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 |
|---|---|---|---|---|---|---|
Q62371 | DDR2_MOUSE | Tyrosine-protein kinase TYRO10 | Mus | MIPIPRMPLVLLLLLLILGSAKAQVNPAICRYPLGMSGGHIPDEDITASSQWSESTAAKYGRLDSEEGDGAWCPEIPVQPDDLKEFLQIDLRTLHFITLVGTQGRHAGGHGIEFAPMYKINYSRDGSRWISWRNRHGKQVLDGNSNPYDVFLKDLEPPIVARFVRLIPVTDHSMNVCMRVELYGCVWLDGLVSYNAPAGQQFVLPGGSIIYLNDSVYDGAVGYSMTEGLGQLTDGVSGLDDFTQTHEYHVWPGYDYVGWRNESATNGFIEIMFEFDRIRNFTTMKVHCNNMFAKGVKIFKEVQCYFRSEASEWEPTAVYFPLVLDDVNPSARFVTVPLHHRMASAIKCQYHFADTWMMFSEITFQSDAAMYNNSGALPTSPMAPTTYDPMLKVDDSNTRILIGCLVAIIFILLAIIVIILWRQFWQKMLEKASRRMLDDEMTVSLSLPSESSMFNNNRSSSPSEQESNSTYDRIFPLRPDYQEPSRLIRKLPEFAPGEEESGCSGVVKPAQPNGPEGVPHYAEADIVNLQGVTGGNTYCVPAVTMDLLSGKDVAVEEFPRKLLAFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLAVCITEDPLCMITEYMENGDLNQFLSRHEPLSSCSSDATVSYANLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLSDEQVIENTGEFFRDQGRQIYLPQPALCPDSVYKLMLSCWRRETKHRPSFQEIHLLLLQQGAE | Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing. | Q62371 |
I2N045 | TSUKU_STRT9 | Tsukubadiene synthase | Streptomyces | MIEVPPFWCPLPIAIHPAADQAEKDARAWAERYGVRLRIADQVQPGRLGAYWAPHGTYEGMLAVGCWNFWAFAFDDHLDEPLPLDVPVTTSLVQQAVDIPSPPITDDPWAAGAQAVFNMFRDLATPTQVRYCADNHRRWLHGACWRHSNHVNRRLPPLAEYIPLRMQDAAAQATCLIAVLIGSDISVPEQEMDSPRVRALLETASWTATIDSDLHSFQLEDTQRPVSQHIVSVLMHERGIGVDEALRQSVALRDRFMTRFLHLQQECARTGSSELARFAHTLGYVISGYLQWAVDTSRYGQTEATFSFTDTPRDDTPEPPPGIPSVEWLWTL | Catalyzes the formation of the 5-9-5 ring skeleton (3S,6S,11R,14S)-tsukubadiene from geranylgeranyl diphosphate (GGPP) via a 1,11-cyclization and a 10Re,14Re-cyclization. | I2N045 |
Q5ZYA8 | AROQ_LEGPH | Type II DHQase | Legionella | MKKILVLHGPNLNLLGSREPSIYGHASLTQINGDLIQEADNAGIRLSCFQSNAEAELIQAVHQAGIDKINYIIINPAAFTHTSIALRDALSAVAIPFIEVHLSNIFSRETFRHHSYFSDIAVGVISGLGTKGYLLALQAIIKELK | Catalyzes a trans-dehydration via an enolate intermediate. | Q5ZYA8 |
B7UK55 | TUSD_ECO27 | tRNA 2-thiouridine synthesizing protein D | Escherichia | MRFAIVVTGPAYGTQQASSAFQFAQALIAEGHELSSVFFYREGVYNANQLTSPASDEFDLVRGWQQLNAQHGVALNICVAAALRRGVVDETEAGRLGLASSNLQPGFTLSGLGALAEASLTCDRVVQF | Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Accepts sulfur from TusA and transfers it in turn to TusE. | B7UK55 |
P50984 | CA1A_CONPE | Alpha-conotoxin PnIA | Darioconus | GCCSLPPCAANNPDYC | Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks mammalian alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=7-68 nM) and alpha-7/CHRNA7 (IC(50)=253 nM) nAChRs . It also shows a high inhibition on alpha-6/alpha-3-beta-2-beta-3 (CHRNA6/CHRNA3-CHRNB2-CHRNB3) (IC(50)=11 nM) and a low inhibition on alpha-6-beta-4/CHRNA4-CHRNB4 (IC(50)>500 nM) . It interacts with a hydrophobic pocket between two acetylcholine receptor subunits. In vivo, inhibits Ehrlich carcinoma growth and increase mouse survival . These effects are greatly enhanced when the toxin is applied with the selective 12-lipoxygenase inhibitor baicalein . | P50984 |
Q9N003 | ZN425_MACFA | Zinc finger protein 425 | Macaca | DDVALYFSGQEWEILEKWQKQMYKQEMKTNYQTLDSLGYAFSKPDLITWMEQGRMLFISEQGCLDKTRRTTSPPTDEQLDMKDTGKLPCFDHEGTLRTKEEDCRLNGPQKQDLGAALPGKERKILSARRDTFQSPSLQETEIPNKKVSITASDPDKKDLRHKPRETPGRLEIPTGPRCYSCYVCRKVFQVRRDLLKHKRSHSKSQLRRYPKYRNTSRGKSELRRTQRLLCQKKRFQCSECEKSYFLKGSLVTHQVVHTGQRPYPCPECDKTFRYRANLKKHLCLHRGERPFCCGECGRAFVQQCELTEHLRLHSGEKPFQCPQCDRCFRLKRGMKVHLSQHSGKRPFHCPECGRSFSRKAALKTHQRTHSEEKPFSCDECGRKFIYKIKLDEHIRVHTGEKPFSCPECNKSFRLKRSLKAHGLQHSGKRPFQCPECSRGFFWRNAMRAHQRLHSEQKPFPCAECGKRFTRPSKLACHTRVHDRQKEFPCGECKKTFSQQSRLTQHLKVHNTEKPFSCAECGRSFRRRAHLTEHTRLHSGEEPFQCPECDKSFSWKASMKFHQRMHRDEKPFACSECGKTYTHQSQLTEHLRLHSGEKPYQCPECQKTFRLKGNLKSHLLQHSGQKPFSCVMCGKSFTQQYRLTEHIRVHSGEKPFQCPECDKSYCIRGSLKVHLYTHSGERPFQCPECGKGFLQKRSLKAHLCLHSGERPFSCDECGRSFTYVGALKTHIAVHAKEKPSSL | Acts as a transcriptional repressor. | Q9N003 |
A4SV75 | MURC_POLAQ | UDP-N-acetylmuramoyl-L-alanine synthetase | Polynucleobacter | MKHIVQQIHFIGIGGTGMSGIAEVLLNLGYQVSGSDLVEGAATKRLKELGAVIHIGHDPKNVGTAEAVVISTAVAGNNPEVLAARAAKIPVIQRAVMLGELMRLKQGIAIAGTHGKTTTTSLVASVLAEGDLDPTFVIGGKLNSAGANARLGRGDFIVVEADESDASFLQLFPAMEVVTNIDADHMDTYQHDMARLKQAFVQFIQRMPFYGVAVLCIDDANVRDIIPFVSQPILRYGLSEDADIRASNVRADGTRMHFTVERRTVRRHGNKPGPLNVTLNLPGLHNVRNALAAIGIATELGVGDQAIIKALSEFSGVGRRFQRYGDIPLASGGKFTLIDDYGHHPVEMAATLAAARGAYPDRRLVLAFQPHRFTRTRDCFGEFVQVLKNFDALVLTEVYPAGEAKIPGADGKSLMKAALVDDKTSKALLNSAAVAFASSVAEMPEKLGQVLKDGDVLITMGAGSISALPHTLSEAKHV | Cell wall formation. | A4SV75 |
Q8CVC6 | PRSA_STRMU | Foldase protein PrsA | Streptococcus | MKKRTIATGLVTLLSIVTLAACSKTNQNSKIATMKGDTITVADFYNEVKNSTASKQAVLSLLVSKVFEKQYGDKVSDKEVTKAYNEAAKYYGDSFSSALASRGYTKEDYKKQIRSEKLIEYAVKEEAKKEITDASYKSAYKDYKPEVTAQVIQLDSEDKAKSVLEEAKADGADFAKIAKDNTKGDKTEYSFDSGSTNLPSQVLSAALNLDKDGVSDVIKASDSTTYKPVYYIVKITKKTDKNADWKAYKKRLKEIIVSQKLNDSNFRNAVIGKAFKKANVKIKDKAFSEILSQYAAASGSGSSGSTTTTTAASSAATTAADDQTTAAETTAAE | Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins. | Q8CVC6 |
Q6CQN7 | DUT_KLULA | dUTP pyrophosphatase | Kluyveromyces | MTESLSNSLKVQLRSADAKVPTKGSTTAAGYDIYASQPGVIPARGQGIAKTDISFTVPVGTYGRIAPRSGLAVKHGIQTGAGVVDRDYTGEVGIVLFNHSDKDFQINKGDRVAQLILEKIVEDAEIVVVESLEETQRGAGGFGSTGKN | 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. | Q6CQN7 |
Q0V340 | CD123_PHANO | Cell division cycle protein 123 | Parastagonospora | MANIENRVHWVILTLPRYRAVTPKARLVPLPAAFLDYLRSDGIILPPEDGDNPTWSDNDSGIFSGADNNDEDDEAAADPSVDWRDTHEAIERTIEELGGKVAPKLNWSAPKDATWMNATNSMECRTPNDIYLLLKSSDFVTHDLAHAFDDTADQSSEDDQEIPYHLVLRKWITLNPSVEFRCFVRDRRLIALCQRDLNHFDFLFNMQDKLRNAVQDFFELRLRNTFPDPNFTFDVYVPPPHDKVWLVDVNPWALRTDPLLFSWMELLTMDVPDVEQEETTVRLRLAQPGSSGRTGADESSGADDSEDDDIEEIWQPEFRLVRRDDPEAYGFATPQYSAHKLPKDVVDASKDGGGGMREFAQQWEEAQRLAEQQRAEDSETD | Regulates the cell cycle in a nutrient dependent manner. | Q0V340 |
Q67WQ7 | GLO13_ORYSJ | Protein GLOSSY l | Oryza sativa | MAISMASPLSSWPWAFLGSYKYLLYGPVVGKVVQEWREQGRLPLGTSWCLHLILLLALRSLTMLFFTRRRRVVDDGVDFRQIDTEWDWDNMVIMQTLIAAVLVTSRVFPATSDLSAWDLRGWAIAVVLHVAVSEPAFYWAHRALHLGPLFSRYHSLHHSFQATQALTAGFVTPLESLILTLVAWAPLAGAFMAGHGSVSLVYGHILLFDYLRSMGYSNVEVISHKTFQDFPFLRYLIYTPSYLSLHHREKDSNFCLFMPLFDALGGTLNPKSWQLQKEVDLGKNHRVPDFVFLVHVVDVVSSMHVPFAFRACSSLPFATHLVLLPLWPIAFGFMLLQWFCSKTFTVSFYKLRGFLHQTWSVPRYGFQYFIPSAKKGINEMIELAILRADKMGVKVLSLAALNKNEALNGGGTLFVRKHPDLRVRVVHGNTLTAAVILNEIPGDVAEVFLTGATSKLGRAIALYLCRKKIRVLMLTLSTERFMNIQREAPAEFQQYLVQVTKYQAAQNCKTWIVGKWLSPREQRWAPAGTHFHQFVVPPIIGFRRDCTYGKLAAMRLPEDVEGLGTCEYTMGRGVVHACHAGGVVHFLEGWDHHEVGAIDVDRIDAVWNAALRHGLTPA | Aldehyde decarbonylase involved in the conversion of aldehydes to alkanes. Core component of a very-long-chain alkane synthesis complex. | Q67WQ7 |
P95468 | TYRB_PARDE | Aromatic-amino-acid aminotransferase | Paracoccus | MLGNLKPQAPDKILALMGEFRADPRQGKIDLGVGVYKDATGHTPIMRAVHAAEQRMLETETTKTYAGLSGEPEFQKAMGELILGDGLKSETTATLATVGGTGALRQALELARMANPDLRVFVSDPTWPNHVSIMNFMGLPVQTYRYFDAETRGVDFEGMKADLAAAKKGDMVLLHGCCHNPTGANLTLDQWAEIASILEKTGALPLIDLAYQGFGDGLEEDAAGTRLIASRIPEVLIAASCSKNFGIYRERTGCLLALCADAATRELAQGAMAFLNRQTYSFPPFHGAKIVSTVLTTPELRADWMAELEAVRSGMLRLREQLAGELRDLSGSDRFGFVAEHRGMFSRLGATPEQVKRIKEEFGIYMVGDSRINIAGLNDNTIPILARAIIEVGV | Shows activities toward both dicarboxylic and aromatic substrates. | P95468 |
