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 |
|---|---|---|---|---|---|---|
B0K2K5 | CBID_THEPX | Cobalt-precorrin-6A synthase | unclassified Thermoanaerobacter | MEVYTIKEGKKLRYGYTTGSCAAAASKAATYMLFTGEKIDTVEIDTPKGWHLILDVLDVTSGEGWVKCGIRKDGGDDPDATHGLIIYSKVELKEGEGIDVYGGEGVGVVTKPGLPVNPGKPAINPVPMSMILNEVKKVLPEGKGVKITISVPGGEKVALKTFNPRLGIVGGISILGTSGIVEPMSEEALKSSLELELSILSAEGHKKVVFAPGNYGKDYAMKEGLEERLIISYGNFLGFMLEKAVEYGFTHVVLAGHIGKLVKVAAGIFNTHSHVADARAEIMAAYVAHFGADKKTVDKVLDSNTTEEALDIIEKAGVNI... | Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. | B0K2K5 |
A5GLQ5 | APT_SYNPW | Adenine phosphoribosyltransferase | unclassified Synechococcus | MDLRQYVRDIPDFPKPGILFRDITPLLRDPAGWHEVIQRLVAVCDRWQPDLIVGIESRGFIVGTALATQLGKGFVPVRKPGKLPGEVIGIDYTLEYGSDRLEIHADALSDHPKVLLVDDLLATGGTASASAELVTKAGGELVGCGFVIELADLAGRAKLPEGVPVESLIIYG | Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | A5GLQ5 |
Q21SE9 | UNG_ALBFT | Uracil-DNA glycosylase | Rhodoferax | MFASDVPRLTGWAPERWPVAADWRPVVDRFLTSETGRALERFVRARLAGGAVIYPQQPLRALALTPLAQVKVVILGQDPYHGPGQAEGLAFSVAPGVRPPPSLCNIFREIARDPLLSPGNLIPHGDGSLVAWARQGVLLLNSCLTVEEGQPASHAGRGWEALTDEVVKAVASIDNPVVFLLWGAHAQAKQRLIAATARQGGRAAADHLVLTANHPSPLSARRPPLPFLGCGHFGLANAYLLQHGCAPIAW | 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. | Q21SE9 |
Q5BU73 | CYB_COLGU | Ubiquinol-cytochrome-c reductase complex cytochrome b subunit | Colobus | MTSTRKSNPIMKMVNHAFIDLPTPSNISMWWNFGSLLATCLLLQIITGLFLAMHYSPDTSSAFSSIAHITRDVNYGWIIRYLHANGASMFFICLFLHVGRGLYYGSFLLLETWNIGILLLLTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWVWGGYSIDKPTLTRFFTIHFTLPFIIVALTTLHLLFLHETGSNNPCGIISNSDKIPFHPYYTTKDILGLTLLLLLLMMLVLFLPDLLSDPDNYTPANPLSTPPHIKPEWYFLFAYAILRSVPNKLGGVLALLLSILILMAMPMLHKSKQQSMTFRPL... | 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... | Q5BU73 |
B8F3D4 | RRF_GLAP5 | Ribosome-releasing factor | Glaesserella | MINEIKKDTQERMEKSLEALKGHISKIRTGRAQPSLLDAIQVEYYGSATPLRQLANVVAEDARTLAVTVFDRSLISAVEKAILTSDLGLNPSSAGTTIRVPLPPLTEERRRDLIKIVKGEGEQGKVSIRNIRRDANDKIKTLEKEKQISENDERKAQDDIQKITDIYIKKVDEILADKEKELMDF | Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another. | B8F3D4 |
P38889 | SKN7_YEAST | Peroxide sensitivity protein 9 | Saccharomyces | MSFSTINSNVNKTTGDSNNNTTENSSTADLLGMDLLQSGPRLMNTMQPNNSSDMLHINNKTNNVQQPAGNTNISSANAGAKAPANEFVRKLFRILENNEYPDIVTWTENGKSFVVLDTGKFTTHILPNHFKHSNFASFVRQLNKYDFHKVKRSPEERQRCKYGEQSWEFQHPEFRVHYGKGLDNIKRKIPAQRKVLLDESQKALLHFNSEGTNPNNPSGSLLNESTTELLLSNTVSKDAFGNLRRRVDKLQKELDMSKMESYATKVELQKLNSKYNTVIESLITFKTINENLLNNFNTLCSTLANNGIEVPIFGDNGNRN... | Transcription factor that is part of a SLN1-YPD1-SKN7 two-component regulatory system, which controls gene expression in response to changes in the osmolarity of the extracellular environment. Under low osmotic conditions, phosphorylated and activated by the phosphorelay intermediate protein YPD1. Also activated in res... | P38889 |
Q2NEL6 | TF2B_METST | Transcription initiation factor IIB | Methanosphaera | MKEDVAEMEKKETKCPECGSTKLINDHERGEVVCGACGLVIDDNIVDMGPEWRAFDHEQRDKRTRVGAPITYTIHDKGLSTMIDWRNKDIYGRDIPARNRAQWYRLRKWQRKIRISGATERNLAFALSELDRDSSRLGLPRSVRESASVVYRNAVENKLIRGRSIEGVVAASLYAACRRCKVPRTLDEIADVSRVSKKEVGRTYRFLTRELHIRLPPTSPIDYVPRFASELNLSGVVQSKAIEIINQAMDNGLTSGRGPTGVAAAALYIASVLLGERKTQRDVADIAGVTEVTIRNRYKELTEQLDMGVNL | Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB). | Q2NEL6 |
Q8NGS0 | OR1N1_HUMAN | Olfactory receptor OR9-22 | Homo | MENQSSISEFFLRGISAPPEQQQSLFGIFLCMYLVTLTGNLLIILAIGSDLHLHTPMYFFLANLSFVDMGLTSSTVTKMLVNIQTRHHTISYTGCLTQMYFFLMFGDLDSFFLAAMAYDRYVAICHPLCYSTVMRPQVCALMLALCWVLTNIVALTHTFLMARLSFCVTGEIAHFFCDITPVLKLSCSDTHINEMMVFVLGGTVLIVPFLCIVTSYIHIVPAILRVRTRGGVGKAFSTCSSHLCVVCVFYGTLFSAYLCPPSIASEEKDIAAAAMYTIVTPMLNPFIYSLRNKDMKGALKRLFSHRSIVSS | Odorant receptor. | Q8NGS0 |
P91660 | L259_DROME | Wunen region A protein | Sophophora | MDKQPVLEPTFDSVSERENTSIEESSLLENNGFDHRNKDESLSVNTSPPLVCRKCFELGHQTENCKQKLTVNSENNSAQNEKEKVLPENPRARSNFISSLCFWYTIPIFRKGYRKTLDSTDLYRPLEEQKSDILGNRLCASWERELKNDGRSPSLVRALLRVFGWQLGFPGLAIFVVELGLRTLQPIFLVKLISYFSGEPDAANAGFYYAVAQIVISALTVMILTPTTFGIHHVCFKMRVAMGSMIFRKALRLTKGALGDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGISAVFGVLFMLLFM... | Vital for development. | P91660 |
A6VA56 | KUP_PSEA7 | Probable potassium transport system protein kup | Pseudomonas | MSDAATRTEGTSGGHSSSAVGLMVGAVGVCYGDIGTSPLYTLKEVFIGGYGVQANHDGVLGVLSLIFWSLIWVVSIKYVIFVLRADNQGEGGVMALSALARRAAAPFGRLQTFVVVAGLIGAALFYGDSMITPAISVLSAVEGLEIAFDGLEHWTVPLALIVLIGLFLIQKHGTARIGILFGPVMVLWFGALAALGVYGVIQQPEVLQAMNPVWAVRFFGSHPGIGVAILGATVLALTGAEALYADMGHFGRKPIARAWFLLVLPALVLNYFGQGATILSNAEAARNPFYLLAPGWALLPMVALSTLATVIASQAVISGA... | Transport of potassium into the cell. | A6VA56 |
Q9SY91 | PBL15_ARATH | PBS1-like protein 15 | Arabidopsis | MRDSSTTASTKSSPLWKPFASNCCSVDDQTVFGNLSRCRPSRSEFSKNHLGPLPSFRRLSFADLSRSSSARINEDLAQTLGADLVDFQMCELKMITQSFSGNYLLGEGGFGKVYKGYVDDYLRQSLKAQPVAVKLLDIEGLQGHREWLSEVIFLGQLKHPNLVKLIGYCCEEEERVLIYEFMPRGSLENHLFRRISLSLPWATRLKIAVAAAKGLAFLHDLESPIIYRDFKTSNILLDSDFTAKLSDFGLAKMGPEGSKSHVTTRVMGTYGYAAPEYVSTGHLTTKSDVYSYGVVLLELLTGRRATEKSRPKNQQNIIDW... | May be involved in plant defense signaling. | Q9SY91 |
A9M3P6 | HISZ_NEIM0 | ATP phosphoribosyltransferase regulatory subunit | Neisseria | MQTWQLPEHIADVLPTNARQLESAREQLLALFRVHGYELVQPPLMEYAHSLLTHIDAGLSLKTILVTDRLSGRQLGIRADITPQVARIDAHLLSANQGINRLCYAGPVLHAQPDGLLNMREPLQAGAEMYGFADIRGDIELIDLMLKSMKIADMGKVLLSLGHIGIFRALSDAAHLDAGQSATLLALMQDKDTGAVEAQVKAWKLDGMWAKAFSLLPRLYGGREVLSDARGRLPDLSAVGGALGELQAVCDAFPDCEIHIDLSELRVDNYHTGLLYAAYAADFHDAVARGGRYDGLGGYFGRARPATGFSFDLRSFIGRL... | Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. | A9M3P6 |
