habdine/Prot2Text-Data · Datasets at Hugging Face

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
A5CSL4	MIAA_CLAM3	Isopentenyl-diphosphate:tRNA isopentenyltransferase	Clavibacter	MIPIVAVVGATGTGKSGLSLDIADRLRAQGRVAEIVNADAMQLYRGMDIGTAKLPEAARRDVPHHMLDVLDVTAEATVAGYQGEARRVITGILGRGAVPILVGGSGLYVSSVLFDYEFPGTDPEIRQRLERELAETGPGMLHRRLRELDPAAAQRIGAHNGRRLVRALEVVEITGPQPERASAEPRPWHPARILALTLPREELVPRLDARVSGMWADGLVDEVAGLLPAGLADGVTASRAIGYAQAARQLAGELTEEEAMEETRALTRRYARRQVSWFGRYADAVRLDARDERLLEHALDALPAARP	Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).	A5CSL4
P29685	ATPBM_HEVBR	ATP synthase subunit beta, mitochondrial	Hevea	MASRRLLSSLLRSSSRRSVSKSPISNINPKLSSSSPSSKSRASPYGYLLTRAAEYATSAAAAAPPQPPPAKPEGGKGGGKITDEFTGKGAIGQVCQVIGAVVDVRFDEGLPPILTSLEVLDHSIRLVLEVAQHMGEGMVRTIAMDGTEGLVRGQRVLNTGSPITVPVGRANPWTYHEVIGEPIDERGDIKTSHFLPIHREAPAFVDQATEQQILVTGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKLGDKQADSKCALVYGQMNEPPGARARVGLTGLTVAEHFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLATDLGGLQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQRFLSQPFHVAEVFTGAPGKYVELKESITSFQGVLDGKYDDLPEQSFYMVGGIDEVIAKADKIAKESAS	Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.	P29685
P75053	DEOD_MYCPN	Purine nucleoside phosphorylase DeoD-type	Mycoplasma	MTPHINAKKDDIAKVVLMPGDPLRAKWIAEQFMEKPRLVNEVRGMLAFTGQYKGKTITIMGHGMGIPSIGIYSYELMKFYEVNTIIRIGSCGALQGSLNLQDLIIAAKAWSESIYANDMGVEVPADKILMASPQLVELAKKTANQLQLAFHEGLVFCEDAFHQIRKDVLKLAQEKHALAVEMEAHALYANAMLLNKQALTMLTVSDSLVTHAALPAEQRQATFKNMAILSLEMASQLV	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.	P75053
Q88RX5	MNME_LACPL	tRNA modification GTPase MnmE	Lactiplantibacillus	MPTTTEFDTIAAISTPPGEGGISIIRISGDQTFNVVTQIFKGKDLSRVQSHTINYGHIVDPDTHQEVDEVMATVMRAPKTYTREDVVEINCHGGLVATNEILQLILSHGARMAEPGEFTKRAFLNGRLDLSQAEAVMDLIRAKTDKSMKVALNQLDGDLSKLIRHLRQDILDVLAQVEVNIDYPEYDAVETMTTKMLKEKATEVAQSINQLLATAKQGKVLREGLATAIIGRPNVGKSSLLNHLLHEDKAIVTDVAGTTRDVIEEYVNVRGVPLKLVDTAGIRDTEDKVEKIGVERSRKAIGAADLVLLVLDNSQPLTAEDRELLQETDQSKRIVILNKTDLPARLDQAELAQLVDLSDVLSMSVLEQSGVTQLEQRIAKMFFNEGIESSQNNVMVTNARHIGLLNQAKQALQDVQTGLAAGMPVDLVQIDMTRCWEFLGQITGDSYEDELLDQLFSQFCLGK	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.	Q88RX5
Q5FW14	CHMP7_XENTR	Chromatin-modifying protein 7	Silurana	MAALSCYPPEWDDDERMSFLFSAFKQTRDVNTSDWDGKMKFWIPLILKHARAQGLLSISLSQLERDFRRKGFAPLGLRIVIQEMMRQGTLRKESDYVSNVSSGWLSWGMRQLVIRPLRWTIGTVLGSQMGPDEPLVIPEIIKERAALVLQRYQSSPLRALPLLSEEEVRTLCAEICPNPSALNLVLLQLQGDKKICVLERAGKKLVKFVRVSVGQVDPISESDLGIYELQQSEKLLSERLQSAGEESDRLTEEARTYNRAGNKHQALRCLRKRKLLERRITELQNKQDTVQGILERIAAAETDRKVVSAYQMGVSALKLALKDVTMEKAESIVDQIQEYCDLQDDLSQTLASVSDADIDSEDLEKELNDILQNKEMIVDLPDVPSGPVVISPQRPTEWETDQDIDSEDLEKELNDILQKEEMIVDLPDVPSGPVVISPQRPTEWKTDQASRSPADGSFSRSVPEPVLQ	ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope during late anaphase. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway.	Q5FW14
Q7NF26	PSAD_GLOVI	Photosystem I reaction center subunit II	Gloeobacter	MADVKELPFGGSTPLFGGSTGGLLRKAQIEEKYLIVWNSKEEQVFEMPTGGAATMVAGTNVLYLARKEQCHALHRQLVSTFKIRDSKIYRVYPNGEQVLIFPMDGVPSEKSNPGREVVGYVPRKIGDNPNPVDVKFTGKETFDV	PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center.	Q7NF26
Q4QN00	IF1_HAEI8	Translation initiation factor IF-1	Haemophilus	MAKEDCIEMQGTILETLPNTMFRVELENGHVVTAHISGKMRKNYIRILTGDKVTVEMTPYDLSKGRIIFRSR	One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.	Q4QN00
C4LBX3	PYRI_TOLAT	Aspartate carbamoyltransferase regulatory chain	Tolumonas	MSEKKQLQVEAICNGSVIDHIPAGQGIKILKLFHLLDTRQRITVGLNLPSAALGSKDLIKVENTQLTADQANQLALFAPQATVNIIEDFKVVTKHQLELPGEIVGVFACPNSNCISHREPVRSRFGVRSTQGEVRLKCHYCEKSFTKEIVSEAF	Involved in allosteric regulation of aspartate carbamoyltransferase.	C4LBX3
P67595	SYW_STRPN	Tryptophanyl-tRNA synthetase	Streptococcus	MTKPIILTGDRPTGKLHIGHYVGSLKNRVLLQEEDKYDMFVFLADQQALTDHAKDPQTIVESIGNVALDYLAVGLDPNKSTIFIQSQIPELAELSMYYMNLVSLARLERNPTVKTEISQKGFGESIPTGFLVYPIAQAADITAFKANYVPVGTDQKPMIEQTREIVRSFNNAYNCDVLVEPEGIYPENERAGRLPGLDGNAKMSKSLNNGIYLADDADTLRKKVMSMYTDPDHIRVEDPGKIEGNMVFHYLDVFGRPEDAQEIADMKERYQRGGLGDVKTKRYLLEILERELGPIRERRIEFAKDMGEVYNMIQKGSERAREVAGQTLSEVKGAMGLHYFN	Catalyzes the attachment of tryptophan to tRNA(Trp).	P67595
P07997	HEM1_CHICK	Delta-aminolevulinate synthase 1	Gallus	MEAVVRRCPFLARVSQAFLQKAGPSLLFYAQHCPKMMEAAPPAAARGLATSASRGQQVEETPAAQPEAKKAKEVAQQNTDGSQPPAGHPPAAAVQSSATKCPFLAAQMNHKSSNVFCKASLELQEDVKEMQVDRKGKEFAKIPTNSVVRNTEAEGEEQSGLLKKFKDIMLKQRPESVSHLLQDNLPKSVSTFQYDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDYSDSLITKKEVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAKMLPGCEIYSDSGNHASMIQGIRNSRVPKHIFRHNDVNHLRELLKKSDPSTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDIISGTLGKAFACVGGYISSTSALIDTVRSYAAGFIFTTSLPPMLLAGALESVRTLKSAEGQVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPIRVADAAKNTEICDKLMSQHSIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSYFLEKLLATWKDVGLELKPHSSAECNFCRRPLHFEVMSERERSYFSGMSKLLSVSA	Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products.	P07997