B0KA48 | PDRP_THEP3 | Putative pyruvate, phosphate dikinase regulatory protein | Thermoanaerobacter | MEEGVSIYLVSDSNVDTAENIASIAAAHFDTFIEKIKKYPYVGDKNQIEEIIMEAANDANSIIIHTMVVPELKDYLLKKAQKFGIKIVDVMGPVINAIEDSTGISPHTNLAKNNKEDYLKKIEVIEFAVKYDDGKDAMGILLADVVVIGVSRTSKTPLCMYLAHKYIKAANLPLVPEIEPPQELFEINPKKIFGLTIDPEVLVKIRKERLKSLGLDANAIYATEERVKKEIKYAEEVMKRLGCTVIDVTNKAVEETANVILNVLKGGEIS | Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation. | B0KA48 |
Q57T14 | SYP_SALCH | Prolyl-tRNA synthetase | Salmonella | MRTSQYLLSTLKETPADAEVISHQLMLRAGMIRKLASGLYTWLPTGLRVLKKVENIVREEMNNAGAIEVSMPVVQPADLWQESGRWEQYGPELLRFVDRGERPFVLGPTHEEVITDLVRNELSSYKQLPLNFFQIQTKFRDEVRPRFGVMRSREFLMKDAYSFHTSQESLQETYDAMYAAYSRIFSRMGLDFRAVQADTGSIGGNASHEFQVLAQSGEDDIVFSDVSDYAANIELAEAIAPQTPRAAATQEMTLVDTPNAKTIAELVEQFNLPIEKTVKTLLVKAAKDSKSTLVALLVRGDHELNEVKAEKLPHVASPLTFATEEEIRAVINAGPGSLGPVNMPIPVIIDRTVAAMSDFAAGANIDGKHYFGINWDRDVATPVVADIRNVVAGDPSPDGQGTLLIKRGIEVGHIFQLGTKYSEALKASVQGEDGRNQILTMGCYGIGVTRVVAAAIEQNFDERGIVWPDAIAPFQVAILPMNMHKSFRVQELAEKLYSELRAQGIEVLMDDRKERPGVMFADMELIGIPHTIVIGDRNLDNDDIEYKYRRSGKKSLIKTGDIVDYLVKAIKG | Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS. | Q57T14 |
B9DY75 | MURD_CLOK1 | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase | Clostridium | MKRNFDDFKQFIKCKKIGVVGIGISNKPLIDFLLKLGARVSAFDKKSPDEIGEVARELKEKNVDLVLGEKYLNDLSDFDIIFKTPSMRIDSPAFVKAKEKGAYITSEMEEFIRYCPAKIYGVTGSDGKTTTTTLMYNILKKQGYKSWIGGNIGTPLFSEVEEITPDDRVVIELSSFQLMTMNISPEVAVITNVSPNHLDIHKDMEEYIMAKKNIFKYQSNSDLLVLNKDNELTNSMTGEALGKVRQFSIKEKLNKGGYLNKDSLCIDGDEVCKLSEIKLKGMHNVENLLAAFCALKDDVNIESMREIATTFSGVEHRCEFVREINGVKYYNDSIASSPTRTLAGLKAFEKPVILIAGGYDKKIPFDILAEEGYSKIKTLVLMGATKYKIKEAFENLELKKHVHIPIIMANSLVEAVNSARKVSCRGDVVTLSPACASFDMFANFEIRGNMFKEIVNDM | Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). | B9DY75 |
C6DF10 | DNAK_PECCP | Heat shock protein 70 | Pectobacterium | MGKIIGIDLGTTNSCVAIIDGTQVKVLENSEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPKNTLFAIKRLIGRRFKDEEVQRDANIMPYKIIAADNGDAWLEVKDQKMAPPQISAEVLKKMKKTAEDYLGETISEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKEVGNRTIAVYDLGGGTFDISIIEIDEVDGEKTFEVLATNGDTHLGGEDFDSRMINYLVDEFKKEQGFDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHLNIKVTRAKLESLVEELVNRSLEPLKVALQDAGLSVSEIQDVILVGGQTRMPLVQKKVADFFGKEPRKDVNPDEAVAIGAAVQGGVLSGDVKDVLLLDVTPLSLGIETMGGVMTALIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRAHDNKSLGQFNLDGIQAAPRGMPQIEVTFDIDADGILHVSAKDKNSGREQKITIKASSGLNEEEIQKMVRDAEANAEADRKFEELVQARNQGDHLLHSTRKQLEEVGDKLAADDKTAIDDALKALESALKGEDKAEIEAKIQALVQVSGKLLEASQPQPGAEGAADDASARRDDDVVDAEFEEVKDKK | Acts as a chaperone. | C6DF10 |
Q136H1 | TATA_RHOPS | Sec-independent protein translocase protein TatA | Rhodopseudomonas | MGSLSIWHWIVVIAVVLLLFGRGKISDLMGDVAQGIKSFKKGLQDDEKTAEKPDPVKSIDHNAPTAAAPTRTDVGSKAV | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. | Q136H1 |
Q57CS0 | RL5_BRUAB | 50S ribosomal protein L5 | Brucella | MAEAKALPRFKKLYQDNIRKALLEEFKYDNEMQIPRITKVVLNMGVGEATGDSKKPAVAAEDLAMIAGQKAVVTRARNSIATFKLREGMPIGAKVTLRQDRMYEFLDRLITIALPRVRDFRGLNPKSFDGRGNYAMGIKEHIVFPEINYDKVDQIWGMDIIVCTTAKTDDEARSLLRAFNFPFRQ | This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. | Q57CS0 |
Q03KK1 | DEOD_STRTD | Purine nucleoside phosphorylase DeoD-type | Streptococcus | MSIHISAKQGDIADKILLPGDPLRAKFIAENFLEDAVCFNEVRNMFGYTGTYKGERVSVMGTGMGMPSISIYARELIVDYGVKKLIRVGTAGSLNENVHVRELVLAQAAATNSNIIRNDWPQYDFPQIANFNLLDKAYHIAKNFGMTTHVGNVLSSDVFYSNYFEKNIELGKWGVKAVEMEAAALYYLAAQHQVDALAIMTISDSLVNPDEDTTAEERQNTFTDMMKVGLETLIAD | Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. | Q03KK1 |
Q5SK89 | METXA_THET8 | Homoserine transacetylase | Thermus | MSEIALEAWGEHEALLLKPPRSPLSIPPPKPRTAVLFPRREGFYTELGGYLPEVRLRFETYGTLSRRRDNAVLVFHALTGSAHLAGTYDEETFRSLSPLEQAFGREGWWDSLVGPGRILDPALYYVVSANHLGSCYGSTGPLSLDPRTGRPYGRDFPPLTIRDLARAQARLLDHLGVEKAIVIGGSLGGMVALEFALMYPERVKKLVVLAAPARHGPWARAFNHLSRQAILQDPEYQKGNPAPKGMALARGIAMMSYRAPEGFEARWGAEPELGETYLDYQGEKFLRRFHAESYLVLSRAMDTHDVGRGRGGVEEALKRLRAIPSLFVGIDTDLLYPAWEVRQAAKAAGARYREIKSPHGHDAFLIETDQVEEILDAFLP | Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. | Q5SK89 |
C5D8T6 | RNC_GEOSW | Ribonuclease III | unclassified Geobacillus | MSKPKDKERINEKRRAKFKELQKKIGIFFTNEKLLIQAFTHSSYVNEHRRRPHEDNERLEFLGDAVLELTVSQYLFKKFPHMSEGELTKLRAAIVCEPSLVKFANALSFGELVLLGKGEELTGGRTRPALLADVFEAFIGALYLDQGMDAVMQFLGQTIFPKIDEGAFSHVMDFKSQLQELVQRDGIGVLEYSILEEKGPAHNKEFVSRVSLNGQELGIGVGKSKKEAEQHAAQMALQKLKTIGKE | Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. | C5D8T6 |
A1V0T9 | NADK_BURMS | ATP-dependent NAD kinase | pseudomallei group | MKIGHQFHTVALVGRSNTPGIAEPLASLAACIAKRGFEVVFEADTAQAIGSAGYPALTPAEIGARAGVAVVLGGDGTMLGMGRQLAPYKTPLIGINHGRLGFITDIPASDMREVVPMMLAGSYEREERTLLEARIVRNGEPIYHALAFNDVVVNRSGFSGMAELRVSVDGRFMYNQRSDGLIVATPTGSTAYALSSQGPILHPQLQGIVLVPIAPHALSNRPIVLPDDSKIAIQIIGGRDVNVNFDMQSFTALELNDTIEVRRSKHTVPFLHPVGYSYYATLRKKLHWNEHPSSEEDDDA | 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. | A1V0T9 |
B2GII4 | RL1_KOCRD | 50S ribosomal protein L1 | Kocuria | MAKRSKAYRAAAEKIEAGKFYAPAEAVALAKELAEGSKSDPTVEVAMRLGVDPRKADQMVRGTVNLPNGTGKTARVVVFATGDKAAAAEAAGADFVGNDDLIARIQGGWTDFDAAVATPDMMGKVGRLGKILGPRNLMPNPKTGTVTMDVAKAVNDIKGGKIDFRVDKHSNLHFIIGKASFDAQKLAENYGAALEEVLRLKPSASKGRYITKATVATTFGPGIPVDPNATEVTTQA | Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. | B2GII4 |
Q6F0H9 | RL31_MESFL | 50S ribosomal protein L31 | Mesoplasma | MPKKDIQPKYFEEAKFICTTCANEFICGTTKREEMRIDVCSNCHPFFSGAQNFANTTGRVEQFKSKFARKEAINATAQKNSEDQKSKNKENK | Binds the 23S rRNA. | Q6F0H9 |
A7RHG8 | WDR12_NEMVE | Ribosome biogenesis protein WDR12 homolog | Nematostella | MADVEQVQVRFFTKQKKYEIADTPFSLSANIGHGDLNDLINGLLGAGNVGQSIQFDFLIDSQYLQDTIQKHMKAKEISAESVVEIEYLEKHPAPQPDNILVHDDWVSSVSRCKNCIITGSYDNCVQIWDDQGSCLAKVKGHTSPVKDVEWVSKDEQKGVFLSSSQDQSIRVMEWSIGSGEASCVHVCKGHTQSVDSISINPSATKFCSGSWDKTLKLWSAVVNPEGGDEGENGSLSKKQKTTGVKKKATTRTPLMTFTGHTQAVSSVVWMDRTTICSAGWDHCIRLWDAESGVNKQTLTGSKVFCEIAYSALNQCLASGSADKYIRLWDHRAEDGQVVRGILTSHQGWVSSVSWSPSNQFELASASYDTTVKIWDTRSPYTPLYTLTGHQDKVMCVRWSSSRHLMSGGTDNQLILY | Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit. | A7RHG8 |
B8DTN1 | RLMH_BIFA0 | rRNA (pseudouridine-N3-)-methyltransferase RlmH | Bifidobacterium | MNIDIVCVGKVKERYLRDAIDEYRKRLSRFAKVDVIEVADEKTPEHASDTLNAQIKEKEGERILKHLRDGAFVVALAIEGDQLTSEQLAARIAQWGLHGVSHLQFVIGGSLGLDPRVLRRANMPLSFSKMTFPHQLMRVILLEQIYRAFKINAHEPYHK | Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. | B8DTN1 |
Q7M9Z9 | LEUC_WOLSU | Isopropylmalate isomerase | Wolinella | MGQTLTEKIFSAHTNKQVSAGEIIESPIDMVIGNDITTPLSIRAFEESGATKLANPDGFCIVMDHFIPAKDIASANQARISRDFAKKHQLKHYFDERDMGIEHAILPEKGLVLPGDVIIGADSHTCTHGALGAFATGMGSTDLAYAMITGKNWFKVPPSIRVVFKGKLQEHVYGKDLILEIIRQIGVDGALYKALEFQGDTIEQLSMDDRFSLCNMAIEAGAKNGIIAADSITKEFLASRKSLRAEPKYYQADADALYEQTIEIDVEKLEPVIAYPFLPSNGKSISQAVKDDLKIDQAFIGSCTNGRLSDLRIAAQILKGKRVHPDVRLIITPGTQQIYKDAHQEGLIDTLLEAGALISNPTCGACLGGYMGILGDNERCVSTTNRNFVGRMGARSSEVYLANSAVAAASALKGKITDPRKL | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | Q7M9Z9 |
