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 |
|---|---|---|---|---|---|---|
A5FSU1 | SYA_DEHMB | Alanyl-tRNA synthetase | Dehalococcoides | MFSSDELRENYLKFFEEKGHKRIASSSLIPHNDPTLLLTTAGMVQFKPYYLGVAKPENPRMASCQKCFRTTDIESVGDASHLTMFEMLGNFSIGNYFKKEAIAWAWEYVTQRLNIPAERLWITVYLDDDEAIALWKEQGVPENRIVRLGAADNFWGPAGDSGPCGPCSEIHYDFGQETGCGKADCNPSCKCGRFCEIWNLVFVQFNQDKSGKRQNLPAPSIDTGMGLERLTILMQSKKNVYETDIFAPIVEKACLLSGRKYGCDAATDRALRIVSEHSRGITFLIADGVIPDKAGRGYVLRRLLRRAVLFGRRLGLERPFLVDMAGAVINRMSGIYPELKKRQTYVLEMIASEEARFSETLATGLELLEEIVRQTKGGRISGQDAFKLYDTYGFPVEMTTEIAAEKGLSVDLDGFESEMEIQRTKARSSRKFSFDAAATAEAVKNMRHAEKTCFVGYELAIQKSTIKDILTEGGTVDSIEEGDEASIVLDESPFYAEMGGQVGDTGEIITDAGRFEVKNTLHLPNGVFLHQGRVINGCLKISEAATAHINEERRRDIARNHTATHILQTALREVLGEQVQQRGSVVTPDRLRFDFSHLKPMSKDEMRRVEEFVNDKIRRNLPVYAEEMPYRHALEEGVTALFGEKYGDRVRVLRVGRPAVSAELCGGTHVTASGEIALFKIMSESSVGAGLRRIEAVTGREAEAFINLQQDSLSELSGMLESTAEESPRKLAELKEEIDTLKKAVQNLERQMSRGEAEELLSKAEDYKGVKLLVSRMTSVNADTLRETADFLRDKLGSGVIVLGTVTEDKPFFLCMVTPDLIAKGYHAGNIVKKLSQIAGGGGGGKPNMAQGGGRDKSKLDEALQAVKGMI | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. | A5FSU1 |
O29995 | CDC61_ARCFU | ORC1-type DNA replication protein 1 | Archaeoglobus | MNIFDNILSSATIFKNRDVLRHSYTPEKLPHREEQINQLALLLSPMLRGGTPSNIFIYGKTGTGKTATVLFVARQLEEASRKAKLNVAVHYINCEIVDTAYRVLASLARKFGSNVPMTGWPTDQVYEEVKKALERRGTRVVVILDEIDKLVKKAEEALYGLTRINSELENSSICIVGISNNLKFKEYLDARILSSLSEEEIVFPPYNAEQLEDILQQRAKLAFEDGVLEDGVIQLCAAIAAQEHGDARKALDLLRVSAEIAERERDSMVRVEHVKKAVRKIETDYMIETVRTLPVHSKILLYSMSLISENSPKFTTGEVYCVYKKLCGKVGVDPLTQRRISDLISELDMLGILNSVVISKGRYGRTREMKLEADEKVLRKALEEDYRLQNLRKFEGELKKLANLNLFQF | Involved in regulation of DNA replication. | O29995 |
Q211T9 | MURC_RHOPB | UDP-N-acetylmuramoyl-L-alanine synthetase | Rhodopseudomonas | MRLPREIGPIHFVGIGGIGMSGIAEVLCNLGYTVQGSDASEGANVSRLRDKGIAIHVGHQAENVAGADVVVVSTAIKRDNPELLAARAQRIPVVRRAEMLAELMRLKSCVAIAGTHGKTTTTSMVAALLDAGEFDPTVINGGIINAYGTNARLGAGEWMVVEADESDGTFLKLPADVAIVTNVDPEHLDHFKTFDAVQEAFRDFVENVPFYGFAVMCIDHPVVQALVGKIEDRRIITYGENPQADVRLLDLTPNGGSSAFRVAFRDRKAGTAHEIADLVLPMPGRHNALNATAAIAVAHELGLSDDTIRKALAGFGGVRRRFTKTGEWNGVTIIDDYGHHPVEIAAVLKAARESTKGKVIAVVQPHRFTRLQSLFEEFCTCFNDADVVVVAEVYPAGEAPIEGVDRDHFVLGLRAHGHREVIPLQESAALASVVYGAAHSGDYVVCLGAGNITQWAYALPGELKALD | Cell wall formation. | Q211T9 |
Q6G8L2 | THII_STAAS | tRNA 4-thiouridine synthase | Staphylococcus | MKYDHLLVRYGELTLKGSNRKKFVNQLRNNVNKSLKGLDGFVVKGKRDRMYIELEDHADINEITYRLSKIFGIKSISPVLKVEKTIEAMSAAAIKFAQQFEENSTFKIDVKRADKNFPMDTYELQRELGGAILKHFDNISVNVKRPDHEIRVEVRLDAIYMYEEVVPGSGGLPVGTGGKTLLMLSGGIDSPVAGMEVMRRGVTIEAIHFHSPPFTSDQAKEKVIELTRILAERVGPIKLHIVPFTELQKQVNKVVHPRYTMTSTRRMMMRVADKLVHQIGALAIVNGENLGQVASQTLHSMYAINNVTSTPVLRPLLTYDKEEIIIKSKEIGTFETSIQPFEDCCTIFTPKNPVTEPNFDKVVQYESVFDFEEMINRAVENIETLEITSDYKTIKEQQTNQLINDFL | Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. | Q6G8L2 |
B2KWI0 | RTA1_AJECA | Siderophore biosynthesis cluster protein RTA1 | Histoplasma | MSPESKKITAHGSTSMPLSRTSKPQKFTIPLTVGAIFSVIGFLQRFFLASGKGDVQSLYTLSTMFILGAGPTYAGADYFICGRLFSFVPSAAPMSPIRVVRTFITFDVLAEVCVWTGAGLLAGAHTDTAARYKIGLNLIRAAMITQAFLFTSFVAILASFHVRVCALRAEWSVTSNGGTGRRFMMVVHSLYASSIFIIIRSAYHIAGHSFRTNEQPFLICEASLMLLNTAMFNVFHPGHILPIDSRVYVGIDGQERANETIEGAFTDSRPLLQKILDPLDVKGLFSRDKKRWHDPTAELEMDINSTLYAALT | Lipid-translocating exporter-like protein; part of the gene cluster that mediates the biosynthesis of hydroxamate-containing siderophores that play a critical role in virulence via intracellular iron acquisition during macrophage infection . | B2KWI0 |
B8E2U4 | GATC_DICTD | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C | Dictyoglomus | MEKRDFKEQLKKTAHLARLYLTPEEEELYAKQLQDILDYFKKLQEVDTSNIEPMAHVLSLSNIWREDEPKGSISQEEAFKNAPEIENLGFKIPRIIKREE | Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). | B8E2U4 |
Q28UX7 | RPOB_JANSC | Transcriptase subunit beta | unclassified Jannaschia | MPQTYAGQKRIRKFYGKIREVLEMPNLIEVQKSSYDLFLKSGDQLEPMDGEGIKGVFQSVFPIKDFNETAILEFVKYELETPKFDVEECQQRDLTYAAPLKVTLRLIVFDIDEDTGAKSVKDIKEQDVFMGDMPLMTPNGTFVVNGTERVIVSQMHRSPGVFFDHDKGKTHSSGKLLFACRIIPYRGSWLDFEFDAKDIVFSRIDRRRKLPVTTLLYALGLDQEGIMDAYYDTVTFKMVKNKGWSTKFFPERVRGTRPTTDLVDAKTGEVIAEAGKKVTPRAVKKWIDEGSIENLLVPFDGIVGRFAAKDIINEETGAIYVEAGDELTWELDKAGEVSGGTLKELIDAGITEIPVLDIDNVNVGPYMRNTLAVDKNLNRESALMDIYRVMRPGEPPTVEAASNLFDQLFFDSERYDLSAVGRVKMNMRLDLDAEDTMRTLRKEDIISCIKALVELRDGRGDIDDIDHLGNRRVRSVGELMENQYRVGLLRMERAIKERMSSVEIDTVMPQDLINAKPAAAAVREFFGSSQLSQFMDQTNPLSEVTHKRRLSALGPGGLTRERAGFEVRDVHPTHYGRMCPIETPEGPNIGLINSLATYARVNKYGFIETPYRRVNDAVVSDDVVYMSATEEMRHTVAQANANLDDDGKFVNDMVNTRMSGEYTLNPREAIDLIDVSPKQLVSVAASLIPFLENDDANRALMGSNMQRQAVPLLQADAPFVGTGIESVVAKDSGAAIMAKRGGVIDQVDAQRIVIRATEDLELGDAGVDIYRLRKFQRSNQNTCINQRPLVKVGDKIGKGEVIADGPSTDIGELALGKNVIVAFMPWNGYNYEDSILISERISRDDVFTSIHIEEFEVAARDTKLGPEEITRDIPNVGEEALRNLDEAGIVYIGAEVEPGDILVGKITPKGESPMTPEEKLLRAIFGEKASDVRDTSLRVKPGDYGTIVEVRVFNRHGVEKDERALQIEREEVERLARDRDDELVILERNIYARLRGMIMGKTAVKGPKGVKPNTVIDEDLLDGQLSRGQWWQLALEDEKDAAHIEALNQQFDTQKRALDHRFEDKVEKVRRGDDLPPGVMKMVKVFIAVKRKLQPGDKMAGRHGNKGVISKVVPMEDMPFLADGTPVDFVLNPLGVPSRMNVGQILETHMGWAARGMGLQIDEALDEYRRSGDMTPVRDALKIAYGDDVYDDAFADRDEESLLEAAGNVTKGVPIATPVFDGAKEADVNDALIRAGFSTSGQSKLFDGRTGEQFAREVTVGVKYLLKLHHLVDDKIHARSTGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVAGRTKVYESIVKGEDNFEAGVPESFNVLVKEVRGLGLNMELLDAEDDEGGIAAE | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Q28UX7 |
A2BH40 | ARI1A_MOUSE | SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1 | Mus | MAAQVAPAAASSLGNPPPPPSELKKAEQQQREEAGGEAAAAAAERGEMKAAAGQESEGPAVGPPQPLGKELQDGAESNGGGGGGGAGSGGGPGAEPDLKNSNGNAGPRPALNNNLPEPPGGGGGGGSSSSDGVGAPPHSAAAALPPPAYGFGQAYGRSPSAVAAAAAAVFHQQHGGQQSPGLAALQSGGGGGLEPYAGPQQNSHDHGFPNHQYNSYYPNRSAYPPPPQAYALSSPRGGTPGSGAAAAAGSKPPPSSSASASSSSSSFAQQRFGAMGGGGPSAAGGGTPQPTATPTLNQLLTSPSSARGYQGYPGGDYGGGPQDGGAGKGPADMASQCWGAAAAAAAAAAAVSGGAQQRSHHAPMSPGSSGGGGQPLARTPQSSSPMDQMGKMRPQPYGGTNPYSQQQGPPSGPQQGHGYPGQPYGSQTPQRYPMTMQGRAQSAMGSLSYAQQIPPYGQQGPSAYGQQGQTPYYNQQSPHPQQQPPYAQQPPSQTPHAQPSYQQQPQTQQPQLQSSQPPYSQQPSQPPHQQSPTPYPSQQSTTQQHPQSQPPYSQPQAQSPYQQQQPQQPASSSLSQQAAYPQPQPQQSQQTAYSQQRFPPPQELSQDSFGSQASSAPSMTSSKGGQEDMNLSLQSRPSSLPDLSGSIDDLPMGTEGALSPGVSTSGISSSQGEQSNPAQSPFSPHTSPHLPGIRGPSPSPVGSPASVAQSRSGPLSPAAVPGNQMPPRPPSGQSDSIMHPSMNQSSIAQDRGYMQRNPQMPQYTSPQPGSALSPRQPSGGQMHSGVGSYQQNSMGSYGPQGSQYGPQGGYPRQPNYNALPNANYPNAGMAGSMNPMGAGGQMHGQPGIPPYGTLPPGRMAHASMGNRPYGPNMANMPPQVGSGMCPPPGGMNRKTQESAVAMHVAANSIQNRPPGYPNMNQGGMMGTGPPYGQGINSMAGMINPQGPPYPMGGTMANNSAGMAASPEMMGLGDVKLTPATKMNNKADGTPKTESKSKKSSSSTTTNEKITKLYELGGEPERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQCLYAFECKIERGEDPPPDIFAAADSKKSQPKIQPPSPAGSGSMQGPQTPQSTSSSMAEGGDLKPPTPASTPHSQIPPLPGMSRSNSVGIQDAFPDGSDPTFQKRNSMTPNPGYQPSMNTSDMMGRMSYEPNKDPYGSMRKAPGSDPFMSSGQGPNGGMGDPYSRAAGPGLGSVAMGPRQHYPYGGPYDRVRTEPGIGPEGNMGTGAPQPNLMPSTPDSGMYSPSRYPPQQQQQQQQQHDSYGNQFSTQGTPSSSPFPSQQTTMYQQQQQNYKRPMDGTYGPPAKRHEGEMYSVPYSAGQGQPQQQQLPAAQSQPASQPQAAQPSPQQDVYNQYSNAYPASATAATDRRPAGGPQNQFPFQFGRDRVSAPPGSSAQQNMPPQMMGGPIQASAEVAQQGTMWQGRNDMTYNYANRQNTGSATQGPAYHGVNRTDEMLHTDQRANHEGPWPSHGTRQPPYGPSAPVPPMTRPPPSNYQPPPSMPNHIPQVSSPAPLPRPMENRTSPSKSPFLHSGMKMQKAGPPVPASHIAPTPVQPPMIRRDITFPPGSVEATQPVLKQRRRLTMKDIGTPEAWRVMMSLKSGLLAESTWALDTINILLYDDNSIMTFNLSQLPGLLELLVEYFRRCLIEIFGILKEYEVGDPGQRTLLDPGRFTKVYSPAHTEEEEEEHLDPKLEEEEEEGVGNDEEMAFLGKDKPSSENNEEKLVSKFDKLPVKIVQRNDPFVVDCSDKLGRVQEFDSGLLHWRIGGGDTTEHIQTHFESKIELLPSRPYVPCPTPPRKHLTTVEGTPGTTEQEGPPPDGLPEKRITATMDDMLSTRSSTLTDEGAKSAEATKESSKFPFGISPAQSHRNIKILEDEPHSKDETPLCTLLDWQDSLAKRCVCVSNTIRSLSFVPGNDFEMSKHPGLLLILGKLILLHHKHPERKQAPLTYEKEEEQDQGVSCDKVEWWWDCLEMLRENTLVTLANISGQLDLSPYPESICLPVLDGLLHWAVCPSAEAQDPFSTLGPNAVLSPQRLVLETLSKLSIQDNNVDLILATPPFSRLEKLYSTMVRFLSDRKNPVCREMAVVLLANLAQGDSLAARAIAVQKGSIGNLLGFLEDSLAATQFQQSQASLLHMQNPPFEPTSVDMMRRAARALLALAKVDENHSEFTLYESRLLDISVSPLMNSLVSQVICDVLFLIGQS | Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Binds DNA non-specifically . Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth . | A2BH40 |