Q1BSV1 | FLGH_BURCA | Basal body L-ring protein | Burkholderia cepacia complex | MKQVRLPSSATVRAACAVAVAALAGCAQIPRDPIIQQPMTAQPPMPMSMQAPGSIYNPGYAGRPLFEDQRPRNIGDILTIMIAENINATKSSGANTNRQGNTDFNVPTAGFLGGLFAKANLSATGANKFAATGGASAANTFNGTITVTVTNVLPNGNLVVSGEKQMLINQGNEFVRFSGVVNPNTISGANSVYSTQVADAKIEYSSKGYINEAETMGWLQRFFLNIAPW | Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. | Q1BSV1 |
Q2RMI9 | PDXT_MOOTA | Pyridoxal 5'-phosphate synthase glutaminase subunit | Moorella | MRIGVLAMQGAFREHIQSLEALGVQGVEIRHANQLEGIAGLIIPGGESTTIGKLMVEFNLLEPVRHLAEGGLPVFGTCAGMVLLARDIIGSDQPRLGLMNARVQRNAFGRQVDSFEVDLEIPVLGEEPFHAVFIRAPYIEEIEPPAEALATFKDKIVMVRQGNLLATAFHPELTKDLRVHSYFLKMIG | Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. | Q2RMI9 |
Q2SKX2 | PYRG_HAHCH | UTP--ammonia ligase | Hahella | MTRYIFVTGGVVSSLGKGIASASLAAILEARGLKVTILKLDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFIRTTMTKRNNFTTGRVYETVLRKERRGDYLGGTVQVIPHITDEIKRRIVEGAGDADVALVEIGGTVGDIESLPFLEATRQLKVEVGSRRALFMHLTLVPYIATAGEVKTKPTQHSVKEMRSIGLQPDILVCRSEHSIDQSSRRKIALFTNVEERAVIALEDAKSIYSIPMMLHAQGLDEIIVERFGLECGPADLSEWQSVVDNEANPEHEVTIAMVGKYMELLDAYKSLIEALKHAGIRNKT... | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | Q2SKX2 |
Q8RH07 | GRPE_FUSNN | HSP-70 cofactor | Fusobacterium | MKDKEIKEEVLKEEINKEVNEKKKCECEEGKEEAHEHKNDEHACCGKHNHKEEIEKLKAEIEEWKNSFLRKQADFQNFTKRKEKEVDELKKFASEKIITQFLGSLDNFERAIESSSESKDFDSLLQGVEMIVRNLKDIMSSEDVEEIPTEGAFNPEYHHAVGVETSEDKKEDEIVKVLQKGYMMKGKVIRPAMVIVCKK | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-b... | Q8RH07 |
Q9H503 | BAFL_HUMAN | Barrier-to-autointegration factor 2 | Homo | MDNMSPRLRAFLSEPIGEKDVCWVDGISHELAINLVTKGINKAYILLGQFLLMHKNEAEFQRWLICCFGATECEAQQTSHCLKEWCACFL | May play a role in BANF1 regulation and influence tissue-specific roles of BANF1. | Q9H503 |
Q97WW0 | CS3HD_SACS2 | CRISPR-associated endonuclease Cas3-HD | Saccharolobus | MIKPCAYEKQGLIDHAIGSYRVLDGKISESYYKIISRRLERYGIVLDLNGVKEMVKDVVVLHDMGKAGEYYQNQFDDNCNPLKSNFSFIYHELGSALFFYYDYEPIDVEKAEEVKSLLTLAVLNHLNAIRVISDYLVNKFPDNFDERMIKLNKYGSIMLQNLRGVISKSLKVRDYTFDDYHDMLYAFSKKSDKYLKLYNLFLAPIMLGDNLDSSLVRNNGSKTGFVRILEGELNGGSTL | CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic ac... | Q97WW0 |
A3DJK5 | ECFA2_ACET2 | null | Acetivibrio | MSIKVTGLTYVYMKGTPYEKKALDNINLSIETGEFVGIIGHTGSGKSTLVQHFNGLLKPTSGSVYINGEELTGQRAKELKKQVGIVFQYPEHQLFEETVYKDIAFGLVRRGEEKDEIYRKVRKTIRLVGLSEDILDKSPFELSGGQKRRVAMAGILVLEPSILVLDEPAAGLDPKGREEIFELVSNLHKNNKMTVILVSHSMEDVAKYVQRVIVMNQGRIEMCGPVRSVFKNTETLEEIGLAAPQITYLMKKLKEKIPQINDDILTIAEAKEELAKYIRKA | ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. | A3DJK5 |
Q7SFB0 | GUS79_NEUCR | Beta-D-glucuronoside glucuronosohydrolase | Neurospora | MKRILGLIAYASVPTVINAVQISVDETAPSNPVFDAYVSYSIEFSSFPDYAGNNSRPNTFSENLLDNLGKITGTKPYIRVGGNTQDYALYNASLPYSLNGTIDPKRSSDYPTTIFIGPSFFESYNSFKNTRFIHGFNLGLGGNRTSGWQTLLDTVPLACKALGGGKLFAWTYGNEPDLFSTSAQGPVRPPSWNEAEYVDQWLNGTRKIHELLERNCPDLAKNGTYGYIAPSFAGVGNKLKAPKAWGEGLNEDKNIKLFATHNYISGATSPGVTLQGTLMNHSMTKASVDAHIVEYNQVKAIDAAAPPLIFGETNSLYNQG... | Beta-glucuronidase that hydrolyzes beta-glucuronosyl and 4-O-methyl-beta-glucuronosyl residues of arabinogalactan-protein. Hydrolyzed heparan sulfate only very weakly. Has no activity on xylan from birchwood. Able to catalyze the transglycosylation of glucuronic acid (GlcA) residues from p-nitrophenyl-beta-glucuronic a... | Q7SFB0 |
Q1QZX9 | PYRG_CHRSD | UTP--ammonia ligase | Chromohalobacter | MTRYIFVTGGVVSSLGKGIASASLAAILEARGLKVTILKLDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFIRTKMTQGNNFTTGRVYEHVLRKERRGDYLGGTVQVIPHITDEIKRRVYEGGDGFDVALVEIGGTVGDIESLPFLEATRQIRSEKGANQAIFMHLTLVPYIKTAGETKTKPTQHSVKELRSIGIQPDILICRSEVELEESERRKIALFTNVEERAVVPLQDADTIYRIPLMLHEHGLDDIICDKLRIEADEVDLAEWVRVLDAKLNPLKSVNIAMVGKYMELLDAYKSLNEALIHAGIQGRV... | Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. | Q1QZX9 |
A7IC11 | RIMP_XANP2 | Ribosome maturation factor RimP | Xanthobacter | MTEIQAVLDDPNEPRLITETGVAARVAAIASGVLGALGYRLVRVKVTNRDGGTLQIMAERPDGTMSIDDCEAASRALSPVLDVEDPISSAYRLEMSSPGIDRPLVRQSDFVRWAGHEVKVEMARPVDGRKRFRGILIGAEDGIAVVRRLDAPATEEPTVRLPVADIHDAKLMLTDALIREALRAAKAAGQAIDEEAEAFLDGEDGDDTGVDAGDPDQDDADDALAEATAQPAAPYKGPSRKDGGNKLVGRKAKGKKASPKKSNAKKKAGLETAASSANASTVKETH | Required for maturation of 30S ribosomal subunits. | A7IC11 |
B2J914 | BIOB_NOSP7 | Biotin synthase | Nostoc | MVGIRYDWQELEIRAIYNTPLLELIYQAASVHRQYHDPTKIQVCKLISIKTGGCPEDCSYCAQSSRYKTEVKAEALLEKETVVNIAQKAKETGVSRICMGAAWREVRDNSQFEEVLEMVKDITAMGLEVCCTLGMLTANQARKLEEAGLYAYNHNLDTSQEYYSTIITTRTYSDRLNTIENVRQTNVTVCSGGILGLGETVDDRVGMLQTLANLHPHPESVPINILSQVPGTPLENQPDVPIWDIVRMIATARILMPASDVRLSAGRARLSQVEQAFCFMAGANSIFSSDDNKMLTVTTPCPDYDTDREMLNLLGLGMRP... | Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. | B2J914 |
Q0IY07 | ORC3_ORYSJ | Origin of replication complex subunit 3 | Oryza sativa | MAAPPGEAPLTAATNIEPFYVLHKGGAAASSSSSSAPSLPSSGRARRRIDVSGLASPNPKPGKRSRDDDAAEDDDDDELYERLRLDAFHRVWSKIQSTINEVLRGISLKLFDQVLRWVQESFSAVRSIARPSAAEVRQPYPLLTDVICRKIPTAFVLTKNAEFVDDITTFRDLAEYLESNGCHLAKLSATELSEKNGVGCCFRSLLRQLLSDVPDVADIFALASWYSAAENYDQPIVVVIDDLEQCSGDVLGELVMMLSEWVIKIPIFFVMGIATTLDAPRKLLSSEDLQRLEPCKLTLGSPSDRMNALVEAILVKPCAG... | Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. | Q0IY07 |
