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 |
|---|---|---|---|---|---|---|
Q9RYU5 | MURQ_DEIRA | N-acetylmuramic acid 6-phosphate lyase | Deinococcus | MTDPRRTEQVHPDYADLDTLAPDALIAALADDQLGAVRAVQAAAPQLTAALNAAVPQLERGGRLVYVGAGTSGRLGVLDATELTPTFSWPPERAVPLIAGGERAIRQAVEGAEDDEAAGERDVQAVNIGPDDVLIAVAASGTTPYVLGAARSGRAAGALTVGLANNPGAPLLAAVDCPVLLDTGPEIISGSTRLKAGTAQKIALNTLSSALMVRLGKLYGNLMVDVRATNAKLEDRARRLVQHATGADADAAQAALSECGGSVKTALVMLKLGLGAQEAAQRLEGAGGHARQVLGEGEALGTSAS | Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. | Q9RYU5 |
Q92BE4 | PFKA_LISIN | Phosphohexokinase | Listeria | MKRIAILTSGGDAPGMNAATRAVVRKAIYEGLEVYGINYGFLGLVNGDIRKLELGSVGDLLHRGGTFLYSARYPEFATEEGQLKGIEQLKKHQIDGLVVIGGDGSYHGAEALTKRGFPTIGIPGTIDNDISGTDFTIGFDTALNTVLDALDKIRDTATSHERTFIIEVMGRDAGDIALWSGLAGGAEAIIVPEESFNMDDVVDRLNKGRERGKKHSIIVVAEGVMSGNEFAKQLAEYGDYHARVTVLGHVQRGGSPTAFDRVLASRLGARSVELLLENRGGLAVGIRENRIVENNIGEILKEKHTLDQKLFDLASILSI | Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. | Q92BE4 |
P57977 | LIPB_PASMU | Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase | Pasteurella | MSNLSPLLVRQLGIQDYQTVWQQMQTFTDSRDVDTQDEIWLVQHPAVFTQGQAGKAEHLLQQTTIPVVQSDRGGQITYHGLGQQVMYVLVDIKRQKALGNEFNVRQLVSALEQAVVNTLADYGIHAYPKADAPGVYIDEKKICSLGLRIRKGCSFHGLALNINMDLSPFHFINPCGYAGLEMCQLADFIDPQQASCEKVAPKLVAHFAQLLGYNATNF | 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. | P57977 |
Q4K3A6 | ATPD_PSEF5 | F-type ATPase subunit delta | Pseudomonas | MAELTTLARPYAKAAFEHAQAHQQLASWSAMLGLAAAVSQDDTMQRVLKAPRLTSAEKASTFIEVCGDKFDAQAQNFIHVAAENDRLLLLPEISALFDLYKAEQEKSVDVDVTSAFALNQEQQDKLAKVLSARLGREVRLHAAEDASLIGGVVIRAGDLVIDGSIRGKLANLAEALKS | This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. | Q4K3A6 |
Q253S7 | NTPPA_CHLFF | Nucleotide pyrophosphatase | Chlamydia | MEPQLILGSSSPRRKSILQYFRIPFTCISPSFEERSVPYQGDPVAYSQELAVGKAESIVQDHNPEGVILTADTVVIYKGKVFNKPGSHDEAIEMLKTLSGQTHSIITSVALLQQKKLMVGQETTQVTFNKLPEEYLGRYVEAFSTLDKCGGYSTQEGGGLIIHNIQGCAYNVQGLPIRTLYHLLLEFDINLWDYLV | 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. | Q253S7 |
Q83C29 | SSRP_COXBU | Small protein B | Coxiella | MNKQISKKPAQRTIALNKKALHDYYVEQRFEAGLVLEGWEVKSIRAGRVQLRDSYVVFKGGEAWLIGAHLSPLPNVAEYMKADPQRSRKLLLNKREIGKLFGAVQKQGLTVVPLDLHWHKNHVKVEIVLAKGKKTHDKRETIKRREWEREKHRVLKSHG | Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemb... | Q83C29 |
B5EXM8 | RECR_SALA4 | Recombination protein RecR | Salmonella | MQTSPLLTQLMEALRCLPGVGPKSAQRMAFTLLQRDRSGGMRLAQALTRAMSEIGHCADCRTFTEQDVCNICSNPRRQENGQICVVESPADIYAIEQTGQFSGRYFVLMGHLSPLDGIGPDDIGLDRLEQRLASEKISELILATNPTVEGEATANYIAELCAEAGVEASRIAHGVPVGGELEMVDGTTLSHSLAGRHKIIF | 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. | B5EXM8 |
Q59244 | LDH_BACCL | L-lactate dehydrogenase | Geobacillus thermoleovorans group | MKNNGGTRVVVIGTGFVGASYAFALMNQGIADEIVLIDANESKAIGDAMDFNHGKVFAPKPADIWHGDYDDCRDADLVVICAGANQKPGETRLDLVDKNIAIFRSIVESVMASGFQGLFLVATNPVDILTYATWKFSGLPHERVIGSGTILDTARFRFLLGEYFSVAPQNVHAYIIGEHGDTELPVWSQADIGGVPIRKLVESKGEEAQKELERIFVNVRDAAYQIIEKKGATYYGIAMGLARVTRAILHNENAILTVSAYLDGPYGERDVYIGVPAVINRNGIREVIEIELNDDEKNRFHHSAATLKSVLARFFTR | Catalyzes the conversion of lactate to pyruvate. | Q59244 |
P0CO59 | LIPA_CRYNB | Lipoic acid synthase | Cryptococcus neoformans species complex | MVKLPSASRIRSLATVPSTATRAFATVNPTPPAAQPTKSKPRFEKLDDGLTFDDFLSGDVPPENERVVLGNTKQPRLPSFLKHPIPTGASYSGIKKELRGLGLHTVCEEAKCPNIGECWGGGKGNATATIMLMGDQCTRGCRFCSVKTSRAPPPLDVHEPENTAEAISRWGLGYIVLTSVDRDDLVDGGAAHIASTISKIKQKAPNILVEALTPDFATKGVNVIHTVASSGLDVFAHNVETVERCTPFVRDRRAGFSQSLKVLEEAKKGAKAAGREILTKSSIMLGVGEMEEEIHETLRRLRASDVDVVTFGQYMRPTKR... | Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. | P0CO59 |
Q0DHJ5 | MTP6_ORYSJ | Metal tolerance protein 6 | Oryza sativa | MAAAAGVAAGTGRGSGEGEELLPNAVEGDGGCGGGGTCAGDRPWRLNFDGLRRPEAHQEKPPRRFHDRLGGLVQSPGDDVAEYYQQQSELLEGFNEMDTLTDRGFLPGMSKEECEKVARSEALAIRLSNIANMVLFAAKVYASIRSGSLAIIASTLDSLLDLLSGFILWFTAFSKKTSNPYRYPIGKRRMQPLGILVFASVMATLGLQIILESTRSLFYDGDTFRLTKEQEKWVVDIMLSVTSVKLLLVVYCRSFTNEILAIYTIRTWSMTVLENVHSLVGQSASPEYLQKLTYLCWNHHKAVRHIDTVRAYTFGSHYFV... | Involved in sequestration of excess metal in the cytoplasm into vacuoles to maintain metal homeostasis. | Q0DHJ5 |
B7GQ87 | DTD_BIFLS | Gly-tRNA(Ala) deacylase | Bifidobacterium | MKVVLQRVSEASVDVVNELGTLDPTFEPQQIGPGFMILVGVTDEDGDKQIAWLAHKILNLRVFEDAQGKMNRSIQDIGGEILSISQFTLFADVHKGNRPSFIKAGKPEHADLMWIKFNEALRSGGVPVKEGRFGAHMRVGLVNDGPVTIVIDTEHDMPDGTR | An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By rec... | B7GQ87 |
C4KGR1 | CCA_SULIK | tRNA-NT | Sulfolobus | MIEEEVLKIIKPTEEDKKGIEKVLEIIRERLNKLDFEVEGSFRKGTWLRQDTDIDVFVFYPKDVGKEYLERNALNDIINRIKDLDYTLAYAEHPYVIVNINNVEVDIVPALRVESGDKAITAVDRTPFHTKYVTSHLDERGKDEVRLLKRFMKGIGVYGAELKVQGFSGYATELLIIYYGNFRKVLEEASKWKHPIKIELTKPMKIFSEPLIIPDPVDPKRNVTAAVSLKNIATFSIAAKYYLKNPSIEFFFPSKKVEEKVKGDVLILRLNLDEKSSEDIVWGQIKRSVNKIERALKQYGFRVIDVQAWGDTNNITIAVQ... | 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. | C4KGR1 |
Q2IPE3 | TTCA_ANADE | tRNA 2-thiocytidine biosynthesis protein TtcA | Anaeromyxobacter | MQQIHRLERKLLRATAEAIRDFDLVSQGDRIMVAVSGGKDSYTLLHLLMRLRERAPIDFDLVAVNLDQGQPGFPAHVVEDHLRSLGVPYRMLQRDTYSVVRRLVPEGKTTCPVCSRLRRGVLYNAAVEMGCTKIALGHHRDDLVETLLLSALYSGALKSMPPKLRSRDGRNVVIRPLCYAAEEDVAAFAEAMRFPIVPCDLCGSQPNLRRKRVKRLLAELSAEHPAVKGNLLHALGHVVPSHLLDRDLHRQLADATGRDPWLDAEDEEAEDCGEPAGDGVVSLGGARGGR | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | Q2IPE3 |