B4ECL8 | LPXB_BURCJ | Lipid-A-disaccharide synthase | Burkholderia cepacia complex | MPLPTNQLRLAMVAGEPSGDLLAASLLGGLRERLPESAQYYGIGGQRMIAQGFDSHWQMDKLTVRGYVEALGQIPEILRIRGELKRQLLAERPDAFIGVDAPDFNFSVEQAARDAGIPSIHFVCPSIWAWRGGRIKKIAKSVDHMLCLFPFEPAILDKAGVASTYVGHPLADDIPLEPDTHGARIALGLPADGPVIAVLPGSRRSEIALIGPTFFAAMALMQQREPGVRFVMPAATPALRELLQPLVDAHPQLALTITDGRSQVAMTAADAILVKSGTVTLEAALLKKPMVISYKVPWLTGQIMRRQGYLPYVGLPNILAGRFVVPELLQHFATPEALADATLTQLRDDANRRTLTEVFTEMHLSLRQNTAAKAAEAVVRVLEQRKGRA | Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | B4ECL8 |
Q92GT4 | FPG_RICCN | DNA-(apurinic or apyrimidinic site) lyase MutM | spotted fever group | MPELPEVETLKNSLKDKLIGLIIENVELKRDNLRYKLSPLLATETLNTNILDVRRRAKYLIIDFNNDYSLIVHLGMSGRFTLQSANYKTQKHDHVIFDLSNGEKLIFNDTRRFGMIYSFKTDLLEKEFLNDLGIEPFSDLLTLEYLKDKLQTKKIPIKNLIMDNRVIVGVGNIYASESLHLARIHPDKSGNNLRDDEIENLIKAIRDVLTKAITAGGTTLKDFVNGDNKPGYFTKQLKVYGREGQSCLSCSSTIIKIKHSGRSTFYCKTCQYS | Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. | Q92GT4 |
Q3J803 | HFQ_NITOC | RNA-binding protein Hfq | Nitrosococcus | MSRGQSLQDPFLNALRKERVPVSIYLVNGIKLQGQIESFDQFVVLLKNSVSQMVYKHAISTVVPARNVKLSSNEGENIHPIGGTRSADAD | RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. | Q3J803 |
A0JZ73 | RL24_ARTS2 | 50S ribosomal protein L24 | Arthrobacter | MAKIKKGDLVQVITGAKAERGGDRGKQGKVLRVFPDTNRVLVEGINRVTKHTKVGQSQRGTKTGGIEVVEASIHISNVALVDPSTKKPTRVGFRTETVERNGKKREVRVRVAKSSGKDI | One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. | A0JZ73 |
A8AHC4 | CHBG_CITK8 | Chitotriose-6P deacetylase | Citrobacter | MERLLIVNADDFGLSKGQNYGIVEACRNGVVTSTTALVNGDAIDHAAQLCRDVPKLAVGMHFVLTLGKPLTAMPGLTREGLLGKWIWQMAEEETLPLDEISHELECQYQRFIDLFGREPTHLDSHHHVHMFPQIFPIVAMFAAERGVALRIDRQSVLNADDLPVALRSSQGFSSEFYGDAISEALFLQVLDASADRGEKSLEVMCHPAFIDNIIRQSAYCYPRLTELDVLTSASLKYAIAERGYRLGSFLDV | Involved in the degradation of chitin. ChbG is essential for growth on the acetylated chitooligosaccharides chitobiose and chitotriose but is dispensable for growth on cellobiose and chitosan dimer, the deacetylated form of chitobiose. Deacetylation of chitobiose-6-P and chitotriose-6-P is necessary for both the activation of the chb promoter by the regulatory protein ChbR and the hydrolysis of phosphorylated beta-glucosides by the phospho-beta-glucosidase ChbF. Catalyzes the removal of only one acetyl group from chitobiose-6-P to yield monoacetylchitobiose-6-P, the inducer of ChbR and the substrate of ChbF. | A8AHC4 |
Q8KCS5 | PURQ_CHLTE | Phosphoribosylformylglycinamidine synthase subunit I | Chlorobaculum | MADVTVGIVVFPGSNCDHDTEYAVASFPGVKPVMLWHNDHDLKGCDAVILPGGFSYGDYLRCGAIARFSPIMREVIDFAGKGRPVLGICNGFQVLVECGLLEGALIRNAGRRFVSRQTTISVANNATIFTDRYQKGEVLRVPVAHGEGNYYASPETIESLESNGQVVFRYTDAWGNATAEANFNGSMNNIAGIVNKQGNVLGLMPHPERASEKLLGSEDGRRLFESLFAHLAGA | 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 subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. | Q8KCS5 |
A8LQ63 | DNAJ_DINSH | Chaperone protein DnaJ | Dinoroseobacter | MAKRDYYDVLGVSKGASPDEIKKGFRKKAKELHPDRNSDNPNAEAQFKEANEAYDILKDPDKKAAYDRYGHAAFENGSGGPRGPGGFGGQGQGDFASAFSDVFEDLFGDFMGGQRGGGRQRAARGSDLRYNLRITLEQAFMGMQKTISVPGTVSCSACEGTGAEGGAEPVVCPTCSGMGKVRAQQGFFTIEKTCPTCSGMGQIIKNPCQACRGAGREEKTRALSVNIPAGVETGTRIRLAGEGDAGVRGGPSGDLYIFIEVEEHRIFQREGLDLYCRVPVSMTSAALGGDVEVPTIEGGRSRVKIPSGSQSGRQMRLRGKGMPALRGAGTGDMFIELAVETPVNLTMRQRELLREFEAESQDNQPETSKFFKTVKSFWDGMKS | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins. | A8LQ63 |
A1SJ61 | RECA_NOCSJ | Recombinase A | Nocardioides | MAGGDREKALDAALANIEKQFGKGSVMRLGDEVRAPLEIIPSGSIALDVALGLGGFPRGRVVEIYGPESSGKTTVALHAVANAQRAGGIVAFIDAEHALDPDYAKNLGVDTDALLVSQPDSGEQALEIADMLIRSGALDLIVIDSVAALVPRAEIEGEMGDSHVGLQARLMSQALRKMTGALNNSKTTMIFINQLREKIGVMFGSPETTTGGKALKFYASVRLDVRRIETLKDGTDMVGNRTRVKVVKNKVAPPFKQAEFDIMYGKGISREGGLIDVGVEAGLVRKAGAWYTYEGDQLGQGKENARAFLRDNPDLANELEKKILEKLGVGPTVDQDVAELPAEPIGVGDF | Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage. | A1SJ61 |
Q5PKW4 | PSTB_SALPA | Phosphate-transporting ATPase | Salmonella | MSMVETAPSKIQVRDLNFYYGKFHALKNINLDIAKNQVTAFIGPSGCGKSTLLRTFNKMYSLYPEQRAEGEILLDGDNILTNTQDIALLRAKVGMVFQKPTPFPMSIYDNIAFGVRLFEKLSRADMDERVQWALTKAALWNETKDKLHQSGYSLSGGQQQRLCIARGIAIRPEVLLLDEPCSALDPISTGRIEELITELKQDYTVVIVTHNMQQAARCSDHTAFMYLGELIEFSNTDDLFTKPAKKQTEDYITGRYG | Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. | Q5PKW4 |
G0S7R3 | POM34_CHATD | Pore membrane protein of 34 kDa | Thermochaetoides | MSSTLSVAKAASTPVKQITSAVGPVKESPGNWKHPRLAEITRRQSRNIFGEKNVRQIVYNVAAIVLLEIFRVFASPSIPSQLILPSLRPYSLWIHAVFLVIPLTNIVIALLPLFRPVDDLSDIPLTPAQRKLLGLPPSSKPATPNSVYSTPPRYSRTPSLAGSPASIKSYTSSTLPTASSPTPGAAGIGAGSPAAPIYLSPSKFTTSTSSQQFSPSPSGASPLLHRAISNTSTASGVSPYGSPNSPSKFGASTNSTLAASTISTSTFSVSTTSSIAHVLNNSRLRESVIEGVPATPTPVGKGASVKANSKWLYQRGRRTSSNNWVY | Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. | G0S7R3 |
A3DJE9 | HISZ_ACET2 | ATP phosphoribosyltransferase regulatory subunit | Acetivibrio | MAEWKIYTPEGVQDILQNECFFKKNLEDRIRKVFRASGYYEVETPIVEFYDVFSTEENIIPQETMFKFFDQQGRILVLRPDLTIPIARVAATKLKDAAYPLRISYIGNAFKYNELGGGKQKEFTQAGVEIIGVNTPEADAEVIATAIDAVKATGLENFQIDIGQVEFFKGLMEETGLSEEETEKMRVLIDRKDFLGIEELVEEHNIRDDLKELILDFPKLFGSTDVIDRVEKYPINERSIKALNNLRSIINILDDYGLSKYVSVDLGMVQSLNYYSGTIFRGFTYGVGFPILSGGRYDRLVEKFGKSSPATGFSMGINMVMMALDRQKVEFEKPRVDTLVCYREEGRKTAFQICETLRKQGLAVEVDINGGDFETARNYAALKGIGGILKVLDDENIEIHNLEKGEVSKVTISELLKA | Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. | A3DJE9 |
Q03QX7 | RF1_LEVBA | Peptide chain release factor 1 | Levilactobacillus | MDEMFDKLQAVADRYDELNELISDPEVIADTQRFMALSKEEGELRETVDKYHQYQDVTQQIADDDEMLHDKLDADMESMIKDELKELTAQKAALEEDIKVLLLPKDPNDDKNIIMEIHGAAGGDEASLFAADLFSMYSKYAERQGWQIEVVDENATEVGGFKEIVMMITGNKVYSKLKYENGAHRVQRVPVTESAGRVHTSTATVGVMPEEEDVDIDIDPKDIRTDVYRSSGAGGQHINKTSSAVRMTHLPTGIVVAMQDERSQQQNRAKAMQILRARVYDYYKQQEESAYNAERKSAVGTGDRSERIRTYNYPQNRVTDHRIGLTLNKLDRIMNGELDDIIDALIVSDQAAKLEDLKNNG | Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. | Q03QX7 |
Q8RFV0 | LOLD_FUSNN | Lipoprotein-releasing system ATP-binding protein LolD | Fusobacterium | MKMWRHLDMNNIIMKLEDIDKFYMETGNKLHILRKLNLEVKRGEFVSILGKSGSGKSTLLNIMGLLDKIDGGKIWIDDKEVSSLNEMERNNIKNHFLGFVFQFHYLMSEFTALENVMIPALLNNFKNKTEIEKEAKELLEIVGLAERMKHKPNQLSGGEKQRVAIARAMINKPKLILADEPTGNLDEDTGELIFSLFRKINKEHNQSIVVVTHARDLSQVTDRQIFLKKGVLE | 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. | Q8RFV0 |
P37887 | CYSK_BACSU | Superoxide-inducible protein 11 | Bacillus | MVRVANSITELIGNTPIVKLNRLADENSADVYLKLEYMNPGSSVKDRIGLAMIEAAEKEGKLKAGNTIIEPTSGNTGIGLAMVAAAKGLKAILVMPDTMSMERRNLLRAYGAELVLTPGAEGMKGAIKKAEELAEKHGYFVPQQFNNPSNPEIHRQTTGKEIVEQFGDDQLDAFVAGIGTGGTITGAGEVLKEAYPSIKIYAVEPSDSPVLSGGKPGPHKIQGIGAGFVPDILNTEVYDEIFPVKNEEAFEYARRAAREEGILGGISSGAAIYAALQVAKKLGKGKKVLAIIPSNGERYLSTPLYQFD | Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR-CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression. | P37887 |