Q8ELF0 | LDH_OCEIH | L-lactate dehydrogenase | Oceanobacillus | MRTSQQAVNRVVLIGGGSVGVSYAFALMNQGVTEELAIIDLDADKALGDVMDLNHGKAFAPSLTNVWLGEYGDCKDADIVCICAGANQQSGETRLDLVEKNMKIFKEIVTDVMNSGFNGIFLIATNPVDILTQAVISFSGLPPHRVIGSGTTLDTARLRYELGEYFHLSPKNIHAYIIGEHGDTELPLWSTATIGTVPLLTYLNRSESYTTEDLDDIFTNVRDAAYRIIQKKGATYYGIAMSLVRVTEAILKDEHSILTTSSFLQGEYGVDNVCIGVPTIINRNGVSEIIEVPMNEDEQKQFNHSVQTLKGIYEPTMQMMK | Catalyzes the conversion of lactate to pyruvate. | Q8ELF0 |
Q9EQP6 | ARRC_MOUSE | Retinal cone arrestin-3 | Mus | MSTVFKKTSSNGKFSIYLGKRDFVDDVDTVEPIDGVVLVDPEYLEGRKLFVRLTCAFRYGRDDLDVIGLTFRKDLYVQTKQVAPAEPTSIQGPLTALQERLLHKLGVNAYPFTLQMVANLPCSVTLQPGPEDSGKPCGVDFEVKSFCAENLEEKIPKSDSVQLVVRKVQFSALEPGPGPSAQTIRSFFLSSQPLQLQAWMDREVHYHGEAISVHVSINNYTNKVIRRIKIAVVQTTDVVLYSLDKYTKTVFVQEFTETVAANSSFSQTFAVTPLLAANCQKQGLALDGKLKHEDTNLASSTILRPGMNKELLGILVSYKVRVNLVVSYGGILGGLPASDVGVELPVILIHPKPSPGERAVATSSEDIVIEEFMQHNSQTQS | May play a role in an as yet undefined retina-specific signal transduction. Could bind to photoactivated-phosphorylated red/green opsins. | Q9EQP6 |
Q9UST1 | PAN3_SCHPO | Poly(A)-nuclease deadenylation complex subunit 3 | Schizosaccharomyces | MSVRKNSPASPKPTSRSRESSRSPSVTDLKDHSKAKRTLCRNILLYGSCKHSENGCAFRHDGPFIPSSENLEQYSVKKKLNAASASFQPVRALPVKAAGAAVFVPKSQEKSLFLSRERTPVALSPGSHAINPYNNASMLVNEPFHDDSGVYYTRQNQFKPTLYNLYNPQPSPMPTLLPYERTVNGLFIDDTTRERIERKSEASRQTISALPSIISSYTSLAPLNTKLYRYKEQIGFSSWTYKCTSSIDGNAYVLKRLQDCSINIDTSTVDKLKNVFHPNIVPFHSAFHTDTFHDSSLLLIYDFYPCTTTLGELYLNNSKNSVKLEENRKIPERELWNYFFQLTIALSYLHKSGFACNKLTPSRILVDQTERIRISGCADYELVVSNKPPLEERKKQDFVDLGVVIANLATGRTDMDMSSAARAIYSTYSREFYKAVLYFVSEVPEDKNLELFLQNHIESFFPIMSSPYVECEKMERKISDAFQHGRFFNILCKIMFIIDNNRASREYPIAREKEISLIYLLRDYLFHQIDEDECPVIDLYQVLNRLGKLDAGINQAIALISRDELDCVSVSYGELKAWLDNVYEMEINS | Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pab1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by xrn1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. ppk26/pan3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit pan2 to mRNA via its interaction with RNA and with pab1. | Q9UST1 |
B5XTR5 | GLPG_KLEP3 | Intramembrane serine protease | Klebsiella | MLMITSFANPRVAQAFVDYMATQGIILTIQQHAQSDVWLADESQAGRVRAELARFLENPADPRYLAASWQSGQTNSGLRYQRFPFFATLRHNAGPFTWAILLICIAVFILQNLLGDQPVMIWLAWPYDPSLQFEAWRYFSHAFMHFSLMHILFNLLWWWYLGGAVEKRIGSGKLVVITVISALLSGFVQHQFSGPWFGGLSGVVYALMGYVWLRGERDPQSGIYLQRGLILFSLVWLIAGWFDVFGMAIANGAHVAGLATGLAMAFVDTLHGRKRA | Rhomboid-type serine protease that catalyzes intramembrane proteolysis. | B5XTR5 |
A5EXX2 | RS20_DICNV | 30S ribosomal protein S20 | Dichelobacter | MANTAQALKRIRQTNKARAQNASQRSTIRTVMKKFLKAIEAKDIATAEQEFSTAASLLDRAAQKHIIHKNKASRLKSRMHAKKKALVA | Binds directly to 16S ribosomal RNA. | A5EXX2 |
Q9SXL4 | AHK1_ARATH | Protein AUTHENTIC HIS-KINASE 1 | Arabidopsis | MRGDSFSMSIENLPDSPMGSRKKKMQIRKVFDKMTEWVTPWRSNLESPREMMILRGDVEQDEFQYASSHCLSSYYSVFVVRLAIMVMLAILIGLLTVLTWHFTRIYTKQSLQTLAYGLRYELLQRPVLRMWSVLNTTSELTTAQVKLSEYVIKKYDKPTTQEELVEMYQAMKDVTWALFASAKALNAITINYRNGFVQAFHRDPASSSTFYIFSDLKNYSISGTGPEDVSGWNNKSIHGNMSAIWYQQQLDPVTGENLGKPLKIPPDDLINIAGISQVPDGEASWHVTVSKYMDSPLLSAALPVFDASNKSIVAVVGVTTALYSVGQLMRDLVEVHGGHIYLTSQEGYLLATSTDGPLLKNTSNGPQLMKATDSEEWVIKSGAQWLEKTYGSKRPHVVHAENVKLGDQRYYIDSFYLNLKRLPIVGVVIIPRKFIMGKVDERAFKTLIILISASVCIFFIGCVCILILTNGVSKEMKLRAELIRQLDARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDILISDDCLSNEQYATVTQIRKCSTALLRLLNNILDLSKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDMPALVRGDSARLVQIFANLISNSIKFTTTGHIILRGWCENINSLHDEMSVSVDRRKPWAPMKTKQVQHRNHLQKSCKNANKMVLWFEVDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILSTPDTVDQNIQPDFSKYGLVVMLSMYGSTARMITSKWLRKHGIATVEASDWNELTQIIRDLLETGSRDNSFDSQHNISDPLRAELSNIVEIKNPVFVIVVDIGVLDLTTNIWKEQLNYLDRFSNKAKFAWLLKHDTSNTVKTELRRKGHVMMVNKPLYKAKMIQILEAVIKNRKRGLCNDLRNRGNGSDESHDCLEIDPTQFDTCSSDDSSETSGEKQVDKSVKPSTLHSPVLKNYLIDATTSNDDSTSASMTQKNPEEEDWKDRLYSGIALDGKNQKSLEGIRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNYKSINAQAPTEEHKSFEEETANKVTTRETSLRNSSPYDLILMDCQMPKMDGYEATKAIRRAEIGTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSLTKPSAFQTSLSA | Functions as an osmosensor histidine kinase that detects water stress and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain. Positive regulator of drought and salt stress responses, and abscisic acid (ABA) signaling. Confers drought tolerance, probably by regulating levels of ABA accumulation. Plays a redundant role in regulating plant growth and development. Required for the regulation of desiccation processes during seed formation. | Q9SXL4 |
Q8EG19 | CLPP_SHEON | Endopeptidase Clp | Shewanella | MHNASDIQSALVPMVIEQTAKGERSFDIYSRLLKERIIFLVGQVEEHMANLIVAQLLFLESESPDKDIFLYINSPGGSVTAGMAIYDTMQFIKPNVSTVCIGQAASMGAFLLAGGEKGKRFCLPNSRVMIHQPLGGFQGQASDIAIHAQEILGIKNKLNQMLADHTGQPLEVIERDTDRDNFMSATQAVEYGLVDAVMTKRG | 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. | Q8EG19 |
A5GPA1 | MNME_SYNPW | tRNA modification GTPase MnmE | unclassified Synechococcus | MQEINRDAQTIAAVATAVAPGQGGIAVIRLSGPQAQAAVQSVTRIPGQQSWESHRVLYGHVLAGESGERIDEVLVLLMLAPRSFTGEDVVEIHCHGGVIAVQRVLARVLDQPGVRRALPGEFSQRAVLNGRLDLTRAEAISDLVAARSQRAAELAMAGVDGGIQKRITALRDRLLDQLSELEARVDFEEDLPALDGAALLEELQRVRGALQQLVKDGQVGAALRQGLRVALVGRPNVGKSSLLNRLSRRERAIVTDLPGTTRDLLESEIVLEGVPITLLDTAGIRATSDAVERLGIARSHDALASADLVLLLFDLSVGWTPDDEALRQRIPAAVPHLLVGNKVDVAVSDARAGTSGSAADIRLSASTGAGEAELVQAVLERCGALADGSLLLSLNQRQGDLAQQAADALARSAQVAADGLPWDFWTIDLRQAIHSLGEITGEELTESVLDRIFSRFCIGK | Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. | A5GPA1 |
A5UB80 | LPXK_HAEIE | Lipid A 4'-kinase | Haemophilus | MPFWYSNSKLIWLLSPFSLLFWLISQLRHALFCLGIKSSYRAPKPVIIVGNLSVGGNGKTPVVVWLVEELKKRGLRVGVISRGYGSKSKTYPLFVTENTRPIEGGDEPVLIAKRTNAPVVISPNRQQAIELLLSQAECDIIVSDDGLQHYKLQRDLEIVVMDAERALGNGFVLPAGPLRELPSRLKSVDFVITNGGKNQYSDAVMYLVPHFAINLKTNEKRQLKEFQSGVAIAGIGNPQRFFTMLEKLGIQLERTQAFQDHQHFEASQLEKLAENQPLFMTEKDAVKCQSFAKDNWWYVPVDAEIIEAEKQCENLPHFWGKIDKLVAQYRNG | 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). | A5UB80 |
Q4JA33 | GGR_SULAC | Geranylgeranyl reductase | Sulfolobus | MKELKYDVLIIGGGFAGSSAAYQLSRRGLKILLVDSKPWNRIGDKPCGDAVSKAHFDKLGMPYPKGEELENKINGIKLYSPDMQTVWTVNGEGFELNAPLYNQRVLKEAQDRGVEIWDLTTAMKPIFEDGYVKGAVLFNRRTNEELTVYSKVVVEATGYSRSFRSKLPPELPITEDLDDKDADVAYREVLLTKEDIEDHDYLRIFIDQETSPGGYWWYFPKGKNKVNVGLGIQGGMGYPSIHEYYKKYLDKYAPDVDKSKLLVKGGALVPTRRPLYTMAWNGIIVIGDSGFTVNPVHGGGKGSAMISGYCAAKAILSAFETGDFSASGLWDMNICYVNEYGAKQASLDIFRRFLQKLSNDDINYGMKKKIIKEEDLLEASEKGDLHLSVADKAMRVISGLGRPSLLFKLKAVAESMKKIKELYLNYPRSPSSLGSWRREVDNVLTEFNKSLS | Is involved in the reduction of 2,3-digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di-O-geranylgeranylglyceryl phosphate (DGGGP) via the hydrogenation of each double bond of the isoprenoid chains. Is not active with NADPH or NADH as an electron donor; the physiological reducing agent is unknown. Is also active on the more upstream precursors of membrane lipid biosynthesis, catalyzing the complete reduction of 3-O-geranylgeranylglyceryl phosphate (GGGP) to 3-O-phytanylglyceryl phosphate, and the partial reduction of geranylgeranyl diphosphate (GGPP) to phytyl diphosphate, thus reducing three of four GGPP double bonds and preserving the allylic double bond (at position 2). This reaction product is a reactive prenyl donor, which can be used as a substrate by archaeal prenyltransferases such as GGGP synthases. | Q4JA33 |