A8FG01 | UVRC_BACP2 | Excinuclease ABC subunit C | Bacillus | MNKLIKEKLSVLPDQPGCYLMKDRQNTVIYVGKAKILKNRVRSYFTGSHDAKTQRLVSEIEDFEYIVTSSNIEALILELNLIKKYDPKYNVMLKDDKTYPFIKITNERHPKLIVTRHVKKDKGKYFGPYPNVQAARETKKLLDRLYPLRKCATLPDRVCLYYHLGQCLAPCVYDISEETNKQLVDEIIRFLNGGHQQIKKELTEKMQEAAEQLEFERAKELRDQIAYIDSTMEKQKMTMSDLSDRDVFAYAYDKGWMCVQVFFIRQGKLIERDVSLFPMYQDPEEEFLTFMGQFYSKNNHFLPKEILVPDSVDQEMIEQL... | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | A8FG01 |
Q4AC94 | C2CD3_HUMAN | C2 domain-containing protein 3 | Homo | MKQRKGQGSGGSRGRKKRGLSDISPSTSLPPLVEGQLRCFLKLTVNRVIWKIAKPPTCVLVRVRWWGETSDGTLFCPRDALQTEPKAVRTTTRYAIRCGPKQFTSYLTDMAVLVLEVITKLDGLPIGRVQINGLAQLSPTHQINGFFTIVSSTSKKLGELQVSLALEPLSETYDSYHPLPTTDMTENVLLSKQGFRENTEPSSTQFQVPSRPRDIHTIKIDGKELAANSSRSTTPRGKDHVCFAENPDTIKDSSFGLQHSLNSGQSLESVTLKGRAPRKQMSLLNSSEFQPQIRTVAKSHSDSCILSSNNLPTKDLLSAL... | Component of the centrioles that acts as a positive regulator of centriole elongation . Promotes assembly of centriolar distal appendage, a structure at the distal end of the mother centriole that acts as an anchor of the cilium, and is required for recruitment of centriolar distal appendages proteins CEP83, SCLT1, CEP... | Q4AC94 |
P97927 | LAMA4_MOUSE | Laminin-9 subunit alpha | Mus | MGWSTAWCSVLALWLLWCAVCSNAASGDGNAFPFDIEGSAVVGRQDPSETSDSGVTLGRLPPAAERCDAGFFRTLSGECAPCDCNGNSHECLDGSGFCLHCQRNTTGEHCEKCLDGYIGDSIRGTPRFCQPCPCPLPHLANFAESCYRKNGAVRCICKENYVGPNCERCAPGYYGNPLLIGSTCKKCDCSGNSDPNLIFEDCDEITGQCRNCLRNTTGFKCERCAPGYYGDARTAKNCAVCNCGGGPCDSVTGECLEEGFEVPTGCDKCVWDLTDDLRLAALSIEESKSGLLSVSSGAAAHRHVTDMNSTIHLLRTRLSE... | Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. | P97927 |
P47201 | SODM_MYCAV | Superoxide dismutase [Mn] | Mycobacterium avium complex (MAC) | MAEYTLPDLDWDYAALEPHISGQINEIHHTKHHATYVKGVNDALAKLEEARANEDHAAIFLNEKNLAFHLGGHVNHSIWWKNLSPDGGDKPTGELAAAIDDAFGSFDKFRAQFSAAANGLQGSGWAVLGYDTLGSRLLTFQLYDQQANVPLGIIPLLQVDMWEHAFYLQYKNVKADYVKAFWNVVNWADVQKRYAAATSKAQGLIFG | Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. | P47201 |
Q0IEY3 | EIF3B_AEDAE | Eukaryotic translation initiation factor 3 subunit 9 | Stegomyia | MAKKKGENYDSDGGDDQDYDEEPNFDDPEGFVDDVSDEELLGDFLKQKPCESDGVENVIVVDNIPVVGPARFHKLQGVLEKLFKTAGTIVNIHYPKDDEENTRGYAFIEFKNPEMAEEAVKAFNNYRLDKSHTLLVNLFSDFQKYSDIPKEWSPPEPQPYKMQNDLYNFITEPDAQDQFCVIAESSPGAVQVQFWQNTQPEPVELLTRDRFTETYVKWSPLGTYIVTFHKQGVVIWGGSNFTKINKFPHSGTQYVDFSPCEQYLVTYGPNGQKIIIWDIRTGTEKRSFISDGTSNMSMFRWSHDDKYVARMGDNAIHVYE... | 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... | Q0IEY3 |
C0ZKI1 | PIP_BREBN | Prolyl aminopeptidase | Brevibacillus | MRMQEGYIEVPGGRVWYSRVGEGEKTPLIVLHGGPGNTHDPLKSTLHVLGDDRPVIFYDQLGSGNSDRPTDLTLWKTERFVEELACIRQALDLKEVHILGHSWGTMLAAAYLVDAKPEGVQSIIFSSPCLSAERWKQDADRLIEQLPVDTQQTIATHEEQGTTDSQEYQDAMKEYYKRHVCRLDPMPTVMTESRPKANKEVYMTMWGPSEFCPTGNLKTFDYTPQLHQINIPSLFVCGRYDEATPESTGYYQSLVPKAELHVFENSSHVGYLEETDEYVQVIRRFLQKAESK | Releases the N-terminal proline from various substrates. | C0ZKI1 |
Q2YSC4 | RL11_STAAB | 50S ribosomal protein L11 | Staphylococcus | MAKKVDKVVKLQIPAGKANPAPPVGPALGQAGVNIMGFCKEFNARTQDQAGLIIPVEISVYEDRSFTFITKTPPAPVLLKKAAGIEKGSGEPNKAKVATVTKDQVREIANSKMQDLNAADEEAAMRIIEGTARSMGIVVE | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | Q2YSC4 |
Q52950 | FLGH_RHIME | Basal body L-ring protein | Sinorhizobium | MRTRITAVLAAGLLAGCQNQAFNEIGRAPAMSPIGSGLQYTQTPQLAMYPKQPRHVTNGYSLWNDQQAALFKDARAINIGDILTVDIRIDDKASFENETDRSRKNSSGFNLGASGQSQTSDFAWSGDLEYGSNTKTEGDGKTERSEKLRLLVAAVVTGVLENGNLLISGSQEVRVNHELRILNVAGIVRPRDVDADNVISYDRIAEARISYGGRGRLTEVQQPPWGQQLVDLVSPL | Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | Q52950 |
Q5E9T4 | TPK1_BOVIN | Thiamine pyrophosphokinase 1 | Bos | MEHAITPLDPLLPSGSLKYCLVILNQPLDKCFRHLWHKALLRACADGGANHLYDVTEGERESFLPEFISGDFDSIRPEVREHYAIKGCEIISTPDQDHTDFTKCLEVLQKKIEEKDLQVDMIVTLGGLAGRFDQIMASVSTLFQAPQITSLPVIIIQEESLIYLLQPGKHKLHVDTGMEGDWCGLIPVGQPCNQVTTTGLKWNLTHQMLGFGTLVSTSNTYDGSGVVTVETDHPLLWTMAIKN | Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. Can also catalyze the phosphorylation of pyrithiamine to pyrithiamine pyrophosphate. | Q5E9T4 |
Q3SK77 | PYRF_THIDA | OMP decarboxylase | Thiobacillus | MTHKIIVALDFPAGAPALALADRLDPARCRLKVGKELFTAAGPDLVRALVARGFEVFLDLKFHDIPNTVAAACRAAAGLGVWMLNVHAAGGRRMMDAAREALESLPPGDGAADTPQRPLLIAVTVLTSMSAGDLAETGVADTPAEQVMRLARLAHACALDGVVCSAQEAAGLRAALGADFRLVTPGIRPAGAAAADQRRVMTPVEALRAGATDLVIGRPITGAGDPLAALAAIQADIEENLGRAF | Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). | Q3SK77 |
Q9ZCH1 | FABH_RICPR | 3-oxoacyl-[acyl-carrier-protein] synthase III | typhus group | MTCKIIGSGGYLPPKIISNDELTKFVDTNDKWIRTRTGILQRHIAGDAEYTSHLAFKSAQKAIEDAMISVDDIDLIIICTTTPDNSFPSVATKLHGYLGLTNIPSFDLQAVCAGFIYGLQLAHSLIVSGKYKTILLIGAEKMTSLLDWNDRSTCVLFGDGAGSVILQRSNDDSGLIDSNIFSSGTDYEILYTSGGTSMNGTSGKIVMQGQKLFRHAIEKMLQSIEDLLYANQFSVSDIDYFIPHQANIRIINKLAELLNIEEHKVVKTVEKHANCSAASIPLALSALKESGKIKKGDILLFSAIGAGLTWGGALIRW | 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... | Q9ZCH1 |
A8I0Y1 | DABA_AZOC5 | Probable inorganic carbon transporter subunit DabA | Azorhizobium | MLMTTPGSPLPSPDVLLEAANRAARAIPPLWPLASSVAVNPFLGQTGEPLATAASRLRRVAGIPLTMPRSWYADRLRSGEIAEEDLRAAFESAPAALRPKTFASLKRAVQSERPEPHAIPTLADLARDVAGIDWPAIVNDRISHWASSYFDEGQALWAKGQQGAAYSAWRIIATHDLTPEIAGLEGFAQSVADAPANAEDAIIACVARLGLCGPALESYFHRLLTTLGGWSQLARYRLWQAELTGNTDASVTDLLTIRLIWEAALLRKFGPVVEAQWKAAIAAYAEPVSATPEDVVDAILQEAAERAAQWRLGACLTGTS... | Part of an energy-coupled inorganic carbon pump. | A8I0Y1 |