B3PP95 | SECA_RHIE6 | Protein translocase subunit SecA | Rhizobium | MVSFGGIARKLFGSSNDRRVRSFQPNVTAINSIEEKTKALTDEQLAAKTAEFRALLAEGKTLDDILIPAFAVVREASRRVLDLRPFDVQLIGGMILHSNAIAEMKTGEGKTLVATLPVYLNALSGKGVHVVTVNDYLAQRDAATMGRVYGFLGMTTGVIVHGLSDEERRAAYACDITYATNNELGFDYLRDNMKYEKNQMVQRGHNFAIVDEVDSILVDEARTPLIISGPLDDRSELYNTIDAFIPLLVPSDYEIDEKQRSANFSEEGTEKLENMLRQAGLLKGNALYDIENVAIVHHINNALKAHKLFQRDKDYIVRNGEVVIIDEFTGRMMPGRRYSEGQHQALEAKEKVQIQPENQTLASITFQNYFRMYDKLAGMTGTAQTEAEEFGNIYNLDVIEVPTNLPIKRIDEDDEVYRTFDEKFKAIIEEILDAHKRGQPVLVGTTSIEKSELLAERLRKQGFNDFQVLNARYHEQEAYIVAQAGVPGAVTIATNMAGRGTDIQLGGNLEMRIERELGEIEAGPEREARIQAIVEEIKELKQKALTAGGLYVIATERHESRRIDNQLRGRSGRQGDPGRSKFYLSLQDDLMRIFGSDRMDSMLTKLGLKEGEAIVHPWINKALERAQKKVEARNFDIRKNLLKYDDVLNDQRKVIFEQRLELMESTNISETVSDMRREVIEDLVEKHIPERAYAEQWDAVGLKTGVTNILNLDLPIEDWFKEEGIGEDDIRERLTEAANAAFTEKAERFGDDIMHYVERSIVMQTLDHLWREHIVNLDHLRSVIGFRGYAQRDPLQEYKSEAFELFTGLLNNLREAVTAQLMRVELVQQAPAEPEPPLMQAHHLDPMTGEDDFAPIYQASEVIVAPENRNPEDPTTWGKIGRNEACPCGSGKKYKHCHGAFEQV | Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. | B3PP95 |
Q96JJ7 | TMX3_HUMAN | Thioredoxin-related transmembrane protein 3 | Homo | MAAWKSWTALRLCATVVVLDMVVCKGFVEDLDESFKENRNDDIWLVDFYAPWCGHCKKLEPIWNEVGLEMKSIGSPVKVGKMDATSYSSIASEFGVRGYPTIKLLKGDLAYNYRGPRTKDDIIEFAHRVSGALIRPLPSQQMFEHMQKRHRVFFVYVGGESPLKEKYIDAASELIVYTYFFSASEEVVPEYVTLKEMPAVLVFKDETYFVYDEYEDGDLSSWINRERFQNYLAMDGFLLYELGDTGKLVALAVIDEKNTSVEHTRLKSIIQEVARDYRDLFHRDFQFGHMDGNDYINTLLMDELTVPTVVVLNTSNQQYFLLDRQIKNVEDMVQFINNILDGTVEAQGGDSILQRLKRIVFDAKSTIVSIFKSSPLMGCFLFGLPLGVISIMCYGIYTADTDGGYIEERYEVSKSENENQEQIEESKEQQEPSSGGSVVPTVQEPKDVLEKKKD | Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. | Q96JJ7 |
Q8YT40 | KAIC_NOSS1 | Circadian clock protein kinase KaiC | Nostoc | MSEKEQQEQQNTSGNGVEKIRTMIEGFDDISHGGLPVGRTTLVSGTSGTGKTLLSLQFLFNGISFFDEPGVFVTFEESPSDIIKNAHIFGWNLQRLINEGKLFILDASPDPEGQDIVGNFDLSALIERLQYAIRKYKAKRVSIDSITAVFQQYEAVGVVRREIFRLVARLKQLNVTTIITTERSEEYGPVASFGVEEFVSDNVVIARNVLEGERRRRTIEILKLRGTTHMKGEYPFTITNDGVNIFPLGAMRLTQRSSNVRVSSGVKTLDGMCGGGFFKDSIILATGATGTGKTLLVSKFLQNGCVNNERAILFAYEESRAQLSRNAYSWGIDFEELESQGLLKIICTYPESTGLEDHLQIIKSEIAYFKPARIAIDSLSALARGVSNNAFRQFVIGVTGYAKQEEITGFFTNTTDQFMGSHSITDSHISTITDTILMLQYVEIRGEMSRAINVFKMRGSWHDKGIREYNITADGPEIQDSFRNYERIVSGSPTRVSIDEKAELSRIVRRFEDKQGSDS | Core component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. Binds to DNA. The KaiABC complex may act as a promoter-nonspecific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. | Q8YT40 |
Q57G36 | LPLA_SALCH | Lipoate--protein ligase | Salmonella | MTTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTHIVLAALNSLGVMADASGRNDLVVKTPDGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAKGITSVRSRVANLTELLPGITHEQVCQAVTEAFFAHYGERVDAEVISPDKTPDLPNFAETFARQSSWEWNFGQAPAFSHLLDEHFTWGGVELHFDVEKGVITRAQVFTDSLNPAPLEALAGRLQGCQYRADVLEQACKSLIAEFPAQKGELRELAAWMAQAVR | Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. | Q57G36 |
Q5KXT0 | DER_GEOKA | GTP-binding protein EngA | Geobacillus thermoleovorans group | MANPVVAIVGRPNVGKSTIFNRIVGERISIVEDVPGVTRDRIYSRAEWLNHSFYLIDTGGIDIGDEPLLVQIRQQAEIAIDEADVIIFMTNGRDGVTAADEEVAKLLRRSNKPVVLAVNKIDNPEMRDLIYDFYALGFGEPYPISGAHGTGLGDLLDAVVRHFPKGGGQEYEEDVIKFCLIGRPNVGKSSLVNAILGEERVIVSDIAGTTRDAVDTSFVREGQEYVIIDTAGMRKRGKIYESTEKYSVLRALRAIERSDVVLVVLNAEEGIIEQDKKIAGYAHEAGRGVILIVNKWDAIEKDDKTMVEFERKIRDHFPFLDYAPILFVSAKTKQRLHKLLPLVRLVSDNHAMRVQTNVLNEVIMDAVAMNPTPTHNGRRLKVYYMTQVAVKPPTFVAFVNDPELMHFSYERFLENRIRDAFGFEGTPIKIIARPRK | GTPase that plays an essential role in the late steps of ribosome biogenesis. | Q5KXT0 |
P60165 | KA112_PARVI | Parabutoxin-2 | Parabuthus | DEEPKETCSDEMCVIYCKGEEYSTGVCDGPQKCKCSD | Binds and inhibits voltage-sensitive potassium channels. Inhibits the vertebrate potassium channel Kv1.1/KCNA1 with low affinity. | P60165 |
Q6CUB5 | PFA4_KLULA | Protein fatty acyltransferase 4 | Kluyveromyces | MAIKLKNRWLGVAIPAFLVALIGYGSHYFILSNFLSWNEQIFYQTCQTMIWVSYYLAIYTNPGIPPKDFKPSAEEWHNYCKKCRVYKPERAHHCKTCNQCVLAMDHHCPWTLNCVGHSNFPHFMRFLFWVIFSTAYLLFLLIGRIYLLWSIRHTAFHHRSTSEIIFICIMTPMDAFVLLTVSSLLGRCIYNQCLHGMTQIESWEMDRIQSLHYKNRLLAQVIDRLVERRPEILPAKQHEINKLLSKRYVNQEDFTNFPYDVNPWTNINNAMGPWYLWLWPWSKPPTIGTSFAKNELFFYDPNSSIEDMLMSLPWPPDGLTHHSRALGSGSSIETIVSGGEQVIRDKSVDLRDRLGRNSWYNDWGEDLSDFGVDTELE | Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function. | Q6CUB5 |
B6JKG8 | HEM3_HELP2 | Pre-uroporphyrinogen synthase | Helicobacter | MGNLVIGSRGSELALWQANHIKERLKKECLIESEIQIVKTKGDKILDTPLNKIGGKGLFTKELEELLLKGTIDLAVHSLKDVPVVFEKGLDLACITKRADVRDTFLSVKFPDLMSLPKGAKVGTTSLRRSMQLKLKRQDLDTESLRGNVQTRLKKLECGEFDAIILAEAGLCRLEIQGAKYRKAFSVKEMIPSMGQGALGVEMLKNHKHFATLQKLNDEKSAFCCRLEREFIKGLNGGCQIPIGVHASLMGDRVKIQAVLGLPNGKEVITKEKRGDKTKAFDLVQELLEEFLQSGAKEILEKAQLF | Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. | B6JKG8 |
A8AV19 | METE_STRGC | Methionine synthase, vitamin-B12 independent isozyme | Streptococcus | MSTTIIGFPRLGEFRELKFTTEKYFRKEISADELLAAAKELRAKHWNIVKEKGISEIPSNDFSHYDNVLDAAFLFNVVPSSVRGLELTDLERYFALARGYQGEKGDVRALPMKKWFNTNYHYIVPKFEKETQVKLAGHKIFEEFAEAKELGLVTRPVVVGPFTLLQVSDFEDGVAPADFVDALATAYQEVFAKLAELGAKRIQLDEPSLVKDLSAEEKALFLDLYKKLLADKKGLEVLIQTYFGDVRDIYSDLVQLPVDAIGLDFVEGKKTLELVKGGFPADKTLYAGIVNGKNIWRNNYEKSLAVLEQIPAENIVLTSSCSLLHVPFTTANEEFEPAILNHFAFAVEKLDEIRDLDAIRNGQGAEALAANKELFATERVGENAELRARIAGLTDADYTRLPAFAEREAIQEEAFKLPALPTTTIGSFPQTKEVRAKRLAFRKGELSAEDYDKFLAEQIDEWIKWQEEVGFDVLVHGEFERNDMVEYFGQNLSGYLFSKNGWVQSYGMRGVKPPIIWGDVTRLNPITVKWSSYAQSRTEKPVKGMLTGPVTILNWSFPREDISIKDSTLQIALAIKDEVLDLEAAGVKIIQIDEAALREKLPLRRSDWYEDYLDWAIPAFRLVHSTVAPDTQIHTHMCYSEFTDIIPAIDNMDADVISFEASRSNLEILDELKAKNFQTEVGPGVYDIHSPRVPNEGEIDHTIEAILAKVPSKKVWINPDCGLKTRGIPETKASLVRLVEAAKAARQHLK | Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation. | A8AV19 |
Q2N7E3 | FOLD_ERYLH | Methenyltetrahydrofolate cyclohydrolase | Erythrobacter | MTAEIIDGKAFAARLRERVGALAEKFEAAAGRKPGLAVVLVGEDPASEVYVRNKGKATLAANMESFEYKLPADTTAQDLLALVKKLNGDPAVDGILVQLPLPDHLDEQSIIAAISPDKDVDGFHVINAGRLSVGQRGFVPCTPLGCMMLLADRLGDLSGLEAVVIGRSNIVGKPMAQLLLDANATVTIAHSRTRNLPEVVKRADIVVAAVGRAEMVKPEWLKDGATVIDVGINRLPPEPGKERGRLVGDVDFGRASEVAAAITPVPGGVGPMTIAVLLRNTLVAAHRNEGIDLPEDAI | Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. | Q2N7E3 |
Q48NZ0 | RL9_PSE14 | 50S ribosomal protein L9 | Pseudomonas | MQLILLEKVANLGNLGDKVNVKAGYGRNYLLPYGKATAATAANVAAFEERRAELEKLAADKKASAETRAAQLAELEVTITATAGDEGKLFGSIGTHDIADALTASGVEVAKSEVRLPNGTIRNVGEYDVAVHLHSDVEATVRVVVVAA | Binds to the 23S rRNA. | Q48NZ0 |
B1AIM0 | RL3_UREP2 | 50S ribosomal protein L3 | Ureaplasma | MKSLLGTKVGMTQVFTETGKAVAATVIYVEPNKVLAVKTNEKDGYSAIQIGYETVKEKALNKPLLGQFKKANSDPKRHIKEFRDVVAEVGAELTVSEFEPGQLVNAQAYTKGHGFTGSIKRHNFSMGPMGHGAGYPHRYVGSIAKGRGGSQAQRVFKGTKLPGHYGHELVTTKNLLVLDVKANENLILIKGAIPGPKGSIVLLKSAKKVGHIVSDPQVVNYLANKASSSEANE | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | B1AIM0 |
Q9AFA5 | CH60_TSUPA | Heat shock protein 60 | Tsukamurella | MAKTIAFDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNMAAGANPLGLKRGIEKAVEAVTEHLLKEAKEVETKEQIAATAGISAGDPAIGELIAEAMDKVGKEGVITVEESNTFGLQLELTEGMRFDKGFISGYFATDAERQEAVLEDAYILLVSSKISTVKDLLPLLEKVIQSGKPLAIIAEDVEGEALSTLIVNKIRGTFKSVAIKAPGFGDRRKAMLQDMAILTGGQVISEEVGLSLETAGLELLGQARQVVVTKDETTIVDGAGSKEQIEGRVSQIRAEIESSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGAALAQSGKVFETLNLEGDEATGANIVKVALDAPVKQIAINAGLEPGVVAEKVRNSPAGTGLNAATGVYEDLLAAGINDPVKVTRSALQNASSIAALFLTTEAVVADKPEKAGAPVDPTGGMGGMDF | 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. | Q9AFA5 |
Q4WNE1 | CFMC_ASPFU | GPI anchored CFEM domain protein C | Aspergillus subgen. Fumigati | MKFFSVSLALAACLSMAAAQGLDGLPDCAKSCATNSIPASCGLDVKCICTDSSFISGISCCVLQSCGPDQQQEDAHPFFPTAAVEFANRICKTAGVTNMPQSPSCANTTQSATGTASKSSTATSGSSTESNASQTAATATTSTTPPTSPTSPTSTTGSTTSSAASTTNTTTGAAVTQHKDIGLIALAGAALAAFGLLA | GPI-anchored cell wall protein involved in stabilizing the cell wall. Not implicated in virulence, heme uptake, and biofilm formation. | Q4WNE1 |