Q2LPY6 | GATB1_SYNAS | Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B 1 | Syntrophus | MEFEAVIGLEIHIELNCPTKLFCDCPNNPGDEPNVNTCPICLWFPGAIPRLSQAALEKASLLCLGLGAELQPRSAFDQKVYYYPDLPKGYQLSQAHLPLARGGGIDITDENGRPKRLRIHHIHMEEDVAKLVHEIEGRTPISLVDFNRAGAPLVEIVSEPDFRTPHDAMEFLKALRTQVRYVGASECSMENGTMRVDANISVRPRGTDQMNTKVEVKNMNSIRHVGDAVAYEISRQSACVSSGEAVVLHTRLWDPDRKATFPMRAKFEGPCVPDPSVPFIDLSPEWIEKMRARLPEMPAARAERFVARYGLTDEEAVYLS... | 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 ... | Q2LPY6 |
A9VS97 | NUOB_BACMK | NDH-1 subunit B | Bacillus cereus group | MVINFEELHPQERAELERNIFFSTLEQLKGWARSNSLWPMTFGLACCAIEMMGVGSSHYDLDRFGSFFRTSPRQSDVMIVSGTVTKKMAPIVRRLYDQMPEPKWVIAMGSCATAGGPYVNSYAVVKGVDQIVPVDVYIPGCPPNPAALIYGINKLKEKIRYEARTGKQVTNK | 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 a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions ar... | A9VS97 |
Q3A1E5 | GPMI_SYNC1 | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase | Syntrophotalea | MTVEIRRPVALVILDGWGINPVCEHNAVCQADTPRLRALLESWPHARIGASGRDVGLPDGQMGNSEVGHLNIGAGRTVYQDLTRISLSIEEDTFFENTELRKVMQQVVESQGKLHLMGLLSDGGVHSHMEHLYALVEMARRAGVEQVCIHAFMDGRDTPPQSGAGYLAQLEDKLQDIGLGRVATVIGRYWAMDRDNRWERVEKAYRAMTEGVGTSFESSAAAIADAYAQGQTDEFVEPRFVGGEKPCTVDDGDGMIFFNFRADRAREITRTFTSSDFSGFSREKTPRLAGYVCLTEYDASFGLPMAFPPETYPELLGEVV... | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. | Q3A1E5 |
A8FMS6 | CH60_CAMJ8 | Chaperonin-60 | Campylobacter | MAKEIIFSDEARNKLYEGVKKLNDAVKVTMGPRGRNVLIQKSFGAPSITKDGVSVAKEVELKDSLENMGASLVREVASKTADQAGDGTTTATVLAHAIFKEGLRNITAGANPIEVKRGMDKACEAIVAELKKLSREVKDKKEIAQVATISANSDEKIGNLIADAMEKVGKDGVITVEEAKSINDELNVVEGMQFDRGYLSPYFITNAEKMTVELSSPYILLFDKKIANLKDLLPVLEQIQKTGKPLLIIAEDIEGEALATLVVNKLRGVLNISAVKAPGFGDRRKAMLEDIAILTGGEVISEELGRTLESATIQDLGQAS... | 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. | A8FMS6 |
P0CD37 | NU2C2_PSINU | NADH-plastoquinone oxidoreductase subunit 2 B | Psilotum | MKEIESFLVYSSSILPECILIFSSIGILSIDLLSLPNEGDTFWSYSISLAALAISIIILLLQWNKEPVLTFSETFQISRFNDIFRFFLLICSFLCIPLSVDYIRCTKMPVTEFLLFVLTATLGGMFLCGANDLISIFVASECLALSSYLLSGYTKRDVRSNEAMMKYLLMGGASSSILVYGFSLPYGLSGGEIQLRGMVNGLINMQMYNSAGVSIAMIFILVGIGFKLSLVPFHQWTPDVYEGSPTPVVAFFSVTSKVAALALATRLFHILFSSLSNEWHLPLEILAILSMILGNLIAVTQTSMKRMLAYSSISQIGYIL... | NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translo... | P0CD37 |
C6DH76 | GLGA_PECCP | Starch [bacterial glycogen] synthase | Pectobacterium | MRVLHVCSELFPLLKTGGLADVAGALPGAQIAAGMDVRVILPAFPDLKKGIANLQVVRELDTFAGHVTLLFGHFNGVGIYLIDVPELYERAGSPYHDPALYAYADNYLRFALLGWMGCEMACGLDHYWRPDIVHAHDWHAGLTCAYLAARNRPAKSIFTVHNLAYQGLFDARHMPDLHLPREFFQVYGLEFYGQISYLKAGLYYADHITTVSPTYAHEITLPAYGYGMEGLLKSREEEGRLSGILNGVDEMIWNPAHDPLLASHYSRDTLANKAENKRRLQTAMGLKVDDKVPVFAIVSRLTSQKGLDIALSAIPDLLEQ... | Synthesizes alpha-1,4-glucan chains using ADP-glucose. | C6DH76 |
A6UV53 | RPO5_META3 | DNA-directed RNA polymerase subunit H | Methanococcus | MKIALNQMVPKHEVISKEEVQKLLAKYDIKIQQLPKIFDIDPVIEEIGAKPGDVVKISRDSPTSGHATYYRLVVKKTI | DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | A6UV53 |
Q9ABZ9 | TSAD_CAUVC | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Caulobacter | MTSPKQSDLLILGLETSCDETAASVVRRAADGTVTVLSSVIGTQFEKHAPFGGVVPEIAARAHVESIDAIAAEAVRAAGVGFGDLDGVAATAGPGLVGGVMVGLAFGKAVALARGAPLVAVNHLEGHAVSARLGADIAYPFLLLLVSGGHCQLLEVSGVGACKRLGTTIDDAAGEAFDKIAKSLGLPYPGGPALEKLAVGGDPTRYALPRALLGRKDCDFSFSGLKTAAARIAETLTTDDARRDLAAGVQAAIARQLSERVDRAMKLYKDSHDPEDLRFVVAGGVAANGAVRAALLADCEKNGFSFAAPPLAYCTDNAAM... | 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 ca... | Q9ABZ9 |
A7ZY13 | GAL1_ECOHS | Galactose kinase | Escherichia | MSLKEKTQSLFANAFGYPATHTIQAPGRVNLIGEHTDYNDGFVLPCAIDYQTVISCAPRDDRKVRVMAADYENQLDEFSLDAPIVAHENYQWANYVRGVVKHLQLRNNSFGGVDMVISGNVPQGAGLSSSASLEVAVGTVLQQLYHLPLDGAQIALNGQEAENQFVGCNCGIMDQLISALGKKDHALLIDCRSLGTKAVSMPKGVAVVIINSNFKRTLVGSEYNTRREQCETGARFFQQPALRDVTIEEFNAVAHELDPIVAKRVRHILTENARTVEAASALEQGDLKRMSELMAESHASMRDDFEITVPQIDTLVEIVK... | Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). | A7ZY13 |
Q3AC30 | RISB_CARHZ | 6,7-dimethyl-8-ribityllumazine synthase | Carboxydothermus | MQVFEGKLNGKGLKIGIIVSRFNEFITQKLLAGALDCLTRHEVENTNIDVIWVPGAFEIPLVAKRAVHKDYDAIICLGAVIRGATPHFDYVAAEVAKGIAAVGLEANKPVIFGVLTTDTIEQAIERAGTKAGNKGWEAALAAIEMANLFKKV | Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. | Q3AC30 |
Q5R4R3 | OGFD1_PONAB | uS12 prolyl 3-hydroxylase | Pongo | MNGKRPAEPGPARVGKKRKKEVMAEFSDAVTEETLKKQVAEAWSRRTPFSHEVIVMDMDPFLHCVIPNFIQSQDFLEGLQKELMNLDFHEKYNDLYKFQQSDDLKKRREPHISALRKILFEDFRSWLSDISKIDLESTIDMSCAKYEFTDALLCHDDELEGRRIAFILYLVPPWDRSLGGTLDLYSIDEHFQPKQIVKSLIPSWNKLVFFEVSPVSFHQVSEVLSEEKSRLSISGWFHGPSLTRPPNHFEPPIPRSPHIPQDHEILYDWINPTYLDMDYQVQIQEEFEESSEILLKEFLKPEKFMKVCEALEHGDVEWSS... | Prolyl 3-hydroxylase that catalyzes 3-hydroxylation of 'Pro-62' of small ribosomal subunit uS12 (RPS23), thereby regulating protein translation termination efficiency. Involved in stress granule formation. | Q5R4R3 |
Q4ULF7 | RHO_RICFE | ATP-dependent helicase Rho | spotted fever group | MNTTNKESTEELNNTESNNNHNNFAENGNIINLKQLKRKLPEELQAQAEELKIENINSLLKQELVFAILKKSVEQGGLIVGEGVLEVLPDGFGFLRSPEVNYLAGPDDIYISPSQIRRFGLRTGDTVEGQIRAPKAGERYFALLKVNRVNFEDPSKAYHRVHFDNLTPLYPDEKLGLELENNSKDSKDFSTRVIELVAPMGKGQRALIVAPPRTGKTVLLQNIAHAITTNNPEVFLIVLLIDERPEEVTDMQRSVRGEVVSSTFDEPASRHVQLAEMVIEKAKRLVEHKKDVVILVDAITRLARAYNTVVPSSGKVLTGG... | Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. | Q4ULF7 |
A2BUT0 | PSBL_PROM5 | Photosystem II reaction center protein L | Prochlorococcus | MQVNENPNKVPVELNRTSLYLGVLSVLVLGILFSSYFFN | One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, a... | A2BUT0 |