B4T0X0 | ARGB_SALNS | NAG kinase | Salmonella | MNPLIIKLGGVLLDSEEALERLFTALVNYRESHQRPLVIVHGGGCVVDELMKGLNLPVKKKDGLRVTPADQIGIITGALAGTANKTLLAWAKKHHIASVGLFLGDGDSVNVTQLDEALGHVGLAQPGSPKLINMLLENGFLPVVSSIGVTDDGQLMNVNADQAATALAATLGADLILLSDVSGILDGKGQRIAEMTASKAEQLIDQGIITDGMIVKVNAALDAARALGRPVDIASWRHAEQLPALFNGTPIGTRILA | Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. | B4T0X0 |
E2A6Z3 | ALLSC_CAMFO | Allatostatin C | Camponotus | MSSVRNIAALALVLLVLAEWSAAMPTTDKDKERLLNTVDLIDDDGSIETALINYLFTKQIVKRLRSQLDIGDLQRKRSYWKQCAFNAVSCFGK | Inhibits juvenile hormone biosynthesis. | E2A6Z3 |
Q07KN2 | RS8_RHOP5 | 30S ribosomal protein S8 | Rhodopseudomonas | MSTHDPISDLITRIRNAQMRAKSKVSTPGSKMRANVLEVLKSEGYIRGYATLEHASGRSEIEIELKYFDGEPVIREIERVSKPGRRVYASVKNLPRVNNGLGISVLSTPKGIMADHEARDANVGGEVLFTVF | 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. | Q07KN2 |
P12031 | HCYB_HELPO | Hemocyanin, beta-C chain unit D | null | DAVTVASHVRKDLDTLTAGEIESLRSAFLDIQQDHTYENIASFHGKPGLCQHEGHKVACCVHGMPTFPSWHRLYVEQVEEALLDHGSSVAVPYFDWISPIQKLPDLISKATYYNSREQRFDPNPFFSGKVAGEDAVTTRDPQPELFNNNYFYEQALYALEQDNFCDFEIQFEVLHNALHSWLGGHAKYSFSSLDYTAFDPVFFLHHANTDRLWAIWQELQRYRGLPYNEADCAINLMRKPLQPFQDKKLNPRNITNIYSRPADTFDYRNHFHYEYDTLELNHQTVPQLENLLKRRQEYGRVFAGFLIHNNGLSADVTVYV... | Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods. | P12031 |
A0A1S3ZP85 | OBL1_TOBAC | Oil body lipase 1 | Nicotiana | MASTKIDDKVSIPGPVTGTGNSRFLIVSHENGGIWDLVRFGVWGNKESGDKFLHYSAGGGLLEEHLVRSDDSGGGDDRGGEVPDHRWVIFVSIIVRKLIAIFGKPMEWTGYLVEFFLNLFSLNGNFLGLLYNILHGKVVMPHRGSETFISAIGHLDGRINLYKSETLTKEIGEPDFWQKIGIGHRDLMDLCMMASKLAYENEKVVRNVVNLHWKMHFVDFYNCWNDFEKEMSTQVFLLCDKPKDANLILVSFRGTEPFDADDWITDFDYSWYEIPKLGKVHMGFLEALGLGNRTNASTFHEQLFVNNLKFANLENVHATI... | Acid lipase that can hydrolyze a range of triacylglycerols without a clear preference for acyl-chains . Can also cleave 1,2-diacylglycerol, 1,3-diacylglycerol and 1-monoacylglycerol, but not phospatidylcholine, phosphatidylethanolamine, or sterol esters . Required for pollen tube growth . Triacylglycerol hydrolysis by ... | A0A1S3ZP85 |
Q58842 | FAEHP_METJA | D-arabino-3-hexulose-6-phosphate formaldehyde lyase | Methanocaldococcus | MIKFGEAVLGNEIKAIVNVALGKGELIENTFTNALTRGNCVFANLRPNLIVKPLTLVVPRHNIESEIQDELFQGVIQYAVAKAVADLDLDEDLKVVVSVNVPEVPITNLNKRKLFQYFYASAKLAINRALNEYPSKEKVKKEKYRALHPLVGFRDVRLEYPPYLQIALDVPTMENLEFLLQTIPNSDHIILEAGTPLIKKFGLEVIEIMREYFDGFIVADLKTLDTGRVEVRLAFEATANAVAISGVAPKSTIIKAIHECQKCGLISYLDMMNVSEPQKLYDSLKLKPDVVILHRGIDEETFGIKKEWKFKENCLLAIAG... | Catalyzes the reversible formation of ribulose-5-phosphate and formaldehyde from 3-hexulose-6-phosphate. | Q58842 |
P52923 | AIF1_YEAST | Cercosporin and photosensitizer-detoxification protein 1 | Saccharomyces | MTINTKNIVVVGAGVFGVSVANHLYRELGGTYAIKLVTASNYVYFLPSAVRLTVSKDYTKSILPLKNVLDSGIEVIKDTAASFDDKEVVLGSDRAIKFDILVLATGSKWADPIGSTYTFGDNYKEYFEREASRISDADHILFLGGGFVNCELAGELLFKYLEEIRSGKKRISIIHNSDKLLPDSGLYNDTLRKNVTDYLSKNGITLYLNTVGASLDTSPKRIFLGEGSSKYIDADLIYRGVGISPNVPVNSISDLCDKKGFIQVEKNFRVKAVEAGNVFAIGDVTNFRYHGLVKRDNWVDVLTRNVISSLQEGTEASLVD... | Putative FAD-dependent oxidoreductase involved in the resistance to cercosporin and other singlet oxygen-generating photosensitizers. Translocates from mitochondria to the nucleus under apoptotic conditions, where it degrades DNA and induces apoptosis. | P52923 |
A0QSB6 | MFTA_MYCS2 | Mycofactocin precursor peptide | Mycolicibacterium | MEPNQHVEAETELVTETLVEEVSIDGMCGVY | Precursor peptide that leads to mycofactocin (MFT) after extensive post-translational modifications by enzymes encoded by adjacent genes. Mycofactocin acts as a redox cofactor of nicotinamide-dependent oxidoreductases encoded in the same locus . Is required for the in vivo ethanol assimilation in M.smegmatis . | A0QSB6 |
P04915 | H4_PHYPO | Histone H4 | Physarum | MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISNTIYEETRGVLKTFLENVIRDAVTYTEHARRKTVTAMDVVYALKRQGRTLYGFGG | 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... | P04915 |
A6VA50 | DPO4_PSEA7 | DNA polymerase IV | Pseudomonas | MRKIIHIDCDCFYAALEMRDDPSLRGKALAVGGSPDKRGVVATCSYEARAYGVRSAMAMRTALKLCPDLLVVRPRFDVYRAVSKQIHAIFRDYTELIEPLSLDEAYLDVSASPHFAGSATRIAQDIRRRVAEELRITVSAGVAPNKFLAKIASDWRKPDGLFVITPEQVDGFVAELPVAKLHGVGKVTAERLARMGIRTCADLRQGSKLSLVREFGSFGERLWSLAHGVDERPVEVDSRRQSVSVECTFDRDLPDLAACLEELPALLEELDGRLLRLDGSYRPDKPFVKLKFHDFTQTTLEQAGAGRDLDSYRQMLGQAF... | Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in... | A6VA50 |
P15781 | PSPB_BOVIN | Pulmonary surfactant-associated proteolipid SPL(Phe) | Bos | MAKSHLLPWLLLLPILCGPGTAAAITYSLACAQGPEFWCQSLEQALQCRALGHCLQEVWGHVEADDLCQECENISRLLTKMAKEAIFQDSVRKFLEQECDVLPLKLLAPLCRHLLDTYFPLIIEHFQSHMNPKFICQHVGLCKPRHPEPGKGPEPWGPLLDKLALPLLPGVPQAKPGPQTQDLSEQLFPIPIPYCWLCRTLIKRIQAVIPKGVLAMTVAQVCHVVPLLVGGICQCLVERYSVILLDTLLGRMLPQLVCGLVLRCSSEDSAGPALPALGSVPGEWLPQDSDCQLCMFVTTQAGNSSEQATPQAMRQACLGT... | Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter. | P15781 |
Q5AGV7 | PFA4_CANAL | Protein fatty acyltransferase 4 | Candida | MAVQLKWPILGVIIPCIIIFSLSYGSHYFILRHHLTMKQQLIYEFYVTMIWISYLLAIYTNPGRVPKNYKPSLASSTRIEQTEDDSDGLGLESREDETLIREEPISGDRCEWIRYCKKCNNYKPPRSHHCKICQQCVLQMDHHCPWTLNCVGNNNLPHFMRFLGWIIWGTGYLMIQLIKLIINYYENSNMPHYLFNKTELVAIIAITPLNFFVFASILVLFIRCLINICKGMTQIEIWEWERLELQWSSKRLWRLIRFNYGRLHKGKPFPELNTWTNTTNNVNYNDNDDDGDEDVELINLATNNNEDSTIVPQNFTIDDL... | Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function. | Q5AGV7 |
