKTKPRFDFANLAVAATQEDHCKLGLMNDQGSPPAMGGLLDVTKLTPEKKPTRGRLPSKTKKEFVCKFCGRHFTKSYNLLIHERTHTDERPYTCDICHKAFRRQDHLRDHRYIHSKEKPFKCQECGKGFCQSRTLAVHKTLHTQVKELKPSKIKC | Transcriptional repressor. Required for pronephric kidney development. | P86413 |
A0M5Z9 | SYM_GRAFK | Methionyl-tRNA synthetase | Gramella | MNKNPQRFTITAALPYTNGPIHIGHLAGVYVPADIYSRFLRMQGYDVAFVCGSDEHGVPITIKAKKEGVTPQDVVDKYNGIIKKSFEDFGITFDNYSRTSGKTHHDTASAFFKKMYEDGKFIEESTEQLYDEEAGQFLADRFVTGTCPKCGNEEAYGDQCESCGTSLNATDLINPKSAITGAVPTLKETRHWFLPLDQYEDFLKEWILKGHKSDWKSNVYGQVKSWIDDGLRARAVTRDLDWGIPVPVEGGDGKVLYVWFDAPIGYISSTKEWAEREGKDWEPYWKDENTKLVHFIGKDNIVFHCIIFPVMLKAHGDYIL... | Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | A0M5Z9 |
A1TD59 | ATPF_MYCVP | F-type ATPase subunit b | Mycolicibacterium | MGELTTSIVAAEEGGGTSNFLIPNGTFFVVLLIFLIVLGVIAKWVVPPVSKVLAEREAMLAKTAADNRKSAEQVAAAQADYDKTMADARGEASSIRDEARVAGRQVVDEKRAVASGEVAETVKSADQQLSQQGSAAQSELQSSVDGLSATLASRILGVDVNSGGSR | Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). | A1TD59 |
Q9ADK2 | GREA_STRCO | Transcript cleavage factor GreA | Streptomyces albidoflavus group | MTQTSENVTWLTQEAYNKLKEELEYLTGPARTEISAKIAAAREEGDLRENGGYHAAKEEQGKQELRVRQLTQLLESAKVGEAPAADGVVAPGMVVTIAFDGDEDDTLTFLLASREYASSDIETYSPQSPLGSGVLGHKVGDDAQYELPNGKPASVRILKAEPYNG | Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factor... | Q9ADK2 |
P0DN10 | VKT6_ANEVI | AsKC6 | Anemonia | MVFLLCFFLVADVSYGINGDCELPKVVGPCRAGFRRYYYNSSSKRCEKFIYGGCRGNANNFHTLEECEKVCGVRSRDSPKEN | Serine protease inhibitor that inhibits both tissue and plasma kallikreins. Has hemolytic activity. Inhibits voltage-gated potassium channels (Kv). | P0DN10 |
F6HDT7 | MTND2_VITVI | Acireductone dioxygenase (Ni(2+)-requiring) 2 | Vitis | MGSFKDDREEVLQAWYMDDSDEDQRLPHHRDPKEFVSLDQLAKLGVLSWRLDADNYETDEELKKIREARGYSYMDFCEVCPEKLPNYEEKIKNFFEEHLHTDEEIRYCVAGSGYFDVRDQNDSWIRVWLKKGGMIVLPAGIYHRFTLDSNNYIKAMRLFVGDPVWTPFNRPHDNLPARQEYLEAFGQKEAANHVVDAAA | Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine... | F6HDT7 |
P00315 | PHAA_MASLA | Allophycocyanin alpha chain | Mastigocladus | SIVTKSIVNADAEARYLSPGELDRIKSFVSSGEKRLRIAQILTDNRERIVKQAGDQLFQKRPDVVSPGGNAYGQEMTATCLRDLDYYLRLITYGIVAGDVTPIEEIGIVGVREMYKSLGTPIDAVAAGVSAMKNVASSILSAEDAAEAGAYFDYVAGALA | Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers. | P00315 |
