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 |
|---|---|---|---|---|---|---|
Q92GB7 | DPO1_RICCN | DNA polymerase I | spotted fever group | MTQKNTLLLIDGYGFVFRAYYAQQPLTSPKGEPVGALYGFTSMLLKLLSDFKPKHVAVVFDSGGKNFRHQIYPDYKANRPPPPEDLIIQLPLVRDVASNLNFPILEKNGYEADDIIATFATKTAALGAHVVIISSDKDLLQLMTENIKIYDPLKGKYITEDDVVKKFGTTSDKLREVMALIGDRSDNIPGVPSIGPKTASSLITQFGSVENIFNSLDQVSSVKQRETLQNSREAALISWQLIGLNSNVDLDFQLNNLEWSPPNSDKLTGFLQEYGFRSLYKRVENLLDIKINDHKEIADSKVTEIKELNNANELADFAKE... | In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. | Q92GB7 |
P75536 | UNG_MYCPN | Uracil-DNA glycosylase | Mycoplasma | MEQLLDQFLSGVLSEWKAFILQEAKQTYFQELLAKLKNVEQELTPKASQVFRPFSFFAPNNTKLIIYGQDPYPNPQHACGLSFASNAPKLPQSLKRMILRLQQEYPELAGQNHWTKQLLEGWAQQGILLLNGVFTTNAFQTNAHRNWGWEQFNCHLLDFLLSQKLYVLLVFLGKQTENFVLKKIGGASQFASLSYPHPSPLTGRKFFDHPDALFKQINQWLKHHNHTPIDWTNGQVQYQF | Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | P75536 |
P31126 | YDEE_ECOLI | Uncharacterized MFS-type transporter YdeE | Escherichia | MNLSLRRSTSALLASSLLLTIGRGATLPFMTIYLSRQYSLSVDLIGYAMTIALTIGVVFSLGFGILADKFDKKRYMLLAITAFASGFIAITLVNNVTLVVLFFALINCAYSVFATVLKAWFADNLSSTSKTKIFSINYTMLNIGWTIGPPLGTLLVMQSINLPFWLAAICSAFPMLFIQIWVKRSEKIIATETGSVWSPKVLLQDKALLWFTCSGFLASFVSGAFASCISQYVMVIADGDFAEKVVAVVLPVNAAMVVTLQYSVGRRLNPANIRALMTAGTLCFVIGLVGFIFSGNSLLLWGMSAAVFTVGEIIYAPGEY... | A transporter able to export peptides. When overexpressed, allows cells deleted for multiple peptidases (pepA, pepB, pepD and pepN) to grow in the presence of dipeptides Ala-Gln or Gly-Tyr which otherwise inhibit growth . Cells overexpressing this protein have decreased intracellular levels of Ala-Gln dipeptide, and in... | P31126 |
B8DP96 | GCSPA_DESVM | Glycine dehydrogenase (aminomethyl-transferring) subunit 1 | Desulfovibrio | MPFIPHSPEEVREMLSVIGVQSIEDLFVDIPAEMRPRSFELPLGLSEMQVLAKMEEMAARNRTDVVSFLGGGFYSHHIPAAVDALVSRGEFYTAYTPYQPEASQGTLQAIFEYQTAVCRLLDMDCANASVYDGGSAIFEAMMMAVRATKRRKLVIDEAVSPIWRTMLASYTSNLSLDLVTVPQVDGRSDMAAMKAAVDTGCAAVVVQNPNFFGVVEDFTDLFAHAKSQKAASVISVYPVMQSVLKTPGEMGADIAVAEGQSLGQPLSFGGPYLGIMTCTKDMVRQMPGRIVGRTNDTEGRTGYVLTLQAREQHIRRAKAT... | 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. | B8DP96 |
A6U619 | CHED_SINMW | Probable chemoreceptor glutamine deamidase CheD | Sinorhizobium | MNTEAAGKRVHVIQGEFKVVNDPHIVLSTILGSCVAACLRDPVTGVGGMNHFLLPGSASSPSSGADATRYGVHLMELLINGLLKQGARRDRLEAKIFGGARTIARFSNVGEQNAAFARRFLMDEGIRIVGESTGGDHGRKLEYWPSSGRARQYALTGVEAQRAMQMDQRPAAPKPVESSIEFF | Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis. | A6U619 |
Q65RX8 | RSMH_MANSM | rRNA (cytosine-N(4)-)-methyltransferase RsmH | Basfia | MSEQNTFSSPEHITVLLHEAVDGLALKDKGIYIDGTFGRGGHSRLILSKLTENGRLIAIDRDPRAIAAAEEIQDSRFHIEHNSFSAIPYICEKLGLVGKIDGILLDLGVSSPQLDDAERGFSFMKDGPLDMRMDTSKGLSAAQWLQQVTEEDLAWVLKTFGEERFAKRIAHAIVNYNKSAVQNGTEPLTRTLPLAELIAQAVPFKDKHKHPATRSFQAIRIFINSELDELESVLHSALTVLAPEGRLSVISFHSLEDRMVKHFMRKQSKGESIPKGLPLREDQINRNRTLKVIGKAIQPKESEVFANPRSRSAVLRVAER... | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | Q65RX8 |
Q83AV6 | ENGB_COXBU | Probable GTP-binding protein EngB | Coxiella | MTEFKSAPAYQEAKYLTSAAEFDQLPPDQGAEIAFIGRSNAGKSSALNIITGIKGLARTSKTPGRTQMINFFALNEHERLVDLPGYGYAKVPRMVQKRWEELVDSYLKNRRCLKGLVVVMDIRHPLKEMDEDVIEWAVNYDIPIHILLTKSDKLSQNAAKKTLGEVQTAISAYGEKLTLQLFSSHDRTGLDEVKAVLSQWFRSEP | Necessary for normal cell division and for the maintenance of normal septation. | Q83AV6 |
Q8EPZ2 | END4_OCEIH | Endonuclease IV | Oceanobacillus | MVKIGSHVSMNGKKMLLGSSEDAVQYGANTFMIYTGAPQNTRRKPIEELNIEAGTEHMKANGIQDIVVHAPYIINIGNSIKPATFELGVNFLKNEIDRTEALGAKQIVLHPGAHVGEGAEKGIPKIIEGLNEVLDPNSNVQIALETMAGKGSEIGRTFEELAQIIEGVTHNDRLSICMDTCHIHDAGYNIVEDFDGVLEQFDKIIGIDRLKVVHVNDSKNERGAHKDRHENIGFGYIGFEALHNIVHHPQLSDLPKILETPFVGTDKKNKKPPYKHEIEMLKEGNFDPHLKEKIMEA | Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. | Q8EPZ2 |
O59837 | TBB_PHYCI | Beta-tubulin | Phytophthora | MRELVHIQGGQCGNQIGAKFWEVISDEHGVDPTGSYHGDSDLQLERINVYYNEATGGRYVPRAILMDLEPGTMDSVRAGPYGQLFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKIREEYPDRIMCTYSVCPSPKVSDTVVEPYNATLSVHQLVENADEVMCLDNEALYDICFRTLKLTNPTYGDLNHLVCAAMSGITTCLRFPGQLNSVLKLFAVNLIPFPRLHFFMIGFAPLTSRGSQQYRALTVPELTQQQFDAKNMMCAADPRHGRYLTAACMFRGR... | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-... | O59837 |
A0JPI4 | GP3LB_XENLA | Golgi phosphoprotein 3-like B | Xenopus | MTTLIRRGRRAEEGQERRADSEDSIKDKDEEDSADSKEIRLTLMEEVLLLGLKDKEGYTSFWNDCISSGLRGGILIELFLRGRVVLEPATIRKKRLTDKKVLLKSDKLTGDVLLDETIKHMKATEPAETVQSWIELLTGETWNPFKLQYQLRNVRERIAKNLVEKGILTTEKQNFLLFDMTTHPVTNTTEKQRLVKKLQESLLEKWVNDPHRMDKRTLALLVLAHSSDVLENAFSSLSDEKYDMAMIRSKELLDLEPDTEGTKPNACEMIWAVLSAFNKS | Phosphatidylinositol-4-phosphate-binding protein that may play a role in the process of vesicle budding at the Golgi and anterograde transport to the plasma membrane. | A0JPI4 |
A4RK96 | YAE1_MAGO7 | Protein YAE1 | Pyricularia | MHMNPTPLPHSEDDGVMFASIGQTTLALTEPPSALHATDTLDDVFGSEDVQGSTSFTTEPSDMRRLQSEHTTAGYREGVTVAKAASVQAGFDEGFGLGATLGLSAGEIVGVLEGLAAAVPGDERLAALLGEARGDFSARSIFGATYWDPNGTWTYPVPGQDGGDVIFRDVVEAHPLIAKWRVVLNEQIQNWGVRCDFFAEDQVVDEEVVSQKKLGNPATALKAATSTAPATQSRMSDALQW | The complex LTO1:YAE1 may function as a target specific adapter that probably recruits apo-RPLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation. | A4RK96 |
Q9RUS2 | RECX_DEIRA | Regulatory protein RecX | Deinococcus | MPVCGRRPWQVKRSSSGGILPVMYRPRRRSSTPASEGEAEPRPRRPKTREEQREALLAYAFRALGARAITEAELRGKLERRSEDPELVEEVLRRVQELGYQNDAEVARAENKRRGVGELRVRQTLRRRGLGADLIEETLQARDPEEEQQQAIDLLTKRWPALSRKRDPRASAYAFLARRGFGGSVIWPAIREVAELFPPDEAEE | Modulates RecA activity. | Q9RUS2 |