A6VR61 | YIDC_ACTSZ | Membrane protein YidC | Actinobacillus | MNSSRSLLALALLFISFLVYQQWEIDKAPKPVVRETAVSQSDTPNSSSASTSAVDSQAKGRVITLQNDVFRLKVDTLGGDVIESELLNYAQELNGEERFTLLENKDGTTYVAQSGLVGKNGIDSAAGRADYQVNGDNFVLAEGQDELSVPFTFEKDGVIYRKIFMLKRGSYDIAVNYEIRNQSDETIEVQPYGQLKHTLVESSGSMAMPTYTGGAYSSSETNYKKYSFDDMKGANLSVNTKAGWVAVLQHYFVSAWIPNQDADNQLYTTTNNGMGFIGFRGPTVTVPAGATETVKTALWTGPKLQNQMGEVAEHLDLTVD... | Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning memb... | A6VR61 |
B7HDF8 | KDPA_BACC4 | Potassium-translocating ATPase A chain | Bacillus cereus group | MIWVAVIITMLLFILVAKPTGVYLEKAFQGSKTLDKVFGPFEKLIFKITGVKEYNQTWKQYALSLVLLNGFMIVVVYFIFRLQGVLPLNPAHIEGMEPTLAFNTAISFMADTNLQHYSGENGLSYLSQLIGITFLMFAAPATTLALVMAFIRGLAGKELGNFFVDFTRALTRVFLPIAFIAALVFVALGVPQTLDGAVTAQTIDGAKQSILRGPVASFVSIKELGNNGGGFFGANSTHPFENPGQMSNILQMMLMMLLPTALPFTYGRMVGNKKQGRILFVSLFMVFLLGFITITTSELNGNPALNGMGIEHVQGSAEGK... | 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... | B7HDF8 |
Q7MWH4 | LPXK_PORGI | Lipid A 4'-kinase | Porphyromonas | MDAPRINKWLKPLSALYGVGVRLRNYLFDKNVLISNSFDIPIVCVGNITIGGTGKTPHVEYLIRLLHPRYRVAVVSRGYKRKTKGMIVATEGSTAWDIGDEPRQIKRKYPDLTVIVDADRSRAIGYLCDLAEEQRPQLIVLDDGFQHRKVKADLNIVLTDYNRILTKDYLLPAGRLREPAGSIQRADMVILTKCPDDLAPIDLRAAKRDLALYPHQKLFFSKFLYGQGLKPLFSDQSPSAEVRSALAIAGIASPKLFFREIRTRFPSGTDRIYPDHHEFTDREICLLIQDWHELHRKDANAIVVCTEKDAMRLALRQSSF... | Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). | Q7MWH4 |
B5Z9Y1 | DAPE_HELPG | N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase | Helicobacter | MNALEITQKLISYPTITPKECGIFEYIKSLFPAFKTLECGENGVKNLFLYRIFNSPKEHAEKEHAKEKHAKENVKPLHFCFAGHIDVVPPGDNWQSDPFKPIIKEGFLYGRGAQDMKGGVGAFLSASLNFNPKTPFLLSILLTSDEEGPGIFGTRLMLEKLKEKNLLPHMAIVAEPTCEKVLGDSIKIGRRGSINGKLILKGVQGHVAYPKKCQNPIDALASVLPLISGVHLDDGDEYFDPSKLVITNLHAGLGANNVTPGSVEITFNARHSLKTTKESLKEYLEKVLKDLPHTLELESSSSPFITTSHSKLTSVLKENI... | Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. | B5Z9Y1 |
Q0TQ38 | DPO4_CLOP1 | DNA polymerase IV | Clostridium | MKENRKIIHIDMDAFYASIEQRDNPKYKGKPLIVGGDPNRRGVVATCSYEARKYGIHSAMPSLTAYKLCPKAIFIRPRMEVYKKVSRQVMNILNEYSNLVEHLSLDEAFVDVSKSKRCKGSATLMALEIKERIFKEVGLTASAGVSFNKFLAKMASDFRKPDGITVITEENSKDFIRNIPIGKFFGVGRVTKNKLNNIGVFKGEDLLKFSEEELIDIFSDRGKILYEFARGIDNRPVNPYRIRKSIGKEITLREDIEDIDEMIEILERIAERVSESLCLLNKKGKTVTLKVKFNDFKHITRSITLEHFLKEQKEIMECVK... | Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in... | Q0TQ38 |
A5VDM3 | DEF_RHIWR | Polypeptide deformylase | Rhizorhabdus | MAIRLILEAPDPRLRTISTPVEAVDDELRALIADMFETMYDAPGIGLAAIQVGVPKRVLVIDLQEEEDAEGKPIRHPRVFINPELFDPSEEQSVYNEGCLSVPEQYAEVERPAVIHARWLDEQGAKHEERLEGLLATCLQHEMDHLEGILFIDHLSRLKREMVMKKLEKARRARKAA | 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. | A5VDM3 |
Q9Y5J3 | HEY1_HUMAN | Hairy-related transcription factor 1 | Homo | MKRAHPEYSSSDSELDETIEVEKESADENGNLSSALGSMSPTTSSQILARKRRRGIIEKRRRDRINNSLSELRRLVPSAFEKQGSAKLEKAEILQMTVDHLKMLHTAGGKGYFDAHALAMDYRSLGFRECLAEVARYLSIIEGLDASDPLRVRLVSHLNNYASQREAASGAHAGLGHIPWGTVFGHHPHIAHPLLLPQNGHGNAGTTASPTEPHHQGRLGSAHPEAPALRAPPSGSLGPVLPVVTSASKLSPPLLSSVASLSAFPFSFGSFHLLSPNALSPSAPTQAANLGKPYRPWGTEIGAF | Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGTG-3' . Downstream effector of Notch signaling required for cardiovascular development. Specifically required for the Notch-induced endocardial epithelial to mesenchymal transition, which is itself criticial for cardiac valve an... | Q9Y5J3 |
Q8D889 | RNFB_VIBVU | Rnf electron transport complex subunit B | Vibrio | MTTIMIAVLAIALLATLFGAILGFASIRFKVEADPIVDQIDAILPQTQCGQCGYPGCRPYAEAIANGDSINKCPPGGQATIEKLADLMGVEAEESAHDLEGKVKKVAFIHEDMCIGCTKCIQACPVDAIVGGTKALHTVIKDECTGCDLCVAPCPTDCIEMIPLETTTETWKWQLNAIPVVNISEANPNSATSRDQNN | Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. | Q8D889 |
Q8D3T7 | NADE_VIBVU | NH(3)-dependent NAD(+) synthetase | Vibrio | MEQLIRDEMRVLPTIDPHFEIERRVAFIKKKLVESGCKSLVLGISGGVDSTTCGRLAQVAVDQLNQESNSNDYQFVAVRLPYGEQKDEEEAQLALSFIQPTHSVSVNIKAGVDGLHAASHIALEGTGLIPQDAAKVDFVKGNVKARARMVAQYEIAGYVGGLVLGTDHSAENITGFYTKFGDGACDLAPLFGLSKRQVRLVAETLGAPELLVKKVPTADLEELAPQKADEDALNLTYEQIDDFLEGKPVSEAVSARLVSIYKATQHKRQPIPTIYD | Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. | Q8D3T7 |
Q5QVM3 | YQGF_IDILO | Putative pre-16S rRNA nuclease | Idiomarina | MSTVIGFDFGTKSIGVAVGQTITATASPLAAITAKEGIPDWQLIEKLFAEWQPEQLVVGLPLNMDGTEQPLTQKAKKFGNRLHGRFGLPVAFQDERLTSTSARESLFAEGGFRKLKKGAVDSQAALIIVEDFMNGYLPKSDNSL | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | Q5QVM3 |
Q5NLZ3 | SYY_ZYMMO | Tyrosyl-tRNA synthetase | Zymomonas | MTQFRSDFLRLLETRGYIHQITDAKSLDEKASQSVIAAYIGFDPTAASLHVGSLLQIMMLRRLQQAGHKPIVLMGGGTGKIGDPSFKDEARKLLDEDTIKANIASIKRVFEHFLHFGDGENDAVMVDNAEWLDRLEYIPFLRDVGQHFSVNRMLSFDSVKLRLDREQSLSFLEFNYMILQAYDFLELSRRFGVCLQLGGSDQWGNIVNGIELARRMDGKEVFGLTSPLMTTADGVKMGKTVGGAVWLNGDMCSPYDYWQFWRNTHDADVERFLKLFTDLPLDEIARLAALEGSEINEAKKILANEATKLAHGEKAAEEAA... | Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). | Q5NLZ3 |
Q16134 | ETFD_HUMAN | Electron-transferring-flavoprotein dehydrogenase | Homo | MLVPLAKLSCLAYQCFHALKIKKNYLPLCATRWSSTSTVPRITTHYTIYPRDKDKRWEGVNMERFAEEADVVIVGAGPAGLSAAVRLKQLAVAHEKDIRVCLVEKAAQIGAHTLSGACLDPGAFKELFPDWKEKGAPLNTPVTEDRFGILTEKYRIPVPILPGLPMNNHGNYIVRLGHLVSWMGEQAEALGVEVYPGYAAAEVLFHDDGSVKGIATNDVGIQKDGAPKATFERGLELHAKVTIFAEGCHGHLAKQLYKKFDLRANCEPQTYGIGLKELWVIDEKNWKPGRVDHTVGWPLDRHTYGGSFLYHLNEGEPLVA... | Accepts electrons from ETF and reduces ubiquinone. | Q16134 |