C1FPH3 | DNAA_CLOBJ | Chromosomal replication initiator protein DnaA | Clostridium | MSTHLTETWEKAINIIKGELTEVSFNTWIKSINPISLENNSLKLAVPNDFTKGILESRYKDLIVNALKLLTSKKYNIDFIVTTEEKIEKNHNNEKSNIVVNDEMSTMLNPKYTFDSFVIGNSNRFAHAASLAVAESPAKAYNPLFIYGGVGLGKTHLMHAIGHYILHNNPKSQVVYVSSEKFTNELINSIKDDKNVEFRNKYRNIDILLVDDIQFIAGKERTQEEFFHTFNALYEANKQIIISSDRPPKEIPTLEDRLRSRFEWGLIADIQAPDFETRMAILKKKADVEKLNIPNEVMVYIATKIKSNIRELEGALIRIV... | Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. | C1FPH3 |
A4QKP4 | CCSA_CAPBU | Cytochrome c biogenesis protein CcsA | Capsella | MIFSILEHILTHISFSVVSIVLTIYFLTLLVNLDEIIGFFDSSDKGIIITFFCITGLLFTRWIYSGHFPLSNLYESLIFLSWSFSIIHMVSYFNKKQQNHLNAITAPSAIFIQGFATSGLLNKMPQSAILVPALQSQWLMMHVSMMILGYGALLCGSLLSIALLVITFRKVGPTFWKKNIKKKFLLNELFSFDVLYYINERNSILLQQNINFSFSRNYYRYQLIQQLDFWSFRIISLGFIFLTVGILSGAVWANETWGSYWNWDPKETWAFITWTIFAIYLHIKTNRNVRDINSAIVASIGFLLIWICYFGVNLLGIGLH... | Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. | A4QKP4 |
Q6CZ24 | OTNC_PECAS | 3-oxo-tetronate 4-phosphate decarboxylase | Pectobacterium | MSEHHNGTEASLSSEQRARAEMVKLGASFFQRGYATGSAGNLSLLLDDGTLLATPTGSCLGELDAERLSKVSLSGEWISGDKPSKEVSFHLSIYRNDPECKAIVHLHSTYLTALSCLEGLDTQDAIKPFTPYVVMRVGKVPVVPYYRPGDARLGEDLAKLASRYKAFLLANHGPVVTGKNLRAAADNMEELEETAKLIFILGDRKIRYLTADDIAELS | Catalyzes the decarboxylation of 3-oxo-tetronate 4-phosphate to dihydroxyacetone phosphate (DHAP) and CO(2). | Q6CZ24 |
Q1LU10 | TAL_BAUCH | Transaldolase | Candidatus Baumannia | MNQLESLKQFTTIVADSGDIELIRHYTPQDTTTNPSLILKATSLSYYQNMLEDVLAYARKQSGNHNAKMRAASDKLAVNIGLEILKIIPGRISTEIDARFSFNSDMCINHAHKIVSLYQEQGINKSRVLIKLASTWEGIKAAEELEKAGINCNLTLIFSFAQARACAEANVYLISPFVGRIYDWYNQRKLLTEDSYDREDPGVKSVHKIYDYYKQHRYQTIVMGASFRKIDQILALAGCDYLTISPVLLEKLRSSYQHVERQLFPATKFFHKPIPLSESQFRWEHNQDAMAVDQLADGIRKFALDQYNIEKILAKKL | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | Q1LU10 |
Q8DV70 | NAGB_STRMU | Glucosamine-6-phosphate isomerase | Streptococcus | MKTIKVKNKTEGSKVAFRMLEEEITFGAKTLGLATGSTPLELYKEIRESHLDFSDMVSINLDEYVGLSADDKQSYAYFMKQNLFAAKPFKKSYLPNGLAADLAKETEYYDQILAQYPIDLQILGIGRNAHIGFNEPGTAFSSQTHLVDLTPSTIAANSRFFEKAEDVPKQAISMGLASIMSAKMILLMAFGEEKAEAVAAMVKGPVTEEIPASILQTHPKVILIVDEKAGAGI | Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. | Q8DV70 |