Q8U4R1 | NUCS_PYRFU | Endonuclease NucS | Pyrococcus | MEMTKAIVKENPRIEEIKELLEVAESREGLLTIFARCTVYYEGRAKSELGEGDRIIIIKPDGSFLIHQKKKREPVNWQPPGSKVKMEGNSLISIRRNPKETLKVDIIEAYAAVLFMAEDYEELTLTGSEAEMAELIFQNPNVIEEGFKPMFREKPIKHGIVDVLGVDREGNIVVLELKRRRADLHAVSQLKRYVDALKEEHGNKVRGILVAPSLTEGAKKLLEKLGLEFRKLEPPKKGKKKSSKQKTLDFLNDTVRITGASPPEAIQ | Cleaves both 3' and 5' ssDNA extremities of branched DNA structures. | Q8U4R1 |
Q8ZM80 | YGFZ_SALTY | tRNA-modifying protein YgfZ | Salmonella | MAFISFPPRHPSSSARLPLTLIALDDWALSTITGVDSEKYIQGQVTADVSQMTEQQHLLAAHCDAKGKMWSTLRLFRERDGFAWIERRSVLEAQLTELKKYAVFSKVVIAPDDERVLLGVAGFQARAALANVFSELPNSENQVVRDGASTLLWFEHPAERFLLVTDVATANMLTEKLHGEAELNNSQQWLALDIEAGIPVIDAANSGQFIPQATNLQALGGISFKKGCYTGQEMVARAKFRGANKRALWLLAGKASRVPEAGEDLELQMGENWRRTGAILAATQLDDGQLLVQAVMNNDLEAESVFRVRDDANTLHIVPLPYSLEE | Folate-binding protein involved in regulating the level of ATP-DnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication. | Q8ZM80 |
Q9Y6E2 | 5MP1_HUMAN | Basic leucine zipper and W2 domain-containing protein 2 | Homo | MNKHQKPVLTGQRFKTRKRDEKEKFEPTVFRDTLVQGLNEAGDDLEAVAKFLDSTGSRLDYRRYADTLFDILVAGSMLAPGGTRIDDGDKTKMTNHCVFSANEDHETIRNYAQVFNKLIRRYKYLEKAFEDEMKKLLLFLKAFSETEQTKLAMLSGILLGNGTLPATILTSLFTDSLVKEGIAASFAVKLFKAWMAEKDANSVTSSLRKANLDKRLLELFPVNRQSVDHFAKYFTDAGLKELSDFLRVQQSLGTRKELQKELQERLSQECPIKEVVLYVKEEMKRNDLPETAVIGLLWTCIMNAVEWNKKEELVAEQALKHLKQYAPLLAVFSSQGQSELILLQKVQEYCYDNIHFMKAFQKIVVLFYKADVLSEEAILKWYKEAHVAKGKSVFLDQMKKFVEWLQNAEEESESEGEEN | Translation initiation regulator which represses non-AUG initiated translation and repeat-associated non-AUG (RAN) initiated translation by acting as a competitive inhibitor of eukaryotic translation initiation factor 5 (EIF5) function . Increases the accuracy of translation initiation by impeding EIF5-dependent translation from non-AUG codons by competing with it for interaction with EIF2S2 within the 43S pre-initiation complex (PIC) in an EIF3C-binding dependent manner . | Q9Y6E2 |
Q1IC09 | IHFA_PSEE4 | Integration host factor subunit alpha | Pseudomonas | MGALTKAEMAERLYEELGLNKREAKELVELFFEEIRHALEDNEQVKLSGFGNFDLRDKRQRPGRNPKTGEEIPITARRVVTFRPGQKLKARVEAYAGTKP | 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. | Q1IC09 |
A5U894 | TSAD_MYCTA | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Mycobacterium tuberculosis complex | MTTVLGIETSCDETGVGIARLDPDGTVTLLADEVASSVDEHVRFGGVVPEIASRAHLEALGPAMRRALAAAGLKQPDIVAATIGPGLAGALLVGVAAAKAYSAAWGVPFYAVNHLGGHLAADVYEHGPLPECVALLVSGGHTHLLHVRSLGEPIIELGSTVDDAAGEAYDKVARLLGLGYPGGKALDDLARTGDRDAIVFPRGMSGPADDRYAFSFSGLKTAVARYVESHAADPGFRTADIAAGFQEAVADVLTMKAVRAATALGVSTLLIAGGVAANSRLRELATQRCGEAGRTLRIPSPRLCTDNGAMIAAFAAQLVAAGAPPSPLDVPSDPGLPVMQGQVR | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. | A5U894 |
Q11TJ3 | APT_CYTH3 | Adenine phosphoribosyltransferase | Cytophaga | MATSEEILEQTIKSTIRDIVDFPEPGIIFKDITPLLKDPQLCKAIVQSITDQLRPLQPDALACLDSRGFWFGLSIAMELGIPMIPIRKKGKLPYETVYEEYALEYGTNTIEMHTDAVQPGCRVAIHDDILATGGTAEATSKLIKKAKGEIIAYSFLIELDFLKGKDKLAPYCTTIQSLINY | Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | Q11TJ3 |
P02399 | RLA2_ARTSA | EL12 | Artemia | MRYVAAYLLAALSGNADPSTADIEKILSSVGIECNPSQLQKVMNELKGKDLEALIAEGQTKLASMPTGGAPAAAAGGAATAPAAEAKEAKKEEKKEESEEEDEDMGFGLFD | Plays an important role in the elongation step of protein synthesis. | P02399 |
O77448 | TERT_TETTS | Telomerase subunit P133 | Tetrahymena | MQKINNINNNKQMLTRKEDLLTVLKQISALKYVSNLYEFLLATEKIVQTSELDTQFQEFLTTTIIASEQNLVENYKQKYNQPNFSQLTIKQVIDDSIILLGNKQNYVQQIGTTTIGFYVEYENINLSRQTLYSSNFRNLLNIFGEEDFKYFLIDFLVFTKVEQNGYLQVAGVCLNQYFSVQVKQKKWYKNNFNMNGKATSNNNQNNANLSNEKKQENQYIYPEIQRSQIFYCNHMGREPGVFKSSFFNYSEIKKGFQFKVIQEKLQGRQFINSDKIKPDHPQTIIKKTLLKEYQSKNFSCQEERDLFLEFTEKIVQNFHNINFNYLLKKFCKLPENYQSLKSQVKQIVQSENKANQQSCENLFNSLYDTEISYKQITNFLRQIIQNCVPNQLLGKKNFKVFLEKLYEFVQMKRFENQKVLDYICFMDVFDVEWFVDLKNQKFTQKRKYISDKRKILGDLIVFIINKIVIPVLRYNFYITEKHKEGSQIFYYRKPIWKLVSKLTIVKLEEENLEKVEEKLIPEDSFQKYPQGKLRIIPKKGSFRPIMTFLRKDKQKNIKLNLNQILMDSQLVFRNLKDMLGQKIGYSVFDNKQISEKFAQFIEKWKNKGRPQLYYVTLDIKKCYDSIDQMKLLNFFNQSDLIQDTYFINKYLLFQRNKRPLLQIQQTNNLNSAMEIEEEKINKKPFKMDNINFPYYFNLKERQIAYSLYDDDDQILQKGFKEIQSDDRPFIVINQDKPRCITKDIIHNHLKHISQYNVISFNKVKFRQKRGIPQGLNISGVLCSFYFGKLEEEYTQFLKNAEQVNGSINLLMRLTDDYLFISDSQQNALNLIVQLQNCANNNGFMFNDQKITTNFQFPQEDYNLEHFKISVQNECQWIGKSIDMNTLEIKSIQKQTQQEINQTINVAISIKNLKSQLKNKLRSLFLNQLIDYFNPNINSFEGLCRQLYHHSKATVMKFYPFMTKLFQIDLKKSKQYSVQYGKENTNENFLKDILYYTVEDVCKILCYLQFEDEINSNIKEIFKNLYSWIMWDIIVSYLKKKKQFKGYLNKLLQKIRKSRFFYLKEGCKSLQLILSQQKYQLNKKELEAIEFIDLNNLIQDIKTLIPKISAKSNQQNTN | Catalytic component of telomerase, an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER . TERT is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme . | O77448 |
O24384 | CPI8_SOLTU | PCPI-8 | Solanum | IPSINILSFLLLSSTLSLVAFARSFTSENPIVLPTTCHDDDNLVLPEVYDQDGNPLRIGERYIIKNPLLGAGAVYLDNIGNLQCPNAVLQHMSIPQFLGKGTPVVFIRKSESDYGDVVRLMTAVYIKFFVKTTKLCVDETVWKVNNEQLVVTGGNVGNENDIFKIKKTDLVIRGMKNVYKLLHCPSHLECKNIGSTFKNGYPRLVTVNDEKDFIPFVFIKA | Inhibitor of cysteine proteases. May protect the plant by inhibiting proteases of invading organisms. | O24384 |
Q0T133 | MUTH_SHIF8 | Methyl-directed mismatch repair protein | Shigella | MSQPRPLLSPPETEEQLLAQAQQLSGYTLGELAALDGLVTPENLKRDKGWIGVLLEIWLGASAGSKPEQDFAALGVELKTIPVDSLGRPLETTFVCVARLTGNSGVTWETSHVRHKLKRVLWIPVEGERSIPLAQRRVGSPLLWSPNEEEDRQLREDWEELMDMIVLGQVERITARHGEYLQIRPKAANAKALTEAIGARGERILTLPRGFYLKKNFTSALLARHFLIQ | Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair. | Q0T133 |
A1RKM2 | RLMKL_SHESW | rRNA (guanine-N(7)-)-methyltransferase RlmK | Shewanella | MLNFFAAAPKGFEYSLAQELTEFGATEIKESVAGVYFTAPLTLAYRITLWTRLASRIVLVIYKGSCESAEQLYNAAYCIDWPAHFSNRNTFSIDFHGTGGFINNTQFGALKIKDAIVDRFRDDGDERPNVSRTDADFKVDAHFRNGVITIAMNFSGPSLHQRGYRSTTGEAPLKENLAANMLVRSGWQAAPTTLLDPFCGSGTVLIEAALMAADIAPGLQRNRFGFEHWRRHDKAVWQDIVAEAKARASLGVKRCEIKFYGSDIDSRLVALAKRNAENAGVLELIEFKVANALNIEPPAAEGYLITNPPYGERLGNVSELLQLYYQLGDKFKKEFGGWKVAMLCSDIELISSLKLKADKQMKMFNGALECAFNLYTLHANSTRRDTPVLPEGVDIADIAPAFANRIKKNAKQLEKWAQKEGIDSYRIYDADIPEYNVAVDKYLDYVIVQEYMAPATIPEAVTKRRLSDVLLALPAAIGINPNKIIMKTRERQKGTSQYQKLDERKLELITTEYGAKFKLNLTGYLDTGLFLDHRLTRRLVGQKAKGRRVLNLFSYTGSASVHAALGGAKSVTTVDMSNTYIAWAKDNFALNGLQGKQYEFVQADCLQWIRDCNEQFDLIFIDPPTFSNSKRMEDSFDVQRDHVNLLSALVKLLSPTGELVFSNNKRKFKMDIETLTKMNITVKNIDDITLPMDYKRNPHIHNTWLITHA | Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. | A1RKM2 |
A0KZB1 | NADK_SHESA | ATP-dependent NAD kinase | Shewanella | MGINFDVSRPKARSSINMTTKFHTIGLIGKPHHPGTNQTLKRLHHWLTVQGYEVLVEERVASELGTNIIAVDLLEIGARCDLAIVVGGDGNMLGAARVLARFDVGVIGVNRGNLGFLTDLPPDAFEEALAKVLDGEFDTEHRFLLEAEVYRHGMLKASNTAVNEAVLHPGKIAHMIEFEVYIDNQFMYSQRADGMIVSTPTGSTAYALSAGGAILTPNLQALILVPMFPHTLSCRPIVVDACSTIKMVVSPENGENLEVSCDGHVHLAVLPGDEIIVRRSSEQLRLIHPKGHNYFHVLRSKLGWGSKLF | 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. | A0KZB1 |
B0VR13 | GCSH_ACIBS | Glycine cleavage system H protein | Acinetobacter calcoaceticus/baumannii complex | MNHPSELKYARTHEWVKIEGDLVITGITDHAQDELGDLVYVETPEVGSQVTAGEQARVVESVKTASDIHAPVSGTVVEVNTDLEDDPDFVNEDPYGKGWIYKIKPDNIADVEKLLTNAEYEAGL | The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. | B0VR13 |