Q4V8J4 | GPAT3_RAT | Lysophosphatidic acid acyltransferase theta | Rattus | MEGTDLVVKLLSTWLTLVGSLILLPSAFGLSLGISEIYMKILVKTLEWATLRIEKGAPKESVLKSPASMGIIQRDESPMEKGLSGLRGRDFELSDVFYFSKKGLEAIVEDEVTQRFSSEELVSWNLLTRTNVNFHYISPKLTIVWVLGVLVRYCFLLPLRVTLAFIGISLLIIGTTLVGQLPDSSLKNWLSELVHLTCCRICVRSLSGTIHYHNKQYRPQKGGICVANHTSPIDVLILATDGCYAMVGQVHGGLMGIIQRAMVKACPHVWFERSEIKDRHLVTKRLKEHIADKKKLPILIFPEGTCINNTSVMMFKKGSF... | Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) by incorporating an acyl moiety at the sn-1 position of the glycerol backbone. Also converts LPA into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the gl... | Q4V8J4 |
Q1ICV9 | LEUD_PSEE4 | Isopropylmalate isomerase | Pseudomonas | MKAFTQHIGLVAPLDRANVDTDQIIPKQFLKSIKRTGFGPNLFDEWRYLDVGQPYQDNSKRPLNQDFVLNHARYQGASVLLARENFGCGSSREHAPWALDEYGFRSVIAPSFADIFFNNSFKNGLLPIILDAAEVDELFKQVEATPGYQLTIDLEAQAVTRPDGKVLKFEIDAFRKHCLLNGLDDIGLTLQDSDAIKAFEGKHRASQPWLFRDA | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | Q1ICV9 |
A2SJD1 | RPOZ_METPP | Transcriptase subunit omega | Methylibium | MARITVEDCLTKIPNRFQLVLAATYRARMLSQGHAPKVESKNKPGVTALREIAEGHVGLEMLRKVPV | 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. | A2SJD1 |
B7N626 | HEM6_ECOLU | Oxygen-dependent coproporphyrinogen-III oxidase | Escherichia | MKPDAHQVKQFLLNLQDTICQQLSAVDGAEFVEDSWQREAGGGGRSRVLRNGGVFEQAGVNFSHVHGEAMPASATAHRPELAGRSFEAMGISLVVHPHNPYVPTSHANVRFFIAEKPGAEPVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCQPFGEDVYPRYKKWCDEYFYLKHRNEQRGIGGLFFDDLNTPDFDHCFAFMQAVGKGYTNAYLPIVERRKAMAYGERERNFQLYRRGRYVEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYHPEDGSPEAALSEFIKVRDWV | Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX. | B7N626 |
Q9VCS8 | OR94B_DROME | Odorant receptor 94b | Sophophora | MESTNRLSAIQTLLVIQRWIGLLKWENEGEDGVLTWLKRIYPFVLHLPLTFTYIALMWYEAITSSDFEEAGQVLYMSITELALVTKLLNIWYRRHEAASLIHELQHDPAFNLRNSEEIKFWQQNQRNFKRIFYWYIWGSLFVAVMGYISVFFQEDYELPFGYYVPFEWRTRERYFYAWGYNVVAMTLCCLSNILLDTLGCYFMFHIASLFRLLGMRLEALKNAAEEKARPELRRIFQLHTKVRRLTRECEVLVSPYVLSQVVFSAFIICFSAYRLVHMGFKQRPGLFVTTVQFVAVMIVQIFLPCYYGNELTFHANALTN... | Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged o... | Q9VCS8 |
A8Y9A9 | RK20_LOLPR | 50S ribosomal protein L20, chloroplastic | Lolium | MTRVPRGYIARRRRTKMRSFASNFRGAHLRLNRMITQQVKRAFVSSHRDRGRQKRDFRRLWITRINAATRIYKVFDSYSKLIHNLYKKKLILNRKMLAQVAVSNPNNLYTISNKIKIIN | Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. | A8Y9A9 |
Q5VUA4 | ZN318_HUMAN | Endocrine regulatory protein | Homo | MYRSSARSSVSSHRPKDDGGGGPRSGRSSGSSSGPARRSSPPPPPSGSSSRTPARRPRSPSGHRGRRASPSPPRGRRVSPSPPRARRGSPSPPRGRRLFPPGPAGFRGSSRGESRADYARDGRGDHPGDSGSRRRSPGLCSDSLEKSLRITVGNDHFCVSTPERRRLSDRLGSPVDNLEDMDRDDLTDDSVFTRSSQCSRGLERYISQEEGPLSPFLGQLDEDYRTKETFLHRSDYSPHISCHDELLRGTERNREKLKGYSIRSEERSREAKRPRYDDTVKINSMGGDHPSFTSGTRNYRQRRRSPSPRFLDPEFRELDL... | Acts as a transcriptional coactivator for AR-mediated transactivation function. May act as a transcriptional regulator during spermatogenesis and, in particular, during meiotic division. | Q5VUA4 |
Q55BI2 | IDHA_DICDI | Isocitrate dehydrogenase [NAD] regulatory subunit A, mitochondrial | Dictyostelium | MFSRKSLSIFSTLRNYSSSTSKIQKVTLIPGDGIGPEISESVKRVFSAVKAPIEWETVVVDANTGISKEVIESISKNKIGLKGPISTPIGTGHQSLNLGLRKTFNLYANIRPCLSIPGHKTRYNNVNTVVVRENTEGEYSGIENQPVKGVAQSIKIITKEASTRIAHYAFQYALANGRKKVTCIHKANIMKQSDGLFVKSCREVSTRYPSIKYEELTIDNNCMQLVLDPNQMDVMVLPNLYGDIVSDLCAGLIGGLGLTPSGNIGENGSAIFEAVHGTAPDIAGKNKANPTALILSSIMMLRHLGHFHEASIIENAVLNT... | Performs an essential role in the oxidative function of the citric acid cycle. | Q55BI2 |
A5UU35 | DCUP_ROSS1 | Uroporphyrinogen decarboxylase | Roseiflexus | MTHSRFLAACRRQPVDATPVWFMRQAGRYMPEYRAIRERYGFLEMVKTPELAAEITMQPIRAFSVDAAIIFADILPLLEGMGLHLTYEQGEGPVIHNPVRSPADVAALRTPDPRETVAYTIQAIRLVKRDLEGRAPLIGFSGAPFTLAAYAIEGGSSRDHRLTKALMYAEPQAWRELMERLTAQVSAYLIAQIEAGADAVQIFDSWAGALAPGDYADYVLPFVQKCIIAVRAGCGIVPPPPIIYFGVGLSGMLGLLRQTDADVIGLDWRIHLDDGWAQVGPGVAVQGNLDPHTLLAPWTEVRRRTADILDRAAGRPGHIF... | Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. | A5UU35 |
A6WEK6 | RF2_KINRD | Peptide chain release factor 2 | Kineococcus | MAIDFPSEISALRTTYASIREVSDLDALRKELADLNDEAAAPSLWDDPEHAQTVTSRLSAVQAELDRIEKMGGRIDDLEVLVELSEDEHDADSLAEAETELNEVKEQLAQLEVRTLLSGEYDSREAIVTIRSEAGGVDAADFAEMLMRMYLRWAERRGYKSEVYDTSYAEEAGIKSATFKVAAPYAYGTLSVEQGTHRLVRISPFDNQGRRQTSFAGVEVLPVVAETDHVDVPENEVRVDVYRSSGPGGQSVNTTDSAVRLTHLPTGIVVTCQNEKSQLQNKAAAMRVLQAKLLEKARKDRQAELDALKGDDSGSWGNQM... | Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. | A6WEK6 |
B1J6H6 | NUDC_PSEPW | NADH pyrophosphatase | Pseudomonas | MSARWTSAVLDPQITGGWAVARSPEGFLVDANGALFPRDWLKRQDLDVLAEHGIGHFDGEPVFLLELRSTAEVPGCGWRGLRSFMLEGDFDLYKVLGYAAQIGTWAREHRFCGSCGQPMTQIRWERAMYCQPCDLRSYPRISPSMIVLVTRGDEILLARSPRFVTGVYSTLAGFAEPGESAEDCLVREVREEVAVEVTNIQYVGSQCWPFPHSMMLGFHAEYAGGEIVMQPDEIEDARWFNVHDLPPLPAGRSIARYLIDLYVARRSGLPEPVLPR | mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processin... | B1J6H6 |
Q1QN29 | RL4_NITHX | 50S ribosomal protein L4 | Nitrobacter | MELNVTTLEGNAAGSVQLSDGIFGLEPRKDLIQRCVNWQLAKRQAGTHKTKGRAEIWRTGKKMFKQKGTGNARHGSARVPQFRGGGRAFGPVVRSHAHDLPKKVRALALRHALSAKAKDGGLIVIDSAELNEAKTKALVGHFSGLGLTNALIVDGAAVHAGFATAARNIPNIDVLPIQGINVYDILRRRKLVLTKAAVDALEARFK | Forms part of the polypeptide exit tunnel. | Q1QN29 |
P65644 | EUTT_ECOL6 | EutT adenosyltransferase | Escherichia | MKDFITEAWLRANHTLSEGAEIHLPADSRLTPSARELLESRHLRIKFIDEQGRLFVDDEQQQPQPVHGLTSSDEHPQACCELCRQPVAKKPDTLTHLSAEKMVAKSDPRLGFRAVLDSTIALAVWLQIELAEPWQPWLADIRSRLGNIMRADALGEPLGCQAIVGLSDEDLHRLSHQPLRYLDHDHLVPEASHGRDAALLNLLRTKVRETETVAAQVFITRSFEVLRPDILQALNRLSSTVYVMMILSVTKQPLTVKQIQQRLGETQ | Converts cyanocobalamin (CN-B12) to adenosylcobalamin (AdoCbl), the inducer of the eut operon. Is not active on cobinamide nor other intermediates in the adenosylcobalamin synthetic pathway. Allows full induction of the eut operon. | P65644 |