Q4KHG0 | ACCA_PSEF5 | Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha | Pseudomonas | MNPNFLDFEQPIADLQAKIEELRLVGNDNSLNIGDEISRLQDKSNTLTEDIFGKLTSWQIARLARHPRRPYTLDYIQHIFTEFDELHGDRHFSDDAAIVGGVARLDEQPVMIIGHQKGREVREKVRRNFGMPRPEGYRKACRLMEMAERFKMPILTFIDTPGAYPGIDAEERNQSEAIAWNLRVMARLKTPIIATVIGEGGSGGALAIGVCDQLNMLQYSTYAVISPEGCASILWKTSEKAADAAEAMGITAERLKGLGIVDKVIGEPLGGAHRDPAAAAASIRAELSTQLAMLKEMDNDTLLARRYDRLMSYGL | 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. | Q4KHG0 |
Q2J764 | RECA_FRACC | Recombinase A | Frankia | MAGLDREKALDNALAQIDKQFGKGSVMRLGDDTRPPVQAIPTGSIALDVALGIGGLPRGRIIEIYGPESSGKTTVALHAVANAQAAGGIAAFIDAEHALDPEYAGKLGVDTDGLLVSQPDTGEQALEIADMLVRSGALDIIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKMTAALANSGTTAIFINQLREKIGVMFGSPETTTGGKALKFYASVRLDVRRIETLKDGTEAVGNRTRVKVVKNKVAPPFRTAEFDIVYGGGISREGSLIDMGVEHGIIRKSGAWYTYDGDQLGQGKENARSFLRDNPDLANEIE... | 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. | Q2J764 |
Q9LSD0 | RIR2C_ARATH | Ribonucleotide reductase small subunit C | Arabidopsis | MPSMPEEPLLTPTPDRFCMFPIHYPQIWEMYKKAEASFWTAEEVDLSQDNRDWENSLNDGERHFIKHVLAFFAASDGIVLENLASRFMSDVQVSEARAFYGFQIAIENIHSEMYSLLLDTYIKDNKERDHLFRAIETIPCVAKKAQWAMKWIDGSQTFAERIIAFACVEGIFFSGSFCSIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYTLLKTKLSEERVKSIVCDAVEIEREFVCDALPCALVGMNRDLMSQYIEFVADRLLGALGYGKVYGVTNPFDWMELISLQGKTNFFEKRVGDYQKASVMSSVNGNGA... | Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Involved in DNA damage repair and programmed cell death inhibition. | Q9LSD0 |
P0C632 | ISPH_CAMJE | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | Campylobacter | MIIELAKNYGFCFGVKRAIKKAEQIKDAATIGPLIHNNEEISRLQKNFNVKTLENIQALSNEKKAIIRTHGITKQDLEELRKKDIEIFDATCPFVTKPQQICEQMSKEGYEVVIFGDENHPEVKGVKSYVSTKAYVVLDKKELQNIKLPNKIAVVSQTTKKPEHFMEIVNFLILKTKEVRVFNTICDATFKNQDAIKELSLKSDVMVVVGGKNSANTKQLFLIAKTNCEDSYLIETEEELKKEWFLDKKHCGISAGASTPDWIIQKVIAKIENFRIN | Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. | P0C632 |
Q2JHG9 | YCF4_SYNJB | Photosystem I assembly protein Ycf4 | unclassified Synechococcus | MSAIVPEIRSADLLRYTVIGSRRPSVYFWAVALTGGGLGFTLAGLSSYLHRNLLPFSDPASLVFIPQGIAMLFYGVLGSLAGLYQWLSLYWNLGGGYNEFDRRTQKITLVRQGFPGKNREVRLEYDFADVQSLRVELREGLNPRRAIYLRVKGRGDIPLTGVGQPPPLTEIENQAAEIARFLNVSLEGI | Seems to be required for the assembly of the photosystem I complex. | Q2JHG9 |