P59584 | RP8HA_ARATH | RPP8 homolog A | Arabidopsis | MAEGFVSFGLEKLWDLLSRESERLQGIDEQLDGLKRQLRSLQSLLKDADAKKHGSDRVRNFLEDVKDLVFDAEDIIESYVLNKLRGEGKGVKKHVRRLARFLTDRHKVASDIEGITKRISEVIGEMQSFGIQQIIDGGRSLSLQERQRVQREIRQTYPDSSESDLVGVEQSVTELVCHLVENDVHQVVSIAGMGGIGKTTLARQVFHHDLVRRHFDGFAWVCVSQQFTQKHVWQRILQELQPHDGEILQMDEYTIQGKLFQLLETGRYLVVLDDVWKKEDWDRIKAVFPRKRGWKMLLTSRNEGVGIHADPTCLTFRASILNPEESWKLCERIVFPRRDETEVRLDEEMEAMGKEMVTHCGGLPLAVKALGGLLANKHTVPEWKRVSDNIGSQIVGGSCLDDNSLNSVYRILSLSYEDLPTHLKHCFLHLAHYPEDSKIYTQDLFNYWAAEGIYDGSTIQDSGEYYLEELVRRNLVIADNRYLISEFKIKNCQMHDMMREVCLSKAKEENFLQIIKDPTCTSTINAQSPSRSRRLSIHSGKAFHILGHKRNAKVRSLIVSRFEEDFWIRSASVFHNLTLLRVLDLSWVKFEGGKLPCSIGGLIHLRYLRLYGAVVSHLPSTMRNLKLLLYLNLSVHNEDLIHVPNVLKEMIELRYLSIPVKMDDKTKLELGDLVNLEYLYGFSTQHTSVTDLLRMTKLRNLTVSLSERYNFKTLSSSLRELRNLETLYVLFSRKTYMVDHMGEFVLDHFIHLKELGLVVRMSKIPDQHQFPPHLVHIFLFYCGMEEDPMPILEKLHHLKSVQLRYKAFVGRRMVCSKDGFTQLCALDISKQSELEDWIVEEGSMPCLRTLTIHDCEKLKELPDGLKYITSLKELKIEGMKREWKEKLVPGGEDYYKVQHIPDVQFINCDQ | Disease resistance protein. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. In contrast to RPP8, it does not specifically recognize the Emco5 avirulence protein from Hyaloperonospora parasitica. | P59584 |
A1SYN3 | Y2894_PSYIN | Nucleotide-binding protein Ping_2894 | Psychromonas | MKLIVISGRSGSGKTIALHVLEDLGYNCIDGVPFQLLAQLIDTVDPKNNKVAISLDIRNLPTDASQIQTLLSSLQQKVEVEIIYLDAISAELIRRYSETRRLHPLSKNKLSLSQALELENELLEPIHKRAALSIDTTTLSIHNLNERLKIHLQGSTKSNLLIIFQSFGFKNIHPDDADYIFDVRFLPNPHWEPTLQKYTGKDQPVKAFLNGHLVVKQTINQIENLFHSWLPYLEENNRNYVTIAIGCTGGKHRSVYVAEQLAAQFKQKYQVQIEHKGLKDQL | Displays ATPase and GTPase activities. | A1SYN3 |
Q9XT00 | DHB8_PIG | Testosterone 17-beta-dehydrogenase 8 | Sus | MASQLRLRSALALVTGAGSGIGRAVSVRLAAEGAAVAACDLDGAAAQETVQLLGGPGSEKGAPSGPMAAFQADVSEAETARRLLEQVQAYFFRPPSVVVSCAGITRDEFLLRMSEDDWDKVIAVNLKGIFLVTQAAAQALVSSGCPGSIINISSIIGKVGNMGQTNYAASKAGVIGLTQAVARELGRYRIRCNSVLPGFIKTPMAQKVPQKVLDKVVGMIPMGHLGGPPDVADVVAFLASEDSGYITGASVEVTGGLFM | Required for the solubility and assembly of the heterotetramer 3-ketoacyl-[acyl carrier protein] (ACP) reductase functional complex (KAR or KAR1) that forms part of the mitochondrial fatty acid synthase (mtFAS). Alpha-subunit of the KAR complex, acts as scaffold protein, required for the stability of carbonyl reductase type-4 (CBR4, beta-subunit of the KAR complex) and for its 3-ketoacyl-ACP reductase activity, thereby participating in mitochondrial fatty acid biosynthesis. Catalyzes the NAD-dependent conversion of (3R)-3-hydroxyacyl-CoA into 3-ketoacyl-CoA (3-oxoacyl-CoA) with no chain length preference, this enzymatic activity is not needed for the KAR function. Prefers (3R)-3-hydroxyacyl-CoA over (3S)-3-hydroxyacyl-CoA and displays enzymatic activity only in the presence of NAD(+)(H). Cooperates with enoyl-CoA hydratase 1 in mitochondria, together they constitute an alternative route to the auxiliary enzyme pathways for the breakdown of Z-PUFA (cis polyunsaturated fatty acid) enoyl-esters. NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol (17beta-estradiol or E2). Has very low activity towards testosterone and dihydrotestosterone (17beta-hydroxy-5alpha-androstan-3-one). Primarily an oxidative enzyme, it can switch to a reductive mode determined in the appropriate physiologic milieu and catalyze the reduction of estrone (E1) to form biologically active 17beta-estradiol. | Q9XT00 |
Q3ILK1 | PANB_PSET1 | Ketopantoate hydroxymethyltransferase | Pseudoalteromonas | MSKITVSTLNKMKAEKNKITALTAYDASFAKLFHDNGVEVILVGDSLGMVLQGGDDTLGVTNQDIAYHTRCVRAGSRELFVIADMPFMTYSSPNDTCKNAAELMRAGANMVKLEGGEWLFESIEALTQQGIPVCGHLGLTPQSVHVFGGFKVQGRAEEQALKIIADAKALEAAGAQLLVLECIPSALAKRVTDALTIPTIGIGAGNTTDGQILVMHDLVGISAGFIPKFSKNFLLETGNMPEAVKKYCTDVKSGAFPSAEHEFK | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. | Q3ILK1 |
C1DKL6 | RL2_AZOVD | 50S ribosomal protein L2 | Azotobacter | MAIVKCKPTSAGRRFVVKVVNQELHKGAPYAPLLEKKSKSGGRNNNGRITTRHIGGGHKQHYRLVDFRRNKDGIPATVERIEYDPNRTAHIALLKYADGERRYIIAPKGVVAGDQLISGVNAPIKAGNTLPLRNIPVGSTIHGVELKPGKGAQIARSAGASAQLVAREGAYVTLRLRSGEMRKVLADCRATLGEVSNSEHSLRSLGKAGAKRWRGVRPTVRGVAMNPVDHPHGGGEGRTSGGRHPVSPWGFPTKGAKTRSNKRTDNMIVRRRK | 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. | C1DKL6 |
A3QFJ5 | DNLJ_SHELP | Polydeoxyribonucleotide synthase [NAD(+)] | Shewanella | MQAIQDEIKQLTDELNQHNYRYYVDDAPSIPDAEYDRLMRRLQELEAEHPELALADSPTQRVGGEALSKFNQVTHLKPMLSLDNVFSEEEFNAFYKRVGDKLPDTPAFCCEPKLDGLAVSILYRDGVFERAATRGDGTVGEDITENVRTIKSVPLRLRGSGFPPLLEVRGEVFMPKAAFEAVNDKARAKGEKLFVNPRNAAAGSLRQLDSKITASRSLAFYAYALGVVEPETWPLAASHFEQLVQLKEWGCPVSSEVKVCADIPSVLAYYQDILTRRSELAYEIDGVVLKVNDIAQQQTLGFVAKAPRWATAYKFPAQEEITQLEGVDFQVGRTGAVTPVARLQPVFVGGVTVSNATLHNADEIARLGVMIGDSVIIRRAGDVIPQVVAVVPEKRPSDAQAIQFPPQCPVCGSDVERVEGEAVARCTGGLVCEAQRKEAIKHFASRKALDIDGMGDKVVEQLIDKELVASPADLFKLTASAITMLDRMGMKSATNLVNALEAAKQTTFARFLYSLGIREVGEATAANLANYFKTLEHLKQADAETFMKVDDVGVIVAQHLVHFFEQPHNLEVIDGLLQAGVHWPDIEEVAEEALSLKGQTWVLTGTLTQLNRNDAKAKLQALGAKVAGSVSKNTDCLVAGEAAGSKLTKAQELGVKVIDEAELLAILGS | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | A3QFJ5 |
C3PPA4 | RL2_RICAE | 50S ribosomal protein L2 | spotted fever group | MALKNFNPITPSLRELVQVDKTSLWKGRPLKSLTKGISKTGGRNNQGRITSWHRGGGHKKLYRIIDFKRNKIDISAIVERIEYDPNRTAFIALIKYEDGEYSYILAPQKLSVGDRVISSQDADIKIGNCLPLKCIPIGTTLHNVEMKVGKGGQIARSAGTSVDLVGKDSGYAQIKLRSGEFRLVPLDCKATIGSISNPDQKNINLGKAGRNRWLGWRPHVRGVAMNPVDHPHGGGEGKTSGGRHPVTPWGFPTKGKKTRKNKRTSKFIVKKRK | 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. | C3PPA4 |
P22626 | ROA2_HUMAN | Heterogeneous nuclear ribonucleoproteins A2/B1 | Homo | MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY | (Microbial infection) Involved in the transport of HIV-1 genomic RNA out of the nucleus, to the microtubule organizing center (MTOC), and then from the MTOC to the cytoplasm: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) sequence motifs present on HIV-1 genomic RNA, and promotes its transport. | P22626 |
Q969P5 | FBX32_HUMAN | Muscle atrophy F-box protein | Homo | MPFLGQDWRSPGQNWVKTADGWKRFLDEKSGSFVSDLSSYCNKEVYNKENLFNSLNYDVAAKKRKKDMLNSKTKTQYFHQEKWIYVHKGSTKERHGYCTLGEAFNRLDFSTAILDSRRFNYVVRLLELIAKSQLTSLSGIAQKNFMNILEKVVLKVLEDQQNIRLIRELLQTLYTSLCTLVQRVGKSVLVGNINMWVYRMETILHWQQQLNNIQITRPAFKGLTFTDLPLCLQLNIMQRLSDGRDLVSLGQAAPDLHVLSEDRLLWKKLCQYHFSERQIRKRLILSDKGQLDWKKMYFKLVRCYPRKEQYGDTLQLCKHCHILSWKGTDHPCTANNPESCSVSLSPQDFINLFKF | Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins during skeletal muscle atrophy. Recognizes TERF1. | Q969P5 |
B3PN01 | HRCA_META1 | Heat-inducible transcription repressor HrcA | Metamycoplasma | MEKRTNYPQLTEKQNHFFKLIVDTYIKTGASVASKELVKRCNLKCSSATIRNVMASLEQIGFLEKYHISSGRVPSTLGLEYYAKFLVYNPKKYFDQKLEDLLAKRRIKIDATLEEAAAIVSEVAGVTVVATSNNAAETMKSIQLTTLSELSAIVVIVTSSGRVESKIFNFENSDISLEDLRVAIRLFKERLVDTPLIHLANKARALTPIFGQQLKNYELILQKFIKNIFVFEEETTNKTFNKGAIVLSRNISREEIANVLDLIEKHSVWESIDNDLDEDNNIKLDVSRPNLSIISKKIDFSNEKNIKEITVIGPNNLDYGESFEALEMLEKIIKEKK | Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. | B3PN01 |
O47667 | COX2_CANAD | Cytochrome c oxidase polypeptide II | Canis | MAYPFQLGLQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETVWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLNFDSYMIPTQELKPGELRLLEVDNRVVLPMEMTIRMLVSSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMAMRPGLYYGQCSEICGSNHSFMPIVLEMVPLSYFETWSALMV | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. | O47667 |
A8L6G0 | RS15_FRASN | 30S ribosomal protein S15 | unclassified Frankia | MPLSGDVKQKIMSDYATVDRDTGSPEVQVAMLTRRISDLTEHLKVHKHDHHSRRGLLLLVGRRRRLLNYLAKTDINRYRALIERLGLRR | Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. | A8L6G0 |