Q63GT3 | PURL_BACCZ | Phosphoribosylformylglycinamidine synthase subunit II | Bacillus cereus group | MSLMLEPNPTQIKEERIYAEMGLTDEEFAMVEKILGRLPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTTGERVLQGPGEGAGIVDIGDNQAVVFKMESHNHPSAIEPYQGAATGVGGIIRDVFSMGARPVALLNSLRFGELQSPRVKYLFEEVVAGIAGYGNCIGIPTVGGEVQFDPCYEGNPLVNAMCVGLINHEDIKKGQAHGAGNTVMYVGASTGRDGIHGATFASEELSESSEAKRPAVQVGDPFMEKLLIEACLELIQSDALVGIQDMGAAGLTSSSAEMASKAGMGIEMYLDDVPQRETGMTPYEMMLSESQE... | Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three su... | Q63GT3 |
A1R0N4 | TGT_BORT9 | tRNA-guanine transglycosylase | Borrelia | MFSIIKNDKNSNARLGVLELPHGKVETPCFMPVGTLGAMKALKHDVLEKLGCDLMLANTYHLYLRPGIDVIKKYGSLHNFTAWDKNFLTDSGGFQVFSLANFRKIETEGVDFKSHIDGSRHYFTPESVFKMQEIFESDIIMALDICSSYGIDYSEASLYTNITTSWARRTLRAYENRKEGYDGLLFLITQGNFFKDLRKRSTEAILELDSPGIAIGGISVGEPRDKYLEILEYNSSLIPKVKPKYVMGIGTPHYILDAIYYGIDIFDCVNPTRIARHGSLLTDNGILRIKRAEFNFDTCPVERDCSCTLCTRYSRGYLRH... | Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks th... | A1R0N4 |
Q1QTP6 | DAPA_CHRSD | 4-hydroxy-tetrahydrodipicolinate synthase | Chromohalobacter | MITGSIVALATPMKASGEIDWEALRRLVGFHLDNGTDAIVAAGTTGEPTTMSFAEHFDVIRCVVEEVAGRIPVIAGTGANATSEAVELARYAREVGADLCLSVAPYYNKPTQEGLYQHFKAVAEGGGLPVILYNVPGRTCSDIYNETVFRLAELENIVGLKDATGNLERAEELVDRLKGSDFALYSGDDPTACDFMLMGGHGDISVCANVAPRAMHELCEAAVAGDDERAHQINTRLMPLHTALGVEANPIPVKWALHRMGLAEQGIRLPMTWLSDKYHSTVSEALQLAGVTEG | Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). | Q1QTP6 |
A9M1G2 | XERC_NEIM0 | Tyrosine recombinase XerC | Neisseria | MVLDGFAAHFDAYLENIVREGKSEHTVAAYRRDLEELFALLAQMPSEAEGGVPQGLSRRDFTAALRRLSQRGLNARTLARKLSSWRQYCVWLVERGLLHTDPTADIKPPKQPERVPKALPQEWLNRMLDLPVDGGDPLAVRDHALFELMYGSGLRVSEIHGLNADDVYLDEAWVHVTGKGRKQRQVPLTGKSVEALKNYLPLRQTASDGKALFTGRNGTRLSQRQIQKRLAQWAAQNGDGRHVSPHMMRHSYAGHLLQASRDIRAVQELLGHSSLSTTQIYTKLDFDHIARLYDEAHPRAKRQDE | Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plas... | A9M1G2 |
P30627 | GLBH_CAEEL | Globin-like protein | Caenorhabditis | MSMNRQEISDLCVKSLEGRMVGTEAQNIENGNAFYRYFFTNFPDLRVYFKGAEKYTADDVKKSERFDKQGQRILLACHLLANVYTNEEVFKGYVRETINRHRIYKMDPALWMAFFTVFTGYLESVGCLNDQQKAAWMALGKEFNAESQTHLKNSNLPHV | May be a globin and may play a role in oxygen transport. | P30627 |
B4P528 | BOP1_DROYA | Ribosome biogenesis protein BOP1 homolog | Sophophora | MTKKLALKRKGKDAEPTNEVVASSEASENEEEEEDLLQAVKDPGEDSTDDEGIDQEYHSDSSEELQFESDEEGNYLGRKQSSSAEEDEESSDEDDDEEEGSSDEEGEEDEEKDSKSKQADDKPSSSGAASKKAPTTELSKRDTSKPEYQDSDTSDEEDIRNTVGNIPMHWYDEYKHIGYDWDAKKIIKPPQGDQIDEFLRKIEDPDFWRTVKDPLTGQDVRLTDEDIALIKRIVSGRIPNKDHEEYEPWIEWFTSEVEKMPIKNVPDHKRSFLPSVSEKKRVSRMVHALKMGWMKTTEEVEREKQAKRGPKFYMLWETDT... | Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit. | B4P528 |
Q4L5M5 | GGI1_STAHJ | Antibacterial protein 1 homolog | Staphylococcus | MQKLAEAIAAAVQAGQDKDWGKMGTSIVGIVENGISVLGKIFGF | Has hemolytic activity and also inhibits the growth of gonococci. | Q4L5M5 |
Q9Y7L2 | BIN3D_SCHPO | Probable RNA methyltransferase C2A9.10 | Schizosaccharomyces | MSNFQHGNYHSYYSMRGGTSIIDPRLKCLPDSLFYEASVLDIGCNNGTVSAQIASIFGASFVLGLDIDHVLIQKARKHLEFVSSRIGPVRNPGSIVEDQFNYYPISSIKKFSRIPVQLQPPLNKQNFPHNIEFETADFLRWESKRKFKIILALSVSKWVHLNNHDEGIIKFFGKISSLLETNGVLILEPQGWDSYLKAAKKISVFNQTPENLKIQPDAFEHLLNQAGLVLEYSIEPQVNNSEYKNFAKRTMYIYKKKGIGIIKLLTST | Probable RNA methyltransferase. | Q9Y7L2 |
B1Z0T3 | PHNW_BURA4 | AEP transaminase | Burkholderia cepacia complex | MPDPILLTPGPLTTSATTRHAMQHDWGSWDAAFNQLTASVCADLVAIARGGDEYVCVPMQGSGTFSVEAALGTLVPRDGVVLVPDNGAYCARILKILGRLGVEAIALPFGEDAAVDPAAVEAAFAREPRITHVALVHLETSAGILNPLDAIAAMCRQHGRRLIVDAMSSFGALPIALADSGIDALVSASGKCLEGVPGMGFAIVRRDALDACEGNSPSLALDLQDQHAYLRKTGQWRFTPPTHVIAALRAALDQYLAEGGQPARGARYAENCRTLVESMRALGFAPFLDASVQAPVIVTFHAPDHPAYDFRRFYDAVRDA... | Involved in phosphonate degradation. | B1Z0T3 |
Q9W0P5 | GALE_DROME | UDP-galactose 4-epimerase | Sophophora | MAPPTVLVTGGAGYIGSHTVLEMLNAGYNVICVDNLCNAYSSGAKLPEALSRVQEITGKKVNFYRVDITDREQVRSVFQEHKIDMVAHFAALKAVGESCRIPLQYYHNNMTGTNVLLEAMADNNVFKFVYSSSATVYGEPKFLPVTEEHPTGNCTSPYGKTKYFTEEILKDLCKSDKRWAVVSLRYFNPVGAHISGRIGEDPNGEPNNLMPYIAQVAVGRRPSLSVYGSDFPTHDGTGVRDYIHIVDLAEGHVKALDKLRNIAETGFFAYNLGTGVGYSVLDMVKAFEKASGKKVNYTLVDRRSGDVATCYADATLADKK... | Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine . The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactose is conv... | Q9W0P5 |
A7IFY8 | RL16_XANP2 | 50S ribosomal protein L16 | Xanthobacter | MLQPKRTKFRKQFKGRIHGVAKGGTELNFGEFGLKAVEPERVTARQIEAARRALTRHMKRAGRVWIRVFPDVPVSAKPTEVRMGKGKGAPEYWAARIKPGRIMFEIDGVSVETAREALTLAAAKLPIKTRFIQRIAE | Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs. | A7IFY8 |
Q2LVU6 | RIMM_SYNAS | Ribosome maturation factor RimM | Syntrophus | MKFFEIGEIVKSHGLKGRMKAKSYVENGEDLSSVHEAMIVKGKEEPRGYKVRKIVLHKTYFFLELETIDTVESADSLVGSTVLIPEDDRAALSGDEYYWRDLMGLQVVTEEGRFLGRIESIFPTGSNDVYVCAGGSREILLPAISDVILKIDLDKKEMVVRLLPGL | An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosoma... | Q2LVU6 |
C7PC56 | AROC_CHIPD | 5-enolpyruvylshikimate-3-phosphate phospholyase | Chitinophaga | MNSFGRLFRVNVFGESHGASVGVNIDGIPAGIPLTQEDFLPDLERRKAGAKGTTPRKEEDLPFIKSGVFNDHTTGAPITILFENNNTRSTDYEKLREFPRPGHADFVATHKYGGFEDYRGGGHFSGRLTLNLVAAGVIAKKILGPGISVKATLKEVAGLPDAEQGLEAAIAAKDSVGGIVECVVEGLPIGLGEPFFDSVESTIAHAVFSIPAIKGIEFGAGFAAARMKGVEHNDAILDASGKTATNHAGGVVGGITNGNPLVFRVAVKPTSSTPKEQHTLNIKSGEVENFSVKGRHDLCIALRVPVVLEAVAAMALADFM... | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a s... | C7PC56 |