Q31VY9 | FMT_SHIBS | Methionyl-tRNA formyltransferase | Shigella | MSESLRIIFAGTPDFAARHLDALLSSGHNVVGVFTQPDRPAGRGKKLMPSPVKVLAEEKGLPVFQPVSLRPQENQQLVADLQADVMVVVAYGLILPKAVLEMPRLGCINVHGSLLPRWRGAAPIQRSLWAGDAETGVTIMQMDVGLDTGDMLYKLSCPITAEDTSGTLYDKLAELGPQGLITTLKQLADGTAKPEVQDETLVTYAEKLSKEEARIDWSLSAAQLERYIRAFNPWPMSWLEIERQPVKVWKASVIDTATNAAPGTILEANKQGIQVATGDGILNLLSLQPAGKKAMSAQDLLNSRREWFVPGNRLA | 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. | Q31VY9 |
Q2YWT8 | MNHE1_STAAB | Mnh complex subunit E1 | Staphylococcus | MAVQLVLNFIIAVFWLFVTNSYTTNNFVLGFIFGLVLVYLLHRVLPGRFYVITLYRIIKLIIIFLIELIKANFDVLKIIIKPSIKNEPGFFVYHTDLKKDWQIVLLSNLITLTPGTVVLGVSDDRTKIYIHAIDFSTKEQEVESIKTSLEKIVREVGEI | Mnh complex is a Na(+)/H(+) antiporter involved in Na(+) excretion. | Q2YWT8 |
Q7UCG7 | SOTB_SHIFL | Probable sugar efflux transporter | Shigella | MTTNTVSRKVAWLRVVTLAVAAFIFNTTEFVPVGLLSDIAQSFHMQTAQVGIMLTIYAWVVALMSLPFMLMTSQVERRKLLICLFVVFIASHVLSFLSWSFTVLVISRIGVAFAHAIFWSITASLAIRMAPAGKRAQALSLIATGTALAMVLGLPLGRIVGQYFGWRMTFFAIGIGALVTLLCLIKLLPLLPSEHSGSLKSLPLLFRRPALMSIYLLTVVVVTAHYTAYSYIEPFVQNIAGFSANFATALLLLLGGAGIIGSVIFGKLGNQYASALVSTAIALLLVCLALLLPAANSEIHLGVLSIFWGIAMMIIGLGMQ... | Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites. | Q7UCG7 |
Q52472 | FCDH_PSESP | L-fucose dehydrogenase | Pseudomonas | MSSTEPAAAAAGLAIPALGYGAANVGNLFRALSDDEAWAVLEAAWDAGIRYYDTAPHYGLGLSEKRLGAFLQTKPRDEFVVSTKAGRLLRPNPERRPSGLDTDNDFHVPDDLRREWDFTEQGIRASIAESQERLGLDRIDLLYLHDPERHDLDLALASAFPALEKVRAEGVVKAIGIGSMVSDALTRAVREADLDLIMVAGRYTLLEQPAATEVLPACAENATGIVAASVFNSGLLAQSEPKRDGRYEYGQLPDELWDRLVRIAAICRNHDVPLPAAAIQFPLQSALVRSVVVGGSRPAQLTQNAEYAALEIPAGLWAEL... | Catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). Also active against L-galactose and, to a much lesser degree, D-arabinose. Uses NADP(+) as a hydrogen acceptor much more efficiently than NAD(+). | Q52472 |
P08077 | STRA_STRGR | Streptomycin 6-phosphotransferase | Streptomyces | MSSSDHIHVPDGLAESYSRSGGEEGRAWIAGLPALVARCVDRWELKRDGGVRSGEASLVVPVLRADGTRAALKLQMPREETTAALIGLRAWGGDGMVRLLDHDEESSTMLLERLDGSRTLASVEDDDEAMGVLAGLLNRLHSVPAPPGLRGLGEIAGAMVEEVPSAVDSLADPEDRSRLRGWASAVAELVGEPGDRVLHWDLHYENVLAAEREPWLAIDPEPLVGDPGFDLWPALDTGWERIEATGDARRVVRRRFDLLTESLELDRGRAAGWTLARLLQNTLWDIEDGLTAIAPSQIAVAEALAKP | The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation. | P08077 |