B4THH4 | METK_SALHS | Methionine adenosyltransferase | Salmonella | MAKHLFTSESVSEGHPDKIADQISDAVLDAILQQDPKARVACETYVKTGMVLVGGEITTSAWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADPLEQGAGDQGLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVGIDAVVLSTQHAEDIDQKSLQEAVMEEIIKPILPSEWLNTSTKFFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSYAIGVAEPTSIMVETFGTEKVPVEQLILLVREFFDLRPYGLIQMLDLLHPIYKETAAYGHFGRENFPWEKTDKAQLLRDAAGLK | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | B4THH4 |
Q5PF36 | NORW_SALPA | Flavorubredoxin reductase | Salmonella | MSRGIIIIGSGFAARQLVKNIRKQDAHVPLTLIAADSMDEYNKPDLSHVISQSQRADDLTRQLAGEFAEQFNLRLFPHTWVTDIDADAHVVKSQDKQWQYDKLVLATGAAAFVPPIAGRELMLTLNNQQEYRACETPLRDAQRVLIVGGGLIGSELAMDFCRAGKTVTLMDNAASLLASLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKIEAGIRATLASQRSIEVDAVIAATGLRPETALARRAGVVVNRGVCVDSYLQTSHPDIYAIGDCAEINGQVLPFLQPIQLSAMYLAKNLLGGNAPLKLPAMLVKVKTPELPLHLAGETQRRDLSWQITAESDGMIAKGMSGEGQLRAFVVSEDRMKEAFALLKTLSV | One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase. | Q5PF36 |
B2GM13 | ENO_KOCRD | 2-phosphoglycerate dehydratase | Kocuria | MAMIIALQARQILDSRGNPTVEVEALLDDGSFGRAAVPSGASTGEFEAVERRDGDKKVYQGKGVLDAVHAVDEELEQVVVGLDASDQRAVDQAMLELDGTDNKAKLGANAILGASMAIARAAASSADLPLYKYLGGPNAHVLPVPMMNILNGGSHADSNVDIQEFMIAPIGAPTFSEALRWGVEVYHSLKSVLKDRGLSTGLGDEGGFAPNLESNAAALDLILEAIDKAGYKPGRDIALALDVASSEFFDKGTYTFEGKKRSAEEMSAYFADLVEKYPLVSIEDPLDEDDWKGWATLTEHIGDKVQLVGDDLFVTNPERLARGIQEGVANALLVKVNQIGSLTETFDAVELAQRNGYRCMISHRSGETEDTTIADIAVAVNAGQIKTGAPARSERVAKYNQLLRIEEELGDAATYAGASAFPRFAAK | Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. | B2GM13 |
P23789 | XRE_BACSU | Putative PBSX repressor | Bacillus | MIGGRLKSLRGKRTQEEIASHIGVSRARYSHYENGRSEPDYDTLQKLADYFQVTTDYLLTGKDKKSDDDMFSDPDLQLAYRDMQDFSPESKQQAIEFINYLKEKEKNRKPKNK | Repressor of PBSX. Binds to four sites close to its own gene. Necessary for the maintenance of the lysogenic state. | P23789 |
Q6YQC1 | END4_ONYPE | Endonuclease IV | Candidatus Phytoplasma asteris | MLFLGSHVAMKKPHNFQGAIQTAISYGANALMVYSGAPQNTIRTKTEELKIKQALEIVQNNNLSLNNLVGHAPYIINLANPDETKRAFAIDFLSQELERFAAMKINKMVLHPGNYLKTNPQEGISLIAQSLDLIFEKTKHLKTQVALETMAGKGTEIGKNLEELQQIRTQVKNNTRVSFCLDTCHLFDAGYDLKENLEEIIQKIDSILGFQNISVIHINDSKNECNSHKDRHENIGFGKIGFETLLKIIYHRAFACIPKILETPYINDKAPYKREIEMIKAKAFNPELKKLF | 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. | Q6YQC1 |
Q86TU7 | SETD3_HUMAN | SET domain-containing protein 3 | Homo | MGKKSRVKTQKSGTGATATVSPKEILNLTSELLQKCSSPAPGPGKEWEEYVQIRTLVEKIRKKQKGLSVTFDGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEELFLWVPRKLLMTVESAKNSVLGPLYSQDRILQAMGNIALAFHLLCERASPNSFWQPYIQTLPSEYDTPLYFEEDEVRYLQSTQAIHDVFSQYKNTARQYAYFYKVIQTHPHANKLPLKDSFTYEDYRWAVSSVMTRQNQIPTEDGSRVTLALIPLWDMCNHTNGLITTGYNLEDDRCECVALQDFRAGEQIYIFYGTRSNAEFVIHSGFFFDNNSHDRVKIKLGVSKSDRLYAMKAEVLARAGIPTSSVFALHFTEPPISAQLLAFLRVFCMTEEELKEHLLGDSAIDRIFTLGNSEFPVSWDNEVKLWTFLEDRASLLLKTYKTTIEEDKSVLKNHDLSVRAKMAIKLRLGEKEILEKAVKSAAVNREYYRQQMEEKAPLPKYEESNLGLLESSVGDSRLPLVLRNLEEEAGVQDALNIREAISKAKATENGLVNGENSIPNGTRSENESLNQESKRAVEDAKGSSSDSTAGVKE | Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-73' . Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery . Does not have protein-lysine N-methyltransferase activity and probably only catalyzes histidine methylation of actin . | Q86TU7 |
Q6GGB8 | HRCA_STAAR | Heat-inducible transcription repressor HrcA | Staphylococcus | MITDRQLSILNAIVEDYVDFGQPVGSKTLIERHNLNVSPATIRNEMKQLEDLNYIEKTHSSSGRSPSQLGFRYYVNRLLEQTSHQKTNKLRRLNQLLVENQYDVSSALTYFADELSNISQYTTLVVHPNHKQDIINNVHLIRANPNLVIMVIVFSSGHVEHVHLASDIPFSNDKLNTISNFVTNKLTEFNQNLQDDIVSFVQSEQEEIFINKLLNTMNNHISNQSNSIYMGGKVKLIDALNESNVSSIQPILQYIESNRIAELLQDISSPNINVKIGNEIDDSLSDISIVTSQYHFDETLKGQIAVIGPTAMHYQNVIQLLNRIW | Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. | Q6GGB8 |
Q9FFP1 | ARI14_ARATH | RING-type E3 ubiquitin transferase ARI14 | Arabidopsis | MEYDGRRPYSVLTRNEITVKMKKQINEISDIFFISNSDATVLLMYLRWDSLRVSERLGENKEKLLMDSGLKSVMIDPSPDSSSEISLETDVYEFDGDNDLISMPFCSHKFDSKYWREYLEKNFYYVEKIQTTISCPDQDCRSAVGPDTIEKLTVRDQEMYERYIWRSYIEGNKVLMIKQCPARNCDYVIEFHQENDDDDEYSLNVVCICGHIFCWRCRLESHRPVSCNKASDWLCSATMKISDESFSLYPTKTKTVTCPHCLCSLESDTKMPQFLTCVCRLRFCSRCLRSEEAHKIEAVDSGFCIKTEVGILCEDRWNVCQKLLEQAKSDLEAFEETNIKKPSDLLREQDIMIIREGLMLIVQCRRVLKWCCVYDYFHTEYENSKEYLRYLQGNAIATLQSYSNTLQEQKDIVLAAATYEECTFFRHTIPTATSNIGNYFYDFMKTLQDGLVDVKVKSYNGGTGPFWYCDRCTYANTWEDNECEMCYDDSASLVGEISDLFLNKVS | Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates . Regulates negatively male gametophyte formation and double fertilization . | Q9FFP1 |
B5F5L4 | METK_SALA4 | Methionine adenosyltransferase | Salmonella | MAKHLFTSESVSEGHPDKIADQISDAVLDAILQQDPKARVACETYVKTGMVLVGGEITTSAWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADPLEQGAGDQGLMFGYATNETDVLMPAPVTYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVGIDAVVLSTQHAEDIDQKSLQEAVMEEIIKPILPSEWLNTSTKFFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSYAIGVAEPTSIMVETFGTEKVPAEQLILLVREFFDLRPYGLIQMLDLLHPIYKETAAYGHFGRENFPWEKTDKAQLLRDAAGLK | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | B5F5L4 |
Q1QS30 | IHFB_NITHX | Integration host factor subunit beta | Nitrobacter | MIKSELVQRIAEHNPHLYQRDVENIVNAILDEIVTALARGDRVELRGFGAFSVKHRPARAGRNPRTGEHVPVDQKSVPFFKTGKEMRERLNRENATSEASA | This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. | Q1QS30 |
Q5E2K3 | PLSY_ALIF1 | Lysophosphatidic acid synthase | Aliivibrio | MTPLALIMIIIAYLLGSISSAVLICRLKGLPDPRTSGSHNPGATNVFRIGGRSAAGLVLLCDILKGMLPVWGGYFLEINPFMLGIIAISACLGHMYPLFFHFKGGKGVATALGALAPIGLDLTGMLFGCWVVTVLVTGYSSLASMITALLAPLFTWLVKPQYTLPVAMLSCLIVLKHHENIKRFFEGKETKIWQRKRD | Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. | Q5E2K3 |
A8MVX0 | ARG33_HUMAN | Rho guanine nucleotide exchange factor 33 | Homo | MEKTKTKQGENEHMPVNNPSTQIYQLQALASELKTGFTEAMQELSRIQHGEYALEEKVKSCRCSMEEKVTEMKNSLNYFKEELSNAMSMIQAITSKQEEMQQKIEQLQQEKRRESRKVKAKKTQKEEHSSQAGPAQAQGSPFRSINIPEPVLPSEDFTNLLPSQAYEKAQESRSVHVGDSNVKGMMGPGVNPTTPEAEENLKSCLSADIQSKGHLPSGMWRQPKDGKEWGEEYVTKDHPDKLKEAGQGRHSSLENVLCETSLAAKRQTVALELLESERKYVINISLILKIKATFQGSDGKRNSKERSLFPGSLRYLVQQHLDLLHALQERVLKWPRQGVLGDLFLKLTNDENNFLDYYVAYLRDLPECISLVHVVVLKEGDEEIKSDIYTLFFHIVQRIPEYLIHLQNVLKFTEQEHPDYYLLLVCVQRLRVFISHYTLLFQCNEDLLIQKRKKLKKSSMAKLYKGLASQCANAGQDASPTAGPEAVRDTGIHSEELLQPYPSAPSSGPAITHLMPPVKKSQQQQSLMESMQPGKPSDWELEGRKHERPESLLAPTQFCAAEQDVKALAGPLQAIPEMDFESSPAEPLGNVERSLRAPAELLPDARGFVPAAYEEFEYGGEIFALPAPYDEEPFQAPALFENCSPASSESSLDICFLRPVSFAMEAERPEHPLQPLPKSATSPAGSSSAYKLEAAAQAHGKAKPLSRSLKEFPRAPPADGVAPRLYSTRSSSGGRAPIKAERAAQAHGPAAAAVAARGASRTFFPQQRSQSEKQTYLEVRREMHLEDTTRFCPKEERESEQTSFSDQNPRQDQKGGFRSSFRKLFKKKNGNATGEDFCGPWGWW | May act as a guanine-nucleotide releasing factor. | A8MVX0 |
Q6G252 | IF1_BARHE | Translation initiation factor IF-1 | Bartonella | MSKEEVLEFSGIVTELLPNAMFRVKLENDHEIIAHTAGRMRKNRIRVLAGDKIMVEMTPYDLTKGRIIYRYK | 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-2 and IF-3 are released leaving the mature 70S translation initiation complex. | Q6G252 |
B2AWV6 | AMPP1_PODAN | Prolidase | Podospora anserina | MRHIWALPSLTALSLFQASAASAVPRARQAINTSSPLAPFRTKRRFRTQAQLLSNSATKTTLVEEMVTVDTTSRLAALRSLMKERNLHVYVVPSEDSHASEYIADCDARRTFISGFSGSAGTAIVTLDKAALATDGRYFNQASKQLDSNWYLLKTGMQDVPTWQEWATQEAEGGKLIGVDPQLISSAIAEKLDEDIKNAGGGGLVGIKENLVDLVWGSEQPPRPSNSVFLLGQQYAGKDTAAKLADLRKELDKKKAAGFVLSMLDEIAWLFNLRGSDIAYNPVFFSYAIVTQASATLYIDEAKLTDECKTYLERNKVTIKPYGALFEDSEELARRAEADSKDAKPRKYLISSKGSWALKLALGGNKFVDEVRSPVGDAKAVKNDVELNGMRNCHIRDGAALTEFFAWLEDQLVNQKAQLDEVDAADKLEQIRSKHKDFVGLSFDTISSTGANAAVIHYKPEKGACKIIDPNAIYLCDSGAQYLDGTTDTTRTLHFGTPTAKEKKAYTLVLKGNIALDSVVFPKGTSGFAIDVMARQFLWKYGLDYRHGTGHGVGSFLNVHEGPIGIGTRKQYIDVALAAGNVLSIEPGYYEDEAFGIRIENLAIVKEVKTEHSFGDKPYLGFEHVTMVPYARNLIDETLLTPDEKDWLNRANKKILEKTLGYFENDPLTKAWLLRETQPF | Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. | B2AWV6 |