Q73PM9 | RL2_TREDE | 50S ribosomal protein L2 | Treponema | MALKEYKPMTPGLRGRIDLRKDEITAQKPEKSLTTGKKNRAGRDSRGRISVRGQGGGHKQKYRQIDFKRNKYGIPGTVRTIEYDPNRSANIALIFYADGEKRYIIAPKGLKIGQKIMSGEMATLDVANALPLEAIPVGFTVHNIELTIGRGGQMARSAGAGALVAAKEGEYVTIRLPSGETRLVNKKCYATIGEVGNEDHMNTSLGKAGRSRWLGIRPTVRGMAMNPIDHPLGGGEGRGKGRHPVTPWGQPCKGYKTRKKRNPSDSFIVSRRKKKN | One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. | Q73PM9 |
Q8ESL6 | NAGB_OCEIH | Glucosamine-6-phosphate isomerase | Oceanobacillus | MKIIQTENYQSMSKLASQHVINTIKQLNKPVLGLATGSTPEGLYQHLIKAYRMHQISFANVSTFNLDEYVGLHKEDKNSYHYYMQKFLFNHVDIPYKNIHLPNGIAKDLSVECTSYEDRIQQAGGIHIQVLGIGRNGHIGFNEPGTSFESQTHVVDLDESTRNANARFFDSIDEVPNQAITMGIQSIMRAKEILLLVSGSEKAEALEKLVNGNVSEEFPASILQTHQNVKIIADKAALQDISYHHFSETM | Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. | Q8ESL6 |
A1RRV7 | TRUD_PYRIL | tRNA-uridine isomerase D | Pyrobaculum | MIEAPPFDKSLGMLYYVTDTCPAGGVIKARPEDFIVEEVLKDGTVVALTGISLKPRVGSWTWIHVVKKNTDTLKLLLYLAKTLGLKARDISIGGIKDTRAVTSQIISIRGDVTNLPKIRNVEFLSFWPMDKPITPSLIYGNRFTITLRNVEKVDCAEATLKTLQYIALPNYYGYQRFGTIRPVSHLLGKALVKKDAEEFFDIMFCKIFAYESDVAKKAREAACKGDYRRALEIFPKRFIEERAVLRGLLRGLDLWNAIMSIPIQILRIYVEALQSYLFNLFLSKRMELGPLNRPIEGDLVEINGQVVHYAEGLGGEVVLP... | Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | A1RRV7 |
Q6APZ3 | LGT_DESPS | Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase | Desulfotalea | MSYYTLPPIDPIIMSLGPISIRWYGLMYVIGFFATYFLVRQQIQRHQFTQLEKNFDNLNTVLILCVILGGRLGYVVFYNLSYYLQHPLEILATWHGGMSFHGACIALILGGLIFCKIKKIDFWATADVYVATIPIGLGLGRIGNLINGELYGRVTEQPWGIIFPNGGPLPRHASQLYESLLEGLILFIILWSLRNRPWKRNSLTPHGTILSLFLCLYGLFRIIIENFRQPDPQLGFIVAHITMGQLLSGAMILCGLTLWFWRIHQKKRATAL | Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins. | Q6APZ3 |
Q6G0D5 | EX7S_BARQU | Exodeoxyribonuclease VII small subunit | Bartonella | MKQEIQTGDITALSFEQALKQLEVIVENLERGDVPLEQSIDIYERGEALRKHCDRLLKAAEAKVEKIQLSEEGSPKGVEPLDSK | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. | Q6G0D5 |
P18847 | ATF3_HUMAN | Activating transcription factor 3 | Homo | MMLQHPGQVSASEVSASAIVPCLSPPGSLVFEDFANLTPFVKEELRFAIQNKHLCHRMSSALESVTVSDRPLGVSITKAEVAPEEDERKKRRRERNKIAAAKCRNKKKEKTECLQKESEKLESVNAELKAQIEELKNEKQHLIYMLNLHRPTCIVRAQNGRTPEDERNLFIQQIKEGTLQS | Stress-induced isoform, counteracts the transcriptional repression of isoform 1. | P18847 |
P25116 | PAR1_HUMAN | Thrombin receptor | Homo | MGPRRLLLVAACFSLCGPLLSARTRARRPESKATNATLDPRSFLLRNPNDKYEPFWEDEEKNESGLTEYRLVSINKSSPLQKQLPAFISEDASGYLTSSWLTLFVPSVYTGVFVVSLPLNIMAIVVFILKMKVKKPAVVYMLHLATADVLFVSVLPFKISYYFSGSDWQFGSELCRFVTAAFYCNMYASILLMTVISIDRFLAVVYPMQSLSWRTLGRASFTCLAIWALAIAGVVPLLLKEQTIQVPGLNITTCHDVLNETLLEGYYAYYFSAFSAVFFFVPLIISTVCYVSIIRCLSSSAVANRSKKSRALFLSAAVFC... | High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development. | P25116 |
B7LVW4 | RLMM_ESCF3 | 23S rRNA 2'-O-ribose methyltransferase RlmM | Escherichia | MNKVVLLCRPGFEKECAAEITDKAGRQEIFGFARVKENAGYVIYECYQAEDGDKLIRELPFSSLIFARQWFVVGELLQHLPPEDRITPIVGMLQGVVEKGGELRVEVADTNESKELLKFCRKFTVPLRAALRDAGVLANYETPKRPVVHVFFIAPGCCYTGYSYSNNNSPFYMGIPRLKFPADAPSRSTLKLEEAFHVFIPADEWDERLANGMWAVDLGACPGGWTYQLVKRNMWVYSVDNGPMAQSLMDTGQVTWLREDGFKFRPTRNNISWMVCDMVEKPAKVAALMAQWLVNGWCRETIFNLKLPMKKRYEEVSHNL... | Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA. | B7LVW4 |
Q662I0 | CSRA_BORGP | Translational regulator CsrA | Borreliella | MLVLSRKVNESIKINSDIEVLILEIKKDTVKIAIKAPENIKIFRSEIYKFIIEENKKSILKDKHNISKIKSLFNHYFKNEN | A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'-UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by Fli... | Q662I0 |
B6J5T7 | RPOZ_COXB1 | Transcriptase subunit omega | Coxiella | MARVTVEDCLEHVENRFDLVLKAAKRAHILELGGAEPMVPRDNDKPAVLALREIAAGYDVTREGQEQETEEVDVDRNVLAETAKMNKAVASQKESEV | Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. | B6J5T7 |
Q9T3Y0 | CYB_BEAHI | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Beamys | MTNIRKTHPLMKIINHSFIDLPTPSNISSWWNFGSLLGICLILQIMTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWLIRYLHANGASMFFICLFIHVGRGIYYGSYTYMETWNIGIILLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTSLVEWIWGGFSVDKATLTRFFAFHFILPFIIVALVMVHLLFLHETGSNNPTGLESNADKIPFHPYYTIKDILGAFLLVFFLIFLVLFAPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSVPNKLGGVLALILSILILALLPHLHMSKLRSLMFRPI... | 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... | Q9T3Y0 |
A9NDR7 | IF1_COXBR | Translation initiation factor IF-1 | Coxiella | MAKEESIEMQGTVVDSLPNTTFRVKLENGHVVTAHISGRMRKHYIRILTGDAVTVELTPYDLTRGRIVYREAGKKPPTSKAEE | One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-... | A9NDR7 |
P54981 | CRTI_STRGR | Phytoene desaturase | Streptomyces | MITVKGPVDHVVVVGAGLAGLAAALHLLGAGRRVTVVEREDVPGGRAGLLESGGFRIDTGPTVLTMPDLVEDAFAAVGERMADRLELIRLAPAYRARFADGSQLDVHTDGAAMEAAVEEFAGARQAVGYRRLRIWLERLYRVQMRRFIDTNFDSPLQLAHPDLARLAALGGFGRLDARIGHFVSDERLRRVFSFQALYAGVPPARALAAYAVIAYMDTVAGVYFPRGGMHALPRAMADAASDAGAVLRYGQRVTRLERSGDRVTAVVTDQEHIPCDAVVLTPDLPVSYRLLGRTPHRPLPLRHSPSAVILHTGTDRTWPD... | This enzyme converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene. | P54981 |
B3QRV1 | NDK_CHLT3 | Nucleoside-2-P kinase | Chloroherpeton | MERTLAILKPDCVRKNLIGAAIEKIQSAGFKVVAMKMTRLTKETAGEFYAVHKARPFYGELVEFMSSGACVPLMLEKENAVADFRTLIGATDPAEAAEGTIRKLYADSKGENIVHGSDSVENAKIECGFFFSTQEAVANMA | 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. | B3QRV1 |
Q8LFP7 | NIP12_ARATH | Nodulin-26-like major intrinsic protein 2 | Arabidopsis | MAEISGNGGDARDGAVVVNLKEEDEQQQQQQAIHKPLKKQDSLLSISVPFLQKLMAEVLGTYFLIFAGCAAVAVNTQHDKAVTLPGIAIVWGLTVMVLVYSLGHISGAHFNPAVTIAFASCGRFPLKQVPAYVISQVIGSTLAAATLRLLFGLDQDVCSGKHDVFVGTLPSGSNLQSFVIEFIITFYLMFVISGVATDNRAIGELAGLAVGSTVLLNVIIAGPVSGASMNPGRSLGPAMVYSCYRGLWIYIVSPIVGAVSGAWVYNMVRYTDKPLREITKSGSFLKTVRNGSSR | Water channel probably required to promote glycerol permeability and water transport across cell membranes. | Q8LFP7 |