Q9BH41 | FAD9_ACHDO | Delta-9 desaturase 3 | Acheta | MAPNITSAPTGVLFEGDTIGPAAKDQQAEVNAPEAKKPREPYRRQIVWRNVILFIYLHLAALYGAYLAFTSAKIATTIFAIILYQVSGVGITGGAHRLWAHRSYKAKWPLRVILMLCNTLAFQNHIYEWARDHRVHHKFSETDADPHNATRGFFFSHVGWLLVRKHPDVKEKGKGIDMHDLEQDKIVMFQKKYYLILMPIVCFLIPTTIPVYMWNETWSNAWFVATLFRYTFTLNMTWLVNSAAHMWGSQPYDKYINPAENLGVALGAMGEGWHNYHHVFPWDYKAAELGNYRANFTTAFIDFFARIGWAYDLKTVPVSM... | Catalyzes the formation of a Delta9 double bond, acting on saturated fatty acyl subtrates like palmitoyl-CoA (hexadecanoyl-CoA) and stearoyl-CoA (octadecanoyl-CoA) with higher desaturation activity on octadecanoyl-CoA than hexadecanoyl-CoA. | Q9BH41 |
P0AB69 | PNTB_ECO57 | Pyridine nucleotide transhydrogenase subunit beta | Escherichia | MSGGLVTAAYIVAAILFIFSLAGLSKHETSRQGNNFGIAGMAIALIATIFGPDTGNVGWILLAMVIGGAIGIRLAKKVEMTEMPELVAILHSFVGLAAVLVGFNSYLHHDAGMAPILVNIHLTEVFLGIFIGAVTFTGSVVAFGKLCGKISSKPLMLPNRHKMNLAALVVSFLLLIVFVRTDSVGLQVLALLIMTAIALVFGWHLVASIGGADMPVVVSMLNSYSGWAAAAAGFMLSNDLLIVTGALVGSSGAILSYIMCKAMNRSFISVIAGGFGTDGSSTGDDQEVGEHREITAEETAELLKNSHSVIITPGYGMAVA... | The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. | P0AB69 |
O67045 | ISCU_AQUAE | Sulfur acceptor protein IscU | Aquifex | MSFEYNEKVLDHFLNPRNVGVLEDANGVGQCGNPACGDAMLFTIKVNPENDVIEDVRFKTFGCGSAIAVSSMLTEMVKGKPIQYALNLTYKDIFEELGGLPPQKIHCTNLGLETLHVAIKDYLMKQGRVEEASKIPDCYEEEEEQEESKEFEFLSGT | A scaffold on which IscS assembles Fe-S clusters. Subsequently gives the nascent cluster to other proteins. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters (Probable). | O67045 |
Q73DA4 | KDPA_BACC1 | Potassium-translocating ATPase A chain | Bacillus cereus group | MIWVAVVITMLLFILVAKPTGIYLEKAFQGSKKLDKVFGPFEKLIFKITGVKEYNQTWKQYALSLVLLNGFMIVVVYFVFRLQGVLPLNPANIKGMEPTLAFNTAISFMADTNLQHYSGENGLSYLSQLIGITFLMFAAPATTLALVMAFIRGLAGKELGNFFVDFTRALTRVFLPIAFMAALVFVALGVPQTLDGVVTAQTIDGAKQSILRGPVASFVSIKELGNNGGGFFGANSTHPFENPGQMSNILQMMLMMLLPTALPFTYGRMVGNKKQGRILFVSLFMVFLLGFITITTSELNGNPVLNGMGIEHVQGSTEGK... | Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunne... | Q73DA4 |