B9JCI9 | RLMN_AGRRK | tRNA m2A37 methyltransferase | Agrobacterium tumefaciens complex | MSAIDVMTPSKLKPMPVSQPVELSPKPSLIGLTREEMGAALKEKGVADKQVKMRVSQLWNWIYVRGVSDFDAMANVSKDMREMLKAHFTIARPEIVEEQVSNDGTRKWLLRFPPRGAGRPVEVETVYIPEEGRGTLCVSSQVGCSLTCSFCHTGTQRLVRNLTAEEILSQLLLARDRLGDFPDREAPQGTIMPAEGRKVSNMVMMGMGEPLYNFESVKTALLIASDGDGLSLSKRRITLSTSGVVPEIYRTGDEIGVMLAISLHAVRDDLRDMLVPINKKYPLKELMDACRAYPGLSNARRITFEYVMLKGVNDSLEDAK... | Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. | B9JCI9 |
Q9S1E6 | NRFH_WOLSU | Cytochrome c-type protein NrfH | Wolinella | MNKSKFLVYSSLVVFAIALGLFVYLVNASKALSYLSSDPKACINCHVMNPQYATWQHSSHAERASCVECHLPTGNMVQKYISKARDGWNHSVAFTLGTYDHSMKISEDGARRVQENCISCHASLSSTLLENADRNHQFNDPKGASERLCWECHKSVPHGKVRSLTATPDNLGVREVK | Subunit of the nitrite reductase complex that mediates electron transfer from quinol to the catalytic subunit. | Q9S1E6 |
Q3K4L8 | KGUA_PSEPF | GMP kinase | Pseudomonas | MTHSTGTLYIISAPSGAGKSSLVKALTDTNPDIRVSISHTTRAMRPGEVDGVNYHFVTREEFVKMGEHGDFLERAEVFGNFYGTSQSRLQQTLDEGHDLILEIDWQGAEQVRKLMPQARSIFILPPSLQALHQRLTNRGQDSDEIIDGRMREAVSEMSHYVEYDYLIINDDFAHALDDLKAIFRANQLQQKRQQVRFGKLLAELLG | Essential for recycling GMP and indirectly, cGMP. | Q3K4L8 |
Q5KXB1 | ARGR_GEOKA | Arginine repressor | Geobacillus thermoleovorans group | MNKGQRHIKIREIIMNHDIETQDELVDRLREAGFNVTQATVSRDIKEMQLVKVPMANGRYKYSLPSDQRFNPLQKLKRALVDVFVKLDGTGNLLVLRTLPGNAHAVGVLLDNLDWNEIVGTICGDDTCLIICRTPKDAEKVSDQLLSML | Regulates arginine biosynthesis genes. | Q5KXB1 |
Q8R2Z3 | S26A7_MOUSE | Solute carrier family 26 member 7 | Mus | MTGAKRKKRSVLWGKMHTPHREDIKQWCKRRLPILEWAPQYNLKENLLPDTVSGIMLAVQQVAQGLSFAMLSSVHPVFGLYGSLFPAIIYAIFGMGRHVATGTFALTSLISANAVERLVPQSSRNLTTQSNSSVLGLSEFELQRIGVAAAVSFLGGVIQLVMFVLQLGSATFLLTEPVISAMTTGAATHVVTSQVKYLLGIKMPYISGPLGFFYIYAYVFENIKSVQLEALLFSLLSIIVLVLVKELNEQFKRKIKVVLPVDLVLIIAASFACYCTNMENTYGLEVVGHIPNGIPPPRAPPMNILSAVLTEAFGVALVGY... | Acts as a sodium-independent DIDS-sensitive anion exchanger mediating bicarbonate, chloride, sulfate and oxalate transport. May play a role in the maintenance of the electrolyte and acid-base homeostasis in the kidney, by acting as a distal excretory segment-specific anion exchanger, specifically chloride. Plays a majo... | Q8R2Z3 |
B3PVH2 | ARGC_RHIE6 | N-acetyl-glutamate semialdehyde dehydrogenase | Rhizobium | MAPKIFIDGEHGTTGLQIRTRMAGRRDVELLSIPEAERRNAAMREDMLNSADIAILCLPDDASKEAVQMVSANNNVRVIDTSTAFRVNPGWAYGFAEMDGAQADKIKAARFVANPGCYPTGAIGLIRPLRAAGILPDGYPVTVNAVSGYTGGGKQMIAQMENPDHPDAITAPHFLYGLPLTHKHVPEMTVHGLLDRAPIFSPSVGKFAQGMIVQVPLHLDDLAEGTTMESIHAALTAHYAGQDIVTVVPLADSKALARVNAVELEGKDTMKLFVFGTPGGSQVNLVALLDNLGKGASGAAVQNMDLMLAS | Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. | B3PVH2 |
Q8P3K1 | FUCM_XANCP | Type-2 mutarotase | Xanthomonas | MSMQRLCYVLDLHDDAALIAQYERWHRPSEVWPEVVASLQQAGIAELEIFRSGDRLVMLMTVGEDYDPAAKAARDAGDPRIQAWEALMWRFQKALPGSAPGEKWREAGRIFALSEAVSVQQGSAA | Plays a role in the catabolism of L-fucose. Involved in the anomeric conversion of L-fucose. | Q8P3K1 |
P41005 | MES1_SCHPO | Protein mes1 | Schizosaccharomyces | MVNTDNKENEPPNMEKAHMDSSNALYRVQRPLQRRPLQELSIELVKPSQTITVKKSKKSTNSSSYFAQLHAASGQNPPPSVHSSHKQPSKARSPNPLLSMR | Specifically required for meiosis II (MII). Binds to slp1, an activator of the anapahase promoting complex/cyclcosome (APC/C), and counteracts its function in promoting proteolysis of cdc13. By suppressing the degradation of cdc13 at anaphase I this protein may help maintain a sufficient level of cdc2 kinase activity t... | P41005 |
C6DH16 | RNFB_PECCP | Rnf electron transport complex subunit B | Pectobacterium | MSTIWIAIAALSALALAFGLVLGYASRRFEVENDPIVEEVEAMLPQSQCGQCGYPGCRPYAEAVALNGENINKCGPGGEAMMLKLAEKLNVDPQPLEGDADVQAPARQVAWIDESNCIGCTKCIQACPVDAIIGSTKAVHTVVSDLCTGCDLCVAPCPTDCIELRPIAPTPANWKWDLDTIPVRVIQVERHA | Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. | C6DH16 |
P0CM27 | ASF1_CRYNB | Anti-silencing function protein 1 | Cryptococcus neoformans species complex | MSIVNIRNIELLNNPAKFDDPYNFRIKFEAIAPLVEDLDWRLIYVGSASSEEFDQELDNCSVGPIPAGINAFDFSAPAPAHHLLPSVEPDEILGVTVIIITASYREKEFVRVGYYVNTYYEDEELKENPPSVVQWDKLHRNVLIEKPKVTRFQNNWDSAPQLNTFDGQQPAAELPPSGGNPELFNAPLPPPVQRATAAGGMDVDQPMA | Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. | P0CM27 |
Q2NZB1 | RSMH_XANOM | rRNA (cytosine-N(4)-)-methyltransferase RsmH | Xanthomonas | MSQPPAAHVPVLYTQVLDGLQVTENGTYLDGTFGRGGHARGVLEHLGPGGRLLVMDKDPDAIAVAEQTFGGDARVSIHRGSFAGLGQVVAAATVDGILLDLGVSSPQLDVAGRGFSFGKDGPLDMRMDPDSGQSAAQWLAQATDREIADVLWAYGEERQSRRIARAIVARRAEQPLLRTAQLADLIASVMPRGDSKTHPATRSFQAIRIYINRELDDLETGLDAALAALKPGGRLAVISFHSLEDRIVKQFMARYAKAPPSNRRLPEAQPFVPTLQLVSGAIKADDTELNVNPRARSAVLRVAEKLELGIGDSGLERRSG... | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA. | Q2NZB1 |
B3CST4 | SYE2_ORITI | Glutamyl-tRNA synthetase 2 | Orientia | MTNIVTRFAPSPTGFLHIGGARTALFNYLFARHHKGKFLLRIEDTDAARSTEEYKLGIIDSLKWLKINWDNDIFYQSANLQRHVNVALELVKSGKAYYCFTSQEEIDLQRQLAIAQKQSFIFRSPWRNNIPSSLSLKNNNKAYVIRFKAPNHGTTIINDYVQGKVVFQNQQIDDMILVRSDGTPTYMLAVVVDDHDMGITHIIRGDDHLTNAAKQIALYDALGWKAPAMVHIPLIYGPDGTKLSKRHGAIGVDAYQKMGYLPEALCNYLLRLGWSYQDEEIISHERAIKLFDIDGLGKSAARLDFDKMLYLNGYYIRSTD... | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). | B3CST4 |
A7MH80 | FADI_CROS8 | Fatty acid oxidation complex subunit beta | Cronobacter | MSQALPLVTRQGDRIAIVSGLRTPFARQATAYHGVPAVDLGKMVVGELLARSEIPPEVIEQLVFGQVVQMPEAPNIAREIVLGTGMSVHTDAYSVSRACATSFQAVANVAESLMAGTIRAGIAGGADSSSVLPIGVSKKLARTLVDANKARTAGQRLKLFSRLRLRDLLPVPPAVAEYSTGLRMGDTAEQMAKTHGITREQQDALAHRSHQLAAQAWAEGKLREEVMTAYTPPYREPLSEDNNIRKTSSLADYAKLRPAFDRKHGTVTAANSTPLTDGAAAVILMTESRARELGLTPLGYLRSYAFTAVDVWQDMLLGPA... | Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. | A7MH80 |