A5F6X0 | CLPP_VIBC3 | Endopeptidase Clp | Vibrio | MSPIFDALVPMVVEQTSRGERSYDIYSRLLKERVIFLTGQVEDHMANLVVAQLLFLESENPDKDIFLYINSPGGSVTAGMSIYDTMQFIKPNVSTVCMGQACSMGAFLLAGGAPGKRYVLPNSRVMIHQPLGGFQGQASDIQIHAQEILTIKNKLNRLLAEHTGQPIEVIERDTDRDNFMSADQAVEYGLVDAVLKHRGE | Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. | A5F6X0 |
A4J3G3 | NADK_DESRM | ATP-dependent NAD kinase | Desulforamulus | MNTIGLVVNSSKGDVAKPVREVISWLAEQRIKVLYNEESAVLLGCPEEGISTRELGAQCDCIMVWGGDGTLLNCARQTASSGTPIFGVNLGRLGFLTEIDIPDLRERLQALIAGHFYIEERMMLEATVIRGGQVVDQAVCLNDAVVSKGASFRMVQLRILVNNEFVGSFAADGVIVASPTGSTAYSLAAGGPIISPDMEAMLITPICPHSLSNRPIVISPQSKVEVQVLPYVDKVGLNLDGQYGLPLREGDRILINRATVKARFLKIQKTGFYDVLREKLKEWQNGLD | Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. | A4J3G3 |
Q90922 | NET1_CHICK | Netrin-1 | Gallus | MPRRGAEGPLALLLAAAWLAQPLRGGYPGLNMFAVQTAQPDPCYDEHGLPRRCIPDFVNSAFGKEVKVSSTCGKPPSRYCVVTEKGEEQVRSCHLCNASDPKRAHPPSFLTDLNNPHNLTCWQSDSYVQYPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGKTWVPFQFYSTQCRKMYNKPSRAAITKQNEQEAICTDSHTDVRPLSGGLIAFSTLDGRPTAHDFDNSPVLQDWVTATDIKVTFSRLHTFGDENEDDSELARDSYFYAVSDLQVGGRCKCNGHASRCVRDRDDNLVCDCKHNTAGPECDRCKPFHYDRPWQRATAREANECVACNCNLHARRCRFNMELYKLSGRKSGGVCLNCRHNTAGRHCHYCKEGFYRDLSKPISHRKACKECDCHPVGAAGQTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPCIKIPAAPPPTAASSTEEPADCDSYCKASKGKLKINMKKYCKKDYAVQIHILKAEKNADWWKFTVNIISVYKQGSNRLRRGDQTLWVHAKDIACKCPKVKPMKKYLLLGSTEDSPDQSGIIADKSSLVIQWRDTWARRLRKFQQREKKGKCRKA | Netrins control guidance of CNS commissural axons and peripheral motor axons. Promotes neurite outgrowth from commissural axons but acts as a chemorepellent for trochlear motor axons. These effects are mediated by distinct receptors. | Q90922 |
Q6PFX2 | BEND6_MOUSE | BEN domain-containing protein 6 | Mus | MQKILQTDDITDNQVLRKRKRKRTETANSENANSALEKAQRDPYSGNAFLPGESSSDEETPLMELSKEELCNKIESLKEKLRSIRKENSRLRQSLVMLQVLPQAVTQFEELVGMAETLLKSGGAVSTPASTLWRATNNSSPDSFASLCSNSNSTSSSPSSVKAEEEQHPGEKQFTIERWQIARCNKSKPQKFINDLMQVLYTNEYMATHSLTGAKSSTSRDKVVKPAMNQNEVQEIIGVTKQVFPSADDVSIRRMIGQKLNNCTKKPNASKAPNSQDGILK | Acts as a corepressor of recombining binding protein suppressor hairless (RBPJ) and inhibits Notch signaling in neural stem cells, thereby opposing their self-renewal and promoting neurogenesis . | Q6PFX2 |
Q6TEN6 | WDR91_DANRE | WD repeat-containing protein 91 | Danio | MASAVERTDDLVREYLIYRGFTSTLKHLDSEIKTDKEKGFRVDKIMDQLQLLIQSCDLTGLKEYWANLERRLFCRLEDVYKPTVSKLRTSLYRFYLIHTVQVKNVEKTQEFFQKQALELQAQAEWRDWFSLPFIPAPEQNPSFSAYFSRQWADTFLVSLHNFLSVLFQCMPLPALLSFDSEVQRITSLQEDNEQLRQTVFALQGESRLKKDEQMVHHKLPPYVQHMDRLGDTELDLVSSQRNVNMATPSRNFFSTFLPQGRRAPGRTAPGPQSSPTQSALGRKDAAASMQSSKAKDKEVKPPSVSSMTAELSTSHPRQRRHQDHEKERKELFSKHAAQGSEKKTDSDPDTQTEAPPDQTDSANQTRVCDVGGAGAEQPFIKLSQEEYGEHHSSIMHCRVDCSGRRVASLDVDGVVKVWAFNPIMQTKATIMSKSPLLSLEWAAKPDRLLLLGSGVGTVKLYDTDAKKCLYEMTIDDVHPRILSLACSPSGTSFVCSAAAHSGAVMESEPRGSAPVSGQLLLWDTKTVKQQLQFALEPGPVAINCTAFNHNGNLLVTGAADGIIRLFDMQRYESALSWKAHDGEVYSVEFSYDENTVFSIGEDGKFVQWNIHRCGVKQSEYSLSQDAVGPFVLSGYSGYKQVQVPRGRLFAFDSEGQHVLTCSSTGGNIYRLNKAEAGLESVLSLAGHKAPVVTVDWCSAMDCGTCLTASMDGKIKLSTLLAQKP | Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport. | Q6TEN6 |
Q9WTM2 | DDX6_CAVPO | Oncogene RCK homolog | Cavia | MGLSSQNGQLRGPVKPSGGPGGGGTQTQQQMNQLKNTNTINNGTQQQAQSMTTTIKPGDDWKKTLKLPPKDLRIKTSDVTSTKGNEFEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALTGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELALQVSQICIQVSKHMGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINLMEELTLKGVTQYYAYVTERQKVHCLNTLFPRLQTNQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEIKPIPSNIDKSLYVAEYHSEPVEDEKP | Essential for the formation of P-bodies, cytosolic membrane-less ribonucleoprotein granules involved in RNA metabolism through the coordinated storage of mRNAs encoding regulatory functions. Plays a role in P-bodies to coordinate the storage of translationally inactive mRNAs in the cytoplasm and prevent their degradation. In the process of mRNA degradation, plays a role in mRNA decapping. Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts. | Q9WTM2 |
P36160 | RPF2_YEAST | Ribosome biogenesis protein RPF2 | Saccharomyces | MIRTVKPKNARAKRALVKREAKLVENVKQALFIPGQSCNKNLHDIMVDLSALKKPDMKRFNRKNDIHPFEDMSPLEFFSEKNDCSLMVLMTSSKKRKNNMTFIRTFGYKIYDMIELMVADNFKLLSDFKKLTFTVGLKPMFTFQGAAFDTHPVYKQIKSLFLDFFRGESTDLQDVAGLQHVISMTIQGDFQDGEPLPNVLFRVYKLKSYKSDQGGKRLPRIELVEIGPRLDFKIGRIHTPSPDMVTEAHKKPKQLEMKTKKNVELDIMGDKLGRIHMGKQDLGKLQTRKMKGLKSKFDQGTEEGDGEVDEDYEDEASYSDDGQEYEEEFVSATDIEPSAKRQKK | Required for biogenesis of the 60S ribosomal subunit. | P36160 |
A4VR22 | PSD_PSEU5 | Phosphatidylserine decarboxylase beta chain | Pseudomonas | MKDRLFVISQYVLPHHLISRLAGCLAECRLPWVKNTFIKWFVRHFQVDMREAQIEEPTAYEHFNAFFTRALKDGARPLDSTPGAILNPCDGAISQLGKIEQGRIFQAKGHSFSAMELLGGDHERAAPFMGGAFATVYLSPKDYHRVHMPVSGTLREMVYVPGRIFSVNTVTAQGVPELFARNERVVCLFDTEHGPMAMVLVGAMIVASIETVWAGLVTPPKRSLKTFRYDEAARAPIHLEKGAEMGRFKLGSTVILLFGPDRVRWAEQLGPLSPVCMGESLGQAAITAAASEAIELQ | Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). | A4VR22 |
Q7T2N4 | RL15_SILME | 60S ribosomal protein L15 | Silurus | MGASKYMQELWRKKQSDVMRFLLRVRCWQYRQLSALHRAPRPTRPDKARRLGYKAKQGYVIYRVRVRRGGRKRPVPKGATYGKPVHHGVNQLKFARSLQSIAEERAGRHCGGLRVLNSYWVGEDSTYKFFEVILIDTFHKAIRRNPDMQWITKAVHKHREMRGLTSAGKKSRGLGKGHKFHLTIGGSRRAAWRRRNTLQLHRYR | Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. | Q7T2N4 |
B8D6X3 | CCA_BUCAT | tRNA-NT | Buchnera | MKIYLVGGAVRDSLLNLPVKDKDWVVVGGTEKILLERNFQQVGKDFPVFLHPETHEEYALARKERKSGKGYTGFDTDCNSDVTLEEDLIRRDLTINAIAQDEYGNYIDPFQGKKDIECGLIRHVSESFIEDPLRVLRVARFAATLVHLGFKIAEETMLLMCIIVKKQELSYLTSNRIWNETEKALKTLNPHVYFQVLYECNALHFFFPEMYFLYEKKNFLNRSFFKKFCNKNIILMGLAEISLLNKDIDVRFSYLCQFLSVNQIDRNYSKIFFDSYAASIIHSLCKRFKIPSYIRDIAVLNTGFYFFLNTIHYQSSKNIINLFSKVDAWRKPDRVKKLAFLSNFNFLRNFKSEFFCIKSGCFLEKCFSVVKNVSIKLILKKGFKGYEIKQEITRLRIKKLEFWRIKNIKHRFYL | 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. | B8D6X3 |
B0CRK4 | EFTS_LACBS | Elongation factor Ts, mitochondrial | Laccaria | MYRNCRKAFTFSLRHYSTAPTEKPSLKLVAELRKRTEVSITKAREALSASNNDVSAALEWLQKDLITSGAKKAAKLGGRPTPEGLISVSVLSRGGESHVAGVRAAMIELNCETDFVGRNELFGRLAADIAHTAAYISDRTGSATAFNRAFPLDVLKDAPLLSQLNPTAPPTGTVGSSIRDMISKVGENVSLRRALAVVENSPSPNGDIALRIGSYVHDYKIGSLALLALKSRGISSSLNSDAFRERLEFLERALARQILGFETTSVNSSEDQTSLYNQPFMMFSREMDSPLVGEVLRNWSEKEGLLKENSDGGVAVLDFAKWKVGETFDE | Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. | B0CRK4 |
P29040 | XPSN_XANCP | Protein XpsN | Xanthomonas | MRLEMIGLRTWLLATVVGWALLVCVLAVAGLGKRVELLPDDPALVQRLPALPAPAPERLGPFEKYAEIAAHPAFAEDRLPHPFFLSGNDGSGAASTVRLTGVLLTSTFKMATLTLDPADSVRVQLGGDAVKGYRLLALQPRSATIEGPGGTQTLELQVFNGQGGQPPTAIGGRPQAPGAVPPLPPNVPPAPATPAPPPAEVPQQQPGGQAPPTVPPQRSDGAQEAPRPSDEQMRAIRERIEARRRQLQQQRQGGSTPGQTQ | Involved in a general secretion pathway (GSP) for the export of proteins. | P29040 |
P61909 | DUT_LEPIC | dUTP pyrophosphatase | Leptospira | MKIFVQKLRPNAELPLLQTKQAAGYDIHACLDSKLVLEPGNVGLVPTGLSFAIPQEFHFEIRPRSGFSTKNRILIPNSPGTIDSDYRGELMIPLLNLGDSSFIIEHGMRIAQLLIRKTWYADWELVSEFADRTERGANGFGSTGH | This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. | P61909 |