Q4G075 | ILEUA_RAT | Serpin B1a | Rattus | MEQLSSANSLFALELFHTLSESSPTGNIFFSPFSISSALAMVFLGTKGTTAAQLSKTFHFDSVEDVHSRFQSLNAEVSKRGASHTLKLANRLYGEKTYNFLPEFLTSTQKMYGADLAPVDFQHASEDARKEINQWVKGQTEGKIPELLAVGVVDSMTKLVLVNAIYFKGMWEEKFMKQDTTDAPFRLNKKNTKSVKMMYQKKKFFFGYISDLKCKVLEMPYQGGELSMVILLPEDIEDESTGLKKIEEQITLEKLREWTKRENLENIDVHVKLPRFKIEESYILNSNLGRLGLQDLFNSSKADLSGMSGSRDLFISKIVH... | Regulates the activity of the neutrophil proteases. | Q4G075 |
A5IM09 | TRUA_THEP1 | tRNA-uridine isomerase I | Thermotoga | MKRVAAVIEYDGSNFFGYQGQPDVRTVQGVIEDALERIFKQRIYIQAAGRTDTGVHANGQLIAFNCPNDRMTTEDIRNAMNANLPDDVYVKEVFEVPVNFHPRFDVTKRIYHYFILTSRQKNVFLRKYVWWFPYELDLDAMRKAVKYLEGTHDFTSFKTGSDERDPVRTIYRIRILRLKNDLVLIRVEGRSFLRRMVRNIVAALVKVGLKQWEPEKMKEVLEARDRSAAAGTAPAHGLYFYKVLF | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | A5IM09 |
P0A9H8 | CFA_ECOL6 | Cyclopropane-fatty-acyl-phospholipid synthase | Escherichia | MSSSCIEEVSVPDDNWYRIANELLSRAGIAINGSAPADIRVKNPDFFKRVLQEGSLGLGESYMDGWWECDRLDMFFSKVLRAGLENQLPHHFKDTLRIAGARLFNLQSKKRAWIVGKEHYDLGNDLFSRMLDPFMQYSCAYWKDADNLESAQQAKLKMICEKLQLKPGMRVLDIGCGWGGLAHYMASNYDVSVVGVTISAEQQKMAQERCEGLDVTILLQDYRDLNDQFDRIVSVGMFEHVGPKNYDTYFAVVDRNLKPEGIFLLHTIGSKKTDLNVDPWINKYIFPNGCLPSVRQIAQSSEPHFVMEDWHNFGADYDTT... | Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge. | P0A9H8 |
Q055U6 | GATB_LEPBL | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B | Leptospira | MAEFETIIGLEVHAQLNTESKIFSTSATKFGSPPNSQTNPVCLGLPGALPVLNESALEKAIMAGIAFGCDISLFTKFDRKNYFYPDLPKGYQISQFDKPICTGGGVTFTIKGEESSRYVRLTRIHMEEDAGKLIHSADPNIPQSYVDLNRAGTPLIEIVSEPDMRSSDEAYYYLNSLKSILKYIRVSDCNMEEGSLRCDANVSIRPKGSDKFGTRVEIKNLNSFKAVKAAIDYEVEWQTEMALEGKTFQQQTKLWDSVANKTVTMRTKEMSHDYRYFPDPDLPVIILQKETVESVRSKLPELPNERKNRFVEKLGLPKYD... | 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 ... | Q055U6 |
Q8C1Y8 | CCZ1_MOUSE | Vacuolar fusion protein CCZ1 homolog | Mus | MAAAAAGPGAWAAQEKQFPPALLSFFIYNPRFGPREGEEENKILFYHPNEVEKNEKIRNVGLCEAIVQFTRTFSPSKPAKSLHTQKNRQFFNEPEENFWMVMVVRNPIIEKQSKDGKAVVEYQEEELLDKVYSSVLQQCYSMYKLFNGTFLKAMEDGGVKLLKERLEKFFHRYLQTLHLQSCDLLDIFGGISFFPLDKMTYLKIQSFINRMEESLSVVKYTAFLYNDQLIWSGLEQDDMRILYKYLTTSLFPRHIEPELAGRDSPVRAEMPGNLQHYGRFLTGPLNLNDPEAKCRFPKIFVNTDDTYEELHLIVYKAMSA... | Acts in concert with MON1A, as a guanine exchange factor (GEF) for RAB7, promotes the exchange of GDP to GTP, converting it from an inactive GDP-bound form into an active GTP-bound form. | Q8C1Y8 |