A0A411PQN2	AGN11_PAEDI	Agnestins biosynthesis cluster protein L11	Paecilomyces	MKRSFDASHGQLEKQSRPRQVPTSCHFCRTKKLKCDRRFPCSNCRARRLSCVPFSDRSQAASLDLPGAGPSSTVSNEELSENINELKARLQRLEELISVNAEEKLDSKGPTSFVTSKGGYGEDVEASKSMNSLEMDAFEHQPLHSNSEERIAQLFASSFVSIIAPAIRLVIDQPTLSLLPSRKQAERLFDYFADQVVVFYYFIHVPTVRSMLDTVYTHLENKRQPQHDHLALLSTVFALSAYFGSSSSRFPFNGAEAKMLCYRWISVAQQALCAANYIVQPTVETLQSVILIAAYLVPNLGSMSIFRVLMASALQGALQLSLHQIDSPANQRRRQNATVNWVDIESKRRIWWHLASTDWIVSFMSGPRCGTYMIHPKQMTVDLPTNVDDQDIRPAGNYAQPLENAPTDMTFSILRTRISVIFREIVDAATDSGCLQEELPYDVVLAFDHRLHGIMADAPACFRTDPRSSRAPSRSPDLRLHRLIANALNRLHRPYLARGARDPKYSYSRMVCLRTARSVIELCKEMTGANEEFQHVKMWTIVHPLFNSVLVLVMDYCLNREEPRGDERKAEILEGFRLLEACQEDSALAQRGLQQMRQLLKGSASARKDKNPIHGDTDRATPPGSSNLPQHDKSSSSSPAPPVWPCLWTDPDLAPLETMDFDVDLDESQFEVLFRDFEGRHPMY	Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of agnestins, dihydroxy-xanthone metabolites.	A0A411PQN2
A7I008	RS18_CAMHC	30S ribosomal protein S18	Campylobacter	MADKRKYTRKYCKFTEAKIEFIDYKDTALLKYCLSERFKIMPRRLTGTSKKYQEMVEKAIKRARQAALIPYIVDRDNVVVNPFEILG	Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.	A7I008
Q81VQ1	ECFA2_BACAN	Energy-coupling factor transporter ATP-binding protein EcfA2	Bacillus cereus group	MEITFQKVEHRYQYKTPFERRALYDVDVSFPSGGYYAIIGHTGSGKSTMIQHLNGLLQPTNGTVQIGEHFISAGKKEKKLKPLRKKVGVVFQFPEHQLFEETVEKDICFGPTNFGVSEEAAKQKAREAIELVGLEPELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGQNELMEMFYKLHKEKGLTVILVTHNMEDAAKYAEQIVVMHKGTVFLQGSAEEVFSHADELEKIGVDLPMSLKYKRAIEEKFGISIPKATLSLEDLTHEVVQVLRKGGHESCSS	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.	Q81VQ1
P0DJ01	P35_MALPE	Lipoprotein p35	Malacoplasma	MKIKKIKLLKALALTGAFGIVATVPVIVSSCSSTSENNGNGNGNGGTDGNTQQTEVTPAIKSEVSLTGALSKIYDTKTGTDRETTSQLIVKDIKANPENYFTNGEALKDVIASATVTVDGGFTESTFTGEAYSVWSAKADVKKGTYSQASKQLDIKSINDLQTVLGDSAAIKGICDLIPNLKLNNGTDYKVTNNGLSLSEDLLHINVTAKDGQTDVSMDLAIPVSDLNLKIDGLKISVSGTGIKTSELTTNYKFNIGIDNTVKTLTPAAVTLAEADRTNAEKVLEKLGYATVSGSTYTLDQDKLADALGLYNCKFEAVKSEKDSTNNNKYTVTLKATPNDGYFWEDGTNGAKEEISFVATFS	Major M.penetrans antigen.	P0DJ01
Q0W131	DHQS_METAR	3-dehydroquinate synthase II	Methanocella	MSDKLVWIDAQGSWNGAKEKVTGALESGANAVLVSPENVERVRELGKMTVAAAEGNPDIRVIGIGSEGDGTLFLPHDLNSSEDMATAKALKAQGTTTAAYVRLAGKEYEQFAARMGKLCDYLIIEGDDWKVIPLENLIAELGGSGTKILAKARDIDEASVALQTLEKGADGVLVDVDDPLKVREIARAVSTKQAGLGLTPVTITAVRDAGTGDRVCIDTCSLMTPGEGMLIGNQSSGLFLVQSEAEESPYVASRPFRVNAGAVHEYVLVGEKTRYLSELASGDPALIVTRDGDARKATIGRVKIERRPLLYVEAETGDRKISAILQNAETIKLVAADGSSTPVTALKPGDRVLAKLEKEARHFGMKIEETIVEK	Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.	Q0W131
O29165	ACDA1_ARCFU	ACDS complex carbon monoxide dehydrogenase subunit alpha 1	Archaeoglobus	MFELKKGALFVDEMKNVSIRIGKVVEEEEEVWEEAGPTPKPGILELRKWDHKLLERYEPFYAPMQDFCNLCTMGPCDLSMNKRGACGIDLKTAKARLVTIACCIGASAHTAHARHLVDHLIEEFGEDFPIDLGGDVNVEAPIIRTVVGIKPKTLGDLREALNWAEKEIVKVLHSTHIGNEESLLDYESKAMHVSMADHVGMEVADIAQIVAYNFPKAEPDTPLVDTGFGIVDKSKPTIVVVGHNVMYARPVADYLEEMGRIDDFELAGLCCTAHDMTRYNAKAKIFGPISYQLRVIRAGIPDVMISDEQCIRADLLEACKKMGIPLIATSDAAARGLPDVSDWPVEKIVDALVSGKLPGVFLPIPEKVGQVAPLVAEAIFKKHGGERKYKFFESDEALMEEINKCTQCMNCVFTCPHSLRVDQGMAHAQKTGDLSKLAQLEEQCLACMKCEQACPKNIKIINVIMRANYDRLYNKTGKTRVGRGPIQDTEIRKVGQPIVFGQIPGVIAAVGCINFPDEMKSIREILEEFLKRRYIVVTSGCHAMDIGMIKDEEGKTLYEKYPGNFDAGGLVNTGSCVANSHIAGAAIKIANIFAMRPLRGNYAEIADYVLNRVGAVGFSWGPYSHKAASIATGFNRLGVPVVVGPHGTKYRRAYIGKPWKKDKWWVYDIKSRQKVFIEPAPDSLLVAVETKEEAIVQLARLCIRPNDTNQGRQIKLTHYIELHQKYYGDLPDDWAVYVRSEADLPLKMRDQLLKVLEEQYGWKIDWDKKKIVEGPVRHFDAGFNPTIVEEVYEKYAGEKAPR	Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.	O29165
Q24JL3	STR2_ARATH	Sulfurtransferase 2	Arabidopsis	MKRAFSSQLRSAYPASKSTHFGRVMASSGSEAKANYAPISTNEPVVSVDWLHSNLGDADIKVLDASWYMAHEQRNPIQEYQVAHIPGALFFDLNGIADRKTNLRHMLPSEEAFAAGCSALGIENNDGVVVYDGMGLFSAARVWWMFRVFGHDKVWVLDGGLPKWRASGYDVESSVSNDAILKASAATEAIEKIYQGQTISPITFQTKFRPHLVLALDQVKENIEDKTYQHIDARSKARFDGIAPEPWKGLPSGHIPGSKCVPFPLMFDSSQTLLPAEELKKQFEQEDISLDSPIAASCGTGVTACILALGLYRLGKTNVAIYDGSWTEWATAPNLPIVGSSS	Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is 3-mercaptopyruvate > thiosulfate. Involved in embryo and seed development.	Q24JL3
A5CDC6	ATPL_ORITB	Lipid-binding protein	Orientia	MDPISFKYIAIAFMAFGMAGAALGVASIFNALMNSIARNPSAIEDLQKAALIGAGLAEAMGLFSFILAILLMFT	Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.	A5CDC6
P0C5X8	TTYH1_RAT	Protein tweety homolog 1	Rattus	MGAPPGYRPSAWVHLLHQLPRADFQLRPVPSGFAPRDQEYQQALLLVAALAGLGLGLSLIFIAVYLIRFCCCRPPEPPGAKSPPPGGGCVTWSCIAALLVGCAGIGIGFYGNSETSDGVSQLSSALQHANHTLSTIDDLVLETVERLGEAVRTELTTLEEVLSERVELVAATRGARRQAEAAAQHLQGLAFWQGVSLSPVQVAEDVTFVEEYRWLAYVLLLLLVLLVCLFTLLGLAKQSKWLVVVMTAMSLLVLVLSWGSMGLEAATAVGLSDFCSNPDTYVLNLTQEETGISSDILNYYFLCNQAVSNPFQQRLTLSQRALASIHSQLQGLEREASPQFPAAQKPLLSLEETLNVTERSFHQLVALLHCRSLHKDYGSALRGLCEDALEGLLFLMLFSLLSAGALATTLCSLPRAWALFPPSDDYDDTDDDDPFNPQESKRFVQWQSSI	Probable chloride channel. May be involved in cell adhesion.	P0C5X8
O35310	HS3S1_MOUSE	Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1	Mus	MTLLLLGAVLLVAQPQLVHSHPAAPGPGLKQQELLRKVIILPEDTGEGTASNGSTQQLPQTIIIGVRKGGTRALLEMLSLHPDVAAAENEVHFFDWEEHYSQGLGWYLTQMPFSSPHQLTVEKTPAYFTSPKVPERIHSMNPTIRLLLILRDPSERVLSDYTQVLYNHLQKHKPYPPIEDLLMRDGRLNLDYKALNRSLYHAHMLNWLRFFPLGHIHIVDGDRLIRDPFPEIQKVERFLKLSPQINASNFYFNKTKGFYCLRDSGKDRCLHESKGRAHPQVDPKLLDKLHEYFHEPNKKFFKLVGRTFDWH	Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan . Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact) . This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site .	O35310