Q9UGU0 | TCF20_HUMAN | Stromelysin-1 PDGF-responsive element-binding protein | Homo | MQSFREQSSYHGNQQSYPQEVHGSSRLEEFSPRQAQMFQNFGGTGGSSGSSGSGSGGGRRGAAAAAAAMASETSGHQGYQGFRKEAGDFYYMAGNKDPVTTGTPQPPQRRPSGPVQSYGPPQGSSFGNQYGSEGHVGQFQAQHSGLGGVSHYQQDYTGPFSPGSAQYQQQASSQQQQQQVQQLRQQLYQSHQPLPQATGQPASSSSHLQPMQRPSTLPSSAAGYQLRVGQFGQHYQSSASSSSSSSFPSPQRFSQSGQSYDGSYNVNAGSQYEGHNVGSNAQAYGTQSNYSYQPQSMKNFEQAKIPQGTQQGQQQQQPQQQQHPSQHVMQYTNAATKLPLQSQVGQYNQPEVPVRSPMQFHQNFSPISNPSPAASVVQSPSCSSTPSPLMQTGENLQCGQGSVPMGSRNRILQLMPQLSPTPSMMPSPNSHAAGFKGFGLEGVPEKRLTDPGLSSLSALSTQVANLPNTVQHMLLSDALTPQKKTSKRPSSSKKADSCTNSEGSSQPEEQLKSPMAESLDGGCSSSSEDQGERVRQLSGQSTSSDTTYKGGASEKAGSSPAQGAQNEPPRLNASPAAREEATSPGAKDMPLSSDGNPKVNEKTVGVIVSREAMTGRVEKPGGQDKGSQEDDPAATQRPPSNGGAKETSHASLPQPEPPGGGGSKGNKNGDNNSNHNGEGNGQSGHSAAGPGFTSRTEPSKSPGSLRYSYKDSFGSAVPRNVSGFPQYPTGQEKGDFTGHGERKGRNEKFPSLLQEVLQGYHHHPDRRYSRSTQEHQGMAGSLEGTTRPNVLVSQTNELASRGLLNKSIGSLLENPHWGPWERKSSSTAPEMKQINLTDYPIPRKFEIEPQSSAHEPGGSLSERRSVICDISPLRQIVRDPGAHSLGHMSADTRIGRNDRLNPTLSQSVILPGGLVSMETKLKSQSGQIKEEDFEQSKSQASFNNKKSGDHCHPPSIKHESYRGNASPGAATHDSLSDYGPQDSRPTPMRRVPGRVGGREGMRGRSPSQYHDFAEKLKMSPGRSRGPGGDPHHMNPHMTFSERANRSSLHTPFSPNSETLASAYHANTRAHAYGDPNAGLNSQLHYKRQMYQQQPEEYKDWSSGSAQGVIAAAQHRQEGPRKSPRQQQFLDRVRSPLKNDKDGMMYGPPVGTYHDPSAQEAGRCLMSSDGLPNKGMELKHGSQKLQESCWDLSRQTSPAKSSGPPGMSSQKRYGPPHETDGHGLAEATQSSKPGSVMLRLPGQEDHSSQNPLIMRRRVRSFISPIPSKRQSQDVKNSSTEDKGRLLHSSKEGADKAFNSYAHLSHSQDIKSIPKRDSSKDLPSPDSRNCPAVTLTSPAKTKILPPRKGRGLKLEAIVQKITSPNIRRSASSNSAEAGGDTVTLDDILSLKSGPPEGGSVAVQDADIEKRKGEVASDLVSPANQELHVEKPLPRSSEEWRGSVDDKVKTETHAETVTAGKEPPGAMTSTTSQKPGSNQGRPDGSLGGTAPLIFPDSKNVPPVGILAPEANPKAEEKENDTVTISPKQEGFPPKGYFPSGKKKGRPIGSVNKQKKQQQPPPPPPQPPQIPEGSADGEPKPKKQRQRRERRKPGAQPRKRKTKQAVPIVEPQEPEIKLKYATQPLDKTDAKNKSFYPYIHVVNKCELGAVCTIINAEEEEQTKLVRGRKGQRSLTPPPSSTESKALPASSFMLQGPVVTESSVMGHLVCCLCGKWASYRNMGDLFGPFYPQDYAATLPKNPPPKRATEMQSKVKVRHKSASNGSKTDTEEEEEQQQQQKEQRSLAAHPRFKRRHRSEDCGGGPRSLSRGLPCKKAATEGSSEKTVLDSKPSVPTTSEGGPELELQIPELPLDSNEFWVHEGCILWANGIYLVCGRLYGLQEALEIAREMKCSHCQEAGATLGCYNKGCSFRYHYPCAIDADCLLHEENFSVRCPKHKPPLPCPLPPLQNKTAKGSLSTEQSERG | Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator. | Q9UGU0 |
P0C8F1 | PATE4_HUMAN | PATE-like protein B | Homo | MRKMNTLLLVSLSFLYLKEVMGLKCNTCIYTEGWKCMAGRGTCIAKENELCSTTAYFRGDKHMYSTHMCKYKCREEESSKRGLLRVTLCCDRNFCNVF | May modulate the function of nicotinic acetylcholine receptors. May enhance sperm motility. | P0C8F1 |
Q61079 | SIM2_MOUSE | SIM transcription factor | Mus | MKEKSKNAAKTRREKENGEFYELAKLLPLPSAITSQLDKASIIRLTTSYLKMRAVFPEGLGDAWGQPSRTGPLDSVAKELGSHLLQTLDGFVFVVASDGKIMYISETASVHLGLSQVELTGNSIYEYIHPSDHDEMTAVLTAHPPLHHHLLQEYEIERSFFLRMKCVLAKRNAGLTCSGYKVIHCSGYLKIRQYMLDMSLYDSCYQIVGLVAVGQSLPPSAITEIKLHSNMFMFRASLDLKLIFLDSRVTELTGYEPQDLIEKTLYHHVHGCDTFHLRYAHHLLLVKGQVTTKYYRLLSKLGGWVWVQSYATVVHNSRSSRPHCIVSVNYVLTDVEYKELQLSLDQVSTSKSQESWRTTLSTSQETRKSAKPKNTKMKTKLRTNPYPPQQYSSFQMDKLECSQVGNWRTSPPTNAVAPPEQQLHSEASDLLYGPPYSLPFSYHYGHFPLDSHVFSSKKPGLPAKFGQPQGSPCEVARFFLSTLPASSECQWHCANSLVPSSSSPAKNLSEPSPVNAARHGLVPNYEAPSAAARRFCEDPAPPSFPSCGHYREEPALGPAKAPRQASRDAARLALARAPPECCAPPAPEPQAPAQLPFVLLNYHRVLARRGPLGSAAPGAPEAAGSLRPRHPGPVAASAPGAPRPHYLGASVIITNGR | Transcription factor that may be a master gene of CNS development in cooperation with Arnt. It may have pleiotropic effects in the tissues expressed during development. | Q61079 |
B1J2Z8 | METK_PSEPW | Methionine adenosyltransferase | Pseudomonas | MSEYSLFTSESVSEGHPDKIADQISDAVLDAIITQDKYARVACETLVKTGVAIIAGEVTTSAWVDLEELVRKVIIDIGYNSSDVGFDGATCAVMNIIGKQSVDIAQGVDRSKPEDQGAGDQGLMFGYASNETDVLMPAPICFSHRLVERQAEARKSGLLPWLRPDAKSQVTCRYENGKVVGIDAVVLSTQHNPEVSQKDLQEAVMELIVKHTLPAELLHKDTQYHINPTGNFIIGGPVGDCGLTGRKIIVDSYGGMARHGGGAFSGKDPSKVDRSAAYAGRYVAKNIVAAGLAERCEIQVSYAIGVAQPTSISINTFGTGKVSDDKIIQLVRECFDLRPYAITKMLDLLHPMYQETAAYGHFGRTPQQKTVGDDTFTTFTWERTDRAQSLRDAAGL | Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. | B1J2Z8 |
Q6MRI1 | CH60_BDEBA | Chaperonin-60 | Bdellovibrio | MSKVITFSEDARTHILKGVNTLANAVKVTLGPKGRNVVIDKSFGSPLITKDGVTVAKEIELENKFENMGAQMVKEVASKTNDEAGDGTTTATVLAQAIYREGAKLVSAGHNPMSIKRGIDKAVGIIIEELKSMSKPVKGSNEVAQVGAISANNDKEIGQMLADAMDKVGREGVITIEESKTAKTEVTVVEGMQFDRGYLSPYFVTNAERMEAVLENAYVLVYDKKISSMKDMIGILEGVAKQGRQLLIIAEDVEGEALATLVVNKLRGTLHIAAVKAPGFGDRRKAMLEDIAILTGAKVISEDVGLKLEAATVADLGVAKRIVVDKDNTTIIDGAGKKNDINGRVGQIKAQIEETSSDYDKEKLKERLAKLAGGVAVIHVGAPSEVEMKEKKHRVEDALNATRAAVEEGIVAGGGTALLRASTKIDKSKFSEEEQFGATIIKRACEEPIRQIAANAGLDGAIVLDRILQNKSTTWGFNAYSDEYTDLIKDGVIDPVKVVRCALTNAASVSSLMLTTETMIAEAPKKESAAPAMPGHDGMGGMGGMM | 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. | Q6MRI1 |
Q9V0D9 | APBC_PYRAB | Iron-sulfur cluster carrier protein | Pyrococcus | MTIKAPALNLPGLGADPLTQRIKEKEKKWKYKVAVLSGKGGVGKSTVAVNLTAALAKMGYFVGILDADIHGPNVAKMLGVEKEEIYAEKFDDGHFEMIPPMADFMGQVTPIKVMSMGMMVPEDQPIIWRGALVTKAIKQLLGDVKWGSLDFMIIDFPPGTGDEILTVVQSIQLDAAIIVTTPQEVALLDTGKAVNMMKKMEVPYIAVVENMSYLICPHCGNKIDIFGEGGGEKLAEKEGVDFLGKIPIDLKAREASDLGIPIVLYGDTPAAKAFMEIAEKLVNKLKEMKGDEKKE | Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP. | Q9V0D9 |
C4K8I6 | HLDD_HAMD5 | ADP-L-glycero-beta-D-manno-heptose-6-epimerase | Candidatus Hamiltonella | MIIVTGGAGFIGSNIVRALNKIGYQDILVVDNLEKGAKFVNLVDLKIADYRDKDDFITSVRAKEVLGNIEAIFHLGACSSTMEWDGQFMMKNNYEYSKTLLHFCLKACIPFLYASSAAVYGGRTDCFIEEPQYEKPLNIYGYSKFLFDQYVRKIWPKARAPICGFRYFNVYGPRETHKGSMASVVFHLDKQIKAGKPPQLFLGSEQFKRDFIFVDDVAQINLWCWQNQISGIFNCGTGHAASFQTLADTVVAYHNSKPVQYVDFPENLKGCYQTFTQADITKLRTIGYDKPFKPLDEGVTHYLDWLNHQ | 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. | C4K8I6 |
Q61137 | ASTN1_MOUSE | Neuronal migration protein GC14 | Mus | MALAGLCALFACCWGPAAVLATAAGDVDPSKELECKLKSITVSALPFLRENDLSIMHSPSASEPKLLFSVRNDFPGEMVVVDDLENTELPYFVLEISGNTEDIPLVRWRQQWLENGTLLFHIHHQDGAPSLPGQDPTEEPQHESAEEELRILHISVMGGMIALLLSILCLVMILYTRRRWCKRRRVPQPQKSASAEAANEIHYIPSVLIGGHGRESLRNARVQGHNSSGTLSIRETPILDGYEYDITDLRHHLQRECMNGGEDFASQVTRTLDSLQGCNEKSGMDLTPGSDNAKLSLMNKYKDNIIATSPVDSNHQQATLLSHTSSSQRKRINNKARAGSAFLNPEGDSSTEAENDPQLTFYTDPSRSRRRSRVGSPRSPVNKTTLTLISVTSCVIGLVCSSHVSCPLVVKITLHVPEHLIADGSRFILLEGSQLDASDWLNPAQVVLFSQQNSSGPWAMDLCARRLLDPCEHQCDPETGRREHRAAGECLCYEGYMKDPVHKHLCIRNEWGTNQGPWPYTIFQRGFDLVLGEQPSDKIFRFTYTLGEGMWLPLSKSFVIPPAELAINPSAKCKTDMTVMEDAVEVREELMTSSSFDSLEVLLDSFGPVRDCSKDNGGCSKNFRCISDRKLDSTGCVCPSGLSPMKDSSGCYDRHIGVDCSDGFNGGCEQLCLQQMAPFPEDPTLYNILMFCGCIEDYKLGVDGRSCQLVTETCPEGGDCGESREVPMNQTLFGEMFFGYNNQSKEVATGQVLKGTFRQNNFARGLDQQLPDGLVVASVPLENQCLEEISEPTPDPDFLTGMVNFSEVSGYPVLQHWKVRSVMYHIKLNQAAISQAFSNALHSLDGATSRADFVALLDQFGNHYIQEAVYGFEESCSIWYPNKQVQRRLWLEYEDISKGNSPSDESEERERDPKVLTFPEYIASLSDSGTKRMAAGVRMECQSKGRCPSSCPLCHVTSSPETPAEPVLLEVTRASPIYELVTNNQTQRLLQEATMSSLWCSGTGDVIEDWCRCDSTAFGADGLPTCAPLPQPVLRLSTVHEPSSNLVVLEWEHSEPPIGVQIVDYLIRQEKVTDRMDHSKVETETVLSFVDDIISGAKAPCAMPSQVPDKQLTTISLIIRCLEPDTIYMFTLWGVDNTGRRSRPSDVIVKTPCPVVDDVKAQEIADKIYNLFNGYTSGKEQQTAYNTLLDLGSPTLHRVLYHYNQHYESFGEFTWRCEDELGPRKAGLILSQLGDLSSWCNGLLQEPKISLRRGSLKYLGCRYSEIKPYGLDWSELSRDLRKTCEEQTLSVPYNDYGDSKDI | Neuronal adhesion molecule that is required for normal migration of young postmitotic neuroblasts along glial fibers, especially in the cerebellum. Required for normal rate of migration of granule cells during brain development and for normal cerebellum development. | Q61137 |
P54450 | CWLH_BACSU | Cell wall hydrolase | Bacillus | MVTIKKDFIPVSNDNRPGYAMAPAYITVHNTANTAKGADAKMHAKFVKNPNTSESWHFTVDDSVIYQHLPIDENGWHAGDGTNGTGNRKSIGIEICENADGDFEKATSNAQWLIRKLMKENNIPLNRVVPHKKWSGKECPRKLLDHWNSFLNGISSSDTPPKETSPSYPLPSGVIKLTSPYRKGTNILQLQKALAVLHFYPDKGAKNNGIDGVYGPKTANAVKRFQLMNGLTADGIYGPKTKAKLKSKLK | Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. Could play a role in mother cell lysis with CwlC. | P54450 |
Q9GPR0 | FA96A_DICDI | MIP18 family protein FAM96A | Dictyostelium | MIMNYNVIDKIDVFDIIRHIKDPEFPKTLEELKVVNEDWITVIDNNDINDSDDINNNNNENYKGYCFIKILFQPTVPHCHLAPTIALCIREKIKEYLPKRSKIEIYIKKGTHQTEDEINKQINDKERIIAALENPEIFQLVKKCIKEDDY | May play a role in chromosome segregation through establishment of sister chromatid cohesion. | Q9GPR0 |