Q9W1N6 | GR59E_DROME | Putative gustatory receptor 59e | Sophophora | MDSSYWENLLLTINRFLGVYPSGRVGVLRWLHTLWSLFLLMYIWTGSIVKCLEFTVEIPTIEKLLYLMEFPGNMATIAILVYYAVLNRPLAHGAELQIERIITGLKGKAKRLVYKRHGQRTLHLMATTLVFHGLCVLVDVVNYDFEFWTTWSSNSVYNLPGLMMSLGVLQYAQPVHFLWLVMDQMRMCLKELKLLQRPPQGSTKLDACYESAFAVLVDAGGGSALMIEEMRYTCNLIEQVHSQFLLRFGLYLVLNLLNSLVSICVELYLIFNFFETPLWEESVLLVYRLLWLAMHGGRIWFILSVNEQILEQKCNLCQLL... | Probable gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. | Q9W1N6 |
P10893 | HBB_LUTLU | Hemoglobin beta chain | Lutra | VHLTGEEKAAVTSLWGKVNVDEVGGEALGRLLVVYPWTQRFFDSFGDLSSPDAVMGNPKVKAHGKKVLNSFSEGLKNLDNLKGTFAKLSELHCDKLHVDPENFKLLGNVLVCVLAHHFGKEFTPQVQAAYQKVVAGVANALAHKYH | Involved in oxygen transport from the lung to the various peripheral tissues. | P10893 |
A0RP87 | MURG_CAMFF | Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase | Campylobacter | MIAITGGGTGGHLAIAKALAIELKNRGENVIFIGSNSGQDRMWFEHSDIFKFKYFFPSRGVVNKKGIHKLFALLNIIKLAFKCRCIFTEHNISSVISVGGYSSAPASFGAVIFRKKLFIHEQNAIKGKLNSILKPFCKKFFSSYGTDTYDYPIDIKFFNTARVRNELKTILFLGGSQGASFINSLALNLALNLKNHNINIIHQCGAKELETTRSKYNEMGVEAVVFDFSNEIEVYMQKSDLCISRAGASTLWELCANALPTIFIPYPYAASNHQFYNAKFLLDSNLAKIYEQNGLDKNILFTDIMNLDINSISMGLRNIV... | Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). | A0RP87 |
Q0ICR0 | PSBM_SYNS3 | Photosystem II reaction center protein M | unclassified Synechococcus | METNDLGFVASLMFVLVPTVFLIVLFIQTNSREGSS | 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... | Q0ICR0 |
B7LLX4 | ULAG_ESCF3 | L-ascorbate utilization protein G | Escherichia | MSKVKSITRESWILSTFPEWGSWLNEEIEQEQVAPGTFAMWWLGCTGIWLKSEGGTNVCVDFWCGTGKQSHGNPLMKAGHQMQRMAGVKKLQPNLRTTPFVLDPFAIRQIDAVLATHDHNDHIDVNVAAAVMQNCADDVPFIGPKTCVDLWIGWGVPKERCIVVKPGDVVKVKDIEIHALDAFDRTALITLPAEQKAAGVLPDGMDERAVNYLFKTPGGTLYHSGDSHYSNYYAKHGNEHQIDVALGSYGENPRGITDKMTSADILRMAEALNTKVVIPFHHDIWSNFQADPQEIRVLWEMKKDRLKYGFKPFIWQVGGK... | Probably catalyzes the hydrolysis of L-ascorbate-6-P into 3-keto-L-gulonate-6-P. Is essential for L-ascorbate utilization under anaerobic conditions. | B7LLX4 |
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