Q03721	KCNC4_HUMAN	Voltage-gated potassium channel subunit Kv3.4	Homo	MISSVCVSSYRGRKSGNKPPSKTCLKEEMAKGEASEKIIINVGGTRHETYRSTLRTLPGTRLAWLADPDGGGRPETDGGGVGSSGSSGGGGCEFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELTFWGIDETDVEPCCWMTYRQHRDAEEALDIFESPDGGGSGAGPSDEAGDDERELALQRLGPHEGGAGHGAGSGGCRGWQPRMWALFEDPYSSRAARVVAFASLFFILVSITTFCLETHEAFNIDRNVTEILRVGNITSVHFRREVETEPILTYIEGVCVLWFTLEFLVRIVCCPDTLDFVKNLLNIIDFVAILPFYLEVGLSGLSSKAARDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGARPSDPRGNDHTDFKNIPIGFWWAVVTMTTLGYGDMYPKTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKRKKHVPRPAQLESPMYCKSEETSPRDSTCSDTSPPAREEGMIERKRADSKQNGDANAVLSDEEGAGLTQPLASSPTPEERRALRRSTTRDRNKKAAACFLLSTGDYACADGSVRKGTFVLRDLPLQHSPEAACPPTAGTLFLPH	This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.	Q03721
Q9KC68	RACA_HALH5	Chromosome-anchoring protein RacA	Halalkalibacterium (ex Joshi et al. 2022)	MAVQWKTKEVSEQLGVNPTTVQRWVKFFGIQCETNEHGHLLFEKEHLTVLKAIQNQLKSGKKMRDVVIEENEQLIQKPETQPMVATEQYEQRTKQFMEKIAELEKQLSQKADDVVSYQILKHRAEIDEMFKTLQSLELRMAKVEEQLEKQQEEFPLAAGDVPKRKRSFMRLFSF	Required for the formation of axial filaments and for anchoring the origin regions at the cell poles in sporulating cells, thus ensuring proper chromosome segregation in the prespore. Binds in a dispersed manner throughout the chromosome but preferentially to sites clustered in the origin portion of the chromosome, causing condensation of the chromosome and its remodeling into an elongated, anchored structure.	Q9KC68
Q31CV7	AROC_PROM9	5-enolpyruvylshikimate-3-phosphate phospholyase	Prochlorococcus	MSSSFGKIFRVSTFGESHGGGVGVILDGCPPKLKIDIKLIQNELDRRRPGQSDITTPRNEDDKIEILSGIKEGLTLGTPIAMLVRNKDQRPGDYNNLEQVFRPSHADGTYHLKYGIQAGSGGGRASARETIGRVAAGAVAKQLLKNLCNTEILSWVKRIHDIDSDVNKEKISLNKIDSNIVRCPDEKVSAEMIDRIKDLKRQGDSCGGVIECLVRNVPSGLGMPVFDKLEADLAKALMSLPATKGFEIGSGFSGTYLKGSEHNDSFIKSDDISKLRTTSNNSGGIQGGISNGENIEMKIAFKPTATIGKEQKTVNAEGKEVLMKAKGRHDPCVLPRAVPMVDAMVALVLADHLLLNNAQCGLMKN	Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.	Q31CV7
Q0AJI2	CLPP_NITEC	Endopeptidase Clp	Nitrosomonas	MQPILDWEKNELNTTGLGLIPMVIESSGRGERAYDIYSRLLRERIIFLVGPVTETSANLVIAQLLFLESENSEKDISLYINSPGGLVTAGLAVYDTMQFIKPDVSTLCIGQAASMGALLLTAGAKGKRYCLPNSRVMIHQPLGGFQGQASDIEIHAKEILALKGRLNEILAKHTSQTIRTIEKDTDRDNFLGAEAAVKYSLVDAVLTSRKVKHE	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.	Q0AJI2
Q85XC3	NDHK_HORVU	NADH-plastoquinone oxidoreductase subunit K	Hordeum	MNLIEFPLLDQTSSNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDALTKLRKKISREIVEDRTLSQNKKRCFTTSHKLYVRRSTHTGTYEQELLYQSPSTLDISSETFLKSKSPVPSYKLVN	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 translocation, and thus conserves the redox energy in a proton gradient.	Q85XC3
Q8LPR5	TCP4_ARATH	Protein MATERNAL EFFECT EMBRYO ARREST 35	Arabidopsis	MSDDQFHHPPPPSSMRHRSTSDAADGGCGEIVEVQGGHIVRSTGRKDRHSKVCTAKGPRDRRVRLSAHTAIQFYDVQDRLGFDRPSKAVDWLIKKAKTSIDELAELPPWNPADAIRLAAANAKPRRTTAKTQISPSPPPPQQQQQQQQLQFGVGFNGGGAEHPSNNESSFLPPSMDSDSIADTIKSFFPVIGSSTEAPSNHNLMHNYHHQHPPDLLSRTNSQNQDLRLSLQSFPDGPPSLLHHQHHHHTSASASEPTLFYGQSNPLGFDTSSWEQQSSEFGRIQRLVAWNSGGGGGATDTGNGGGFLFAPPTPSTTSFQPVLGQSQQLYSQRGPLQSSYSPMIRAWFDPHHHHQSISTDDLNHHHHLPPPVHQSAIPGIGFASGEFSSGFRIPARFQGQEEEQHDGLTHKPSSASSISRH	Transcription factor playing a pivotal role in the control of morphogenesis of shoot organs by negatively regulating the expression of boundary-specific genes such as CUC genes, probably through the induction of miRNA (e.g. miR164) . Required during early steps of embryogenesis . Participates in ovule develpment . Activates LOX2 expression by binding to the 5'-GGACCA-3' motif found in its promoter . Activates YUC5 transcription by binding to the 5'-GTGGGCCA-3' motif found in its promoter . Through the activation of YUC5 transcription, integrates the auxin response to a brassinosteroid-dependent molecular circuit that promotes cell elongation in hypocotyls . Activates GIS transcription by binding to the 5'-TGGTCC-3' motif found in its promoter . Involved in the regulation of trichome branching through the activation of GIS transcription . Activates CO transcription by binding to the 5'-GGACCAC-3' motif found in its promoter . Involved in the regulation of photoperiodic flowering through the activation of CO transcription . Activates TCL1 and TCL2 transcription by binding to the 5'-TGGCCA-3' and 5'-GTGGACCA-3' motifS found in their respective promoters . Involved in the suppression of trichome initiaition through the activation of TCL1 and TCL2 transcription . Activates HAT2 transcription by binding to the 5'-TGGTCCAC-3' motif found in its promoter . Through the activation of HAT2 transcription, involved in the auxin-independent reprogramming of mitotic cells to exit division and acquire differentiation competence within the transition zone .	Q8LPR5