P28473 | GBRG3_RAT | GABA(A) receptor subunit gamma-3 | Rattus | MAAKLLLLLCLFSGLHARSRRVEEDDSEDSPSNQKWVLAPKSQDTDVTLILNKLLREYDKKLRPDIGIKPTVIDVDIYVNSIGPVSSINMEYQIDIFFAQTWTDSRLRFNSTMKILTLNSNMVGLIWIPDTIFRNSKTAEAHWITTPNQLLRIWNDGKILYTLRLTINAECQLQLHNFPMDAHACPLTFSSYGYPKEEMIYRWRKNSVEAADQKSWRLYQFDFMGLRNTTEIVTTSAGDYVVMTIYFELSRRMGYFTIQTYIPCILTVVLSWVSFWIKKDATPARTTLGITTVLTMTTLSTIARKSLPRVSYVTAMDLFVTVCFLFVFAALMEYATLNYYSSCRKPTIRKKKTSLLHPDSTRWIPDRISLQAPSNYSLLDMRPPPPVMITLNNSMYWQEFEDTCVYECLDGKDCQSFFCCYEECKSGSWRRGRIHIDVSELDSYSRVFFPTSFLLFNLVYWVGYLYL | GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. | P28473 |
A9GP79 | URED_SORC5 | Urease accessory protein UreD | Sorangium | MRPLAPDARCAPSRPGRGPWYARRPVTTPSDPPAALREPPPPARRAGKAGSGELVFTRVAGRTVLEKALARSPLKLLAPKNHGQAAWVFVASFGGGLVGGDELNLHARVGRGAAALLSTQASTKVYRSPLVSRQRLEAEVQAGGLLVAIPDPVVCFAGSRYEQDIDVALADDASLVLVDALSSGRSARGERWAFDRYASRVRVSRGGRAVLLDATRLDPAHGALPERMGRFDALATLVALGPRAASAAEALLAPRPPPERRAELVASASPLRGGGAVVRVAGTSVERVAGFLRGALAFLAGELGDDPFARKW | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A9GP79 |
P30841 | CROM_ENTDO | Omega-crystallin | Enteroctopus | MAGLPPPNKTPEIKFTKIFINNQFVDSVNGKAYSVINPCTTKKICDVQEGSKADIDKAVQACKLAFKRGTPWRRMDASRRGHLLYRLADLFERDIAYLSSLETLNTGKPYKSAYQDIVHCIQVLRYYAGWADKNMGQNIPVDGDFFSFTKHEPVGICGLIIPWNYPMLMMTWKMAPALSCGNCIVVKPAEQTPLTALYCASLMEEAGFPPGVVNVVPGYGTICGQSISSHLDINKVSFTGSTEVGKLVMQAAGSSNLKRCSLELSGKCPVVVFPDTDLDFAVQQAHEAAFQNMGQCRWSGSRAYVHESIYEEFVKRSVEQATRRKIGDPYELDTEHGPQIDEEQYTKVLDYIKSAQEQGAKLKYGGNKHGDKGGYYIEPTVFSEVSDNMKIAKEEIFGPVQLLMKFRDLDDVIDRCNNSDYGMAAAIFTNDINRIMTFTNAVNTGTIWVNTFHHWFPQAPFGGFKTSGISREMGKYALREYTEVKSVIYRIPQKDS | Omega-crystallins are structural components of squids and octopi eye lens. Contains relatively little if any DHAL activity. | P30841 |
A9NEN3 | EFG_ACHLI | Elongation factor G | Acholeplasma | MPRQYSLKMTRNIGIMAHIDAGKTTTTERILFHTGKIHKTGETHDGASQMDWMAQEQERGITITSAATTSVWRDHRVNIIDTPGHVDFTVEVSRSLRVLDGAVTVIDAQAGVEPQTETVWRQATEYKVPRIVYVNKMDKIGADFNNAIKTLHRRLGVKANAIQLPIGTELDFSGIIDLVTMTAVEYSGDALETTKEIPIPAHLEEQAIDMRNELIEAVAEFDDELMVTYLEGEEVSVELLKRAIRKGVLAVEFFPVVAGSSFKNKGVRKVLDAVIDYLPSPLDIPPVLGHTSEGVEVYRHADDEEPFTALAFKVMTDPFVGKLTFFRVYSGKIKSGSYVQNTTKGERERFGRILQMHANTRQEIDEVYAGDIAAAVGLKVTTTGNTLATQNDDIILESMNFPEPVIEVAVEPKTKNDQDKMGQALAKLAEEDPTFKTYTNTETGQTIIAGMGELHLDILVDRMKREFKVEANVTEPQVSYRETLTVPNEIEAKFIRQSGGRGQYGHVVIDFEPNPGKGFEFVDKIVGGVIPREYIPSVQKGLEEALGGGILAGFPVVDIKATLKFGSYHDVDSSEMAYKIAASMALKDAKNKANAVILEPIMDVEVVTPNDYVGNVIGDITSRRGRLESQEGRGNAISIRAFVPLSEMFGYATSLRSNTQGRATFVMQFDHFDKVPKSIQEEIIKKRGSN | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. | A9NEN3 |
P04743 | PAPI_ECOLX | Major pilus subunit operon regulatory protein | Escherichia | MSEYMKNEILEFLNRHNGGKTAEIAEALAVTDYQARYYLLLLEKEGMVQRSPLRRGMATYWFLKGEMQAGQNCSSTT | Plays a role in the inhibition of methylation at the GATC1028 site located in the regulatory region upstream of the pabA promoter. May, in conjunction with the Mbf (methylation blocking factor), inhibits deoxyadenosine methylase from methylating the GATC1028 site. | P04743 |
A4J124 | RS14Z_DESRM | 30S ribosomal protein S14 type Z | Desulforamulus | MAKKSMINKANAPQKFTVRGHNRCKLCGRPHGYMRKFGICRICFRELAYRGEIPGVKKASW | Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. | A4J124 |
Q9Z2H1 | RGS11_MOUSE | Regulator of G-protein signaling 11 | Mus | MERVVVSMQDPDQGVKMRSQRLLITVIPHAVAGRDLVEWLVQKFCILEDEALHLGTLLAQHGYIYPLRESRDLTLRPDETPYRFQTPYFWTSTMWPAAELDYAIYLAKKNIQKQGALVDYEKEHYALLHKKINHAWDLVLMQAREQLRAAKQRRKGDRMVISCQEQTYWLVNKPPPGAPNILEQGPERGSYNPSHMQMSSDFYKCEIECFRKALGRNRVKSSACLEAYLKFSSQHGPHDPIMSGCLPSNPWITDDVTYWAMNAPNVAAPTKLRVERWSFSFRELLDDPVGRAHFMDFLQKEFSAENLSFWEACEELRFGGQAQVPTLVDSVYQQFLAPGAARWINIDSRTMERTLEGLRQPHRYVLDAAQLHIYMLMKKDSYPRFLKSDIYKGLLEEAVIPLETKRWPFPFLRKPLHSSPSPALQSTPREPAATSSPEGADGE | Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. | Q9Z2H1 |
Q7PXU6 | RU1C_ANOGA | U1 small nuclear ribonucleoprotein C | Anopheles | MPKYYCDYCDTYLTHDSPSVRKTHCTGRKHKDNVKFYYQKWMEEQAQHLIDATTAAYKAGKIAPNPFTAGPPKPNISIPPPTMNMPPRPGMIPGMPAGAPPLLMGPNGPLPPPMMGMRPPPMMVPTMGMPPMGLGMRPPVMSAAPPQLNPKS | Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region. | Q7PXU6 |
A9WDL8 | THIE_CHLAA | Thiamine-phosphate pyrophosphorylase | Chloroflexus | MSIAHIVDWRLYVVTDAGLSRGRSHRAVIEAAIVGGATVVQYREKHASTRQMIEEALELRDLTRRAGVPLIVNDRVDVALAVDADGVHVGQDDMPVALARRLIGNKLLGVSAHNLSEALQAVRDGADYLGVGPIFATTTKPDAAAPIGLDGLRAIRQHVSIPIVAIGGINQANAADVMRAGADGIAVVSAVVAADDVTAAARQLRALVSVTQEKAL | Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). | A9WDL8 |
Q9PLL6 | PCKG_CHLMU | Phosphoenolpyruvate carboxykinase [GTP] | Chlamydia | MTGDWMSKITHSGLKSWIEEVIALVSPKDVRLCDGSEAEYQQLCQQMQEAGVMTLLNPELHPNCFLVRSSPDDVARVEQFTFICTKTKEEAGPTNNWRDPQEMRAELHELFQGCMQGRTLYIVPFCMGPLHSPFSLVGIEITDSPYVVCSMKIMTRMGASVLEMLGSSGTFYKCLHSVGKPLAPGEKDVAWPCNPGHMRIVHFQDDSSVMSFGSGYGGNALLGKKCVALRLASYLGHKQGWLAEHMLVIGVTNPEGRKKYFAAAFPSACGKTNLAMLMPKLPGWKVECIGDDIAWIRPGDDGRLYAVNPEFGFFGVAIGTSEKTNPNALATCHSDSIFTNVALTSDGDVWWEGKTATPPQGMIDWKGRNWTPGGEPAAHPNARFTAPLDHCPSLDPQWDSPQGVPLEAIIFGGRRTETIPLVYESLSWEHGVMMGAGMSSTTTAAIAGELGKLRHDPFAMLPFCGYNMAAYFEHWLSFAGKGLQLPRIFSVNWFRKDENGQFIWPGFSENLRVLEWIFRRTDGEDSIARRTPIGYLPTEEGLNTTGLNLSRDALQSLLAVDTQGWRAEVNNIREYCSIFGSDMPRQILEELSRIENELK | Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. | Q9PLL6 |
A9CH01 | 3HD4E_AGRFC | Trans-L-3-hydroxyproline dehydratase | Agrobacterium tumefaciens complex | MRSIKTVHVISAHAEGEVGDVIVGGVKPPPGETIWEQSRFIARDETLRNFVLNEPRGGVFRHVNLLVPPKHPDADAAFIIMEPEDTPPMSGSNSICVSTVLLDGGIVPMQEPETHMLLEAPGGLVKVRAECRNGKAERIFVQNLPSFAAKLDAELEVEGLGKLKVDTAYGGDSFVIVDAEAMGFSLKPEEAHEIARLGVRITNAANKALGFDHPENPDWRHFSFCLFAGKVERTAEGLRAGAAVAIQPGKVDRSPTGTALSARMAVLHARGEMKEGETLTAVSLIGSTFTGRILGTTTVGDRPAILPEISGRGWITGIHQHMLDPSDPWPEGYRLTDTWGAR | Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Can also catalyze the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), albeit with 30-fold lower efficiency. Is likely involved in both degradation pathways that convert t3LHyp to L-proline and t4LHyp to alpha-ketoglutarate, which would allow A.tumefaciens to grow on t3LHyp or t4LHyp as a sole carbon source. Displays no proline racemase activity. | A9CH01 |
E4TN31 | TM175_MARTH | Transmembrane protein 175 | Marivirga | MRKVFETVVGLNPNFSFRGKQQTRIETFSDAVFALAITLLVLSSTIPETFEDLWASMRDVIPFAICVALIIVIWYQHYIFFLKYGLQDKVTILLNTILLFVLLVYVYPLKFLARFLSEIYGGIFGIIETDLSRFGEYSHQNLKLLMVNYGLGAFAIFLVFSLMYWRAYKMKSLLDLNSYEIFDTKSSIIANLLMCSVPLLSLIITLIDPWGNFRTTILSGFLYFLYVPIMIVFGRITSKKSRRLLQD | Potassium channel; forms a potassium-permeable leak-like channel with weak selectivity for potassium . The channel is permeable for K(+), Rb(+) and Cs(+) . | E4TN31 |
P09139 | AGT1_RAT | Serine--pyruvate aminotransferase, mitochondrial | Rattus | MFRMLAKASVTLGSRAASWVRNMGSHQLLVPPPEALSKPLSIPKRLLLGPGPSNLAPRVLAAGSLRMIGHMQKEMFQIMDEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPGDSFLVGTNGIWGIRAAEIAERIGARVHQMIKKPGEHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDILYSGSQKVLNAPPGISLISFNDKAKSKVYSRKTKPVSFYTDITYLSKLWGCEGKTRVIHHTLPVISLYCLRESLALISEQGLENSWRRHREATAHLHKCLRELGLKFFVKDPEIRLPTITTVTVPAGYNWRDIVSYVLDHFNIEISGGLGPSEDKVLRIGLLGYNATTENADRVAEALREALQHCPKNKL | Catalyzes the transamination between L-serine and pyruvate and weakly contributes to gluconeogenesis from the L-serine metabolism. | P09139 |