Q0JC27 | NLP2_ORYSJ | Nodule inception protein-like protein 2 | Oryza sativa | MDMPTPSNRAGCNGNTGGTMGPSDDPYGAAAMNLDCYSEIYSPSVADQLFSLLNDPAAHRMFAMWPSMGSSPCAAGTSEDMPLDAYSGLGEAVEEPSQIMSVNPTEAEKTGKSSGELGSDDGAHQGSSMVPRSVVGSSLADRMLMALSLFRESLGSGALAQVWMPVEQEGHVVLSTCEQPFLLDQVLAGYREVSRHFVFSAKEEPGLQPGLPGRVFISGVPEWTSSVLYYNRPEYLRMEHALHHEIRGSLAMPIYDPSKDSCCAVFELVTRKEKPDFSAEMDNVCNALQAVNLKATKGSSNQKFYTENQKFAFTEILDVL... | Probable transcription factor. | Q0JC27 |
B4T399 | RECX_SALNS | Regulatory protein RecX | Salmonella | MSEPTSSRPAYARLLDRAVRILAVRDHSEQELRRKLSAPVMGKNGPEEIDATADDYERVIAWCHEHHYLDDERFVMRFIASRSRKGYGPARIRQELNQKGISRESTEKTMRECEIDWSEMAREQAVRKYGEPLPSNFSEKVKVQRFLLYRGYLMDDIQQIWRNFAD | Modulates RecA activity. | B4T399 |
Q28990 | OVGP1_PIG | POSP-E3 | Sus | MGKLLLWVGLVLVLKHHNGAAHKLVCYFANWAFSRPGPASILPRDLDPFLCTHLVFAFASMNDSQIVAKDARDESIFYPEFNQLKERNEKLKTLLSIGGWNFGTSRFTTMLSTFTNREKFIRSAIGLLRTHGFDGLDLFFLYPGLRGSPRRDRWNFLFLLEELLLAFRREAQLTMRPRLLLSAAVSADPHVIQKAYDVRLLGRLLDFINVLSYDLHGSWEKVTGHNSPLFSLSDDPKSSAYTMNYWRKLGAPPEKLLMGFPTYGRTFRLLKASKNELGAEAVGPASPGKYTKQAGFLAYYEVCSFVQRAKKRWIDHQYVP... | Binds to oocyte zona pellucida in vivo. May play a role in the fertilization process and/or early embryonic development. | Q28990 |
Q9TIA9 | MATK_ASTLA | Intron maturase | Astrebla | MAKFEGYSEKQKSRQQYFVYPLLFQEYIYAFAHDYVLNGSEPVEIFGCNNKKFSSLLVKRLIIRMYQQNFWINSVNHPNQDRLLDHSNHFYSEFYSQILSEGFAIVVEIPFSLGQLSCPEEKEIPKFQNLRSIHSIFPFLEDKFLHLHYLSHIEIPYPIHFEILVQLLEYRIKDVPSLHLLRFFLNYYSNWNSLITSMKSIFLFSKENKRLSRFLYNSYVSEYEFFLLFLRKQSSCLRLTSSGTFLERIHFSRKMEHFGVMYPGFFRKTIWFFMDPLMHYVRYQRKVILASKGTLLFQKKWKSYLVNFSQYFFSFWTQPQ... | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns. | Q9TIA9 |
Q28EW0 | TM87A_XENTR | Transmembrane protein 87A | Silurana | MAAASFQPLKCLLLWVFFVITPPVKAVPEPGIWTVPIGSGAGSLFFRKTLYNSTNIKVKLISPNCPTPVKLTVKWYLRSHRCYNQFTNLEEVLERHHTNLDTTDNFCKNVSKPDFCDKNEDKNIDCNKDMHALPTLKMSKLVPKISVNQSAGSKNPLNQMDFDIVARTYQDGPYLFVLQVKGDENVKWNLSVTVSMKGPHGFISASDWPLMIFYMVMCIMYILLALLWFIWSACYWKDLLRIQFWIAAVIFLGMLEKAVYYAEYQNTDNTGVSSHGLLIFAELISSIKRTLARLLVTIVSLGYGIIKPRLGAVMHRVVGM... | May be involved in retrograde transport from endosomes to the trans-Golgi network (TGN). | Q28EW0 |
P58640 | PYRF_ECO57 | OMP decarboxylase | Escherichia | MTLTASSSSRAVTNSPVVVALDYHNRDAALAFVDKIDPRDCRLKVGKEMFTLFGPQFVRELQQRGFDIFLDLKFHDIPNTAAHAVAAAADLGVWMVNVHASGGARMMTAAREALVPFGKDAPLLIAVTVLTSMEASDLADLGVTLSPADYAERLAALTQKCGLDGVVCSAQEAVRFKQVFGQEFKLVTPGIRPQGSEAGDQRRIMTPEQALAAGVDYMVIGRPVTQSVDPAQTLKAINASLQRSA | Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). | P58640 |
A1A5R8 | SANBR_RAT | SANT and BTB domain regulator of class switch recombination | Rattus | MSRGCPENNNFLTNNNQMVLDMILYPLIGIPQTINWETVARLVPGLTPKECVKRFDELKSCGSSPVDNQYNPLMAAGEGPVETLATYIKSSLLDAQGDFQETPVDQDTVSKAGRHSIATTRNCSSESENCTARNAGEETGDSEGPNMVIHVCDEAKSLKEDFICPRDLLISEMKYFAEYLSVDAQRWEEVDISVHCDVHIFNWLIKYVKRNTKDSKDCELPALEPGNVISILISSEFLKMDSLVEQCIQYCHKNMNAIVAAPCNMNCINVNLLTRIADLFTHNEIDDLKDKKDKFRSKLFCKKIERLFDPEYFNPDSRNN... | Negatively regulates class switch recombination or isotype switching in splenic B-cells. | A1A5R8 |
A3PBB9 | LIPB_PROM0 | Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase | Prochlorococcus | MDNRTAIIKQPDNISSFHDVYKLQKEYQEALILDNSNPDFIWIGEHQLCYTLGRGSNYDNLLFSLNDAKYDVFKIDRGGEVTCHMPGQLVTYLVLDLKNFNKDLNWYLRKIEEIIIKILGAFNIDCHSRKGFTGVWIGNKKIASIGIGCKKWITINGFSINIDCELENFNKIVPCGIENCLMANMIDYNKNLNIQEVKRIVKKTIEEEFNFDFISK | Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. | A3PBB9 |
B6IMR6 | PLSX_RHOCS | Phosphate-acyl-ACP acyltransferase | Rhodospirillum | MSERFCIALDAMGGDHAPDMVVAGADIARERCPNVDYLFVGDEERIRPLLDKYPALAAVSTVRHTPDAVAGDAKPSVALRTGRNSSMRLAIDAVAAGDAACVVSAGNTGALMAMAKFVLKTLPGIDRPAIASFFPTLRGESVMLDLGANLECDADNLVQFAVMGTVFSRTVLGLLEPTVGLLNVGSEEQKGHGSIRQAASALRASALAKNFRGFVEGNDIAAGTVDVIVTDGFSGNIALKTAEGTAKLYAEFLKRTFKSSLLAKLGYLLAHGAFQKLRLRTDPRRYNGAMFLGLRGVCVKSHGGTDAVGFANAIGVASDL... | Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. | B6IMR6 |
Q59637 | ODP1_PSEAE | Pyruvate dehydrogenase E1 component | Pseudomonas | MQDLDPVETQEWLDALESVLDREGEDRAHYLMTRMGELASRSGTQLPYAITTPYRNTIPVTHEARMPGDLFMERRIRSLVRWNALAMVMRANKHDPDLGGHISTFASSATLYDIGFNYFFQAPTDEHGGDLVFFQGHASPGVYARAFLEGRISEEQLENFRQEVDGNGLSSYPHPWLMPDFWQFPTVSMGLGPIQAIYQARFMKYLESRGFIPAGKQKVWCFMGDGECDEPESLGAISLAGREKLDNLIFVINCNLQRLDGPVRGNAKIIQELEGVFRGAEWNVNKVIWGRFWDPLFAKDTAGLLQQRMDEVIDGEYQNY... | Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | Q59637 |
B2IQS1 | DEF_STRPS | Polypeptide deformylase | Streptococcus | MSAIERITKAAHLIDMNDIIREGNPTLRTVAEEVTFPLSDQEIILGEKMMQFLKHSQDPVMAEKMGLRGGVGLAAPQLDISKRIIAVLVPNIVEEGETPQEAYDLEAIMYNPKIVSHSVQDAALGEGEGCLSVDRNVPGYVVRHARVTVDYFDKDGEKHRIKLKGYNSIVVQHEIDHINGIMFYDRINEKDPFAVKDGLLILE | Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. | B2IQS1 |
P0CN57 | EIF3L_CRYNB | Eukaryotic translation initiation factor 3 subunit L | Cryptococcus neoformans species complex | MADPSAFYEPEEDELLSQLAIPIQNYQPLSEGDEYRRLQQLEQHAYAQQTAMAQEQEMEQLAVLELIPEDVKRFLVMFHQAILENDLPTITSMYESGWNKLTQAHYLNNEWPEAELIAPLVGNDQVFLTLYRELYFRHVYARLQPTIDDRFQSYENICELFNYLLNSEGPVPLDLPIQWLWDMLDEFVYQFTSFSHWRSSPKAKTEEELEMLAESPNIWSSYSVLNVLYSLVQKSQINEQLKAERAGKSVEEVTEVAGEYGSKPLYKNLGYFSLICLLHVHVLLGDPTLALQTMENVDLGNAAFLTRITACHVTTYYHVG... | 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 initiates t... | P0CN57 |