Q8N1K5	THMS1_HUMAN	Thymocyte-expressed molecule involved in selection	Homo	MALSLEEFVHSLDLRTLPRVLEIQAGIYLEGSIYEMFGNECCFSTGEVIKITGLKVKKIIAEICEQIEGCESLQPFELPMNFPGLFKIVADKTPYLTMEEITRTIHIGPSRLGHPCFYHQKDIKLENLIIKQGEQIMLNSVEEIDGEIMVSCAVARNHQTHSFNLPLSQEGEFYECEDERIYTLKEIVEWKIPKNRTRTVNLTDFSNKWDSTNPFPKDFYGTLILKPVYEIQGVMKFRKDIIRILPSLDVEVKDITDSYDANWFLQLLSTEDLFEMTSKEFPIVTEVIEAPEGNHLPQSILQPGKTIVIHKKYQASRILASEIRSNFPKRHFLIPTSYKGKFKRRPREFPTAYDLEIAKSEKEPLHVVATKAFHSPHDKLSSVSVGDQFLVHQSETTEVLCEGIKKVVNVLACEKILKKSYEAALLPLYMEGGFVEVIHDKKQYPISELCKQFRLPFNVKVSVRDLSIEEDVLAATPGLQLEEDITDSYLLISDFANPTECWEIPVGRLNMTVQLVSNFSRDAEPFLVRTLVEEITEEQYYMMRRYESSASHPPPRPPKHPSVEETKLTLLTLAEERTVDLPKSPKRHHVDITKKLHPNQAGLDSKVLIGSQNDLVDEEKERSNRGATAIAETFKNEKHQK	Plays a central role in late thymocyte development by controlling both positive and negative T-cell selection. Required to sustain and/or integrate signals required for proper lineage commitment and maturation of T-cells. Regulates T-cell development through T-cell antigen receptor (TCR) signaling and in particular through the regulation of calcium influx and phosphorylation of Erk.	Q8N1K5
Q3UWA4	TRI40_MOUSE	Probable E3 NEDD8-protein ligase	Mus	MGSLDKDNQDICPICLDPLKEAVSTDCRHLFCRMCLTQHMDKASVSGILSCPVCRKPCSEGVLGDNYICHTHQKRVRRFCEASGHLLCEECLQSPEHQSHTELSIENAISHYKERLNRRSRKLRKDLGNLQQLKAQEKKMLQALQVDCECHRLRTDLQNQDQTKEQLKALPWHWLDQEDLPEEVAKIFSFSEAVTQLSILVSGLERMAKDLDASTLKDASDLLDRSAPQKLEGLLSRVSPAGPKLS	E3 ubiquitin-protein ligase that plays a role in the limitation of the innate immune response. Mediates inhibition of the RLR signaling pathway by ubiquitinating DDX58 and IFIH1 receptors, leading to their proteasomal degradation. Promotes also the neddylation of IKBKG/NEMO, stabilizing NFKBIA, and thereby inhibiting of NF-kappa-B nuclear translocation and activation.	Q3UWA4
Q57706	CFBE_METJA	Coenzyme F(430) synthetase	Methanocaldococcus	MVFFMLIIDVNHGALTLAEEYLNLGYEVDVWDIYQKIKKSEDFKVKYQKLKEKFGNKLNLFFEQPNFEKYDRVIAPIHCPIDVDFIPFTDAVSKILKEKFGNIHKKIINVTGVKGKTTTTSLINHILKDKYSTYLHNSNFGSIAPPTILKVLNSLDIDKYDFFIFETSLGLIKCKYGAITNVLENYKIAGGRKDALTAKFSSLKNAELSFINKRDINRYDLNINHKCLNVVDVDRAKILDKYPLKFKYFDEIFEFSKNIFGLHFVENSLFAIEICKNLVDMEEIRYRLKTFTIKNRMEIKEINKKILVKNINPGLDVKAISYAIKDFLEVFGGDIYIGGDFGIVCEEIDVKKLSEVLKRFNCRYIFVGEIGKELLNYLNGGYIKSYDENKIKRDSLVILREKIK	Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the activation the g-propionate side chain of 15,17(3)-seco-F430-17(3)-acid (seco-F430) for intramolecular C-C bond formation to yield the carbocyclic F ring of coenzyme F430.	Q57706
B6JNY0	EX7S_HELP2	Exodeoxyribonuclease VII small subunit	Helicobacter	MQDELFETEKAPPKNAKNAPKKSFEEHVHSLEQAIDRLNDPNLSLKDGMDLYKTAMQELFLAQKLLENAYLEYEKLQTTDKKA	Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.	B6JNY0
Q2YAY1	RL18_NITMU	50S ribosomal protein L18	Nitrosospira	MPNSIESRLRRARQTRAKIAELKVVRLAIHRSNSHIYAQLIDGSGSKVLASASTLEPELRKELPNGGTVTAAAVVGKRVAEKARGLGIETVAFDRSGFKYHGRVKALADAARENGLKF	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.	Q2YAY1
Q9Y9W3	SPT5_AERPE	Transcription elongation factor Spt5	Aeropyrum	MEGGVDARFYAILVTSGAEVNVATIIAERARALGLDIRSIIVPPRIKGYVILEAHDPGDVYDATRGLRHVKRRRPLILKFEEVMKLVKPEVEIPALKPGQVVEIVAGAFKGMKARVIDVNQSKGQVTVSLLEPLFRATATIPIDEVRPVEE	Stimulates transcription elongation.	Q9Y9W3
Q81F14	MTAD_BACCR	5-methylthioadenosine/S-adenosylhomocysteine deaminase	Bacillus cereus group	MKTTYVNATIVTMNEQNEVIENGYIIVENDQIIDVKSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAIMETVSRSGMRAAVSRTLFSFGTKDDEKKAIEEAEKYVKRYYNESDMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMRIATLLQKGIHQDATALPVETALSLATKGAAEVIGMKQTGSLEAGKCADFITIDPSNKPHLQPADEVLSHLVYAASGKDISDVIINGKHVVWNGECKTLDEERIIFEASRYKRGLQR	Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.	Q81F14
Q93PP9	BFR_DESDA	Bacterioferritin	Desulfovibrio	MAGNREDRKAKVIEVLNKARAMELHAIHQYMNQHYSLDDMDYGELAANMKLIAIDEMRHAENFAERIKELGGEPTTQKEGKVVTGQAVPVIYESDADQEDATIEAYSQFLKVCKEQGDIVTARLFERIIEEEQAHLTYYENIGSHIKNLGDTYLAKIAGTPSSTGTASKGFVTATPAAE	Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.	Q93PP9
Q86W28	NALP8_HUMAN	PYRIN and NACHT-containing protein 4	Homo	MSDVNPPSDTPIPFSSSSTHSSHIPPWTFSCYPGSPCENGVMLYMRNVSHEELQRFKQLLLTELSTGTMPITWDQVETASWAEVVHLLIERFPGRRAWDVTSNIFAIMNCDKMCVVVRREINAILPTLEPEDLNVGETQVNLEEGESGKIRRYKSNVMEKFFPIWDITTWPGNQRDFFYQGVHRHEEYLPCLLLPKRPQGRQPKTVAIQGAPGIGKTILAKKVMFEWARNKFYAHKRWCAFYFHCQEVNQTTDQSFSELIEQKWPGSQDLVSKIMSKPDQLLLLLDGFEELTSTLIDRLEDLSEDWRQKLPGSVLLSSLLSKTMLPEATLLIMIRFTSWQTCKPLLKCPSLVTLPGFNTMEKIKYFQMYFGHTEEGDQVLSFAMENTILFSMCRVPVVCWMVCSGLKQQMERGNNLTQSCPNATSVFVRYISSLFPTRAENFSRKIHQAQLEGLCHLAADSMWHRKWVLGKEDLEEAKLDQTGVTAFLGMSILRRIAGEEDHYVFTLVTFQEFFAALFYVLCFPQRLKNFHVLSHVNIQRLIASPRGSKSYLSHMGLFLFGFLNEACASAVEQSFQCKVSFGNKRKLLKVIPLLHKCDPPSPGSGVPQLFYCLHEIREEAFVSQALNDYHKVVLRIGNNKEVQVSAFCLKRCQYLHEVELTVTLNFMNVWKLSSSSHPGSEAPESNGLHRWWQDLCSVFATNDKLEVLTMTNSVLGPPFLKALAAALRHPQCKLQKLLLRRVNSTMLNQDLIGVLTGNQHLRYLEIQHVEVESKAVKLLCRVLRSPRCRLQCLRLEDCLATPRIWTDLGNNLQGNGHLKTLILRKNSLENCGAYYLSVAQLERLSIENCNLTQLTCESLASCLRQSKMLTHLSLAENALKDEGAKHIWNALPHLRCPLQRLVLRKCDLTFNCCQDMISALCKNKTLKSLDLSFNSLKDDGVILLCEALKNPDCTLQILELENCLFTSICCQAMASMLRKNQHLRHLDLSKNAIGVYGILTLCEAFSSQKKREEVIFCIPAWTRITSFSPTPHPPDFTGKSDCLSQINP	Involved in inflammation.	Q86W28