P0DM87 | VM2_TRIST | Snake venom metalloproteinase | Trimeresurus | MIQVLLVTICLAVFPYQGNSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIQNDADLTASISACNGLKGYFKLQGETYLIEPLKLPDSEAHAVFKYENVEKEDEAPKMCGVTETNWESDEPIKKASQLNLTPDEQRFIELVIVADHRMYTKYDGDETEISSKIYEIANDLNVIFRALYIHVALIGLEIWPSGELCNVTLSADDTLDSFAEWTKRDLQKRKRHDNAQLLTGMIFNEKIEGRAYKKTMCHWKRSVGIVRDHRTR... | Snake venom zinc metalloproteinase that inhibits ADP-induced platelet aggregation in human platelet-rich plasma (IC(50) is 175 nM) and cleaves alpha-(FGA) and subsequently the beta-chain (FGG) of bovine fibrinogen, leaving the gamma-chain unaffected. It is also able to inhibit proliferatin of ECV304 cells by inducing a... | P0DM87 |
B1XV46 | TRPA_POLNS | Tryptophan synthase alpha chain | Polynucleobacter | MSKITALFKELKATGKKGLIPFIAAGDPDPKQTVELMHALVRGGSSVIELGVPFSDPMADGPVIQRLSERALTHGVTLHSCLEMVKEFRKKDANTPVVLMGYANPVEQMGAERFATEAKAAGVDGVLVVDCPPEECVDFAARMRVAGIDPIFLLAPTSSQERIKGAAKIASGYIYYVSMRGVTGASHLNTQDVASIIPKIREETDIPIAVGFGISDAASAKAVSTSADAVVIGSQIIRLLEDAPSGQAVQSLETFIREIRDALDS | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | B1XV46 |
Q2RTI8 | TRMFO_RHORT | Folate-dependent tRNA(M-5-U54)-methyltransferase | Rhodospirillum | MTQHPPLTIVGGGLAGCEAAWQAARAGLRVILIEMRPLRTTEAHLGDGLAELVCSNSLRSDDPLYNAVGLLHEEMRRAGSLILAMAEAHRVPAGGALAVDRQGFSDAITRALAEHPLIEIRRGEVDRLPAVEDGPAIIASGPLTSAALAAAIAEATGETSLAFFDAIAPIVHKDSIDFDRAWFQSRYDKGDGRDYINCPLTRDQYDAFVDALLAGEKTMFKEWEGTPYFDGCLPIEVMAERGRETLAFGPMKPVGLTDPRNPGLRPHAVVQLRQDNALGTLYNMVGFQTKLKHGEQARIFRMIPGLENAEFARLGGIHRN... | Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. | Q2RTI8 |
Q28TN0 | RIMO_JANSC | Ribosome maturation factor RimO | unclassified Jannaschia | MSQNPPLLRPDLARARVPDDARPGQPRIGMVSLGCPKALVDSERILTRLRAEGYAISPDYTGAEAVIVNTCGFLDSAKLESLEAIGEALEANGKVIVTGCLGAEPEYITGAHPTVLAVTGPQQYEQVLDAVHGAVPPAPDPFIDLLPPAGVKLTPRHYAYLKIAEGCDHKCKFCIIPDMRGKLVSRPQTAVMREAEKLVDSGVKELLIISQDTSAYGVDWKDRNKAGDEKFPILNLSRDLSTLGAWVRLHYVYPYPHVRELIPLMADPANGLLPYLDIPFQHAHPDVLKRMARPAAASRTLDEIAAWRRDCPNITLRSTF... | Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12. | Q28TN0 |
P0AF25 | NAGD_ECO57 | Ribonucleotide monophosphatase NagD | Escherichia | MTIKNVICDIDGVLMHDNVAVPGAAEFLHGIMDKGLPLVLLTNYPSQTGQDLANRFATAGVDVPDSVFYTSAMATADFLRRQEGKKAYVVGEGALIHELYKAGFTITDVNPDFVIVGETRSYNWDMMHKAAYFVANGARFIATNPDTHGRGFYPACGALCAGIEKISGRKPFYVGKPSPWIIRAALNKMQAHSEETVIVGDNLRTDILAGFQAGLETILVLSGVSSLDDIDSMPFRPSWIYPSVAEIDVI | Catalyzes the dephosphorylation of an unusually broad range of substrate including deoxyribo- and ribonucleoside tri-, di-, and monophosphates, as well as polyphosphate and glucose-1-P (Glu1P). | P0AF25 |
Q8GBB7 | CH10_STRMT | Chaperonin-10 | Streptococcus | MLKPLGDRVVLKVEEKEQTVGGFVLAGSAQEKTKTAQVVATGQGVRTLNGDLVAPSVKAGDRVLVEAHAGLDVKDGDEKYIIVGEANILAIIEK | Together with the chaperonin GroEL, 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. GroES binds to the apical surface of ... | Q8GBB7 |
Q5IHA3 | PSBZ_CRYJA | Photosystem II reaction center protein Z | Cryptomeria | MTIAFQSSVFALIAISTLLVIGVPVALASPNGWSSNKNVLFSGVSLWIGSVFLVGILNSFIS | Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. | Q5IHA3 |
C4LCM1 | FETP_TOLAT | Probable Fe(2+)-trafficking protein | Tolumonas | MTRMVFCQRLKKEAPGMAFQLVPGELGKRIFDNICQEAWAEWQKKQTMLINEKKLNMMNAEHRALLQTEMEKYLFEDGDVQIEGYVPPSEK | Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. | C4LCM1 |
B7KFG7 | NRDR_GLOC7 | Transcriptional repressor NrdR | Gloeothece citriformis | MECPYCQNTSSRVLESRSTEAGQSIRRRRECLQCKHRFTTYERIEFVPISVLKKDKSKESFDRSKLLRGIVRACEKTEVSAQQIENVVEEIEARLQQSPRREITSQEIGQLVLQYLRELNEVAYIRFASVYGEFKGITDFVETLNQLQQEERESSSSPEWSDAGEEATVIEDSSQVMASS | Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes. | B7KFG7 |
A7IGS7 | ATPF1_XANP2 | F-type ATPase subunit b 1 | Xanthobacter | MNEMSLAELWVAVAFLLFVGILIYVGAHRAIGSALDSRGQRIAAELEEARRLKEEAQKLVAEFKRKQREAEAEAESIVTAAKAEAERLASEAKAKLEDFVTRRTKMAEDKIAQAELQAVADVKAIAADAAAKAAEVLLGSAARGDVGDRLISNAIGEVKTKLN | Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). | A7IGS7 |
B1LYI1 | RL9_METRJ | 50S ribosomal protein L9 | Methylobacterium | MEVILLERVAKLGQMGETVNVRPGFARNFLLARGKALRATEANKKHFEAQRAQLEARNLDRKKDAEVVAEKLNGQSFILIRQSGETGVLYGSVSTRDLAEVVSKEGFTVDRGQFTLNQPIKTLGLHTVPVVLHPEVEVEITVNVARSPEEAERQARGESVTEREAFNLDDLGLEVGQALADAGEGADDRG | Binds to the 23S rRNA. | B1LYI1 |
Q8WPJ2 | MANA_MYTED | Endo-beta-1,4-mannanase | Mytilus | MLLTALAVLFASTGCQARLSVSGTNLNYNGHHIFLSGANQAWVNYARDFGHNQYSKGKSTFESTLSDIQSHGGNSVRVWLHIEGESTPEFDNNGYVTGIDNTLISDMRAYLHAAQRHNILIFFTLWNGAVKQSTHYRLNGLMVDTRKLQSYIDHALKPMANALKNEKALGGWDIMNEPEGEIKPGESSSEPCFDTRHLSGSGAGWAGHLYSAQEIGRFVNWQAAAIKEVDPGAMVTVGSWNMKADTDAMGFHNLYSDHCLVKAGGKQSGTLSFYQVHTYDWQNHFGNESPFKHSFSNFRLKKPMVIGEFNQEHGAGMSSE... | Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Hydrolyzes mannohexaose (M6) preferentially to mannotriose (M4) and less preferentially to mannotetraose (M3), mannopentaose (M5), and mannobiose (M2); hydrolyzes M5 preferentially to M2, and M3, and less preferentially to mannotetraose M4; hydrolyzes M4 p... | Q8WPJ2 |
Q6BLS5 | YTM1_DEBHA | Ribosome biogenesis protein YTM1 | Debaryomyces | MADDKSQIKINFFTNEEDESLHTSDAPLYVPVSLKRYGLSEIVNHLLKKDGETDETKPVPFDFLIDGVLLRTSLEDYLVKNGLSSEASLNLEYTRAVLPPSFLASFNNDDWISSLDTINPLSASVKASNMSISQPKILSGSYDGIVRTYNMSGKVEKQYVGHSGPIRSVKWISPTRIVSSGNDRQVRLWKTSIDSNIEDDEEIEDGRTLAILEGHKAPVVSLAVEYQNNRILSAGYDKAIGFWSTNYREMTTIQPLEYDSNVISTSSKKRRKMALQDSTIRRRSPLSFLEGHSQPVEDVIFDFNDATVGYSVSQDHTIKT... | Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome. | Q6BLS5 |