P00452 | RIR1_ECOLI | Ribonucleotide reductase 1 | Escherichia | MNQNLLVTKRDGSTERINLDKIHRVLDWAAEGLHNVSISQVELRSHIQFYDGIKTSDIHETIIKAAADLISRDAPDYQYLAARLAIFHLRKKAYGQFEPPALYDHVVKMVEMGKYDNHLLEDYTEEEFKQMDTFIDHDRDMTFSYAAVKQLEGKYLVQNRVTGEIYESAQFLYILVAACLFSNYPRETRLQYVKRFYDAVSTFKISLPTPIMSGVRTPTRQFSSCVLIECGDSLDSINATSSAIVKYVSQRAGIGINAGRIRALGSPIRGGEAFHTGCIPFYKHFQTAVKSCSQGGVRGGAATLFYPMWHLEVESLLVLK... | Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox-active cysteines. | P00452 |
Q8TVE9 | GGR1_METKA | Geranylgeranyl reductase 1 | Methanopyrus | MEFDVVVVGAGPAGSVAAWAAAEAGCDVLILERKAEIGVPKQCAEGISARALEEVGIRPDDGWIAAEIERGILSLPSGSKFEVEVEGYVLERRVFDKWLVVRAVEAGAEVELLAHARRALLDEGRVVGVEYEGEDGVHEVRARIVIAADGIESRIGRTAGLVPQLEPDHICTCAQYEVVGDRYDPKAFMIHFDPERIPGGYAWVFPKGENRANVGVGIRGSESSPGLALKTLDELVEGPLSELVAGTPVEVNVGGVPVCGPVERTYGDGILLVGDAARQVNPLTGGGLNTALICGRIAGEVAVEAIEEDDTSASFLKRYQ... | Is involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di-O-geranylgeran... | Q8TVE9 |
B1MCH3 | SYDND_MYCA9 | Non-discriminating aspartyl-tRNA synthetase | Mycobacteroides abscessus | MLRTHDAGSLRESNAGQRVTLAGWVARRRDHGGVIFIDLRDASGVAQVVFREDAVLEQAHRLRAEFCVEVSGVVEVRPEGNANDEIATGQIEVNAAELKVLNESAPLPFQLDETAGEEARLRYRYLDLRREGPGNAIRLRSKANAAARSVLSGHEFVEVETPTLTRSTPEGARDFLVPARLQPGSFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDIEMSFVDQDDVIALAEEILVALWDLVGYRVPTPIDRITYAEAMRRYGSDKPDLRFGLELVECTDYFSETSFRVFQAPYVGAVVMPGGA... | Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn). | B1MCH3 |
Q56572 | FLAB_VIBAN | Flagellin B | Vibrio | MAINVSTNVSAMTAQRYLNNAADGTQKSMERLSSGYKINSARDDAAGLQISNRLTSQSRGLDMAVRNANDGISIAQTAEGAMNETTNILQRMRDLSLQSANGSNSSSERQAIQEEVSALNDELNRIAETTSFGGNKLLNGSFGNKSFQIGADSGEAVMLSMSDMRSDTKAMGGKSYVATNGKAPDWSVTNATDLTLSYTDKQGEAREVTINAKAGDDLEEVATYINGQNGDIKASVGDEGKLQLFAANQKVSSDVTIGGGLGTEIGFAAGKDVTVKDINVTTVGGSQEAVALIDGALKAVDSQRASLGAFQNRFGHAISN... | Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. FlaB is not essential for flagellar synthesis and motility. | Q56572 |
Q1IQ75 | Y1974_KORVE | Nucleoid-associated protein Acid345_1974 | Candidatus Koribacter | MGGFNLNEMMAAAKQHAEELQKKMAQTVIEATAGGGSVTVKMNGQKQLLSIKIDPEVVKSGDVEMLQDLVTAAVNEGSRRVDQAMQSNLSGMMGGMGLPGF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q1IQ75 |
B9KIR2 | GATA_ANAMF | Glutamyl-tRNA(Gln) amidotransferase subunit A | Anaplasma | MKRELLKLSILEAHRCLKNKDFSARELTEAYIGAVEQDTLNAFVTTTPELALAAADRTDGLLQRGEPIHPMSGIPVGVKDLFCTKGVRTTACSNILKNFVPTYESTVSQKLWDSGAVMLGKLNMDEFAMGSSNTYSCFGPVKNPWKGTEGKDLTPGGSSGGSSAAVAGLLCAGALGSDTGGSVRQPAALCGVVGAKPTYGRCSRWGMIAYASSLDQAGVLARTVEDAAVMLNAICGYDQKDSTSSQEAVPDFLGGISRDVRGVRIGIPKEYELPKNRGDIAAMWDQNIKHLLDCGAEIVEISLPHTTYALPVYYILASSE... | Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). | B9KIR2 |
A8G8E5 | RL10_SERP5 | 50S ribosomal protein L10 | Serratia | MALNLQDKQAIVAEVNEVAKGALSAVVADSRGVTVDKMTELRKAGREAGVYMRVVRNTLMRRVVEGTPFECLKDTFVGPTLIAFSHEHPGAAARLFKDFAKANAKFEIKAAAFEGEMIPAAQIDRLATLPTYDEAIARLMATMKEAAAGKLVRTLAALRDQKEAA | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | A8G8E5 |
Q8D2L8 | SLYA_WIGBR | Transcriptional regulator SlyA | Wigglesworthia | MESPLGSDLSRLVRIWRALIDHRLKPLELTQTHWITLHNICQLPPEQSQIQLAKAIGIEQPSLVRTLDQLEEKGLITRHTCSNDRRAKRIKLTKSAEPIIQKVNNVIHTTREEILNGINQEEIQWLSQMISKLEKNILELYNKS | Transcription regulator that can specifically activate or repress expression of target genes. | Q8D2L8 |
Q7MQ55 | GLO21_VIBVY | Glyoxalase II 1 | Vibrio | MSLSITHEKSLIDNYIWILFDKSKAIVIDPGESEKIINFLDKNNLTLEFIFLTHGHCDHTKGVFSLKEKFPNASLFVPIGLELGLGESIIKEGDELNLLNSTFNVLELPGHTDNHIGIMYKDNLFCGDVLFSAGCGRVGSNYKDMYLSLKKIKSMDDKTKIYFSHEYTLDNLKFAHYIDPKNKNIINYIEVFKEKPDTVSAPTTLLLEKEINPFLRLSENIDIKNKINNEFDAFVYLRKLKDKFNSI | Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid. | Q7MQ55 |
A2C8B2 | RECR_PROM3 | Recombination protein RecR | Prochlorococcus | MIDQFERLPGIGPRTAQRLALHLLRQPEDQIRAFAEALLAARSQVGQCQTCFHLSAEPLCDICRDGTRCDQLLCVVADSRDLLALERTREYKGRYHVLGGLISPMDGIGPDMLQIPSLIQRVDRDGISEVILALTPSVEGDTTSLYLARLLKPFTQVSRIAYGLPVGSELEYADEVTLTRALEGRRAMQ | May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO. | A2C8B2 |
A8A534 | NANT_ECOHS | Sialic acid/H(+) symporter | Escherichia | MSTTTQNIPWYRHLNRAQWRAFSAAWLGYLLDGFDFVLIALVLTEVQGEFGLTTVQAASLISAAFISRWFGGLMLGAMGDRYGRRLAMVTSIVLFSAGTLACGFAPGYITMFIARLVIGMGMAGEYGSSATYVIESWPKHLRNKASGFLISGFSVGAVVAAQVYSLVVPVWGWRALFFIGILPIIFALWLRKNIPEAEDWKEKHAGKAPVRTMVDILYRGEHRIANIVMTLAAATALWFCFAGNLQNAAIVAVLGLLCAAIFISFMVQSTGKRWPTGVMLMVVVLFAFLYSWPIQALLPTYLKTDLAYNPHTVANVLFFS... | Catalyzes the proton-dependent transport of sialic acid. | A8A534 |
C1L2B3 | COBQ_LISMC | Cobyric acid synthase | Listeria | MVKQIMIQGTASDAGKSVLVAGLCRLFKNKGKRVVPFKSQNMSLNSFITATGDEMGRAQVFQAEAAGVFPDVRMNPVLLKPTNDRQSQVIFMGAILDNMDAVTYHDFKQTLIPKIQAVYQSLADENDIIVLEGAGSPAEINLNDRDIVNMGMAKMVDAPVVLVADIDKGGVFASIYGTIMLLNEEERARIKGVIINKFRGDVALLQPGIDMIEELTNVPVIGVIPYANLQLEEEDSVSLSGKNYVPDSNALLDIAIICLPRISNFTDFHILEIQPDISVRYIRNIADFGNPDLVIIPGSKNTLEDMAFLEESGLKNAIQN... | Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. | C1L2B3 |
Q4K3R4 | KGUA_PSEF5 | GMP kinase | Pseudomonas | MTHSTGTLYIISAPSGAGKSSLVKALTDAKPEIRVSVSHTTRAMRPGEVDGVNYHFVSRETFVKMGEHGDFLERAEVFGNLYGTSQSHLQQTLDAGHDLILEIDWQGAEQVRKLMPQARSIFILPPSLQALHQRLTNRGQDSDEVIDGRMREAVSEMSHYVDYDYLIINDDFAHALGDLKAIFRANQLQQKRQQQRFGKLLAELLG | Essential for recycling GMP and indirectly, cGMP. | Q4K3R4 |