Q2Y873 | LEPA_NITMU | Ribosomal back-translocase LepA | Nitrosospira | MQHIRNFSIIAHIDHGKSTLADRIIHLCGGLSDREMEEQVLDSMELERERGITIKAQTAALEYKSRDGSSYLLNLIDTPGHVDFSYEVSRSLAACEGALLVVDASQGVEAQTVANCYTAIEQGVEVIPVLNKIDLPAAEPERVIKEIEDIIGIEAQDAVRASAKTGVGVEDILEAVISRIPPPKGNPEAPLKALIIDSWFDNYVGVVMLVRVMDGVLKPKDRILLMASKTTHLCEQVGVFTPKSRNRESLSAGEVGFIISGIKELKSAKVGDTVTLVDRPAPQPLLGFKEIKPQVFAGLYPVESNQYDALRDALEKLKLNDSSLQYEPETSQALGFGFRCGFLGLLHLDIVQERLEREYDMNLITTAPTVVYQVVLRDGSVIEIENPSRLPDLSKIEQIREPIITATILVPQEYVGSVITLCISKRGIQKNMQYMGRQVMLTYEIPLNEVVMDFFDRLKSTSRGYASLDYEFKEFRASDLVKLDILINGERVDALSLIVHRASSQYRGRELAQKMRELIPRQMFDIAVQAAIGSHIIARESIKALRKNVLAKCYGGDITRKRKLLEKQKAGKKRMKQVGNVEIPQEAFLAILQVGEK | Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner. | Q2Y873 |
C0MGB3 | YQGF_STRS7 | Putative pre-16S rRNA nuclease | Streptococcus | MRIMGLDVGSKTVGVAISDPLGFTAQGLEIIKINEDKQDFGFDRLAELVKQYQVDRFVIGLPKNMNNTSGPRVEASKAYGDRIEELFHIPVSYQDERLTTVEAERMLIEQADISRGKRKKVIDKLAAQLILQNYLDCNY | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | C0MGB3 |
A0JM51 | CELF5_XENTR | RNA-binding protein BRUNOL-5 | Silurana | MARLTEREARRQQQQHPPQQQQPRACPMSGPEPPAQQSDSMKDLDAIKLFVGQIPRNLEEKDLKPLFEQFGKIYELTVLKDRYTGMHKGCAFLTYCARDSAIKAQTALHEQKTLPGMARPIQVKPADSESRGGDRKLFVGMLSKQQSEEEVTSMFQAFGSIEECSVLRGPDGSSKGCAFVKFSSHAEAQAAIQALHGSQTMPGASSSLVVKFADTDKERTLRRMQQMVGQLGIFTPSLALPISPYSAYAQALMQQQTTVLSTSHGSYLSPSVAFPSCHIQQIGAVNLNGLPAAPITPASGLHSPPVIGTAAVPGLVAPLTNGFPGLVPFPSSHPALDTIYTNSIVPYPAQSPALTVESLHPSFTGVQQYSAIYPTAALTPVTHSTPQPPPILQQREGPEGCNLFIYHLPQEFGDNELTQMFLPFGNIISSKVFMDRATNQSKCFGFVSFDNPSSAQTAIQAMNGFQIGMKRLKVQLKRPKDTTQPY | RNA-binding protein that may be implicated in the regulation of pre-mRNA alternative splicing. | A0JM51 |
Q9NVS9 | PNPO_HUMAN | Pyridoxamine-phosphate oxidase | Homo | MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVKQFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKELDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPDREYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGDSPLGPMTHRGEEDWLYERLAP | Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). | Q9NVS9 |
A1UQU8 | RSMG_BARBK | 16S rRNA 7-methylguanosine methyltransferase | Bartonella | MVVLVEQKYQELLNMLPSVSRETMENLIQFESLIIQWNAHINLISAATVPFLWTRHILDSAQIYPLYSQCLHWCDLGSGGGFPAIVIAIFLKEKQKGHIDLIESNGKKVAFLRTVIAQLNLPATVYHCRIEDVYQKINAPEIITARGLASLNTLLQLTFPWLKQKTIALLQKGRDYAIEVENAYANWRFNLLKHQSKIDENSVILEISHVRSCQG | Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. | A1UQU8 |
Q8XBM3 | GLNE_ECO57 | Adenylyl transferase | Escherichia | MKPLSSPLQQYWQTIVERLPEPLAEESLSAQAKSVLTFSDFVQDSISAHPEWLTELESQPPQADEWQHYVAWLQEALINVSDEAGLMRELRLFRRRIMVRIAWAQTLALVTEESILQQLSYLAETLIVAARDWLYDACCREWGTPCNAQGEAQPLLILGMGKLGGGELNFSSDIDLIFAWPEHGCTQGGRWELDNAQFFTRMGQRLIKVLDQPTQDGFVYRVDMRLRPFGESGPLVLSFAALEDYYQEQGRDWERYAMVKARIMGDSEGVYANELRAMLRPFVFRRYIDFSVIQSLRNMKGMIAREVRRRGLTDNIKLGAGGIREIEFIVQVFQLIRGGREPSLQSRSLLPTLSVIAALHLLSENDAEQLRVAYLFLRRLENLLQSINDEQTQTLPSDELNRARLAWAMDFADWPQLTGALTAHMTNVRRVFNELIGDDESETQEESLSEQWRELWQDALQEDDTTPVLAHLSEDDRKQVLTLIADFRKELDKRTIGPRGRQVLDHLMPHLLSDVCAREDAAVTLLRITALLAGIVTRTTYLELLSEFPAALKHLISLCAASPMIASQLARYPLLLDELLDPNTLYQPTATDAYRDELRQYLLRVPEDDEEQQLEALRQFKQAQLLRIAAADIAGTLPVMKVSDHLTWLAEAMIDAVVQQAWVQMVARYGKPNHLNEREGRGFAVVGYGKLGGWELGYSSDLDLIFLHDCPMDAMTDGEREIDGRQFYLRLAQRIMHLFSTRTSSGILYEVDARLRPSGAAGMLVTSTEAFADYQKNEAWTWEHQALVRARVVYGDPQLTAHFDAVRREIMTLPREGKTLQTEVREMREKMRAHLGNKHRDRFDIKADEGGITDIEFITQYLVLRYAHEKPKLTRWSDNVRILELLAQNDIMEEQEAMALTRAYTTLRDELHHLALQELPGHVPEDCFTAERELVRASWQKWLVEE | Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell. | Q8XBM3 |
Q5Z0W8 | GLGB_NOCFA | Glycogen branching enzyme | Nocardia | MSGPEDPADRRHGEVPAPRRDIPRPLVERRDLMLLAAGTHRDPHTVLGAHPHPDGTVVRVLRPHAAKVSVRVGGVDHPLDSVGYGVFAAVLPHPELMDYRIVTEYPGGPTVIAADGFRFLPTLGELDLHLIGEGRHEHLWHVLGAHPRRYTTLDGPVSGTSFAVWAPNARGVTVIGDFDGWSGNTAPMRALGTSGVWEVFVPDVGSGTKYKYRVHGADGRVVDHADPLAFATELPPATASVVTGSDYTWQDAQWLERRRSTDPTRSPMSVYEVHLGSWRPGLGYRELAEQLADYVRAAGYTHVELLPVAEHPFGGSWGYQVTSYYAPTARFGSPDDFRAFVDHLHGAGIGVLLDWVPAHFPRDEWALARFDGTPLYEHPDPRRGEQLDWGTYVFDFGRNEVRNFLVANARFWIEEFHIDGLRVDAVASMLYLDYSRGENWEPNIHGGRENLEAVAFLRELNDVVHRAHPGVVTIAEESTTWPGVTRGTEVGGLGFTMKWNMGWMHDTLGFLARDPIHRSWHHNEITFSLVYAWSENYVLPISHDEVVHGKGTLWTRMPGDDFAKAAGVRALLAYMWAHPGKQLLFMGQDFGQFREWSHDRGLDWGELDNPLHRGIATAVRDLNRVYRATPALWSQDTTPGGYAWIEADDRDRNVLAFLRYGSDGSTVACVFNFSGALHGEYRVGLPIAGEWTEILNTDAADYGGSGVGNYGVVRTEEIPWHGRPVSATVALAPNSAVWLAAPRA | Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. | Q5Z0W8 |
Q98QX2 | ACKA_MYCPU | Acetokinase | Mycoplasmopsis | MKILVINAGSSSIKFALFEKENLNQIASGIAERIGIENGIISISFDKKYQFEIDMKDHLEAAKKLLELFEQISLIKNADEIELIGFRVVHGGIELNKASKLDQETISIIEKSAKYAPLHNPGALQAIKAFQLALPKAKLSVNLDTAFHSSIDKINYSYPINYELAQKLGIRKFGFHGISHRFITNKLEKILNKKSVNFVNLHIGNGASLCAVKVSKSIDTSMGFTPLAGIMMGTRSGDIDPSIHEFVCKEENMSIEEFTSILNKQSGISGVSQISSDLRDVEEQYAKGNAQAIFALDLYSQKIADYAAIYLNKIAPQIDAIVFTAGVGENSAFVRKNVISRIKIKNIELDEALNSQKVGEYQLISTKNSEIPVYVIRTNEELMIASDAKKLNS | Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. | Q98QX2 |
C1FKZ3 | DRDI_CLOBJ | 5-deoxyribose 1-phosphate isomerase | Clostridium | MAELLAIKWDDNRDKLILLDQTILPNKIEYIEYDTAEGVYDSIKDMIVRGAPAIGVTAAYGLYFAAKVAPEDNFENFFKYLKEKSSYLDSSRPTAVNLSWALKVMESKALENKDKDVKEIKSILREEAKRIHEEDIEICKAIGENLITLLKDGVGILTHCNAGQLATSKYGTATSPMYLAKEKGWNFKVYSDETRPRLQGSTLTALELYEAGIDVTTITDNMAAMVMSQGKIDAVIVGCDRIAANGDTANKIGTMGVSILAKYFGIPMYIAAPTPSIDMNTKTGKDIPIEERNSEEITSRFGVWTAPKGVKVYNPGFDVTPHENITAIVTEKGIVYPPFKENLKKLFEK | Catalyzes the isomerization of 5-deoxy-alpha-D-ribose 1-phosphate to 5-deoxy-D-ribulose 1-phosphate, as part of a 5-deoxyribose salvage pathway that recycles this toxic radical SAM enzyme by-product to mainstream metabolites. | C1FKZ3 |
Q0AK64 | TRUB_MARMM | tRNA-uridine isomerase | Maricaulis | MARRRKGDDIHGWVILDKPLDMTSTQAVSAVRRIYNAKKAGHAGTLDPLASGILPIALGEATKTVPFAVEGSKIYRFTIKWGERTTTLDREGEVVATSDVRPTPEEVAAVLPDFTGEIQQIPPAFSAIKVDGERAYDLARSGEDVQLEARPVQIISLQLLDCPDADMAVLEMRCGKGAYVRSMARDIAHALGTEGHVAALRRIRVGGFVEAESTRLDELEEMAHKGAASEALLPVQTALDDIPALAITEEESFQLKLGRSIVLLPRQAQELKAQRRPREIAGKDCTFTALALCDGVAVALGDARAGKFQPSRVFNLTP | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | Q0AK64 |
Q1ME47 | DNLJ_RHIL3 | Polydeoxyribonucleotide synthase [NAD(+)] | Rhizobium | MPTEGSTVDTLTIEEAAAELARLAKEIAHHDALYHGKDQPEISDADYDALKRRNDALEVRFPELIREDSPSRHVGAAPSVTFSPVVHARPMLSLDNTFSQEDVQDFVAGVYRFLGRLPDQSIAFTAEPKIDGLSMSIRYENGRLVTAATRGDGTTGENVTANIRTIAEIPNELPKGVPAVVEIRGEVYMAKSDFLALNRQMEAEGKQTYVNPRNTAAGSLRQLDAKVTASRKLKFFAYAWGEMSEMPADTQFGMVQTFKDWGFPVNPLMKRLNSVADILAHYDEIGLERPDLDYDIDGVVYKVDSLELQARLGFRSRSPRWATAHKFPAEQAFTIVENIDIQVGRTGALTPVARLTPITVGGVVVTNATLHNADYIQGIGNSGERIRDDEHDIRIGDTVIVQRAGDVIPQVLDVVMEKRPAEARPYEFPKTCPVCGSHAVRERHEKTGKLDSVTRCTGGFICRAQATEHLKHFVSRNAFDIEGLGSKQIDFFFENEDASLQIRTAPDIFTLEKRQQQSLTKLENIDGFGKVSVGKLYGAIDERRSIALHRFIYALGIRHVGETTAKLLARSYGTYEAFETAMREAEALSGDAWNDLNAIEGIGEVVARAIVEFYKEPRNVEVITRLLEEVTPEEAEQPKTAGSPVAGKTVVFTGSLEKLTRDEAKARAESLGAKVAGSVSKKTDIVVAGPGAGSKLDKARELGVQTMDEDQWLALISG | 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. | Q1ME47 |