Q6NKS4	LIL32_ARATH	LHC-like protein 3 isoform 2	Arabidopsis	MSISMALFSPPISSSLQNPNLIPKISTSLLSTKRFSLISVPRASSDNGTTSPVVEIPKPASVAVEEVPVKSPAESSSASENGAVGGEATDSSTETVIKYQNAKWVNGTWDLKQFEKDGKTDWDSVIVSEAKRRKWLEDNPETTSNDELVVFDTSIIPWWAWMKRYHLPEAELLNGRAAMIGFFMAYFVDSLTGVGLVDQMGNFFCKTLLFVAVAGVLFIRKNEDLDKLKDLFDETTLYDKQWQAAWKEPDSSTVSSKK	Light-harvesting-like protein required for biosynthesis of phytylated chlorophylls and alpha-tocopherol in green seedlings. Functions by anchoring geranylgeranyl reductase (GGR) in the thylakoid membrane, leading to the stabilization of GGR activity . Binds chlrophyll a in the thylakoid membrane . Plays a role in the regulation of chlorophyll biosynthesis under light stress and under standard growth conditions .	Q6NKS4
A1KBD3	LEU1_AZOSB	Alpha-isopropylmalate synthase	Azoarcus	MLKNPHTKYRPANPFAGVVPGGRGLSDRTWPDNTITRPPVWMSTDLRDGNQALFEPMNSERKMRMFKMLVEIGLKEIEVAFPAASQTDFDFVRELIEGGHIPDDVTIEVLTQARPHLIERTFESVRGAKRAIVHVYNAVAPNFRRIVFDTDRAGVKQIAVDSARYFVEMAARQPGTDFTFQYSPEVFSGTELDFAVEVANAVIEVWQPTPQQKCIINLPATVEMSTPNVYADQIEWMHRHLARRDSVLLSVHPHNDRGTAVAAAELAVMAGADRVEGCLFGNGERTGNVDLVTLALNLYSQGVHPGLDFSRINEVARTVEHCTQLPIHPRHPYVGDLVFTAFSGSHQDAIKKGFAVQQPDAVWEVPYLPVDPADLGRSYESIIRVNSQSGKGGIAYLLEAEYGLVMPRRLQVEFSAAIQRITDERGTELSAGDIWRAFEEEYLAVAAPYAYVEHHLAEHGGQQGISLTVEEAGVRRVLRGVGNGPIDAALHALDAGAVLLGYEERAIGQGGDARAVAYIELADGEGGGSTFGVGIHANIVTASVLAIVSALDRLAQRRERADGVGRQVAATR	Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).	A1KBD3
B4SBV3	RS3_PELPB	30S ribosomal protein S3	Pelodictyon	MGQKVNPTGFRLGIIRDWASRWYDDSPVISEKIKQDHVIRTYVLARLKKERAGIARIIIERTTKHVKINIYAARPGAVVGRKGEEINNLSQELSRITGKEVKIDVVEVVKPEIEAQLIGDNIAYQLENRVSFRRAMKQAIQQAMRSGAEGVRIRCGGRLGGAEIARSEQYKEGKIPLHTIRANVDYASVTAHTIAGTIGIKVWVYKGEVLVQRIDAIEEDELKRIKERRNDAGARNRDSRTKRRHRTKR	Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.	B4SBV3
B1A925	RPOC2_CARPA	Plastid-encoded RNA polymerase subunit beta''	Carica	MAERANLVFHNKVIDGTAIKRLISRLIDRFGMAYTSHILDQVKTLGFQQATATSISLGIDDLLTIPSKGWLVQDAEQQSLILEKHHHYGNVHAVEKLRQSIEIWYATSEYLRQEMNPNFRVTDPFNPVHIMSFSGARGNASQVHQLVGMRGLMSDPQGQMIDLPIQSNLREGLSLTEYIISCYGARKGVVDTAVRTSDAGYLTRRLVEVVQHIVVRRTDCGTIRGISVSPKNRTMPERIFIQTLIGRVLADDIYMGPRCIAIRNQDIGIGLVNRFITFRTQSISIRTPFTCRSTSWICRLCYGRSPTHGDLVELGEAVGIIAGQSIGEPGTQLTLRTFHTGGVFTGGTAEHVRSPSNGKIKFNEDLVHPTRTRHGHPAFLCYIDLSVVIESEDIIHNVTIPPKSFLLVQNDQYVESEQVIAEIRAGTYTLNYKERVRKHIYSNSEGEMHWSTDVYHAPEFTYSNVHLLPKTSHLWILSGGSSRSSLVPFSLHKDQDQMNIHSLSVEQESISSLAVNNDQGRHKFFSSNFSDKKKCGIPDYSEFHRILDTGHCNLIYFASLHENSDLLAKRRRNRFIIPFQSIQEQEKELMPRSGISIEIPINGIFRRNSILAFFDDPRYRRKSSGILKYGTIGAHSIVKKEDVIEYRGVKKFKTKYQMKVDRFFFIPEEVHILPESSSIMVRNNSIIGVDTRITLNIRSQVGGLVRVERKKKSIELQIFSGDIHFPGKTDKISRHSGILIPPGRGKTNSKESKKLKNWIYVQRITPTKKKYFVLVRPVATYEIADGINLATLFPQDLFREKDNMQLRVVNYILYGNGKPVRGIFDTSIQLVRTCLVLNWDQDNKSSSVEEVRTFFVEVSTNSLIRDFLRIDLVKSQSHISYIRKRNDPSGSGLISDNGSDRINPFYYKERIQQSLSKNHGTIRTLLNRNKECQSLIILSSSNCFQMGPFNHVKYHNVIKQSIKKDPLIPIRNSLGPVGTAIQIANFYSIYHLITHNQISVTKYFQLDNLNQIFEVIKYYLMDETGRVYNPDPCSNIILNPFNLNWYFLYQNYHHNYCEETSTIISLGQFICENVCLAKNGPHLKSGQVLIVQVDSVVIRSAKPYLATPGATVHGHYGEILYEGDTLVTFIYEKSRSGDITQGLPKVEQVLEVRSIDSISLNLEKRVEGWNKRITRILGIPWGFLIGAELTIVQSRISLVNKIQKVYRSQGVQIHNRHIEIIVRQITSKVLVSEEGMSNVFLPGELIGLLRAERTGRALEEAICYRAILLGITRASLNTQSFISEASFQETARVLAKAALRGRIDWLKGLKENVVLGGMIPAGTGFKGLVHCSRQHTSILLETKKKNLYLFEGEMRDIFFHHRELFDSCISKNLHNTSERSFIGLNDS	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	B1A925
A9M0Q6	CH60_NEIM0	Chaperonin-60	Neisseria	MAAKDVQFGNEVRQKMVNGVNILANAVRVTLGPKGRNVVVDRAFGGPHITKDGVTVAKEIELKDKFENMGAQMVKEVASKTNDVAGDGTTTATVLAQSIVAEGMKYVTAGMNPTDLKRGIDKAVAALVEELKNIAKPCDTSKEIAQVGSISANSDEQVGAIIAEAMEKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINDAEKQIAALDNPFVLLFDKKISNIRDLLPVLEQVAKASRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLQDIAILTGGVVISEEVGLSLEKATLDDLGQAKRIEIGKENTTIIDGFGDAAQIEARVAEIRQQIETATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGVVAGGGVALLRARAALENLHTGNADQDAGVQIVLRAVESPLRQIVANAGGEPSVVVNKVLEGKGNYGYNAGSGEYGDMIEMGVLDPAKVTRSALQHAASIAGLMLTTDCMIAEIPEDKPAVPDMGGMGGMGGMM	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.	A9M0Q6
Q12096	GNT1_YEAST	N-acetylglucosaminyltransferase	Saccharomyces	MRLISKRRIRFIVFILFGVLTVFVVSRLVVHFQYNQEIKFYKKYFQQRKDGLHEIYNPLEIKQIPKETIDDLYTARLDKELKNGEVIEWSKFAYVNYVTNADYLCNTLIIFNDLKQEFETKAKLVLLISKDLLDPNTSSNVAYISSLLNKIQAIDEDQVVIKLIDNIVKPKDTTPWNESLTKLLVFNQTEFDRVIYLDNDAILRSSLDELFFLPNYIKFAAPLTYWFLSNSDLEKSYHETRHREKQPINLQSYTKVLTKRIGKGQMIYNHLPSLPHSLYLNSNNIAQDIISSTSSLSPLFDFQSSKKVGKLKFASNLMVINPSKEAFDEIVNVMLPKILNKKEKYDMDLINEEMYNLKKIIYKQFIFFRKVRKLFKPEVLVLPFARYGLLTGSLRNPRHYSIIYNDVLGYKTLDNDGNDIPVGLNDSVAYSKYIHFSDYPLAKPWNYPSMKEFECIVKEEDAEDSKLEHQACDLWNSVYASYIQSREICLV	N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.	Q12096
Q5AGW8	NUP_CANAL	Purine nucleoside permease	Candida	MKLSTLFTLATTISTLTTFTIASPVVVVEKRAINETALAEDIPTTKNNHAQTSYGKPFAIYQPKAFIISMFSLERDPWLKAMDFVHNITIPGLSPVYPDIHCTTNYTICQITTGEGEINAASSISALTLNPLFDLTKTYFLVGGIAGGEPNYTTIGGVTFAKYAVQVGLEYQLAYEDYHKTNPDWISGYIPYGTDDQNTYPGNVYGTEVFEVNEKLRDRAVELASKVHLNNGTEGNAKFRKLYNETAAQGLPKVVKCDSLTSDNYFTGNVLNDYFANFTLLMTNGSATYCSTAQEDNATLEVMTRLAKHGLVDYDRIMIMRTISDFSRPPPSMSAYEYFFNRSDGGISASLENLVIAGTPIIHDIVQNWDKIYESGEKYSSKNYVGDIFATLGGKPDFGKESFDTA	Nucleoside permease that transports adenosine and guanosine. Does not show any transport activities towards cytidine, adenine, guanine, uridine, and uracil.	Q5AGW8
P25378	RHEB_YEAST	GTP-binding protein RSG1	Saccharomyces	MEYATMSSSNSTHNFQRKIALIGARNVGKTTLTVRFVESRFVESYYPTIENEFTRIIPYKSHDCTLEILDTAGQDEVSLLNIKSLTGVRGIILCYSIINRASFDLIPILWDKLVDQLGKDNLPVILVGTKADLGRSTKGVKRCVTKAEGEKLASTIGSQDKRNQAAFIECSAELDYNVEETFMLLLKQMERVEGTLGLDAENNNKCSIM	Involved in the regulation of arginine and lysine uptake. Acts through the CAN1 permease.	P25378