A2RI75 | DPPB_LACLM | Dipeptide transport system permease protein DppB | Lactococcus cremoris subsp. cremoris | MVKYILKRLGLLLLTLFLIVTLTFFMMQVMPGTPFSNPKLTPDQLEILKHAYGLDKPLWQQYFIYVGHMFTGNFGTSFIYTNQPVITMIAQRLPVSMQLGTQALILGTVLGALMGKASARRKNGLLDGIFGFLSVLGISVPSFVIGTLILLYLGFNLNLFPISGWGTFSQTIMPTIALSFAPMAVVTRFVRSEMIESLSSDYILLARAKGLSEKEVVNKHALRNSLIPMLTLIGPMAAGLLTGSVLIEKIFSIPGIGAQFVDSIPAKDFPVIMATTIVYAVILMVFILVTDILTAIVDPRVRL | Part of the ABC transporter DppABCDF involved in dipeptide transport . Responsible for the translocation of the substrate across the membrane (Probable). | A2RI75 |
Q9K6W8 | SECA_HALH5 | Protein translocase subunit SecA | Halalkalibacterium (ex Joshi et al. 2022) | MLGLLKKVVGDPSQRQLKKNQKIADQVEALSDEMKSLSDDGLRQKTEEFKKRYKNGESLDDLLPEAYAVVREAATRVLNMTPYPVQILGAIALHQGNIAEMKTGEGKTLVGTMPVYLNALAGKGVHVVTVNDYLARRDSEQMGAMFEFLGLTVGLNVPGLSKEEKKEAYQADITYGTNNEFGFDYLRDNMVLYKEQMVQRSLNFALVDEVDSILIDEARTPLIISGSVERSTKLYSQANSFVRVLKNEEDYTLDEKTKSVQLTEEGVNKAERAFNIDNLFDQRHVQLLHHINQAMKAHVVMHRDADYVVENGEIVIVDQF... | 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... | Q9K6W8 |
Q9W6S5 | ALLC_XENLA | Allantoate amidinohydrolase | Xenopus | MFAHPKENIALPVPEFLQMNNLACESVGGKVLFATDDWFAPAEHLLKKTEPEFKVGLFTEFGKWMDGWETRRKRIPGHDWCIIQLGVPGIIHGFEADTRFFTGNYAPRISIQAACLKPEEITLQPREDKIGTAASDEEFKAADKLKSEKWSHLLKMTELKPGYAESSHSYFQVNSKERWTHLRLNIYPDGGIARFKVYGIGQRDWTSCGPNDFEDLLSMVNGGVCLGFSDAHYGHPRNLIGNGRACDMGDGWETARRLDRPPILKADSKGILQVPGFEWAVLKLGHPGLVTHIEIDTNHFKGNSPNSCKIDACALKPTEQ... | Utilization of purines as secondary nitrogen sources, when primary sources are limiting. | Q9W6S5 |
Q9YG22 | ARGDC_AERPE | Arginine decarboxylase alpha chain | Aeropyrum | MERREDVIVGKHVYGSLYGVPREKATDEEYLRGVVVRAAESAGATVHAVNSWTIPGEKGGVSVIVLVLESHLALHTWPEYDYATFDIYTCGEHTDPWKAFELLLSELKPRKYTVHYVDRSQEKTVLEAQPRR | Specifically catalyzes the decarboxylation of L-arginine to agmatine. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity. | Q9YG22 |
Q6QUY7 | ECTD_STRAQ | Ectoine hydroxylase | Streptomyces | MTTEVRADLYPSRGAAEMTTPRQDPVIWSAPGAPGPVAAKDLQGYEHDGFLTVDQLIAPDEVAVYQAELNRLISDPAVRADERSIVEKQSQNVRSVFEVHRISEVFAGLVRDERVVGRARQILGSDVYVHQSRINVKPGFGATGFYWHSDFETWHAEDGLPNMRTVSVSIALTENFDTNGGLMIMPGSHKTFLGCAGETPKDNYKKSLQMQDAGTPSDEALTKMADRHGIRLFTGRAGSATWFDCNAMHGSGDNITPYARSNVFIVFNSVENAAQEPFAAPIRRPEFIGARDFTPVK | Involved in the biosynthesis of 5-hydroxyectoine, called compatible solute, which helps organisms to survive extreme osmotic stress by acting as a highly soluble organic osmolyte. Catalyzes the 2-oxoglutarate-dependent selective hydroxylation of L-ectoine to yield (4S,5S)-5-hydroxyectoine. | Q6QUY7 |
Q99YU5 | RLMN_STRP1 | tRNA m2A37 methyltransferase | Streptococcus | MKPSIYSLTRDELIAWAVERGQKQFRATQIWDWLYKKRVQSFEEMTNISKDFVSILNDSFCVNPLKQRVVQESADGTVKYLFELPDGMLIETVLMRQHYGHSVCVTTQVGCNIGCTFCASGLIKKQRDLNSGEITAQIMLVQKYFDDRKQGERVSHVVVMGIGEPFDNYKNVMCFLRVINDDNGLAIGARHITVSTSGLAHKIRDFANEGVQVNLAVSLHAPNNDLRSSIMRVNRSFPLEKLFSAIEYYIEKTNRRVTFEYIMLNEVNDSIKQAQELADLTKTIRKLSYVNLIPYNPVSEHDQYSRSPKERVLAFYDVLK... | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. | Q99YU5 |
C0HJZ4 | HBB2_SOMMI | Hemoglobin beta-2 chain | Somniosus | VHWTAEEKALVNVVWSKTDHQAVVANALGRLFVVYPWTKTYFTKFNGKAGDSAVQTHAGKVVSALTLAYNHIDDVKPHFKHYEGFHVDPENFRLLANCLNVELGHTLHKEFTPELHAAWNKFSNVVVDALSKGYH | Involved in oxygen transport from gills to the various peripheral tissues. | C0HJZ4 |
A1WC14 | RSMH_ACISJ | rRNA (cytosine-N(4)-)-methyltransferase RsmH | unclassified Acidovorax | MNQPLQHTTVLLDEAVHALLGDGDAPAGTFVDGTFGRGGHSRLILQRLGPQGRLVAFDKDTEAIQAAARITDARFSIRHQGFSHLGELPAASVSGVLLDLGVSSPQIDDPQRGFSFRFDGPLDMRMDTTRGQSVAEWLADAETAQIAEVIRDYGEERFAGPIAKAIVARRTERGPIASTAELADIVAGAVKTREPGQNPATRTFQALRIFINAELEELQQALEGSLHVLRPGGRLVVISFHSLEDRIVKQFIAQHSKEVYDRRAPFAPPQPMRLRALERIKPSTDEVAANARARSAVMRVAERTEVPA | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | A1WC14 |
Q5T751 | LCE1C_HUMAN | Late envelope protein 3 | Homo | MSCQQSQQQCQPPPKCTPKCPPKCPTPKCPPKCPPKCPPVSSCCSVSSGGCCGSSSGGSCGSSSGGCCSSGGGGCCLSHHRRRRSHCHRPQSSGCCSQPSGGSSCCGGGSGQHSGGCC | Precursors of the cornified envelope of the stratum corneum. | Q5T751 |
Q31BX4 | HIS1_PROM9 | ATP phosphoribosyltransferase | Prochlorococcus | MFTIALPKGALLEDSISIFKRAGLDFSDALEENNRSLTFESNCKRAKALLVRNGDVPVYVSYGQADLGIVGYDVLRESELKVAKLLDLGFGGCHMSLAVKKNSNYSKPTDLPANCKVASKFTKTARSYFDELNIPVEIVHLTGSVELGPITGMAEAIVDLVATGKTLQENGLIKIDDIFYSTARLIGNPLSIRLDDNHLRDTILSIESINAL | Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. | Q31BX4 |
P61489 | AK_THETH | Threonine-sensitive AK | Thermus | MALVVQKYGGTSVGDLERIHKVAQRIAHYREKGHRLAVVVSAMGHTTDELIALAKRVNPRPPFRELDLLTTTGEQVSVALLSMQLWAMGIPAKGFVQHQIGITTDGRYGDARILEVNPARIREALDQGFVAVIAGFMGTTPEGEITTLGRGGSDTTAVAIAAALGAKECEIYTDTEGVYTTDPHLIPEARKLSVIGYDQMLEMAALGARVLHPRAVYYAKRYGVVLHVRSSFSYNPGTLVKEVAMEMDKAVTGVALDLDHAQIGLIGIPDQPGIAAKVFQALAERGIAVDMIIQGVPGHDPSRQQMAFTVKKDFAQEALE... | Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. | P61489 |
A3PMM1 | RL25_CERS1 | General stress protein CTC | Cereibacter | MAGEIPDFQAEVRTGTGKGAARQARREGYVPGIVYGGGQEPLSINVPYNDLLNRLKKGRFLQTLFNLKVEGQEDVRVICRGVQRDVVKDLPTHVDFMRLRRTSRVNLFIHVTFENHDKAPGLKRGGTLTVVRPEVELEVTAGDIPDHLTVDLTDRQIGDVIHINDIKLPEGAVPTINRNFVIANISAPSGLRSSDNEEEAEEA | This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. | A3PMM1 |
Q3T0C2 | PGDH_BOVIN | Prostaglandin dehydrogenase 1 | Bos | MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVKCKAALDEQFEPQKTLFIQCDVADQEQLRDTFRKVVDHFGKLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGININMSSLAGLMPVAQQPVYCASKHGIVGFTRSAAMAANLMNSGVRLNAICPGFVDTPILKSIEKEENMGKYIEYMGPIKDMMKYYGILDPSMIANGLITLIEDDALNGAIMKITTSKGIHFQDYDTTPFHMKMQ | Catalyzes the NAD-dependent dehydrogenation (oxidation) of a broad array of hydroxylated polyunsaturated fatty acids (mainly eicosanoids and docosanoids, including prostaglandins, lipoxins and resolvins), yielding their corresponding keto (oxo) metabolites. Decreases the levels of the pro-proliferative prostaglandins s... | Q3T0C2 |