Q9X8I9 | IPYR_STRCO | Pyrophosphate phospho-hydrolase | Streptomyces albidoflavus group | MEFDVTIEIPKGSRNKYEVDHETGRIRLDRRLFTSTAYPTDYGFVENTLGEDGDPLDALVILDEPTFPGCLIRCRAIGMFRMTDEAGGDDKLLCVPSTDPRVEHLRDIHHVSEFDRLEIQHFFEVYKDLEPGKSVEGADWVGRTEAEAEIERSYKRFKDQGGH | Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. | Q9X8I9 |
Q4JVM3 | ACNR_CORJK | HTH-type transcriptional repressor AcnR | Corynebacterium | MPKVSDTDLAERKVEILSGARHCFATYGYDGATVARLEETIGKSRGAIFHHYGNKDQLFLEVAHEDMRKMAELAADEGLIGAIRTLVKSNDLTDWWGMRVEITRRVNIDPCFAAKWELDQLALRETVRTRLREQRASGRIRKDVEIETIAQTLELVLEGVLGRLAQRQGTEGLSDALDFVESALRSPGH | AcnR negatively controls the expression of the aconitase gene acn. | Q4JVM3 |
Q5ZW64 | FLGI_LEGPH | Basal body P-ring protein | Legionella | MRRMLVIRWILAIHLIATQVFAERIKDIATLAGVRVNQLVGYGLVVGLSGTGDKTGTKFTEDSFANMLTQLGINIPPGVRLNSKNIAAVMVTANLSSFMKKGQTMDVNISSIGDSKSLLGGTLLLTPLKGADGRVYAMSQGNVVVSGISASGSDGSSVTVNVPSGGRIPNGATIEADIPNPFYYSNSLTYNLHNPDFTTAKRMSDAINELMGPGTAKAIDAGSVVVTAPKKLSQRVDYVSVLENIEFKPGEAMAKIIINARTGTVVISSNVIVKSAAVSHGNLVVSITETPVISQPNAFASGRTVSTQQSQVNIQQKNNRAFILPKGTTLKDIVRGINAVGATPADVISILEALQQAGALSATLIVI | Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | Q5ZW64 |
Q6G0I9 | FOLD_BARQU | Methenyltetrahydrofolate cyclohydrolase | Bartonella | MNNIIDGKKLAEEIIVKVKAETIKLRNNYKIQPGIAVIIVGDDPASHVYVTSKSKKAEECGFFSIKHMLSKETSEKELLQLIATLNSDPKIHGILVQLPLPAHINTNCVTQAIAFQKDVDGFHYINIGKLSCNTLEDAIIPCTPAGAMIMIEQQCGRDLSGLDAVVVGRSNIVGKPMAALLTAANATVTIAHSRTRDLDDVCRSADILVAAVGRPQIIKKDWVKNGAIVIDVGINRIAAPEKGIGKTRLVGDVDFEAIKGKTAAITPVPGGVGPMTIAMLMVNTLNAAARLYNLPVLKL | Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. | Q6G0I9 |
Q5V0J7 | AMZA_HALMA | Archaemetzincin | Haloarcula | MHVDIVPVGEVSAQVKREASDGLRSVYDCEVSMHEPQSIPAGAYDGDRDQYRAEEFIDLARRVGSGGKNIAITPKDLFYRRRNYVFGLAYLGGSGSVISTYRLQTSSDGGFSNRSAGEIFSQRVRKEVVHEVGHTLGLEHCDNKRCVMNFSPTVRQVDVKEVSLCGSCQRNVL | Probable zinc metalloprotease whose natural substrate is unknown. | Q5V0J7 |
Q12SM9 | ARGB_SHEDO | NAG kinase | Shewanella | MSDNKSVLVLKVGGALLQCEMGMSRLMTAAAQMIATGQKVLLVHGGGCLVDEQLTANGKETIKLDGLRVTPEDQIPIVVGALAGTSNKILQAAAAKAGLVSVGMSLGDGNTVHAKIKDERLGLVGEVSPNDATYLNFILDQGWLPICSSIAVSADGLMLNVNADQAATALAKLVNGNLVLLSDVSGVLDGKGQLIASLNKTEIETLVKQGVIEKGMKVKVEAALEVAQWMGKPVQVASWRDAEQLKKLVLGQSVGTQIQP | Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. | Q12SM9 |
Q6G390 | NUOC_BARHE | NDH-1 subunit C | Bartonella | MSESLEELAAYLKSKLGDKLEETVLAFGELTIVSRLDAITDVLIFVRDDSRCQFINITDISGVDYPCRDKRFDVSYQLLSPRHNLRLRVKVRTDENIPVASACSIYPGAEWYERETYDMYGILFSGHPDLRRILTDYGFEGHPLRKDFPVTGFVECRYDNEAKRVIYEPVVLRQEMRNFDFLSPWEGAQYILPCDEKTKDKR | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. | Q6G390 |
Q318F2 | PANCY_PROM9 | Cytidine monophosphate kinase | Prochlorococcus | MKKVIIRKTEEIKNWRRNINSDINFIPTMGNLHNGHKTLISTAKNANSNVNLVSIFVNPLQFDNKSDLENYPKTIDNDIKISFENGADVIFIPSTEEIYPSDNKNITFLKAPLELSSSLCGLNRIGHFDGVCTVVYKLLNLIKPKNLYLGEKDWQQLLILKNLVLTKKLDVAIKSIPTQRDFDGIPLSSRNVHLSNNERKLIRFFSHELLVAKENFQQEKKINLKEIIQKLSAQKISIEYLEHLHPYTLQESKVEDNISILAGAIRCGETRLIDHVFLMKRSPIIAIDGPAGSGKSTVTQLIAKKLKLLYLDTGAMYRALSWLLIKENIDYKEEKKLQNILKDISIVFKSNTNSQQDVFINNYCVTEEIRSQEISSIVSKISSIKEVREFLVEEQRKIGESGGLVAEGRDIGTTVFPDAELKIFLTASIDERAKRRKSDKKSKDSQEIDLHKLKELIKKRDFEDSNREISPLIKANDAIEIITDGCSINEVVDKIIDLYNDKIPKETQIR | Catalyzes the transfer of a phosphate group from ATP to either CMP or dCMP to form CDP or dCDP and ADP, respectively. | Q318F2 |
Q695L6 | CHLL_LARDC | Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein | Larix | MKIAVYGKGGIGKSTTSCNISVALARRGQKVLQIGCDPKHDSTFTLTGFLIPTIIDTLQSKDYHYEDIWPEDVIHKGYGGVDCVEAGGPPAGAGCGGYVVGETVKLLKELNAFYEYDIILFDVLGDVVCGGFAAPLNYADYCVIITDNGFDALFAANRITASIREKARTHPLRLAGLVGNRTSKRDLIHKYVEACPMPVIEVLPIIEDIRVSRVKGKTLFEMVGSEPSLNYVCKYYLDIADQILSQPEGIVPKEIPDRELFSLLSDLYLNPIGGGGQKKKNQENLLGFTRI | Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. | Q695L6 |
A5W9T9 | RSGA_PSEP1 | Small ribosomal subunit biogenesis GTPase RsgA | Pseudomonas | MAKRQLNRRQNWRIEKIQGERAARAAKREQHALQELEGGDLGPEQLGLVIAHFGVQVEVEAQDGETAGQVFRCHLRANLPALVTGDRVVWRAGNQGIGVIVAQMPRSTELCRPNNHGQLKPVAANVDLIVIVFAPAPEPHPNLIDRYLVAAEHAGLRPLLLLNKADLINDENGPGLHALLEVYRELGYPLLEVSAHHGDGMQRLQQQLDGHISVFVGQSGVGKSSLVNSLLPDAGTRVGDLSEWSGQGTHTTTTARLYHFPNGGDLIDSPGIREFGLGHVSRDDVEDGFIEFRDLFGTCRFRDCKHDREPGCALLKALEEGRIKPQRMNSYRSIIASLAEDSY | One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit. | A5W9T9 |
Q12129 | NMD4_YEAST | Nonsense-mediated decay protein 4 | Saccharomyces | MTQYNFIIDASAFEKGLGNIKRWCSDCTEAVTLNFYIPTFTLNELDFLQQRRKSFAARESLKFIDRLDDSKFANLKVFIEFPEVLDIILWSDVMEHNDSSGKINIAKLPKRLKNLLKSCIYKCYLEGNEGLHWFLISEDPQIREMAMQCNIPSCSIVDVDSILSKDMNDKSFRESEKFNNMMLKNGTKEESENGREIIRTNFNKTVYASRGTGELWSP | Involved in nonsense-mediated decay of mRNAs containing premature stop codons. | Q12129 |
A7NEB0 | RL19_FRATF | 50S ribosomal protein L19 | Francisella | MKNKFVELVEKSQLRNDLPEFNPGDSITVNLWIKEGDKQRIQAFKGFVLRKRNRGLHSAFTVRKMSSGMGVERTFQTHSPLIDSIIVEKRADVRRAKLYYMRGLTGKAARIKEKV | This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site. | A7NEB0 |
Q9CCR4 | PYRC_MYCLE | Dihydroorotase | Mycobacterium | MSVLLRGVRLYGEGEQVDVLVEGEQIANIGAGIDIPDTADVIDAIDQVLLPGLVDLHTHLREPGREYAEDIETGSAAAALGGYTAVFAMPNTTPVADSPVVTDHVWRRGQQVGLVDVHPVGAVTVGLAGAELTEMGMMAAGAAQVRIFSDDGNCVHNPLVMRRALEYATGLGVLIAQHAEEPRLTVGAVAHEGPTAARLGLSGWPRAAEESIVARDALLARDAGARVHICHASTAGTVEILKWAKEQGISITAEVTPHHLLLDDSRLASYDGVNRVNPPLRETADAVALRQALADGIIDCVTTDHAPHADHEKCVEFSAARPGMLGLQTALSVVVHTMVVPGLLSWRDVAQVMSENPARIAGLPDHGRPLEVGEPANLTVVDPDVTWTVTGDGLASRSANTPYEAMTLPATVTATLLRGKVTARGQKSPV | Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. | Q9CCR4 |
C3P3F2 | NOC_BACAA | Nucleoid occlusion protein | Bacillus cereus group | MKNTFSRLFGFGDKESEFELQDESHEEIDKKVYEEIQEIPIVNITPNRYQPRTVFDDARIEELALTIRTHGLIQPIVVRQYEDDKYEIIAGERRFRAATKLGWEKVPAIIKNLNDTETASVALIENLQREELTAIEEAVAYQKLIELHNLTQEALAQRLGKGQSTIANKLRLLKLPEEIKSALLEKSITERHARALIPLKNEELQLKVLQEIVEKQLNVKQTEERITKLLEEAKPKRKAKQKAVSRDTRIAMNTIRQSLQMVADSGLNVNSEEEEFDEYYQITIQIPKKK | Effects nucleoid occlusion by binding relatively nonspecifically to DNA and preventing the assembly of the division machinery in the vicinity of the nucleoid, especially under conditions that disturb the cell cycle. It helps to coordinate cell division and chromosome segregation by preventing the formation of the Z ring through the nucleoid, which would cause chromosome breakage. | C3P3F2 |
Q8E7X8 | KPRS1_STRA3 | Phosphoribosyl pyrophosphate synthase 1 | Streptococcus | MSYSNLKLFALSSNKELAKKVSQTIGIPLGQSTVRQFSDGEIQVNIEESIRGHHVFILQSTSSPVNDNLMEILIMVDALKRASAESVSVVMPYYGYARQDRKARSREPITSKLVANMLEVAGVDRLLTVDLHAAQIQGFFDIPVDHLMGAPLIADYFDRQGLVGDDVVVVSPDHGGVTRARKLAQCLKTPIAIIDKRRSVTKMNTSEVMNIIGNIKGKKCILIDDMIDTAGTICHAADALAEAGATAVYASCTHPVLSGPALDNIQNSAIEKLIVLDTIYLPEERLIDKIEQISIAELIGEAIIRIHEKRPLSPLFEMNKLK | Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). | Q8E7X8 |
Q8TW20 | RL14_METKA | 50S ribosomal protein L14 | Methanopyrus | MKAIKAKSPHAALPVGARLVCADNTGARELQIIAVKGYKGVRRRLPNAGIGDMVVCSVKEGTPDMRKEVVNAVIVRQRKEYRRPDGTRVKFEDNAAVIVTPDGAPRGSEIRGPVAKEAAERWPRIGSIASIIV | Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. | Q8TW20 |
Q473G3 | FTSB_CUPPJ | Cell division protein FtsB | Cupriavidus | MRLISLLLFVLLLAIQYPLWLGKGGWLRVWELNHQVQEQATRNQMLKLRNAKLEGEVKDLQDGTGAIEERARYELGMVKDGEVFVQFVAPAPKVSATPPLPPPPNSPAATGRH | Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. | Q473G3 |