B7NM68 | SERC_ECO7I | Phosphohydroxythreonine aminotransferase | Escherichia | MAQIFNFSSGPAMLPAEVLKQAQQELRDWNGLGTSVMEVSHRGKEFIQVAEEAEKDFRDLLNVPSNYKVLFCHGGGRGQFAAVPLNILGDKTTADYVDAGYWAASAIKEAKKYCTPNVFDAKVTVDGLRAVKPMREWQLSDNAAYMHYCPNETIDGIAIDETPDFGKDVVVAADFSSTILSRPIDVSRYGVIYAGAQKNIGPAGLTIVIVREDLLGKANIACPSILDYSILNDNDSMFNTPPTFAWYLSGLVFKWLKANGGVAAMDKINQQKAELLYGVIDNSDFYRNDVAKANRSRMNVPFQLADSALDKLFLEESFAA... | Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine. | B7NM68 |
P29032 | CHIC_POPTR | Acidic endochitinase WIN6.2C | Populus | MSVWAFFAFFSLFLSLSVRGSAEQCGRQAGDALCPGGLCCSFYGWCGTTVDYCGDGCQSQCDGGDGCDGGGGGGGDGDDGYLSDIIPKSTFDALLKFRNDPRCHAVGFYTYDAFISAAKEF | Defense against chitin-containing fungal pathogens. | P29032 |
Q06602 | APD73_APIME | Apidaecin IA | Apis | KNFALAILVVTFVVAVFGNTNLDPPTRPTRLRREAKPEAEPGNNRPVYIPQPRPPHPRLRREAEPEAEPGNNRPVYIPQPRPPHPRLRREAELEAEPGNNRPVYISQPRPPHPRLRREAEPEAEPGNNRPVYIPQPRPPHPRLRREAELEAEPGNNRPVYISQPRPPHPRLRREAEPEAEPGNNRPVYIPQPRPPHPRLRREAEPEAEPGNNRPVYIPQPRPPHPRLRREAEPEAEPGNNRPVYIPQPRPPHPRLRREAKPEAKPGNNRPVYIPQPRPPHPRI | Apidaecins have bactericidal activity; predominantly against Gram-negative bacteria . They seem to interfere with cell propagation . | Q06602 |
P20624 | FER3_RHOCA | Ferredoxin III | Rhodobacter | MPTVAYTRGGAEYTPVYLMKIDEQKCIGCGRCFKVCGRDVMSLHGLTEDGQVVAPGTDEWDEVEDEIVKKVMALTGAENCIGCGACARVCPSECQTHAALS | Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | P20624 |
A6LWG7 | QUEC_CLOB8 | Queuosine biosynthesis protein QueC | Clostridium | MSNKAVVVFSGGQDSTTCLFWALKEFDEVIAVTFDYNQKHRKEIECATSIAKELGIEHHILDMGLLNQLAPNALTRNDIEIKAGENGSLPSTFVEGRNMLFLTFAGVLAKVKGAKHIVTGVCETDFSGYPDCRDIFIKSLNVTLNLAMDYNFVVHTPLMWIDKAETWKMADDFGKLDYIREKTLTCYKGIVGDGCGECPACKLRKNGLDKYLESKKN | Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). | A6LWG7 |
A7I5P5 | RS3_METB6 | 30S ribosomal protein S3 | Methanoregula | MAVERKFIAEGARKARVEKYLTKELKRAGFGGMDIARTPLGTQVTIFAEKPGIVIGKGGKLVHQLTQDLAQNYGVESPQIEVQQVQNPSFNAQIMAERLANALERGWYFRKAGSSIMRRVMDSGALGCEVVIAGKLTGARARTQKFTEGYIKHCGEPSNTIVEKGYAIAIKKLGVIGVQVKIVPADAKMPDHFAIIEQEKKLPAPKTTVTAVIETDNEEPALPDENIDEEV | Binds the lower part of the 30S subunit head. | A7I5P5 |
Q8D2C6 | PSD_WIGBR | Phosphatidylserine decarboxylase beta chain | Wigglesworthia | MKTKLQYYLPKMLITKFFGWLAEKKAGIITYWIILFFIKIYKINLKEIKTKDIKSYNTFNDFFSRRIKIDCRRIDYDPSIIICPADGIITNFGYIENTEKLQLKNHNYTLKSLLAQNETMIDIFQHGIFFTTYLSPKNYHRIHMPCDGSLIKMIYVPGQLFSVNLKFYKNISNIFSKNERVICLFKTNFGYMIQILVGSIISGTISTSWYGKINYKRDGIIKLWKYNINSNNKPIFLKKGDEMGFFTLGSTVITLFSKKNILIKENLSNYKEVRVGDVLAYGIQNVK | Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). | Q8D2C6 |
Q9FGV1 | ARFH_ARATH | Protein FRUIT WITHOUT FERTILIZATION | Arabidopsis | MKLSTSGLGQQGHEGEKCLNSELWHACAGPLVSLPSSGSRVVYFPQGHSEQVAATTNKEVDGHIPNYPSLPPQLICQLHNVTMHADVETDEVYAQMTLQPLTPEEQKETFVPIELGIPSKQPSNYFCKTLTASDTSTHGGFSVPRRAAEKVFPPLDYTLQPPAQELIARDLHDVEWKFRHIFRGQPKRHLLTTGWSVFVSAKRLVAGDSVIFIRNEKNQLFLGIRHATRPQTIVPSSVLSSDSMHIGLLAAAAHASATNSCFTVFFHPRASQSEFVIQLSKYIKAVFHTRISVGMRFRMLFETEESSVRRYMGTITGISD... | Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Seems to act as transcriptional activator. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response ... | Q9FGV1 |
B9JRQ0 | FLGH_AGRVS | Basal body L-ring protein | Agrobacterium | MIKRSAVVLMAVILTGCGNKTLEEVGNAPAMSPVGSGLRYNQAPQLASYPKQTKAVSNGYSLWNDSQAALFKDSRAINVGDLLTVNISIADKAKFKNDTSRSRKNSTSLTWSTVINLFGITPPDSSGDMSTDSNSSSDGKGSVDRSETLTLMVAAVVTSILENGNLLISGSQEVRVNHEVRILNVAGIVRPQDVDAKNTISYEKIAEARISYGGKGRLTEVQQPPVGQQVVDMFSPF | Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | B9JRQ0 |
Q59687 | CH60_PASMU | Chaperonin-60 | Pasteurella | MAAKDVKFGNDARVKMLAGVNILADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIVNEGLKAVAAGMNPMDLKRGIDKAVTAVVTELKALSKPCETSKEIEQVGTISANSDSIVGQIIAQAMDKVGKEGVITVEDGTGLEDELAVVEGMQFDRGYLSPYFINKPETATVELDNPFILLVDKKVSNIRELLPVLEGVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIAILTAGTVISEEIGMELEKATLEDLGQA... | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. | Q59687 |
Q3B1F5 | ATPG_CHLL3 | F-ATPase gamma subunit | Pelodictyon | MPTLKDIRVRIKGVKSTQQVTKAMKMVAAAKLRKAQERAVMARPYAAKLKEMLGSLSGKVDTSASPLLADRADASRVLVVLITSDRGLCGAFNTNIIKLAHRTIHEEYAAAYAAGNVQLICAGTRGFDFFRKRGYSVLKGYPAVFQNLDFSTAREIAETASSMYVKGEVDRVVVVYNEFKSVLAPTLKAEVLLPIKSELPVAEGGDYIYEPSPAAIIEELVPKHLNTQVWGMMLESNAAEQAARMTAMDSATENAKELLRGLNISYNRARQAAITKELSEIVGGADALQN | Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | Q3B1F5 |
Q46J24 | RPOC2_PROMT | Transcriptase subunit beta' | Prochlorococcus | MTSSSPKTRKSSTKSKAKRGSKSKKAAEIIAVQRLSKTPPPFRNKVVDKKVLKNLVAWAFKHHGTAATAAMADNLKDLGFRYATQAAVSISVDDLKVPEAKQDLLGQAEELITATEECYRLGEITEVERHTKVIDTWTETNERLVDAVKKNFNQNDPLNSVWMMANSGARGNMSQVRQLVGMRGLMANPQGEIIDLPIRTNFREGLTVTEYVISSYGARKGLVDTALRTADSGYLTRRLVDVAQDVIVREEDCGTTRSILISAEDGKFGNRLVGRLTSEQVVNADEEVLAERDTPIDPQLSKKFEQSNMQGVRVRSPLTC... | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q46J24 |
A0A2K9RFZ9 | TPS6_VITAC | Terpene synthase 6 | Vitex | MSLRFNLIVTPFSNYEIRNRRETFPVQKFLMTTSKSAIKVKCSLKTSIDLVGKIREKINGKVDNSLEVPTINYLVDIPSNLCMIDSLERLGVARYFQSEIDGVLEKTYRLWQQREKDIFADVTCRAMAFRFLRVKGYEVSSDELAPYADQVHVNPQISDVTTVVELYRASQVRIYEEDSILEKLHAWTSTFLKQQLQSKTISDKKLHEQVEYYLKNYHGIQNQVAVRRSLDLYDIDHYPILKVADRFRIIYNEDFFVFLRQDFNLCQAQHQKELQQLQRWYEDCRLDTLNYGRNVVHVSCFLAAANFGDPELSNARLAFA... | Involved in the biosynthesis of labdane-type diterpenoid including cleroda-dienols, and peregrinol lactones and furan derivatives, dopaminergic diterpenoids that can bind to dopamine receptors in the human pituitary gland, have probably ability to lower prolactin levels, and are used to treat menstrual cycle disorders ... | A0A2K9RFZ9 |