B0TGQ8 | PYRDB_HELMI | Orotate reductase (NADH) | Heliomicrobium | MGSLNLQVNLGGLTMKNPVTTASGTFGFGLEFAPFIDLSRLGAIVVKGTTLEPREGNPTPRMAETPAGMLNAIGLQNPGVEAFIRDYLPPLRQIDTPVIVNVSGNSVEDYGRLASILDEADGVAALEVNISCPNVKEGGIQFGTLPASAAAVTRAVRENTQKPVIVKLSPNVTDITEMARAVVDAGADALALINTLLGMDIDICTRRPVLANIFGGLSGPAIKPVALRMIYQVYRAVHVPILGMGGIMNSQDAIAFMLAGATAIAVGTANFTNPRATMDILEGIEEYCCREGVRDVNELIGAAHSHLTG | Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor. | B0TGQ8 |
P48103 | PSBB_CYAPA | Protein CP-47 | Cyanophora | MGLPWYRVHTVVLNDPGRLIAVHLMHTALVAGWAGSMALYEIAVFDPSDPVLNPMWRQGMFVLPFMVRLGITNSWGGWTINGENVTDPGFWSFEGVAAAHIGLSGLLFLAAIWHWVYWDLELFRDPRTGEPALDLPKMFGIHLFLSGLLCFGFGAFHLTGLFGPGMWVSDAYSITGRVQPVAPAWGPEGFNPFNPGGVVSHHIAAGIVGILAGLFHLSVRPPQRLYKALRMGNIETVLSSSISAVFFAAFIVAGTMWYGSAATPVELFGPTRYQWDQEYFHQEMERRVQKDVAAGASLSEAWNRIPAKLAFYDYIGNNPA... | One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient sub... | P48103 |
B2UH25 | KDPA_RALPJ | Potassium-translocating ATPase A chain | Ralstonia | MNAFLLQLAIYLVVLLVLAKPLGAYMTGVFGDKPSRAHWLGPVERLFYRVAGVNPQAEMGWKHYALAVIVVNVLGALAVYALQRAQQWLPLNPQGFGAVTPDSSFNTAVSFVTNTNWQGYSGESTMSYLTQMLGLAVQNFLSAATGIAVVIALIRGFARHSANTIGNFWVDFTRSTVYVLLPLSIIVSVFFVSQGVIQNFDGYKEVTTVTATTYDNPKMDASGQPIKDAQGNPVTEKATTQTQTLPMGPIASQEAIKMIGTNGGGPFNANSAHPYENPNALTNFVQMLAIFIIPAALCFTFGGMVGDGRQGWAVLAAMTV... | Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel. | B2UH25 |
P51477 | ARRS_XENLA | Rod photoreceptor arrestin | Xenopus | MSGEKKSRHVMYKKTSRDKAVSVYLGKRDYVDHVDSVEPVDGVVLVDPDLLKGKKVYVTLTCAFRYGQEDIDVIGLTFRKDLYYARTQIYPPVEDPKALTKVQERLMKKLGNNAFPFVLEFPDFLPCSVSLQPAPSDVGKACGVDFEIKAFSTNNLEDRIHKKNSVRLMIRKIQYAPDQPGPKPRAETSWQFFMSDKPLHLTASLSKEVFYHGEPITVSVSVTNKSDKTVKKISASVEQVSNVVLYSSDYYIKTVALEESNEKVPSKASYNHTFSLLPLLAYNREKREIALDGKLKHEDTNLASSTLLKEGTDRTVMGIL... | Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO. May play a role in preventing light-dependent degeneration of retinal photoreceptor cells. | P51477 |
Q9M2L4 | ACA11_ARATH | Ca(2+)-ATPase isoform 11 | Arabidopsis | MSNLLKDFEVASKNPSLEARQRWRSSVGLVKNRARRFRMISNLDKLAENEKKRCQIQEKIRVVFYVQKAAFQFIDAGARPEYKLTDEVKKAGFYVEADELASMVRNHDTKSLTKIGGPEGIAQKVSVSLAEGVRSSELHIREKIYGENRYTEKPARSFLTFVWEALQDITLIILMVCAVVSIGVGVATEGFPKGMYDGTGILLSIILVVMVTAISDYKQSLQFRDLDREKKKIIIQVTRDGSRQEVSIHDLVVGDVVHLSIGDQVPADGIFISGYNLEIDESSLSGESEPSHVNKEKPFLLSGTKVQNGSAKMLVTTVGM... | This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol out of the cell or into organelles. | Q9M2L4 |
A9VI58 | GLPK_BACMK | Glycerokinase | Bacillus cereus group | MKKYILSLDQGTTSSRAILFNKEGKIVHSAQKEFTQHFPKPGWVEHNAQEIWGSILAVIATCLSEADVKPEQIAGIGITNQRETAVVWDKTTGKPIYNAIVWQSRQTVEICDELKEKGYSEMVREKTGLLIDAYFSGTKVKWILDNVEGAREKAENGELLFGTIDTWLVWKLSGGKAHITDYSNASRTLMFNIHDLQWDDELLDMLTVPKSMLPEVRQSSEIYGETIDYHFFGQNVPIAGVAGDQQAALFGQACFGEGMAKNTYGTGCFMLMNTGEKAVASEHGLLTTIAWGLDGKVNYALEGSIFVAGSAIQWLRDGLR... | Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. | A9VI58 |
Q8FS13 | ALR_COREF | Alanine racemase | Corynebacterium | MNLLTTRIDLDAIAHNTRLLKNRVGAAKLMAVVKADGYNHGMDRVAPVMAANGADAFGVATIAEALALRATGITTPILCWIWSPEQDWAAAVEAGIDLAVISPRHARVLVDAPPTSRAIRVSVKVDTALHRSGVDEQDWDAVFTLLRDCGHIEVTGLFTHLSCADEPGNPETDHQAETFRRAIDRARALGLEVPENHLCNSPATLTRPDLHMDMVRPGVALYGLEPIPGLDHGLRPAMTWAGAITVVKPIRKGEGTSYGLTWRAEADGFVAVVPAGYADGVPRAAQDHLRVHVNGHDYPQVGRVCMDQFVIFLGDNPHGV... | Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. | Q8FS13 |
A0KWL5 | SYD_SHESA | Aspartyl-tRNA synthetase | Shewanella | MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGLVQVVYDPDLPEVFNVASTLRAEFCVQVKGVVRARPDSQVNAQMKTGEIEVLGKELTIINSSEPLPLSLDNYQNNSEEQRLKYRYLDLRRPEMAQRLMFRAKVTSAVRRFLDSNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSEQVMAKTEEMMRGLFLEMLNVDLGEFPRMTYNEAMRRFGSDKPDLRNPLELVDVADLLKEVEFAVFSGPANDEEGRV... | Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). | A0KWL5 |
Q9LEK8 | PIN1_DIGLA | Rotamase Pin1 | Digitalis | MSSEKVRASHILIKHQGSRRKSSWKDPDGSLISATTRDDAVSQLQSLRQELLSDPASFSDLASRHSHCSSAKRGGDLGPFGRGQMQKPFEEATFALKVGEISDIVDTDSGVHIIKRTG | Prolyl cis/trans isomerase with specificity for phospho-Ser-Pro bonds. | Q9LEK8 |
P84973 | EF1D_POPEU | eEF-1B beta | Populus | LGSAPITEEAIATPPSAETKLVPVGYGIKK | EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP. | P84973 |
Q9RWM4 | COAD_DEIRA | Pantetheine-phosphate adenylyltransferase | Deinococcus | MNAVFPGSFDPVTSGHMDVLTRASHMFEQVTVTVMHNARKQGRHLFTLDERLEILREATAGLPNVRVDSFSGLLVDYVAQQGRSVIVRGLRAVSDYEYELQIAHLNRQIGEVETVFIMAATHWSFVSSSMVKEIASYGGKIHEMVPPASEAALRRKFAEVYDKRDDA | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. | Q9RWM4 |
A0QXJ6 | GCS22_MYCS2 | Gamma-glutamylcysteine synthetase 2-2 | Mycolicibacterium | MRECRSQEASGQLTFAKTPRTVGIEEEFHLVDLTTRRLATRAPELLPLLPDGYVAELQSCVVETNGSVVSTLPELRADLTARRRVLVDTAATLGLGVVAAGAVPLSVPSEMRVTQTSRYQQMLADYQLLAREQLICGTQIHVGIDDPDESVLVAGRVAAYVPTLLALSASSPFWSDGSDTGYSSVRTLVWQRWPTTGLAPPATSAAEYDALISDLIATGVITDAGMSYFDVRPALRTPTLELRVCDSCPRADTIVLIAALFRALVEREIEGLRAGVPAAIVVPPLGRAALWRAARSGLEGDLVDLIHPASRPAGDVVTDL... | ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. | A0QXJ6 |
O00219 | HYAS3_HUMAN | Hyaluronic acid synthase 3 | Homo | MPVQLTTALRVVGTSLFALAVLGGILAAYVTGYQFIHTEKHYLSFGLYGAILGLHLLIQSLFAFLEHRRMRRAGQALKLPSPRRGSVALCIAAYQEDPDYLRKCLRSAQRISFPDLKVVMVVDGNRQEDAYMLDIFHEVLGGTEQAGFFVWRSNFHEAGEGETEASLQEGMDRVRDVVRASTFSCIMQKWGGKREVMYTAFKALGDSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYHQKFLGSKCSFGDDRHL... | Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of ... | O00219 |