Q887M0	AMPA_PSESM	Leucyl aminopeptidase	Pseudomonas	MELVVKSVSPETLKTATLVVTINESRVLIGAAQLVDIKSGGAISAVLERGDLAGKSGQTLLLTNLQNIKAERVLLVGIGKDGELSDRQLKKIAGSVLSSLKGLGGSDAVIALDDLSVKNRDTYGKARLFVEALADGEYVFDRFKTQKAEVRPLKKITLLTDKVSVADVERAANHAQAIATGMALTRDLGNLPPNICHPTYLGEEAKALGKAHKNLKVEIHDEKKLAELGMGSFLAVAQGSAQPPRLIVMNYQGGKKGDKPFVLVGKGITFDTGGISIKPAAGMDEMKFDMCGAASVFGTLRAVLELKLPINVVCILACAENMPSGTATRPGDIVTTMSGQTVEILNTDAEGRLVLCDALTYAERFKPQAVIDIATLTGACVVALGGHTSGLLGNNDALINQLLDAGKLADDRAWQLPLFDEYQEQLDSPFADIANIGGPKGGTITAACFLSRFTKAYEWAHLDIAGTAWLSGGKDKGATGRPVPLLTQYLLDRAGV	Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.	Q887M0
P84088	CPLX2_BOVIN	Synaphin-1	Bos	MDFVMKQALGGATKDMGKMLGGEEEKDPDAQKKEEERQEALRQQEEERKAKHARMEAEREKVRQQIRDKYGLKKKEEKEAEEKAALEQPCEGSLTRPKKAIPAGCGDEEEEEEESILDTVLKYLPGPLQDMFKK	Negatively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles. Also involved in mast cell exocytosis.	P84088
F4JRF4	MUTYH_ARATH	MutY homolog	Arabidopsis	MACLLRVALNPTFERSTVASQRQNPKTILSFHCKVSSFKTKTMSQSFAPREKLMRKCREKKEAEREAEREAEREAEEEEKAEEAEAEADKEEAEEESEEEEEEEEEEAEAEEEALGGDIEDLFSENETQKIRMGLLDWYDVNKRDLPWRNRRSESEKERRAYEVWVSEIMLQQTRVQTVMKYYKRWMQKWPTIYDLGQASLENLIVSRSRELSFLRGNEKKEVNEMWAGLGYYRRARFLLEGAKMVVAGTEGFPNQASSLMKVKGIGQYTAGAIASIAFNEAVPVVDGNVIRVLARLKAISANPKDRLTARNFWKLAAQLVDPSRPGDFNQSLMELGATLCTVSKPSCSSCPVSSQCRAFSLSEENRTISVTDYPTKVIKAKPRHDFCCVCVLEIHNLERNQSGGRFVLVKRPEQGLLAGLWEFPSVILNEEADSATRRNAINVYLKEAFRFHVELKKACTIVSREELGEFVHIFTHIRRKVYVELLVVQLTGGTEDLFKGQAKDTLTWKCVSSDVLSTLGLTSAVRKVPPFRLQHIKRLSLDVMVEKEQILECRCIQWLKHTSKAYLFLMSHQIEQPYRGNENSHDLLLTLFFMLLSFYSSCLALGIKFGDLGLKLNSLVSTEKSDGDV	Involved in oxidative DNA damage repair. Initiates repair of AoxoG to CG by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2-OH-A DNA glycosylase activities.	F4JRF4
Q9UZ56	IORB_PYRAB	Indolepyruvate ferredoxin oxidoreductase subunit beta	Pyrococcus	MKEYNIVITGVGGQGILTAANLLGWAALRAGYKVRVGEVHGMSQRFGSVIAYVRFGEDVYGAMVPEGKADVILSFEPVEALRYINYLKKGGLVFTNARPIPPVQVSMGLASYPSMEEIRKIVEEDFGGKFLAFDAEKLAIEAGNVITTNVVLIGALTQTPGFPLSAEHVKEVIRISVPPKAVDVNMRAFELGVKAAKEMLNL	Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.	Q9UZ56
Q9SY97	LHCA3_ARATH	LHCI type III LHCA3	Arabidopsis	MAAQALVSSSLTSSVQTARQIFGSKPVASASQKKSSFVVKAAATPPVKQGANRPLWFASSQSLSYLDGSLPGDYGFDPLGLSDPEGTGGFIEPRWLAYGEIINGRFAMLGAAGAIAPEILGKAGLIPAETALPWFQTGVIPPAGTYTYWADNYTLFVLEMALMGFAEHRRLQDWYNPGSMGKQYFLGLEKGLAGSGNPAYPGGPFFNPLGFGKDEKSLKELKLKEVKNGRLAMLAILGYFIQGLVTGVGPYQNLLDHLADPVNNNVLTSLKFH	The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated, here photosystem I.	Q9SY97
Q6DI51	NDK6_DANRE	Nucleoside diphosphate kinase 6	Danio	MRCVKALQLTLAVIKPDAMAHPLILEALHQKILENFIIIRKKDLIWRKADSEMFYAEHSGRFFFQRLVEFMSSGPMRAYILAREDAITHWRTMMGPTKVFRARFSSPETLRGKYGLTDTRNTTHGSDSIESAKREISFFFPEFSAEEWMMREEPHFRLGHTEYNEESQIHTVKHT	Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.	Q6DI51
O74095	RL23_PYRHO	50S ribosomal protein L23	Pyrococcus	MDPYKVIIRPVVTEKAISLIEKENKLTFIVDRRATKTDIKKAIEEIFNVKVEKVNTLITPKGEKKAYVKLKPEYSASEIAARLGLF	Binds to 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome.	O74095
C6DKI3	RLME_PECCP	rRNA (uridine-2'-O-)-methyltransferase	Pectobacterium	MANKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYVVTQIGGNGRIIACDILPMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPKSMYLVELALGMCRDVLAPGGSFLVKVFQGEGFDEYLREIRSLFTKVKIRKPDASRARSREVYIVATGRKL	Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.	C6DKI3
Q92F41	Y266_LISIN	Putative RNase Lin0266	Listeria	MLTWVIRVCFLILGGTTGVFSLPALWVKLGIGHILLINNPYTDALIGALIFYLITFWAVKYVEAALNWLEEKLAKIAIATLIYGGLGLFVGLVIAFFASNALSQTNIPLLNSVVPVILTLVLGYLGFRIGISRRNEFGNFVNNRNAKKKTPEEEQTEEKSKKTYKILDTSVIIDGRIADILATGFLDGTVVIPLFVLAELQHIADSSDTLKRTRGRRGLDILNRIQKEDSIQVEMYEGDFEDTPEVDSKLVKLAKVMGGIVVTNDYNLNKVCEFQNVPVLNINDLANAVKPVVLPGEKMTVLMVKDGKEHNQGVAYLDDGTMIVVEDGRKFINETIQVEVTSVLQTSAGRMIFAKPS	An RNase.	Q92F41
Q8AY50	3NO22_BUNCA	Weak toxin 2	Bungarus	MKTLLLTLVVVAIVCLDLGYTLTCLICPEKDCQKVHTCRNEEKICVKRSYDKNQLGWRAQRGCAVSCPKAKPNETVQCCSTDKCNK	Binds with low affinity to muscular (alpha-1-beta-1-delta-epsilon/CHRNA1-CHRNB1-CHRND-CHRNE) and very low affinity to neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR).	Q8AY50
A0KG33	NHAA_AERHH	Sodium/proton antiporter NhaA	Aeromonas	MSDVIKKFLKLEAASGIILIMAAMLAMILANSGLAGSYQAFLDTQVQVRIAALDINKPLLLWINDGFMAVFFLLVGLEVKREMLEGALSSRVQATFPAIAAVGGMLAPALIYAFFNYSDEVARAGWAIPAATDIAFALGVMALLGKRVPVSLKVFLLALAIMDDLGVIIIIALFYTQQLSLTALAIGILATLTLLWMNRRGEDRISLYMLVGLVLWVAVLKSGVHATLAGVIVGFMIPLSGKRYASPLKQLEHALHPWSAYLILPLFAFANAGVSLEGIGLSALLSPVPLGIMLGLFIGKPLGVFTISWLAVKLGIAQLPNGVNFKQIFAVSILCGIGFTMSMFIASLAFEHGGLDYGSYSRLGILVGSTLAAIVGYLALRIALPNREADQSTEGL	Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.	A0KG33
P59733	RLMH_NITEU	rRNA (pseudouridine-N3-)-methyltransferase RlmH	Nitrosomonas	MKFHILAVGNKMPDWVRKGYTEYCQRMPKEAELLLVEIKPEKRVGSKNTRQLLQAESERIRTVLPPGCHIVVLDETGKQATTMKLAEMMDRWMGSGQDVAFIIGGADGLHQDIKQMAHEKLALSAMTLPHGLARVLLAEQLYRAFSINRNHPYHRA	Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.	P59733