B3CMH6 | RUVA_WOLPP | Holliday junction ATP-dependent DNA helicase RuvA | unclassified Wolbachia | MIGNLRGIVDEVCSDHIILNVNDVGYIVYLSAKTLSACSIGSRVKLLIDTYANSRENVTQLYGFISKEEQQCLRLLVKVSGVSYKTAMSILSKLTPEQLFLAIINEDKLALKVSGLGLKLINRIITELNGKVSKLEINNNHFHSISEDALSALINLGYERTKAYDTIKKIEDESPNLDTKDIIRMALKTI | The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA... | B3CMH6 |
Q0W6G4 | DPCKG_METAR | Dephospho-coenzyme A kinase | Methanocella | MIYKLTPALRDDLKTPFGTLYPGKGESCLAKVVKALDKPPKIISIGDVTTFYLIKAGVVPDMCLVDDQTMRLPVDHEVRKGTSHHTFKELRVSNPAGVVTQALMDLIKDNMSSTEPVRIFVDGEEDLAVIPACLYAPIGSAVIYGQPNEGVVVVRVTEEKRKETKALLDKMERVDE | Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA). | Q0W6G4 |
Q8LEQ4 | DPM3_ARATH | Dolichol phosphate-mannose biosynthesis regulatory protein | Arabidopsis | MKHIVKILSLLVAISAFWIGLLQAAIIPRSHTWLLPIYFVVSLGCYGLLMVGVGLMQFPTCPQEAVLLQKDIAEAKDFFKHKGVDVGSN | Regulates the biosynthesis of dolichol phosphate-mannose. Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization and stable expression of DPMS1. | Q8LEQ4 |
A7GUR8 | GPMI_BACCN | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase | Bacillus cereus group | MRKPTALIILDGFGLREETYGNAVAQAKKPNFDRYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRVNVAIREGEFDKNETFQNAIKHVKEKGTALHLFGLLSDGGVHSHIDHMFALLRLAAKEGVEKVYIHAFLDGRDVGPQTAKGYIDATNAVIKETGVGQFATIAGRYYSMDRDKRWDRVEKCYRAMVYGEGPTYKNAYECVEDSYANGIYDEFVLPSVIVNEDETPVATINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRGEKVPHIPEFVCMTHFSETVNGYVAFKPVNLDNTLGEVV... | Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | A7GUR8 |
Q8X0V0 | TFB5_NEUCR | RNA polymerase transcription factor-1 | Neurospora | MPRAIRGVLIQCEPAIKSIIVHLDSVNNDIIIEDLDEQTLVVKENMVQLLKQKLEDRLKETYRPEEPLADSD | Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to al... | Q8X0V0 |
A1JQY4 | KDPA_YERE8 | Potassium-translocating ATPase A chain | Yersinia | MAASGFLLIASFMLVLLVLARPLGSFLARLIEGDPFMPLQKIEAGLWRCSGVKNVEMNGWQYALAILLFNILGIALLFALLMMQGALPLNPENMPGMSWHLALNTAVSFVTNTNWQAYSGENTLSYLSQMAGLTVQNFLSAATGIAVAFALIRAFSRHSAATLGNAWVDLVRITLYVLLPIALIIALIFVSQGVLQNLDGYLHITTLEGVKQTLPMGPVASQEAIKMLGTNGGGFFGANSAHPFENPTAFSNFVQMLAIFLIPCALCFAFGQVVGDTRQGHALIWAMSLIFVVAVVVVMYAELAGNPHLIKLGADSNINM... | 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 periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel. | A1JQY4 |
Q8IYY4 | DZI1L_HUMAN | DAZ-interacting zinc finger protein 1-like | Homo | MQSPAATAEGLSGPLFGAYTFPTFKFQPRHDSMDWRRISTLDVDRVARELDVATLQENIAGITFCNLDREVCSRCGQPVDPALLKVLRLAQLIIEYLLHCQDCLSASVAQLEARLQTSLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLMQTGTHSYHTCHLCDKTFMNATFLRGHIQRRHAGVAEGGKQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKLFWDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQA... | Involved in primary cilium formation . Probably acts as a transition zone protein required for localization of PKD1/PC1 and PKD2/PC2 to the ciliary membrane . | Q8IYY4 |
O74510 | BQT3_SCHPO | Bouquet formation protein 3 | Schizosaccharomyces | MSGSKCCSSSNTIKVSIYLFLHTLTYGLLNYHLNPRLLASTGVVESDIPYWMSYLSIIMHVGQSLLLQKFNLGYGWLLLTKYPVYVLLSTYYLTPLSQIAWAFIIDAISLLVARCFSRANPIKCSNQVNTQYSVSFLFTIMASVLISVLNYISQKIFLNGLILGNSHNVVTSLVAPPLPLQYLAHVPIGYVIQRVVFSERPIPQSLFLMIFLTLWNCFIPYSILFSMNWSAMFQVVGAYLSQIWIITFICWALSL | Connects telomeres to the nuclear envelop (NE) during both vegetative growth and meiosis. This connection ensures clustering of telomeres to the spindle pole body (SPB) when cells enter meiotic prophase. | O74510 |
B6ISU1 | LPXD_RHOCS | UDP-3-O-acylglucosamine N-acyltransferase | Rhodospirillum | MADPRFFRRAGPFSLAQLASLSGAEIAPGADPALLLHDVAPLESAGPEQLSFLDNRKYADAFARTGAGACIVHPDLAGRAPAGTALLLSRKPYRAYALCAQAFYPAPAAEGGVSPGAHLHPTARVGEGTEVAPGAVIEAGAEIGNGCRIGPNAVIGRNVRIGDGTTVGACASLSHCEIGSRVVIYPGVRIGQDGFGFAMDVAGHVRVPQLGRVLVEDDVEIGANVTIDRGAGPDTVIGRGCMIDNLVQIGHNVHLGPGCVVVAQAGISGSTKLDHHVILAAQAGITGHLKIGAGARIAAQSGVMRDVAPGEQVGGSPAVP... | 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. | B6ISU1 |
Q7N9P2 | KGUA_PHOLL | GMP kinase | Photorhabdus | MIQGTLYIVSAPSGAGKSSLIQALLKTQPLYDTQVSVSHTTRAMRPGENQGEHYFFITEEAFRQMIDNNEFLEHARVFDNYYGTSRKVIEETLASGVDVFLDIDWQGAQQIRKKMPSARSIFILPPSKEELCRRLRGRGQDSEDIIEKRMDQAVAEMVHYNEYDYLIVNDDFNTALADLHTIIRSERLHRERQAQRHDALISKLLAD | Essential for recycling GMP and indirectly, cGMP. | Q7N9P2 |
Q6TPH0 | SLOA_PROMU | Snaclec mucrocetin subunit alpha | Protobothrops | MGRFIFVSFGLLVVFLSLSGTGADFDCIPGWSAYDRYCYQAFSEPKNWEDAESFCEEGVKTSHLVSIESSGEGDFVAQLVAEKIKTSFQYVWIGLRIQNKEQQCRSEWSDASSVNYENLYKQSSKKCYALKKGTELRTWFNVYCGRENPFVCKYTPEC | Platelet-agglutinating factor that acts in a vWF-independent manner. Binds specifically to platelet GPIbalpha (GP1BA) to a distinct binding site from that of flavocetin-A. | Q6TPH0 |
Q7UX73 | LOLD1_RHOBA | Lipoprotein-releasing system ATP-binding protein LolD 1 | Rhodopirellula | MLVVSELSKSYPTAGEPLSVLRGVNLELSPGQSAAIVGPSGSGKTTLLQILGTLDEPDSGSVQINGQDPFALDARERAAYRNQTIGFIFQDHHLLPQLSVTENVLIPALANGKPTSDDVSRAAELIDAVGLSHRATHLPRELSGGERERVAIARALLMQPSVVLADEPTGNLDSKTAKTITELLLRLQAEQNTVLVTVTHSLSLADEMNERFELVDGALVRRGRFGITA | 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. | Q7UX73 |
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