Q8NQW7 | THIC_CORGL | Thiamine biosynthesis protein ThiC | Corynebacterium | MTPTQNEIHPKHSYSPIRKDGLEVPETEIRLDDSPSGPNEPFRIYRTRGPETNPKQGLPRLRESWITARGDVATYQGRERLLIDDGRSAMRRGQASAEWKGQKPAPLKALPGKRVTQMAYARAGVITREMEFVALREHVDAEFVRSEVARGRAIIPNNVNHPESEPMIIGRKFLTKINANIGNSAVTSSIEEEVSKLQWATRWGADTVMDLSTGDDIHTTREWIIRNSPVPIGTVPIYQALEKVNGVAADLNWEVFRDTIIEQCEQGVDYMTIHAGVLLAYIPLTTRRVTGIVSRGGSIMAGWCLAHHRESFLYEHFDEL... | Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. | Q8NQW7 |
P01442 | 3SA2_NAJAT | Cardiotoxin analog II | Naja | MKTLLLTLVVVTIVCLDLGYTLKCNKLVPLFYKTCPAGKNLCYKMFMVSNLTVPVKRGCIDVCPKNSALVKYVCCNTDRCN | Basic protein that binds to cell membrane and depolarizes cardiomyocytes. It also shows lytic activities, but 2-fold less important than that of CTX-A4. It binds to the integrin alpha-V/beta-3 (ITGAV/ITGB3) with a moderate affinity. It may interact with sulfatides in the cell membrane which induces pore formation and c... | P01442 |
Q8U544 | URED_AGRFC | Urease accessory protein UreD | Agrobacterium tumefaciens complex | MQSEQQAIGASGCEDAQQPVRQQRARGRGRIVTKAVEGRSRLDELFQEGCAKIRLPDTFSNEAEAILINSSGGLTGGDDIEWQATAGAGTSLVVTTQACEKVYKASSGTATVTARISAGPGAKLHWLPQETILFDRASLNRRLEADLDQSSEFIAVEAVLLGRQAMGEAMTHGLFRDRWRIRHGGRLVHAEELLLEGEVAELTAKPAVLAGQVAFATLLYIGPLSEALLPKIRAIAGESGGASEWQGKLVVRVSAADGFSLRKLLFPIISLLRNGAPVPKVWNL | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | Q8U544 |
Q9KCL9 | RHAA_HALH5 | L-rhamnose isomerase | Halalkalibacterium (ex Joshi et al. 2022) | MSMKSQFERAKIEYGQWGIDVEEALERLKQVPISIHCWQGDDVGGFELSKGELSGGIDVTGDYPGKATTPEELRMDLEKALSLIPGKHRVNLHAIYAETDGKVVERDQLEPRHFEKWVRWAKRHGLGLDFNPTLFSHEKAKDGLTLAHPDQAIRQFWIDHCIASRKIGEYFGKELETPCLTNIWIPDGYKDTPSDRLTPRKRLKESLDQIFAAEINEAYNLDAVESKLFGIGSESYVVGSHEFYLSYALKNDKLCLLDTGHYHPTETVSNKISAMLLFHDKLALHVSRPVRWDSDHVVTFDDELREIALEIVRNDALDRV... | Catalyzes the interconversion of L-rhamnose and L-rhamnulose. | Q9KCL9 |
P06512 | PSAB_SPIOL | PsaB | Spinacia | MALRFPRFSQGLAQDPTTRRIWFGIATAHDFESHDDITEERLYQNIFASHFGQLAIIFLWTSGNLFHVAWQGNFESWVQDPLHVRPIAHAIWDPHFGQPAVEAFTRGGALGPVNIAYSGVYQWWYTIGLRTNEDLYTGALFLLFLSVISLLGGWLHLQPKWKPSVSWFKNAESRLNHHLSGLFGVSSLAWTGHLVHVAIPGSRGEYVRWNNFLDVLPHPQGLGPLFTGQWNLYAQNPDSSSHLFGTSQGAGTAILTLLGGFHPQTQSLWLTDMAHHHLAIAFVFLVAGHMYRTNFGIGHSMKDLLEAHIPPGGRLGRGHK... | PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically... | P06512 |
C3P6Y7 | DAPEL_BACAA | N-acetyldiaminopimelate deacetylase | Bacillus cereus group | MAVSKFVQIRRDLHKIPEIGFKEWKTQQYILDYIGTLSNEHVEVKVWRTGVIVKVKGKNPEKVIGYRADIDGLPITEETGYEFASVHEGMMHACGHDLHTTIGLGLLTAAVTERIDDDLVFLFQPAEEGPGGALPMLESEELKEWKPNIILGLHIAPEYPVGTIATKEGLLFANTSELYVDLKGKGGHAAYPHTANDMIVAASHLVTQLQSVISRNVNPLDSAVITIGKITGGTVQNIIAEKSRLEGTIRTLSVESMSRVKSRIEAIVAGIEASFQCEAVIDYGAMYHQVYNHEALTREFMQFVSEQTDMKVITCTEAMT... | Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate. | C3P6Y7 |
Q59818 | ILVC_STRAW | Ketol-acid reductoisomerase type I | Streptomyces | MAELFYDADADLSIIQGRKVAVIGYGSQGHAHALSLRDSGVDVRVGLHEGSKSKAKAEEQGLRVVTPSEAAAEADVIMILVPDPIQAQVYEESIKDNLKDGDALFFGHGLNIRFGFIKPPAGVDVCMVAPKGPGHLVRRQYEEGRGVPCIAAVEQDATGNGFALALSYAKGIGGTRAGVIKTTFTEETETDLFGEQAVLCGGTAALVKAGFETLTEAGYQPEIAYFECLHELKLIVDLMYEGGLEKMRWSISETAEWGDYVTGPRIITDATKAEMKKVLAEIQDGTFAQAWMDEYHGGLKKYNEYKTQDENHLLETTGKE... | Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobu... | Q59818 |
P18812 | MALF_KLEAE | Maltose/maltodextrin transport system permease protein MalF | Klebsiella | MDAVKKKHWWQSPQLTWSVIGLLCLLVGYLVVLMYAQGEYLFAIMTLILSSVGLYIFSNRKAYAWRYVYPGLAGMGLFVLFPLICTIAIAFTNYSSTNQLTFERAQQVLMDRSFQAGKAYNFSLYPAGDEWQLALTDGESGKNYLSEAFKFGGEQKLALKEADALPQGERANLRVITQNRAALNQLTAVLPDESKVIMSSLRQFSGTQPLYALANDGTLTNNQSGVKYRPNADIGFYQSINADGSWGNEKLSPGYTVTIGWDNFTRVFQDEGIQKPFFAIFVWTVVFSVLTVILTVAVGMVLACLVQWEALKGKAIYRVL... | Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane. | P18812 |
A8MLG7 | RS11_ALKOO | 30S ribosomal protein S11 | Alkaliphilus | MAKVAKKRTTRTRRRERKNIERGQAHIQSTFNNSIITLTDMQGNALSQASAGQLGFKGSRKSTPYAAQMAAETAAKAAMEHGLKTVEVYVKGPGAGREAAIRSLQAAGLEVNLIKDVTPIPHNGCRPPKRRRV | Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome. | A8MLG7 |
Q28Q60 | ISPDF_JANSC | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | unclassified Jannaschia | MEKPAQRATAIIVAAGRGIRAGGGEPKQWRRIAGRSIVEWSVNRFAAHHAGFDVVLVIHPDDEWRLNGLDLPTTLRVVHGGDSRAASVKAGLAVCCDAGHVLIHDVARPCVSLAVIQSVLDATRAGGAAAPALPVTDALWRGDTHVSGTQNRDGLWRAQTPQGFDVSAIRAAHAAHDGTAADDVEVARLAGIDVAIVPGDEANLKITGPEDFARAEALLTGGDMDIRVGNGFDVHRFGPGDQVWLCGISVPHTRGLQGHSDADVGLHTLTDAIYGALAEGDIGTHFPPSDPQWKDAESHIFLTHAVELAANRGFSITNAD... | Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a ... | Q28Q60 |
Q9DGK7 | NPY_CYPCA | C-flanking peptide of NPY | Cyprinus | MHPNMKMWIGWAACAFLLFACLGTLTEGYPTKPDNPGEDAPAEELAKYYSALRHYINLITRQRYGKRSSADTLISDLLIGETESHPQTRYEDHLVW | NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. | Q9DGK7 |
Q5NYP9 | MUTS_AROAE | DNA mismatch repair protein MutS | Aromatoleum | MGMSEIAKAAQKDKAIGGADRDSHTPMMQQYLRIKAQHPDTLLFYRMGDFYELFFDDAEKAARLLDITLTTRGQSAGTPIRMAGVPFHAVEQYLARLVKLGESVVIAEQVGEPGATKGPMERAVSRIVTPGTLTDAALLDDRIDSLLLAATLHRGVLGLAWLNLANGDLRVMECPAEQLQAQFERLRPAEVLVPDGLALPLVESLSPVLRRLADWQFDAGNGERLLTAHFGTRDLAGFDAEGLPVALAAAAALFEYARSTQRQSLEHVTGLRVEREAEYLRLDAATRRNLELTETLRGEASPTLFSLLDSCITSMGSRWL... | This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | Q5NYP9 |