Q1WUQ1 | PRSA_LIGS1 | Foldase protein PrsA | Ligilactobacillus | MKKKWLVAISGIVLTFGLAACSKTVATTSGGKITESEYYSSMKKTSSGKQVLQQMILNKVLEKEYGSKVSDKKVNEQYNTYKKQYGSSFDSVLAQNDMTKSSFKQEIRSNLLLKEAVKDNTKITNKQLKAQWKEYEPKVTVAHILVSKKSTAEDIINKLKEDGSYANFKKLAKKYSTDSSTKNDGGKLAAFDNTDTSLDSTFKKAAFGLKQGSFTTEPVKTEYGYHVIYSIKNPGKGKMSDHTSELKSQIIDSKMSDSTTLQTVVSKVLKKGNVSIKDKDLQNILSSYLGSSSSSK | Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins. | Q1WUQ1 |
Q8T277 | PRKAG_DICDI | 5'-AMP-activated protein kinase subunit gamma | Dictyostelium | MWYPGDEDEEFTSIIENIEKKETQEIKIKTEKLRQASLNQLPIEQSEGVGGGELSEYNNNTTNNNTPTNTTTTTNTNTTTMNNSNNNNERILSTSNGFDIRLPPNSIEQPSPSFISSSQDGVLTVDPLAVDGEKGNKESQSPPNGDNQILNNNNMFFKDITSLPSTDNKSSTNTNNNNNENPLKQTISSSPSKSTTTTTTSTSTTTTPSLSSLSSNNNNNSNSNNNYINHSSISTVSEGLENLNLKSGIKKIDSETEKYIEEGKQVFVNFLKGHTCYDVIPISGKVVVLDTKLAVKSAFYALEENGIKSAPLWNSEQHDF... | AMPK may be responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. | Q8T277 |
Q9SUV1 | BRT1_ARATH | Protein SODIUM HYPERSENSITIVE 1 | Arabidopsis | MGKTGIQLFDDSRNGFFSVSDLGFDSSLNSSNYHPIGGLFASVNQTNPFASLSSSDLSNRGNNSFSTQLNDLYTKYMPGKEEEEEVVNGEKRKRKKKGGLTLKIKIANPSLRRLLSGAVAGAVSRTVVAPLETIRTHLMVGSGGNSSTEVFSDIMKHEGWTGLFRGNLVNVIRVAPARAVELFVFETVNKKLSPPHGQESKIPIPASLLAGACAGVSQTLLTYPLELVKTRLTIQRGVYKGIFDAFLKIIREEGPTELYRGLAPSLIGVVPYAATNYFAYDSLRKAYRSFSKQEKIGNIETLLIGSLAGALSSTATFPLE... | Probable mitochondrial adenylate carrier that catalyzes the transport of ATP, ADP and AMP, but not ADP-glucose. Recombinant BT1 shows a unidirectional mode of transport in intact E.coli cells. May function as a plastidial nucleotide uniport carrier required to export newly synthesized adenylates into the cytosol. May b... | Q9SUV1 |
P11064 | PPAC_BOVIN | Low molecular weight cytosolic acid phosphatase | Bos | MAEQVTKSVLFVCLGNICRSPIAEAVFRKLVTDQNISDNWVIDSGAVSDWNVGRSPDPRAVSCLRNHGINTAHKARQVTKEDFVTFDYILCMDESNLRDLNRKSNQVKNCRAKIELLGSYDPQKQLIIEDPYYGNDADFETVYQQCVRCCRAFLEKVR | Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. | P11064 |
O02839 | MCP_PIG | Membrane cofactor protein | Sus | MMAFCALRKALPCRPENPFSSRCFVEILWVSLALVFLLPMPSDACDEPPKFESMRPQFLNTTYRPGDRVEYECRPGFQPMVPALPTFSVCQDDNTWSPLQEACRRKACSNLPDPLNGQVSYPNGDMLFGSKAQFTCNTGFYIIGAETVYCQVSGNVMAWSEPSPLCEKILCKPPGEIPNGKYTNSHKDVFEYNEVVTYSCLSSTGPDEFSLVGESSLFCIGKDEWSSDPPECKVVKCPYPVVPNGEIVSGFGSKFYYKAEVVFKCNAGFTLHGRDTIVCGANSTWEPEMPQCIKDSKPTDPPATPGPSHPGPPSPSDASP... | Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. May act as a costimulatory factor for T-cells which in... | O02839 |
Q2UNJ0 | CHS7_ASPOR | Chitin synthase export chaperone | Aspergillus subgen. Circumdati | MGFGDFDTICQKAALPLCSLVGPASSISGATGIIPNCYARNIELANTIIFEGAASFVHIIALAMTVIMILHIRSKFTAVGRKEIITFFYIYMLLTMCSLVIDAGVVPPRSGPFPYFVAVQNGLTSALCTSLLVNGFVGFQLYEDGTALSVWLLRLTSTAMFAISFVISLLTFKSWGGLSPTNTVGMFVVLYILNAICIAVYLIMQLLLVMNTLEDRWPLGHIAFGLLVFICGQVLLYAFSDTICENVQHYLDGLFFTTICNLLAVMMVYKFWDYITKEDLEFSVGIKPNTWEVKEFLPEEDRRATVYQDTNSEYAGSMYH... | Chaperone required for the export of the chitin synthase chs3 from the endoplasmic reticulum. | Q2UNJ0 |
P57529 | RECB_BUCAI | Helicase/nuclease RecBCD subunit RecB | Buchnera | MKIDSLKEKLNIFKIPLNGIKLIEASAGTGKTFTIVLLYLRLLLGIGEKKIYKKKLLVHEILVVTFTNKAKEELYIRIKDGIQNMYLTCINKTTSDSSFQFFFKEIHDIKEAIYVLKRAQNDMNSSSIYTIHSFCQHILQLHTFHFNDIFEEKIIENEDNLYLQATQDFWRRFFYTLPEDIIKIIYQDYKSPDHLLKTIKPFFYIKSINFPTKILNNKKLIMYHEENIKKIIFFKEMWLIYHKIIQKTINDLEINKKIYSKFNLIKWINKITEWAKSETKDYTIPSILKYFTKKNIEKNTINNTCSKYIIFEESEKILKK... | A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucl... | P57529 |
B1X0G3 | MOAA_CROS5 | Molybdenum cofactor biosynthesis protein A | Crocosphaera subtropica | MNRVDYLRISLIDRCNFRCQYCMPEGAELDYILRQELLTHEELITLLKEVFIPLGFSKFRLTGGEPLLRPGIVDLVQDIASLPATEDLSMTTNGFLLSSLAEDLYQAGLKRINISLDSLNPDTFQTIIGHKKANMWQQTWLGIQTAYEVGFDPLKLNVVVIPGVNENEIEALAELSIHKNWHIRFIEFMPIGNPELFSDLEEIRFAGRAWVASEEIREKIRQKWGLIESNIKGNGPADVFKIPGAKGTVGFISQMSECFCDRCNRMRLSADGWLRPCLLNETGQIDLKTLLRSGISATNIRDKVAHLLTIKPDINYKQRD... | Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate. | B1X0G3 |
B5F8J0 | CYSG_SALA4 | Sirohydrochlorin ferrochelatase | Salmonella | MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLEAGARLTVNALTFIPQFTVWANEGMLTLVEGPFDETLLDSCWLAIAATDDDTVNQRVSDAAESRRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVARYAGQLRARVKKQFATMGERRRFWEKFFVNDRLAQSLANADEKAVNATTERLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADIVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCHA... | Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yie... | B5F8J0 |
B4F231 | CYSD_PROMH | Sulfate adenylate transferase | Proteus | MNETQLTHLQQLEAESIYILREVVAEFENPVMLYSIGKDSSVMLHLARKAFYPAKLPFPLLHVDTGWKFREMYEFRDKTAKEYGFDLKVYRNPQGAQLGINPFIHGSAKHTDIMKTEGLKQALDKYGFDAAFGGARRDEEKSRAKERIYSFRDRSHRWDPKNQRPELWQNYNGQINKGESIRVFPLSNWTELDIWQYIYLENIDIVPLYFAKHRPVIERDGTLIMVDDDRIDLKAGEVITQQKVRFRTLGCWPLTGAIPSQADTLPAIIEEMLISTSSERQGRLIDSDQSASMELKKRQGYF | With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysi... | B4F231 |
Q3BWX2 | RL24_XANC5 | 50S ribosomal protein L24 | Xanthomonas | MANRIKKGDQVVINTGKDKGKQGEVVRVEGDRVIVSNANVIKRHTKPNPQAGVAGGVVEREASIHISNVNIVNPATGKGERVGFKVLEDGRKLRVFRSSGEALDA | One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. | Q3BWX2 |