A5IJ45 | SYT_THEP1 | Threonyl-tRNA synthetase | Thermotoga | MKIKVKLPDGKEKEYDRGITPAEIAKELGVKKAIGAVVNGELWDLKRPIENDCELRLVTLEDPEAPEFYRHTMAHILAQAVMRIYGKENVKLGIGPTIENGFYYDFDIKNGKLTEEDLPKIEQEMKKIIKENLPIERKEISKEEARKLFNNQPYKLELIEEIEGDRVTIYRQGEFVDLCRGPHLPSTGVVKHFKLLSVSGAYWRGSEKNPMLTRVYGTAFAKKEDLDNYLKFLEEAQRRDHRKLGPHLELFMLNTEYAPGMPFFLPKGVVVLNELMRFSRELHRERGYQEIFTPLIMNEQLWKISGHWDHYAENMYFIEKDEERYAVKPMNCPGHILVYKSRTVSYRDLPLRFFEFGRVHRYERSGVLHGLMRVRSFTQDDAHIFCTPDQIEEEILGVLDLINTIYGQFGFTYRVELSTMPEDHMGDEAIWEKATTALKNALERAGLSYKVNEGEGAFYGPKIDFHIRDSIGREWQCATIQLDFMMPEKFNVTYIGPDNKEHRAVMIHRAIYGSLERFFGILIEHFAGAFPTWLAPIQVAVIPISEKHNDGAEKIAKRISQEGFRVFFDNRRETLGYRIRQAQTQKIPYMIILGDKELESGKISVRTRTGKEIKDVDLEHFVETLRNEVLSRKLELLMEG | Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr). | A5IJ45 |
Q11137 | ZAPA_PROMI | Extracellular metalloprotease | Proteus | MGSFLLKKAVGLSNISDLLDKSGIFYNYSTKVLPSFDYDTAGKHIAREDSTWNGKYVIGQPAEVTYSFPKWEGKFNQFGNKNPYEFNELQKEHARKSLDAWSDIANIKFTEVAVGNVDGMKASDVKTDITFGNIYDPNGTFQAYATLPNTYAYGKDLSGQAWFSDYHYAGNTTPELGNYGRLTIIHEIGHTLGLMHPGDYNAGQNVPGYLKSDYAEDSRQYTVMSYWDEYETGAHFQGAYAGAPLLHDISAMQYLYGANTTTRTGDDVYGFNSNTGIDYYTATDSNDKLIFSVWDSGGNDTFDFSGFYQDQLIDLRAGNFSDVGGLQKNVSIAQNVTIENAIGGFGNDIIHGNDADNTLIGGEGDDIIYGHSGNNTIYGGRGQDTLHGGTGSNTFIYKEIADSLVTAADKIMDFKTGIDKIDLSTLIQDTFSSKILNFVDNFTGNAGEATLSYNEVTNASELAINAYGYNYNPDFKIDIVGFVNYETDFIV | One of the virulence factors produced during swarmer cell differentiation of the bacteria, which seems to be associated with pathogenesis. The protease activity is limited to IgA1, IgA2, as well as IgG degradation. | Q11137 |
P46676 | SUM1_YEAST | Suppressor of mar1-1 protein | Saccharomyces | MSENTTAPSDNITNEQRLPSGPKDDVDTLALTSAQNQANSLRKLDTDANAKALPSITDIPVSDDSDIKRQVGSGFGSNPLHIKDSEAFPHSSIEALKEGMDKVTKQCNDLKTALLSKDTSLTDSVQDLFNSLKVLSHNQSVLENKLDDVMKNQVNTDILVNNLNERLNKLSTMLQNTSKVNHSNLLIENSSNNTSSQHNTSSSRRGPGRPRKDASTSTMNKLVSNAASVNLKSASNQGAPFSPVNITLPTAVVQTSKSKRYFVEPSTKQESLLLSAPSSSRDDADMSLTSVPQRTNNENGKERPSTANSSSITPTPVTPNNLIQIKRKRGRPPKKRTVETMISNSTDTIDKSDASNRIKNEIPINSLLPSSKFHQIPSSPSNPVSQPAPVRTSRSATQEIDIKSLELASLISTNGDPNAEDSNTTDTVHNNVEGKVNVEENKTEKEKIITIKSSSENSGNNTTNNNNTDNVIKFSANSDINSDIRRLMVNDQFSLSYDASGNITVKLPPVSSPAAATAAAAAAVTSEMNRQQRELDKRRDSREKMLVNMKYNDRDKAKSFMESNKKLLKAMKEEERRKRMTSIIHDNHLNLNLNEISTRSKIKSAEKPTTKGSSMSPKPRSASISGISDHQQEGYQPLEQEKLVDIDNEGSNANSDSLKMGLTISAADTVHKVGIQSMLNSGEEAITKENAEYERKTPGDEETTTFVPLENSQPSDTIRKRTAGDDGALDQTENTSISPKKRRTEDHTKGEEDEGERGVGNSGTLATVENVSGDISADLSKGTSSIHNDTESANDSSNGNGNLGLGTESRNTLLTATPIELICREGFFYRRDIPDVPITTGAYLEFKFKAKEEELINSSINEEDYAAKSKHEKMNAHFFKPDIQEETELAFEILSKTTLTEKYVNSLEYFLMEFRWENKLVGLGLKLRESKRTWQRRKALFALFEFWRDQSRDKRRFHNYTILHAVKEMENYRIFINRSVSWFYNHITLLKMILYDLCDNVTTQWREWMFPHNETLPALGQDGINEDNLNETIDNMLIFDFLDDGSENNQVKYSRIIPPDIR | DNA-binding protein that specifically binds the regulatory region of middle sporulation genes (MSE). Required for the repression of middle sporulation genes during vegetative growth. Represses expression via the recruitment of histone deacetylase HST1. | P46676 |
O15552 | FFAR2_HUMAN | G-protein coupled receptor 43 | Homo | MLPDWKSSLILMAYIIIFLTGLPANLLALRAFVGRIRQPQPAPVHILLLSLTLADLLLLLLLPFKIIEAASNFRWYLPKVVCALTSFGFYSSIYCSTWLLAGISIERYLGVAFPVQYKLSRRPLYGVIAALVAWVMSFGHCTIVIIVQYLNTTEQVRSGNEITCYENFTDNQLDVVLPVRLELCLVLFFIPMAVTIFCYWRFVWIMLSQPLVGAQRRRRAVGLAVVTLLNFLVCFGPYNVSHLVGYHQRKSPWWRSIAVVFSSLNASLDPLLFYFSSSVVRRAFGRGLQVLRNQGSSLLGRRGKDTAEGTNEDRGVGQGEGMPSSDFTTE | G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins but also to the Gq family . Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. May play a role in glucose homeostasis by regulating the secretion of GLP-1, in response to short-chain fatty acids accumulating in the intestine. May also regulate the production of LEP/Leptin, a hormone acting on the central nervous system to inhibit food intake. Finally, may also regulate whole-body energy homeostasis through adipogenesis regulating both differentiation and lipid storage of adipocytes. In parallel to its role in energy homeostasis, may also mediate the activation of the inflammatory and immune responses by SCFA in the intestine, regulating the rapid production of chemokines and cytokines. May also play a role in the resolution of the inflammatory response and control chemotaxis in neutrophils. In addition to SCFAs, may also be activated by the extracellular lectin FCN1 in a process leading to activation of monocytes and inducing the secretion of interleukin-8/IL-8 in response to the presence of microbes . Among SCFAs, the fatty acids containing less than 6 carbons, the most potent activators are probably acetate, propionate and butyrate . Exhibits a SCFA-independent constitutive G protein-coupled receptor activity . | O15552 |
P16359 | CYB_DIPCA | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Dipodomys | SALFLAMHYTPDTLTAFSSVAHICRDVNYGWLIRYMHANGSSLFFICLYLHIGRGIYYGSYSYTETWNIGIILLFLTMA | Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. | P16359 |
C5BHH8 | RIBB_EDWI9 | 3,4-dihydroxy-2-butanone 4-phosphate synthase | Edwardsiella | MNQILLSDFGTPMERVERALSALRDGRGVMVLDDENRENEGDMIFAAEKMTVEQMALTIRHGSGIVCLCITEARRQQLDLPMMVSNNTSHYGTAFTVTIEAAEGVTTGVSAQDRLTTVRAAIADDAKPGDLHRPGHVFPLRARPGGVLARRGHTEATIDLVSLAGFRPAGVLCELTNDDGTMARAPQVMAFARQHEMPVVTIEDLVAYRQAREPQEQAD | Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate. | C5BHH8 |
O49459 | NAC73_ARATH | Protein SECONDARY WALL-ASSOCIATED NAC DOMAIN PROTEIN 2 | Arabidopsis | MTWCNDRSDVQTVERIIPSPGAAESPVASLPVSCHKTCPSCGHNFKFHEQAGIHDLPGLPAGVKFDPTDQEVLEHLEGKVRDDAKKLHPLIDEFIRTIDGENGICYTHPEKLPGVNKDGTVRHFFHRPSKAYTTGTRKRRKVHTDSDVGGETRWHKTGKTRPVLAGGRVRGYKKILVLYTNYGKQKKPEKTNWVMHQYHLGTSEEEKEGELVVSKVFYQTQPRQCGGSVAAAATAKDRPYLHGLGGGGGRHLHYHLHHNNGNGKSNGSGGTAGAGEYYHNIPAIISFNQTGIQNHLVHDSQPFIP | Transcriptional activator that plays a regulatory role in the development of secondary cell wall fibers . Involved in the regulation of cellulose and hemicellulose biosynthetic genes as well as of genes involved in lignin polymerization and signaling . Is not a direct target of SND1 . | O49459 |
A8EXJ9 | RS12_RICCK | 30S ribosomal protein S12 | belli group | MPTYNQLVRFGRKSKTRKTKSPALESNPFKSGVCLVVKTVTPKKPNSALRKIATVRLSNKRTVNAYIPGEKHSVKEHDRVLVRGGQVPDLPGVKYHIVLGAYDIAGVKGRKQGRSRYGAPSKQVAVTKK | Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. | A8EXJ9 |
Q8IIU6 | RTCB_PLAF7 | 3'-phosphate/5'-hydroxy nucleic acid ligase | Plasmodium (Laverania) | MKGIPKRPISNYIEKTNETNLYKIRKGLVNEMNVEGHIYVNEKLKTLLDEEIATYELNKNSTFLPAVMQIANVSTLPGIVKASIALPDVHAGYGFSIGNVAAFDMDNEKAIVSPGGVGFDINCGVRLIRTNLFYEDIKPKQEELTQLLFNHIPVGVGSQGFILCNQENLDDALCLGMDWCVKEGYSWIEDKLNCEDNGRSLYADSNFVSIRAKKRGITQMGTLGAGNHYAEIQIVDQIYDKKSAKLMGIEKKNQVCIMIHSGSRGLGHQIATDALIDMEKSMNKYKINVIDKQLACTPIHSKEGQNYLKAMGSACNFAWINRSSMTFLARQAFSKIFNQSPDDLDMHVIYDVSHNIAKIEEHYIDGKIKKLLVHRKGSTRAFPPFHPLVPLDYQYCGQPILIGGTMGTYSYVLTGNEKAMQATFGSTCHGAGRALSRNKSRNTLSYLDVLNKLKEQNISIRVASPKLIMEEAPESYKNVCDVVQTCHDAGISNKCFRLKPVAVIKG | Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs. | Q8IIU6 |
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