Q8PFZ6 | UNG_XANAC | Uracil-DNA glycosylase | Xanthomonas | MTEGEGRIQLEPSWKARVGDWLLRPQMRELSAFLRQRKAAGARVFPPGPQIFAAFDATPFEQVKVVILGQDPYHGEGQAHGLCFSVLPGVPVPPSLLNIYKEIQDDLGIARPDHGYLMPWARQGVLLLNAVLTVEQGRAGAHQNKGWEGFTDHVVETLNREREGLVFLLWGSYAQSKGKVIDQTRHRVLKAPHPSPLSAHRGFLGCQHFSKTNDHLRRRGLSPIDWSLPPRSALDLTSAGA | 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. | Q8PFZ6 |
Q9LW26 | PES2_ARATH | Phytyl ester synthase 2, chloroplastic | Arabidopsis | MAVTVLPSVSGLSAVASSSNLRRLTSASNHRLTAIKSVTSTSSPPTPSSGVQRRRKNNDENRATVAKVVENPYSKVEAARPDLQKRLSDFLEEAREFVGDGGGPPRWFSPLECGAQATNSPLLLYLPGIDGTGLGLIRHHKKLGEIFDIWCLHIPVSDRTPVKDLVKLIEETVKSENFRLPNRPIYLVGESIGACLALDVAARNPNIDLSLILVNPATHVNNFMVQPLSGMLNVLPDGLPTLLEDIFDFGFKQGDPLTGMLDALSNEFSVQRMGGVGGGMLRDVLAVSANLPTLSRMFPKDTLLWKLEMLKYAIASVNSHIYSVRAETLILLSGRDHWLLKEEDIDRYSRTLPKCIVRKLDDNGQFPLLEDGVDLATIIKCTCFYRRGKSHDHITDYIMPTTFELKQQVDDHRLLMDGTSPVMLSTLEDGTVVRSLEGLPSEGPVLYVGYHMILGFELAPMVIQLMTERNIHLRGLAHPMLFKNLQDSLVDTKMFDKYKIMGGVPVSHFNIYKLLREKAHVLLYPGGVREALHRKGEEYKLFWPERSEFVRVASKFGAKIVPFGVVGEDDICEIVLDSNDQRNIPILKDLMEKATKDAGNIREGDESELGNQECYFPGLVPKIPGRFYYYFGKPIETAGKEKELKDKEKAQELYLQVKSEVEQCIDYLKVKRESDPYRHLLPRMLYQASHGWSSEIPTFDL | Acyltransferase involved in fatty acid phytyl ester synthesis in chloroplasts, a process required for the maintenance of the photosynthetic membrane integrity during abiotic stress and senescence . Exhibits phytyl ester synthesis and diacylglycerol acyltransferase activities with broad substrate specificities, and can employ acyl-CoAs, acyl carrier proteins, and galactolipids as acyl donors . | Q9LW26 |
Q9CS42 | PRPS2_MOUSE | Phosphoribosyl pyrophosphate synthase II | Mus | MPNIVLFSGSSHQDLSQRVADRLGLELGKVVTKKFSNQETSVEIGESVRGEDVYIIQSGCGEINDNLMELLIMINACKIASSSRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLQWIRENITEWRNCIIVSPDAGGAKRVTSIADRLNVEFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAGATKVYAILTHGIFSGPAISRINSAAFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPL | Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. | Q9CS42 |
A9M3X8 | RL11_NEIM0 | 50S ribosomal protein L11 | Neisseria | MAKKIIGYIKLQIPAGKANPSPPVGPALGQRGLNIMEFCKAFNAATQSMEPGLPIPVVITAFADKSFTFVMKTPPASILLKKAAGLQKGSSNPLTNKVGKLTRAQLEEIAKTKEPDLTAADLDAAVRTIAGSARSMGLDVEGVV | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | A9M3X8 |
A3MI96 | RS15_BURM7 | 30S ribosomal protein S15 | pseudomallei group | MSVADIKKSEVVAQFARGANDTGSPEVQVALLTARITELTGHFKTHAKDHHSRRGLLRMVSRRRKLLDYLKGKDADRYRALIEKLGLRK | Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome. | A3MI96 |
Q0BU46 | PANC_GRABC | Pantoate-activating enzyme | Granulibacter | MHLARTLPTLQQAVHQLRHAGKRIAFVPTMGALHEGHQSLVRAAIAQDYAVVTSVFVNPTQFGPSEDLARYPRDEKGDIAILERTGCSIAWLPDVDTMYPPGDATGFVMGGPALGWEGARRPGHFNGVAQVVAKLFGQVRPDAAFFGEKDWQQLQVIRRLTADLLLPVAIHGVPTQREEDGLAMSSRNRFLSPEERAIAPLLFRTLLQAGHALSSSPDAEEICKNAIAALNGQGFDVDYFALIEGSSLSSIAILPEGDDWRLITAARLGSVRLLDNLGRAELARFRA | Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. | Q0BU46 |
B2VG94 | RL10_ERWT9 | 50S ribosomal protein L10 | Erwinia | MALNLQDKQAIVAEVSEVAKGALSAVVADSRGVTVDKMTELRKAGREAGVYMRVVRNTLLRRVVEGTQFECLKDTLTGPTLIAYSMEHPGAAARLFKEFAKANAKFEVKAAAFEGELISAAQIDRLATLPTYDEAIARLMATMKEAAAGKLVRTLAAVRDQKEATAA | Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. | B2VG94 |
D7A0Y0 | PY2CR_STAND | Delta(1)-pyrroline-2-carboxylate reductase | Starkeya | MDEPVRLSLAEVHVLCRDTLVAAGLGEEHAQAIARSITRAEADECHSHGLYRLIGYVASVRSGKAERHALPALARATPAVLRVDAKHGFAPLAVETGVPALIAAAKEIGIAALAIHDCYHFSALWADIEPAVEAGLAAWCFTVGQCCVAPAGGTTPLLGTNPFAFGWPGPSGRPFIFDFATSAAARGEIELKRRGGEKIPPGWAVGPDGAPTTDPAAALAGALLPFGGHKGSALSMMVELIAGPLIGDLTSRQSKAVENGDGGPPLGGELFIAIDPAVFGTGNLSSRLADADELFALAKAQPGVRLPSERRYQARERSRTNGIAVPAALFAELQALGPRGS | Catalyzes the reduction of Delta(1)-pyrroline-2-carboxylate (Pyr2C) to L-proline, using NADPH as the electron donor. Is likely involved in a degradation pathway that converts cis- and trans-3-hydroxy-L-proline (c3LHyp and t3LHyp) to L-proline, which would allow S.novella to grow on c3LHyp or t3LHyp as a sole carbon source. | D7A0Y0 |
Q5YYX3 | SEPF_NOCFA | Cell division protein SepF | Nocardia | MSTLHKFKAYFGMVPLEDYEDDYVDDRAPRASERGGARGPRPYSERAGYGADRYGEDRYSADRFGPERFGAERFGPDRFGADRFDEDADYPEPAYKSYKSGYPVARRDDYPEDAYGEDRYEAPRRPTRIDAAPSSGRFRAGGGAPMLRGATRGALAVDPEAEERRLEERMRPEPVVARRPGIFEDGGPLSKITTLRPRDYSEARIIGERFREGNPVIMDLVELSNADAKRLVDFAAGLAFALRGSFDKVATKVFLLSPADVDVSAEERRRIAETGFYNQK | Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA. | Q5YYX3 |
B7L7A1 | AES_ECO55 | Acetyl esterase | Escherichia | MKPENKLPVLDLISAEMKTVVNTLQPDLPSWPATGTIAEQRQYYTLERRFWNAGAPEMATRAYMVPTKYGQVETRLFCPQPDSPATLFYLHGGGFILGNLDTHDRIMRLLASYSQCTVIGIDYPLSPEARFPQAIEEIVAACCYFHQQAEDYQINMSRIGFAGDSAGAMLALASALWLRDKQIDCGKIAGVLLWYGLYGLRDSVTRRLLGGVWDGLTQQDLQMYEEAYLSNDADRESPYYCLFNNDLTREVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMKTADEALRDGAQFFTAQL | Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose binding. Inhibits MelA galactosidase activity. | B7L7A1 |
A6Q6N9 | RL13_SULNB | 50S ribosomal protein L13 | unclassified Sulfurovum | MKMTKVLKPSEVQRDWVLIDAEGKTFGRILTEVATLLRGKHKPSFTPNVDCGDYVVIINAEKAKFTGVKLEDKEYFTHSGYFGSTKSKKLGDMLENHTEKLYKLAVRGMLPKTTLGRQMLKKLKVYAGAEHPHTAQINKEA | 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. | A6Q6N9 |
Q2NRM1 | RNH2_SODGM | Ribonuclease HII | Sodalis | MTESFIYPAATLIAGVDEVGRGPLVGAVVTAAVILDPARPVLGLADSKKLSEKRREALYEEITRYALAWSVGRAEASEIDSINIYQATLLAMQRAVAALAVVPDFVLVDGNRCPLLPMPSQAIVKGDSRVAEISAASIIAKVTRDREMAALHLQFPEYGFAQHKGYPTAFHLEKLALHGATVHHRRSFAPVRRVLELA | Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. | Q2NRM1 |
Q9LXB8 | PLPK1_ARATH | Protein Pro-Glu-Leu|Ile|Val-Pro-Lys 1 | Arabidopsis | MALMKKSLSAALLSSPLLIICLIALLADPFSVGARRLLEDPKPEIPKLPELPKFEVPKLPEFPKPELPKLPEFPKPELPKIPEIPKPELPKVPEIPKPEETKLPDIPKLELPKFPEIPKPELPKMPEIPKPELPKVPEIQKPELPKMPEIPKPELPKFPEIPKPDLPKFPENSKPEVPKLMETEKPEAPKVPEIPKPELPKLPEVPKLEAPKVPEIQKPELPKMPELPKMPEIQKPELPKLPEVPKLEAPKVPEIQKPELPKMPELPKMPEIQKPELPKMPEIQKPELPKVPEVPKPELPTVPEVPKSEAPKFPEIPKPELPKIPEVPKPELPKVPEITKPAVPEIPKPELPTMPQLPKLPEFPKVPGTP | Positive regulator of germination and plant growth. | Q9LXB8 |
Q9VLA1 | B3G2S_DROME | UDP-glucuronosyltransferase S | Sophophora | MSSARLLESQTSDEDNEDIERRPHQSHSRSCSNNTTPTHPPHPMVRKGGVARRICLIGGALFLLLVALCYLTLSGDTRLGGSEDSEEGSHHGLDSMNFRPLNETVHICSESYEDRRQFMQDKPQSDYVQLPVIYFVTPTYPRREQIPELTRLAHTLLHIPRLHWLVADDQEKCNDYMDTLLYRFGMPFTHMVSPMPSKFRNEKPAPRGVANRRAALQWIRQHNLTNGILYFGDDDNTYDLRLFSEIRKTQRVSMFPVGLIADYGVSGPVVRKGKVVAFLDSWVAGRRWPVDMAGFAVNLEYMAQYPYVNMPYKPGYEEDLFLRSIGLQMNLIEPRGNNCTEILVWHTQTKSKKLGMVRLESKYLDDRSNLGALLHNLKLMGVTSTTESEGRNALISKNGRENPHSKILS | Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins. Enzyme has a broad specificity. | Q9VLA1 |
Q8MLZ7 | IDGF3_DROME | Imaginal disk growth factor protein 3 | Sophophora | MTGSLWLSLALSLAVLAQFKVSAAPNLVCFYDSQGSQRQGLAQFSMIDIELALQFCTHLVYGYAGVNADNYEMQSINKRLDLEQRHLAQITSMKERYPHIKFLLSVGGDADTNEGNQYIKLLESGQQGHRRFIESARDLVRRYNFDGLDLALQLPRNKPRKVHGDVGSAWKSFKKFFTGDFIVDTESETHKGQVTALIKDLSAALKQNDLLLSLTVLPNVNSSWYYDAPSIAPSLDFINLGTFDFLTPQRNPEEADFSAPTYEAVGQNRLGHYNLNFQMEHWLLQRVPANKINIGIATYGRSWKMSKDSGDSGMPVVPSTQGPAPAGPQSKQEGLLNWAEICSLMPNPSNSNARGPNAPVKRVVDPTKRYGSYAFRAADENGDHGLWISYDDPDSASSKAMYARARNLGGVALFDLTQDDFRGQCTNDRFPMLRAIKYRLL | Cooperates with insulin-like peptides to stimulate the proliferation, polarization and motility of imaginal disk cells. May act by stabilizing the binding of insulin-like peptides to its receptor through a simultaneous interaction with both molecules to form a multiprotein signaling complex. | Q8MLZ7 |
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