A1A3P4 | GRPE_BIFAA | HSP-70 cofactor | Bifidobacterium | MSDFNKDEYLNDLPDMDDLSGQAAPAAASADSAAAAAGATQEGAAQPAAAQSQENGDSAAADGADKAGAADGKADDTLTPLGQAKKEAAEYLEALQRERAEFINFRNRAQKEQERFRQHGIIDVLTALLPALDDIDRIREHSEMDDSFKAVANKIDKAFEKFGVEKFGEKGEDFDPTKHDAILHKPDPNAEKETVDTVVEAGYRIGDRVIRAARVVVASPQN | Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-b... | A1A3P4 |
Q5F8M6 | MUTL_NEIG1 | DNA mismatch repair protein MutL | Neisseria | MPRIAALPDHLVNQIAAGEVVERPANALKEIVENSIDAGATAVDVELEGGGIRLIRVGDNGGGIHPDDIELALHRHATSKIKTLNDLEHVASMGFRGEGLASIASVSRLTLTSRQEDSSHATQVKAEDGKLSSPTAAAHPVGTTIEAAELFFNTPARRKFLKSENTEYAHCATMLERLALAHPHIAFSLKRDGKQVFKLPAQSLHERIAAIVGDDFQTASLEIDSGNSALRLYGAIAKPTFAKGKTDKQYCFVNHRFVRDKVMLHAVKQAYRDVLHNALTPAFVLFLELPPEAVDVNVHPTKTEIRFRDSRQVHQLVFHT... | This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part ... | Q5F8M6 |
Q92BB4 | EZRA_LISIN | Septation ring formation regulator EzrA | Listeria | MYYMLIGFIIVVIAVISAGYILKRKHYQRINELEETKIKLRERPVIDELSKVKKLKLTGQTEALFESWRSSWDEIETRLFPDLEEVLLEAEMNADRYRFRSATNTENDIEQMLVVIEKQMDQILGGLKELLISEEKNAKESRMTKEKFAELRREVLTRGFKLGETLPYVEAKLNSLAENLNRYDSLTDQADHLEAREIVISVQKEMAVIEAQMERIPSLLHETDTILPEEMNKLRAGYEEMVRKGYYLAQMELDKEISRMKTQIEKMKQNVINLDLDEAEEGIEELHNEIELFYDTLEHEAEARHFVKENHSPTSDKLKR... | Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization. | Q92BB4 |
Q7NYC6 | SYT_CHRVO | Threonyl-tRNA synthetase | Chromobacterium | MPDIRLPDGSVRSFDKPVTVHEVAASIGAGLARAALAGRVDGQLVDTSYLIDRNADLAIVTDKDADGLSVIRHSTAHLLAYAVKELFPEAQVTIGPEIENGFYYDFAYKRPFTPEDLAAIEKKMAELAKKDIPVERYELPRDEAIAYFKSIGEAYKAEIIESIPQGEVLSLYREGEFTDLCRGPHVPSTGKLKVFKLMKVAGAYWRGDSKNEMLQRVYGTAWAKKEDLDAYLYMLEEAEKRDHRKLGVQLDLFHLQDEAPGMVFWHPKGWQLWQNVEQYMRAKLNHEGYKEVRTPMMMDANLWERSGHAANYRENMFITE... | 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). | Q7NYC6 |
O28970 | TF2B_ARCFU | Transcription initiation factor IIB | Archaeoglobus | MAEVEKVREKEVEKEVERKEIEREEDVEVCPECGSPRLIRDYRRGEFICQDCGLVIEDTYIDAGPEWRAFDSEQRDKRSRVGAPVTYTIHDKGLSTIIDWSNKDYYGKAISVRNRAQLFRLRKWQRRIRISNATERNLAFALSELDRMASALGLPKSVRETAAVIYRKAVEKNLIRGRSIEGVVAAALYAACRQAGVPRTLDEIATYSRVDRKEIGRTYRFITRELGLKLMPTSPADYIPRFCAALGLSGEVQKKAIEIIKKAEERELTSGRGPTGVAAAALYVASILLGERRTQREVAEVAGVTEVTIRNRYKELAEKL... | Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB). | O28970 |
A0A1U8QHS4 | SDGC_EMENI | Aspernidgulenes biosynthesis cluster protein C | null | MDKRSFKVIVVGGSIAGLTLAHSLDLAGIDYIVLEKHSDPLATVGGSVGLLPNGWRILHQLGLRHQLEQEACPVKVAHMTYPDGFVFSDNFPAAIQERQVPEIQFPIGYMPANDERFGYSLSVLTRQQLIEVLYLGLRDKSKIKVGQRVIKIQHHQNRRGVSVFTESGQEHVGDLVAGADGVHSITRSQMWLQLGQKLDAEKERRQLVAEYSCVFGISSPLKGIPPGEQLIACHDNATVLAFPGKDAHIGWGLIQKLNRPCNSPATTQSSDGETALIMAKSAAGLGLCKDLKFHDLWVNTPKYSFTILEEGLFQIWHHGR... | FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the polyenes aspernidgulenes . The carbon backbone of aspernidgulenes is synthesized by the HR-PKS sdgA, which accepts acetyl-CoA as the starter unit and performs malonyl-CoA extensions as well as regioselective methylation and redu... | A0A1U8QHS4 |
Q28705 | KCNE1_RABIT | Minimal potassium channel | Oryctolagus | MIPPNATAVMPFLTTLGEETAHLQGSSATSLARRGPLGDDGQMEALYILMVLGFFGFFTLGIMLSYIRSQKLEHSHDPFNVYIEANDWQEKDRAYFQARVLESCRGCYVLENQLAVEHPDTHLPELKPSL | Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium ch... | Q28705 |
A7Z0P8 | RL14_BACVZ | 50S ribosomal protein L14 | Bacillus amyloliquefaciens group | MIQQETRLKVADNSGAREVLTIKVLGGSGRKTANIGDVIVCTVKQATPGGVVKKGEVVRAVIVRTKSGARRTDGSYISFDENACVIIRDDKSPRGTRIFGPVARELRENNFMKIVSLAPEVI | Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. | A7Z0P8 |
B6QHL9 | RCF1A_TALMQ | Respiratory supercomplex factor 1-A, mitochondrial | Talaromyces sect. Talaromyces | MCSDFEEETSIQKFKRRLKEEPLIPLGCAATCYALYRAYRSGKAKDSVEMNRMFRARIYAQFFTLLAVVAGGMYYKTERKQRREFEKKVEERKAQEKRDAWLRELEARDKEDKGWKERHAAVSVTAKKETEGAVDKNVNQAPTEEVVEKRGTGILDAVKALVQGKKD | Cytochrome c oxidase subunit which plays a role in assembly of respiratory supercomplexes. | B6QHL9 |
P27584 | GPA1_SCHPO | GP1-alpha | Schizosaccharomyces | MGCMSSKYADTSGGEVIQKKLSDTQTSNSSTTGSQNARVPVLENWLNIVLRGKPQNVESSGVRVKGNSTSGGNDIKVLLLGAGDSGKTTIMKQMRLLYSPGFSQVVRKQYRVMIFENIISSLCLLLEAMDNSNVSLLPENEKYRAVILRKHTSQPNEPFSPEIYEAVHALTLDTKLRTVQSCGTNLSLLDNFYYYQDHIDRIFDPQYIPSDQDILHCRIKTTGISEETFLLNRHHYRFFDVGGQRSERRKWIHCFENVTALLFLVSLAGYDQCLVEDNSGNQMQEALLLWDSICNSSWFSESAMILFLNKLDLFKRKVHI... | Implicated in the mating and sporulation pathway. Probably coupled to mating-factor receptors. May act in concert with Ras1. | P27584 |
O80722 | PME4_ARATH | VANGUARD1-like protein 1 | Arabidopsis | MIGKVVVSVASILLIVGVAIGVVAFINKNGDANLSPQMKAVQGICQSTSDKASCVKTLEPVKSEDPNKLIKAFMLATKDELTKSSNFTGQTEVNMGSSISPNNKAVLDYCKRVFMYALEDLATIIEEMGEDLSQIGSKIDQLKQWLIGVYNYQTDCLDDIEEDDLRKAIGEGIANSKILTTNAIDIFHTVVSAMAKINNKVDDLKNMTGGIPTPGAPPVVDESPVADPDGPARRLLEDIDETGIPTWVSGADRKLMAKAGRGRRGGRGGGARVRTNFVVAKDGSGQFKTVQQAVDACPENNRGRCIIYIKAGLYREQVII... | Acts in the modification of cell walls via demethylesterification of cell wall pectin. Plays an important role in growth of pollen tubes in female floral tissues, possibly via enhancing the interaction between the pollen tube and female floral tissues by modification of the cell walls. | O80722 |
B8IYK7 | RL18_DESDA | 50S ribosomal protein L18 | Desulfovibrio | MKYSKNESRQRRKIRISKKVSGTAERPRLVVYRSNLHVYAQIVNDLDGATLVATSTLALGKNESGLHCNKGGAEKVGIEIARMAKEKNIDKVVFDRNGYLYHGRVKAVADGAREGGLEF | This is one 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. | B8IYK7 |
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