P49376	ATPB_KLULA	ATP synthase subunit beta, mitochondrial	Kluyveromyces	MVLPRFYAASSRAALQAARRAVPFTGVRGYAAAASSQGKVRAVIGAIVDVQFEQGQLPAILNALEIDTPEGKLVLEVAQHLGENTVRTIAMDGTEGLVRGENVSDTGAPISVPVGRETLGRIINVIGEPIDERGPINSKMRKPIHADPPLFVEQSTAAEVLETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGDSKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVATQVQQTLQAYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGRLVRLKDTISSFKAVLDGKYDHLPENAFYMVGGIEDVVAKAEKLAAEAN	Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.	P49376
Q14145	KEAP1_HUMAN	Kelch-like protein 19	Homo	MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPNFLQMQLQKCEILQSDSRCKDYLVKIFEELTLHKPTQVMPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSDGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGRSGVGVAVTMEPCRKQIDQQNCTC	Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting NFE2L2/NRF2 for ubiquitination . KEAP1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of NFE2L2/NRF2, a transcription factor regulating expression of many cytoprotective genes . In response to oxidative stress, different electrophile metabolites trigger non-enzymatic covalent modifications of highly reactive cysteine residues in KEAP1, leading to inactivate the ubiquitin ligase activity of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and expression of phase II detoxifying enzymes . In response to selective autophagy, KEAP1 is sequestered in inclusion bodies following its interaction with SQSTM1/p62, leading to inactivation of the BCR(KEAP1) complex and activation of NFE2L2/NRF2 . The BCR(KEAP1) complex also mediates ubiquitination of SQSTM1/p62, increasing SQSTM1/p62 sequestering activity and degradation . The BCR(KEAP1) complex also targets BPTF and PGAM5 for ubiquitination and degradation by the proteasome .	Q14145
Q953L2	NU4LM_ECHGY	NADH dehydrogenase subunit 4L	Echinosorex	MQMTMINMILAFIMATTGLLMFRSHFMSSLLCLEGMMLSIFILMSISTLNFNNSLAMMFPLVLLVFAACEAAIGLSLLVKISNTYGTDYVQNLNLLQC	Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.	Q953L2
A4XLS8	RL23_CALS8	50S ribosomal protein L23	Caldicellulosiruptor	MLPEEIIKRPIITEKSMSMIPQKKYTFEVDRRANKIEIKKAVEQLFGVEVEKVWTMNVKPKRKRVGRFEGRTKAWKKAIVKLTDKSKTIEFFDSLI	One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.	A4XLS8
Q72CG9	RL24_DESVH	50S ribosomal protein L24	Desulfovibrio	MKQFRIHKDDKVMVIAGKDKGKIGKVLKILRNKDRILVEKVNVAKRHVRPNPYRQQPGGIIEKEMPLHVSNVMVVCDACAKPTKVGYRYTEDGKKVRFCKKCNEIID	One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.	Q72CG9
Q4WAX1	FTMH_ASPFU	Fumitremorgin biosynthesis protein H	Aspergillus subgen. Fumigati	MTIPTEISCPEEDAFQLLDKFSWFPSDDQRRWWEYTGPYLLKLLRDAKYPQKDQVPCLYLLQQLLVPYLGTFPVVGQAPLPWWSNVTTYGVPFELSWNLLHNIVRIGFEPLSHLAESGVDAFNKTAPEECVSRLACLDNTIDLARFRHFQHHLLVTPEEETWLLKEKAPLAKSGRGQQTLAVEFQNGGISAKAYFFPGMKSLATGLSPGKLILDSIERLALPGLKEPVHHLRSTLGLQDDGHPTDTAIAPFLLGVDLCTPERSRLKFYVTDQVVSWDRVADMWTLRGKRLEDPQCADGLALLRKLWDLLAIPEGYRSNIRPDFAFGTPPPEDYRPVMMANWTLSPKKKFPDPQIYLLTVGMNDAVVMDALVAFYEVLGWTDLASTYKDKVASYFPGPDFTKTNYIHSGVSFSYRHSKPYLSVYYSPF	12-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities . The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA . Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B . The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively . The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B . Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties . In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).	Q4WAX1
Q4WD43	FSQB_ASPFU	Fumisoquins biosynthesis protein B	Aspergillus subgen. Fumigati	MSIPNSFIIVGSGVFGLSLAYALSLDDRFADKKIILVDRWNFEPPNATGSVHNPAAANADTSRVIRRDYPHGPYASLALEAMKHWRGKFGENNRYVNQRLLFSGEGSSLTTPPKALETVNYIKKAYAISCELTPGGRDAVQVLDSLDEVRAFLGNTPSHPPHLPVNKDPAARDLRGYVSNDCGWADAGASIEWLRQEVLRLGRVECVVGEVESLVYSDDQRAVKGVKLVDGKVLTAELTVIAAGARSSHILGIPKLCDVYSEFVAYIQLTKEEADELRRRQWPILVNCHRGVFAVGPDHDNCLKFGHFSYSGIVDVLREASIQVPTRPDGWEAQQKYWSDPRFAFGGEVKVSALGDVDDYENPAAQRALADYRLFLLELLGPTGLQGVDTLGLDQSDNLLNNIANRPFTRVRKCWYNDTPALDFVVDYHPSYGKTLFVATGGCDHAFKFLPIIGEKTLALILRNRGDSAVSLPAGVEPSLEELSELWRFPVELLQDN	Is able to convert N-methyl-3,4-dihydroxy-DL-phenylalanine (N-methyl-DOPA) directly into cyclic isoquinoline, in vitro . The absence of the meta-hydroxyl group, as in L-N-methyl-tyrosine, leads to a 25-fold lower rate of reduction and the formation of the demethylated product L-tyrosine, instead of a cyclic product . Does not accept the D-stereoisomer of N-methyltyrosine, in contrast to N-methyl-DOPA, for which both stereoisomers are oxidized with similar rates .	Q4WD43
Q21WT4	DAPE_ALBFT	N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase	Rhodoferax	MPKTLHLAEQLIARPSLTPDDAGCQQIIAERLAPLGFSCETITSGPADFRVTNLWAKRAAAPVKSAQHTTKLVVFAGHTDIVPSGPVQQWRCHPFTPTQFDGKLYGRGAADMKTSLAAFVVAVEEFLTAQPDTALAIGFLLTSDEEGPALDGTVKVCEALQARGERIDYCIVGEPTSLERTGDMIKNGRRGTLSARLTVKGVQGHIAYPHLAKNPIHLVAPALAELVGVEWDRGNAFFPPTSWQISNIHSGTGASNVIPGAVVIDFNFRFSTESTPESLQTRLAAVLERHELDYELAWTLGGTPFLTEPGTLVDAVVDAIKQETGLTTVLSTTGGTSDGRFIARICPQVIEFGPPNASIHKIDEHINVADIEPLTNIYRRVLENLSAGLSA	Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.	Q21WT4
Q661D7	RL22_BORGP	50S ribosomal protein L22	Borreliella	MLSQIKREGNRVVMLVNRRYTARGKNLPSSPKKVRPIADNIRGKSYIKAIAVLCSMPNKGAKLLEKVVKSAASNAMYHNKNLSEDMIFVKIVMVDDGRRRKKIWPRARGRADRLVNRNCHIFVEVDEKKDIKG	The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.	Q661D7