B3PIS7 | ATPB_CELJU | F-ATPase subunit beta | Cellvibrio | MSSGRIVQIIGAVIDVEFPRDAVPKVYDALVISEGNLTLEVQQQLGDGVVRTIALGSSEGLRRGLSVTNTNEPIKVPVGTQTLGRIMDVLGNPIDEAGPIGEQERMQIHRAAPAYEELAASEELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMMELINNIAKEHSGLSVFAGVGERTREGNDFYHEMKDSNVVDKVAMVYGQMNEPPGNRLRVALTGLTMAEKFRDEGRDVLLFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKIGSITSVQAVYVPADDLTDPSPATTFAHLDSTVVL... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | B3PIS7 |
Q9CNJ0 | GLMM_PASMU | Phosphoglucosamine mutase | Pasteurella | MAERKYFGTDGVRGKVGTFPITPDFALKLGWAAGKVLATQGSRTVLIGKDTRISGYMLESALEAGLAAAGLSAAFTGPMPTPAIAYLTRTFRAEAGIVISASHNPYYDNGIKFFSAQGTKLPDDVEEAIEAMLDEPMDCVESAELGRASRINDAVGRYIEFCKGTFPAHLSLENYKIVVDCAHGATYHIAPNVMRELGAEVIEIGAKPNGLNINEKCGATDIKALQEKVLEVKADVGLAYDGDGDRLIMVDHLGNKVDGDQVLFIIAREALRAGHLKGGVVGTLMSNMSLELALKQLGIPFVRANVGDRYVLEKMQEKGW... | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. | Q9CNJ0 |
B1W0A3 | ATPB_STRGG | F-ATPase subunit beta | Streptomyces | MTTTVETAAATGRVARVIGPVVDVEFPVDAMPEIYNALHVEVADPAEDGARKTLTLEVAQHLGDGVVRAISMQPTDGLVRQAPVTDTGTGITVPVGDVTKGKVFNTLGQILNEPEAEAQITERWPIHRKAPAFDQLESKTEMFETGLKVVDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIMRVAKLHDGVSVFAGVGERTREGNDLIDEMTESGVLEKTALVFGQMDEPPGTRLRVALSALTMAEYFRDVQKQDVLLFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPTLADEMGVLQERITSTRGHSITSMQAIYVPADD... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | B1W0A3 |
Q82DN2 | RS8_STRAW | 30S ribosomal protein S8 | Streptomyces | MTMTDPIADMLTRLRNANSAYHDTVGMPHSKIKSHIAEILQQEGFITGWKVEDAEVGKNLVLELKFGPNRERSIAGIKRISKPGLRVYAKSTNLPKVLGGLGVAIISTSHGLLTDKQAGKKGVGGEVLAYVW | One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. | Q82DN2 |
B2JE39 | RLMH_PARP8 | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Paraburkholderia | MKLHILAVGHKMPDWIATGFDEYAKRMPPELRIELREIKPEQRSSGRSAESVMASERQKIEAALPRNARIVALDERGKDWTTMQLANALPTWQQDGRDVAFLIGGADGLDPDLKARADMLLRVSSLTLPHAMVRVLLAEQLYRAWTITQNHPYHRV | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | B2JE39 |
B2J8B7 | PURA_NOSP7 | IMP--aspartate ligase | Nostoc | MANVIVIGAQWGDEGKGKITDLLSRSADVVVRYQGGVNAGHTIVVKGQTFKLHLIPSGILYPNTDCIIGCGTVIDPQILIAEIDQLKELNISTDHLLISETAHVTMPYHRLIDQASEERRGSYKIGTTGRGIGPTYADKSERTGIRVLDLMDPDGLREQLEWTINYKNVILEKLYNLPPLDPQEVIEQYLGYAERLRPHVVDTSLKISDAIQRRRNILFEGAQGTLLDLDHGTYPYVTSSNPVAGGACVGTGVGPTMIDRVIGVSKAYTTRVGEGPFPTELDGELGELLCDRGAEFGTTTGRKRRCGWFDAVIGRYAVRI... | 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. | B2J8B7 |
Q3K5K9 | GLYA3_PSEPF | Serine hydroxymethyltransferase 3 | Pseudomonas | MFSKQDQIQGYDDALLAAMNAEEQRQEDHIELIASENYTSKRVMQAQGSGLTNKYAEGYPGKRYYGGCEHVDKVEALAIERAKQLFGADYANVQPHSGSSANSAVYLALLQAGDTILGMSLAHGGHLTHGAKVSSSGKLYNAVQYGIDTKTGLIDYDEVERLAVECKPKMIVAGFSAYSKTLDFPRFRQIADKVGALLFVDMAHVAGLVAAGLYPNPLPYADVVTTTTHKTLRGPRGGLILAKANEEIEKKLNAAVFPGAQGGPLMHVIAGKAVCFKEALEPGFKAYQQQVIDNAQAMASVFIKRGYDVVSGGTDNHLFL... | Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent a... | Q3K5K9 |
B7K221 | RL13_RIPO1 | 50S ribosomal protein L13 | Rippkaea orientalis | MNKTITPNPETLDQKWYVIDAADQRLGRLASEVAQILRGKNKPTFTPHMDTGDFVIIVNAEKVVVTGKKSSQKLYRRHSGRPGGMKVETFEKLQARLPERIVEHAVKGMLPKNSLGRKLFTKLKVYTGPTHPHQAQQPETLIVNTIPTGEN | This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | B7K221 |
Q7VHN8 | SYE1_HELHP | Glutamyl-tRNA synthetase 1 | Helicobacter | MDKIVTRFAPSPTGYLHIGGLRTALFNYLYARANGGKFLLRIEDTDLARNSMEATKAIIESFEWAGLDYDGEVVYQSQRFDLYKTYIQQLLESKKAYYCYMSKEELDALRKEQEKNKQTPRYDNRYRDFTGIPPQGIQPVVRIKAPLEGNIEFEDGIKGQISINAKEIDDFIIARSDGTPTYNFVVAVDDALMGITDVIRGDDHLSNTPKQIIIYNALGFALPRFFHVPMILNSQGKKLSKRDGAMGVMDYAKMGYLPEAILNFLVRLGWSYGDKEIFSLEEMLELFNPNELNSSPSAYNEDKLLWLNQHYIKYMDNTLL... | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | Q7VHN8 |
A1SRT6 | HLDD_PSYIN | ADP-L-glycero-beta-D-manno-heptose-6-epimerase | Psychromonas | MFIVTGGAGFIGSSIVKSLNERGITDILVVDDLTDGAKFVNLVDLQIMDYMDKDEFITQIVSGQDFGDIEAIFHEGACSATTEWNGKFMMENNYEYSKDLLHYCIERDIPFLYASSAATYGGNDTFKEELKYEKPLNVYGYSKFQFDQYVRRIWEDAAAHDETLPQIVGFRYFNVYGPREQHKGSMASVAFHLNNQLNAGENAKLFEGEHKRDFVYIGDVCKVNLWFFDNNVSGIYNLGTGQAESFLEVGQAVVAYHQKGEVERIPFPEHLKGRYQSFTEADLTNLRAAGYKDTFKSVAQGTAEYMAWLNR | Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. | A1SRT6 |
Q9FM80 | MTEF9_ARATH | Protein TWIRT1 | Arabidopsis | MAGFSLYCFKNPRILFTLPSESPLFVLGSDKCSPATRRPSRKTRGFVVTYAHSNPKIINPKKKSRYGQTLSPYDSDEDDDDDDDDDDDDWLLNDDFAEVTEYEKKKPKSHKQTIAKKSVKKGIVKPEESETDEDDLDLGISPNATSEKKKESWRLDGRGKMSSRKYVEKLYPRLAEEIDIDPKCVPLLDYLSTFGLKESHFVQMYERHMPSLQINVFSAQERLDYLLSVGVKHRDIKRMLLRQPQILQYTVENNLKAHISFLMGLGIPNSKIGQIVAATPSLFSYSVENSLRPTIRYLIEEVGIKETDVGKVVQLSPQIL... | Transcription termination factor required for processing and steady-state levels of plastid transcripts. May play a role in response to abiotic stresses. | Q9FM80 |
B0TZM4 | GLMU_FRAP2 | Glucosamine-1-phosphate N-acetyltransferase | Francisella | MSLAVVILAAGKGSRMNSNKPKVLQTLTGKTLIRHVLSRVEPLNPDNIIVVTGHLKEMVEADLADKKVTFVEQKEQLGTGHAVLQALPYIKEDKVLILYGDVPLISTDVLANLIKSASDDLAVLTAIVDNPTGLGRIIRDKFGAVSHIVEEKDATDGQRQIKEINTGMYCVAKSHLDDWLPNLGNTNAQGEYYLTDIVAMARGDNISITVTHPVEEFEIQGVNDRIQLAQLEREWQKHIAEVIMSKGVSVADPSRIDVRGKLEVGKDCWLDINVIIKGHVKLGNNVVIGANCILKNCTIEDNVKIKANSMVDGSIIREGA... | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted ... | B0TZM4 |
B0B7F9 | LPXD_CHLT2 | UDP-3-O-acylglucosamine N-acyltransferase | Chlamydia | MSQSTYSLEQLADFLKVEFQGNGATLLSGVEEIEEAKTAHITFLDNEKYAKHLKSSEAGAIIISRTQFQKYRDLNKNFLITSESPSLVFQKCLELFITPVDSGFPGIHPTAVIHPTAIIEDHVCIEPYAVVCQHAHVGSACHIGSGSVIGAYSTVGQHSYIHPRVVIRERVSIGKRVIIQPGAVIGSCGFGYVTSAFGQHKHLKHLGKVIIEDDVEIGANTTIDRGRFKHSVVREGSKIDNLVQIAHQVEVGQHSMIVAQAGIAGSTKIGNHVIIGGQAGITGHICIADHVIMMAQTGVTKSITSPGIYGGAPARPYQEI... | Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | B0B7F9 |
A9CB18 | GDF9_PAPAN | Growth/differentiation factor 9 | Papio | MALPNKFLLWFYCFAWLCFPVSLGSQASGGDAQIAASAELESGATPWSLLQPIDERDRAGLLPPLFKVLSVGRGGAPRLQPDSRALHYMKNLYKTYATKEGIPKSNRSHLYNTVRLFTPCTQHKQVPGDQVTGILPSVDLLFNLDRITTVEHLLKSVLLYTINNSVSFSSAVKCVCNLMIKEPKFSSKTLHRALYSFTFNSQFEFGKKHKWIEIDVTSLLQPLVASNKRSIHMSINFTCMKDQLEHPSAQNGLFNMTLLVPPSLILYLNDTSAQAYHRWYSLYYKRRPSQGPDQERSLSAYPVGEDAAEDGRSSHHRHRR... | Required for ovarian folliculogenesis. | A9CB18 |
Q6KHN2 | PLSX_MYCMO | Phosphate-acyl-ACP acyltransferase | Mesomycoplasma | MKIIAFDVMGSDKGVGPAVLASINFVKKNLDYKIILVGDKTLITKYVSENERIEIYDEPLEVKKGENLKAVLSKTTSMSVAIDLVKDNKAEVVLSAGDSASYLALCVIKLKRLEGITRPAFMPIFPTILDDKKFVLLDVGANIEVDTEYLVQWAKLGSVFAKIMWNIDKPNVGILNIGTEDFKGFKYHQEANQILKEANLSEMNYKGFVEPRDILKGNFDVIVADGYGGNLVLKSLEGTVIDFSSLIKRKITSTFFRKIGALILKKSFKEIKEHLDYRNVGGAWVIGVNSIAVKAHGSSDEKAFKGAFNQIKIAVENNVI... | Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. | Q6KHN2 |
Q834S5 | CCA_ENTFA | tRNA-NT | Enterococcus | MKLTTIPNEFKEAAPVIREINAQGFEAYFVGGSVRDALLNKPIHDVDIATSAYPEEIKQIFKRTVDVGIEHGTVLVLMEDQQYEVTTFRTESTYQDFRRPDEVTFVRSLKEDLKRRDFTINALALDSTGEIIDLFDGIEDLTNQTIRAVGNPHERFHEDALRMMRGLRFASQLDFKIEEKTLAAIAEFHPLLEKISVERITIEFVKMLLGVNRQGGLAPFIETECYQYCPKLREQGAGLFRLMDLPARQIETEAEAWTLLIQSLNLPEAEIRSFLKAWKLSNQLIQNVSQLVRGLRFRLSNDWQPMMLYELGEESAVLVE... | Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. | Q834S5 |
Q9V120 | RRP4_PYRAB | Exosome complex component Rrp4 | Pyrococcus | MKRIFVQNRELVVPGTLLAQGPYKNGRGTFREGSRIYSTVIGLVDIKGNTIRVIPLEGPYIPEVGDNVIGKIVDVKFSSWVVDIGAPYPANLKIQDFTDEKIDLLRTDLRKFFDIGDIIYAKVKAITEVNNIDLTTKGMPFNGGPLKGGQIVKITPSRVPRVIGRGGSMINMIKKLTMTRIIVGQNGWIWVSGKNDALEKLAIEAILKIDKESHTRGLTDRIKALLLSRLQELKEKGVIEEIPKLEEEPQGEDEVNGNDGEARGA | Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Increases the RNA binding and the efficiency of RNA degradation. Confers strong poly(A) specificity to the exosome. | Q9V120 |
O68215 | SACB2_NEIMD | Stealth protein SacB | Neisseria | MFILNNRKWRKLKRDPSAFFRDSKFNFLRYFSAKKFAKNFKNSSHIHKTNISKAQSNISSTLKENRKQDMLIPINFFNFEYIVKKLNNQNAIGVYILPSNLTLKPALCILESHKEDFLNKFLLTISSENLKLQYKFNGQIKNPKSVNEIWTDLFSIAHVDMKLSTDRTLSSSISQFWFRLEFCKEDKDFILFSTANRYSRKLWKHSIKNNQLFKEGIRNYSEISSLPYEEDHNFDIDLVFTWVNSEDKNWQELYKKYKPDFNSDATSTSRFLSRDELKFALRSWEMSGSFIRKIFIVSNCAPPAWLDLNNPKIQWVYHEE... | Part of a capsular biosynthesis operon and has been suggested to be the polymerase that links individual UDP-N-acetyl-D-mannosamine monomers. In serotype A the capsule is composed of repeated units of (alpha 1-6)-linked N-acetyl-D-mannosamine-1-phosphate. Non-polar disruption of this open reading frame prevented capsul... | O68215 |
B0TXA0 | ACCA_FRAP2 | Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha | Francisella | MNYLDFESKIKEIEDKITSLSHVYEDEKTESEIKKLGKKRLELMESTYSKLTDWQVVQLSRHPDRPYFKDLLSLVFTDFQELHGDRAFGDDLAVIGGLAKLNNKPVMVIGQEKGRDTKSKIKHNFGMMHPEGYRKALRLMKLAEKFNMPIVTFIDTPGAYPGIKAEERGQSEAIARNLLEMSALKVPVVCIVIGEGCSGGALGIGVGDRLLMLQYSYFATISPEGCASILHKTAEKASEVTQMMNITSGRLKELEIVDAVIPEPLGGAHRDYDTTAANIRKAVAAELKVLSEMTVEERNAKRYDKLMSFGRFKEA | 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. | B0TXA0 |
B8N0E8 | ASAC_ASPFN | Aspergillic acid biosynthesis cluster protein C | Aspergillus subgen. Circumdati | MSIFSSISSLGLEACYRHHVRTSPNATAVVDGDQSMTYRELETRVNDLASILGRENIEEEEPIGILVPMGIAHVVAQAAVLRLGGSCVPMDLSFPDQRINDLLRALKTRIVLTVESEKARFAEFQTILVDSKYANLHQNGYHEDTIPAVETGRNHRTHILHTSGTTGLPKPVEIMSKGITRMAFNTQCVEFKSTDRVAQISAPSFDAALFEIWTTLARGAAIVLLPKNVVIDPVALHDSLRKYRITSILVTTALLNHVVSAIPNAFEDLDYVLTGGEAANPSVMQVILENGPPKKLVHAYGPTECTIITTYHLTTLEEVR... | Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of aspergillic acid, a hydroxamic acid-containing pyrazinone with aliphatic side chains that originates from leucine (Leu) and isoleucine (Ile) . Aspergillic acid has antibiotic properties and was shown to be lethal to mice . The f... | B8N0E8 |
Q9XXJ0 | DHYS_CAEEL | Deoxyhypusine synthase | Caenorhabditis | MSTNEAAASQEDIALAQGAVLVKSCQVPDGSIPIRGFDFSTASGPDFSLSAILSSYMSTGFQATHLAQAIQQVNQMLSLRDTPLTCDDDEKLFPYPEGRQKRSCTIFLGYTSNLVTSGLREVLRYCVQRNLVDCIVTSAGGIEEDLIKCLKPSYLGTFTMDGAKLRSNGMNRAGNVLIPNDNYCAFEDWLMPILDECLVEQEEKHLNWTPSKLIQRLGERIGDESSILYWAAKHRIPVFCPALTDGSLGDMLYFHSVKSSPGLRVDIVEDVRHINTIAVKSFKTGSIILGGGVVKHHINNANLMRNGADHTVYINTGQEF... | Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. This is the first step of the post-translational modific... | Q9XXJ0 |
P97052 | NHAB_PSEPU | Nitrile hydratase subunit beta | Pseudomonas | MNGIHDTGGAHGYGPVYREPNEPVFRYDWEKTVMSLLPALLANANFNLDEFRHSIERMGPAHYLEGTYYEHWLHVFENLLVEKGVLTATEVATGKAASGKTATRVLTPAIVDDSSAPGLLRPGGGFSFFPVGDKVRVLNKNPVGHTRMPRYTRAKWGQWSSTMVCFVTPDTAAHGKGEQPQHVYTVSFTSVELWGQDASSPKDTIRVDLWDDYLEPA | NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. | P97052 |
O74522 | ADN3_SCHPO | LisH domain-containing protein adn3 | Schizosaccharomyces | MADFMDIEPSSHSAKASQYESSAPASSSLGNSHPNESLDYYIYDYFVKHNFEEAAQAFLRESKIQIPKSSSSTAFSPSNNNAPSPFPPKNSSLASPSKISESISGDRLYNHMSSAPSPNKKEETNVVHANEDISLDKRQSFGSSSLPPSEVSINVPEGFLVEWFNIFWDVFSARVSRVNSTPIQLYDPSTQRQMARPMSNLQASQPVPSSTFSRSAVVPNPSLPLNPSVLQGQVMNNPTIPKGTPSTSIEGAKTSIPPSHAMQNPHNSFPASADRLQKNHPVQSSNFNPYTPAPSITVPPNYIPNTAMMGPSYSSFGDTD... | Probable transcriptional regulator involved in cell adhesion. | O74522 |
A5GV56 | ATPE_SYNR3 | F-ATPase epsilon subunit | unclassified Synechococcus | MALTLRVLCPDQNVFDGQADEVILPSTTGQLGVLPGHVSLLTALDVGVLRMRDGNQWTAIALMGGFAEVDDDEVSVLVNAAEPASGINAEEAQKQLSEAEQAWSKFDGQPNSPDKIKAQQAFQKARARLQATKAN | Produces ATP from ADP in the presence of a proton gradient across the membrane. | A5GV56 |
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