A1URW3	AROC_BARBK	5-enolpyruvylshikimate-3-phosphate phospholyase	Bartonella	MSHNTFGHLFRVTTWGESHGAALGCVIDGCPPGIAFTLTEIQAYLNKRRPGHSEYTTQRRELDQVEILSGVVSQNDGKALVTTGTPISMFIRNVDHHSEDYNAIMHKYRPGHADYTYDVKYGIRDHRGGGRASARETVVRVAAGALARKIVPGLIVRGAVTAIGPHNIDRDRWDWSEVDKNPFFSPDAQAACVFANYISQLCKTGSSVGAIVEIVAENVPAGLGAPVYAKLDQDIASFLMSINAVKGIEIGDGFAAAHLTGEENADEMRMGSDGKPVFLSNHAGGILGGISNGQPIVARFAVKPTSSILTPSRSIDIEGNDVNVMTKGRHDPCVGIRAVPVGEAMVACAIADHYLRHRGQVGCI	Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.	A1URW3
P32121	ARRB2_HUMAN	Non-visual arrestin-3	Homo	MGEKPGTRVFKKSSPNCKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTCAFRYGREDLDVLGLSFRKDLFIATYQAFPPVPNPPRPPTRLQDRLLRKLGQHAHPFFFTIPQNLPCSVTLQPGPEDTGKACGVDFEIRAFCAKSLEEKSHKRNSVRLVIRKVQFAPEKPGPQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYADICLFSTAQYKCPVAQLEQDDQVSPSSTFCKVYTITPLLSDNREKRGLALDGKLKHEDTNLASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIPLPRPQSAAPETDVPVDTNLIEFDTNYATDDDIVFEDFARLRLKGMKDDDYDDQLC	Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as signaling scaffold for the AKT1 pathway. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Increases ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Involved in CCR7-mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in p53/TP53-mediated apoptosis by regulating MDM2 and reducing the MDM2-mediated degradation of p53/TP53. May serve as nuclear messenger for GPCRs. Upon stimulation of OR1D2, may be involved in regulation of gene expression during the early processes of fertilization. Also involved in regulation of receptors other than GPCRs. Involved in endocytosis of TGFBR2 and TGFBR3 and down-regulates TGF-beta signaling such as NF-kappa-B activation. Involved in endocytosis of low-density lipoprotein receptor/LDLR. Involved in endocytosis of smoothened homolog/Smo, which also requires GRK2. Involved in endocytosis of SLC9A5. Involved in endocytosis of ENG and subsequent TGF-beta-mediated ERK activation and migration of epithelial cells. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in insulin resistance by acting as insulin-induced signaling scaffold for SRC, AKT1 and INSR. Involved in regulation of inhibitory signaling of natural killer cells by recruiting PTPN6 and PTPN11 to KIR2DL1. Involved in IL8-mediated granule release in neutrophils. Involved in the internalization of the atypical chemokine receptor ACKR3. Acts as an adapter protein coupling FFAR4 receptor to specific downstream signaling pathways, as well as mediating receptor endocytosis . During the activation step of NLRP3 inflammasome, directly associates with NLRP3 leading to inhibition of pro-inflammatory cytokine release and inhibition of inflammation .	P32121
Q2NF48	RL37_METST	50S ribosomal protein L37e	Methanosphaera	MKGTPSFGKRNKKNHIRCRRCGRNAYNPTKKYCASCGFGRSKRLRRYSWQNKKPVTGKRLK	Binds to the 23S rRNA.	Q2NF48
Q6B6N4	PCNA_HAPBU	Proliferating cell nuclear antigen	Haplochromis	MFEARLVQGSILKKVLEALKDLITEACWDVSSSGISLQSMDSSHVSLVQLTLRHDGFDSYRCDRNLAMGVNLSSMSKILKCAGNEDIITLRAEDNADTLALVFETLNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSQIGDAVMISCAKDGVKFSASGELGTGNIKLSQTSNVDKEDEAVTIEMNEPVQLIFALNYLNFFTKATPLSKTVTLSMSADIPLVVEYKIADMGHIKYYLAPKIDEEAS	This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.	Q6B6N4
Q8LG54	AGP7_ARATH	Classical arabinogalactan protein 7	Arabidopsis	MNSKIIEAFFIVALFTTSCLAQAPAPSPTTTVTPPPVATPPPAATPAPTTTPPPAVSPAPTSSPPSSAPSPSSDAPTASPPAPEGPGVSPGELAPTPSDASAPPPNAALTNKAFVVGSLVAAIIYAVVLA	Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.	Q8LG54
Q9MUX3	MATK_SORBI	Intron maturase	Sorghum	MEKFEGYSEKQKSRQHYFVYPLLFQEYIYAFAHDYGLNGSEPVEIFGCNNKKFSSILVKRLIIRMYQQNFWINSVNYPNQDRLFDHRNYFYSEFYSQILSEGFGIVVEIPLSLGQLSCPEEKEIPKFQNLQSIHSIFPFLEDKFLHLHYLSHIEIPYPIHLEILVQLLEYRIQDVPSLHLLRFFLHYYSNWNSLITSMKSIFLLKKENKRLFRFLYNSYVSEYEFFLLFLRKQSSCLRLTSSGTFLERIIFSGKMEHFGVMYPGFFRKTIWFFMDPLMHYVRYQGKAILASKGTLLLKKKWKSYLVNFSQYFFSFWTQPQRIRLNQLTNSCFDFLGYLSSVPINTLLVRNQMLENSFLIDTRMKKFDTTVPATPLVGSLSKAQFCTGSGHPISKPVWTDLSDWDILDRFGRICRNLFHYYSGSSKKQTLYRLKYILRLSCARTLARKHKSTVRTFMQRLGLVFLEEFFTEEEQVFSLMFTKTKTIHFSFHGSQSERIWYLDIIRINDLVNPLTLN	Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.	Q9MUX3
B0K9P1	DUT_THEP3	dUTP pyrophosphatase	Thermoanaerobacter	MSIILKIKKTDDAKDLPLPAYMSEGAAGMDLYANVKEEVILQPGEIKLIPTGIQIELPPNFEAQIRPRSGLALNYGITLLNTPGTIDSDYRGEIKLIVINLGKEAVKIARGQRIAQMVINQIVRPTIVEAEILSETKRDEGGFGHTGI	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.	B0K9P1
Q6GF05	MAZF_STAAR	mRNA interferase MazF	Staphylococcus	MIRRGDVYLADLSPVQGSEQGGVRPVVIIQNDTGNKYSPTVIVAAITGRINKAKIPTHVEIEKKKYKLDKDSVILLEQIRTLDKKRLKEKLTYLSDDKMKEVDNALMISLGLNAVVHQKN	Toxic component of a type II toxin-antitoxin (TA) system. Ribosome-independent, sequence-specific endoribonuclease that cleaves mRNA, thus inhibiting protein synthesis and inducing bacterial stasis. It cuts between the first and nucleotides of 5'-UACAU-3' in single-stranded RNA. Neutralized by coexpression with cognate antitoxin MazE.	Q6GF05
Q03646	MSA2_PLAF2	Merozoite surface antigen 2	Plasmodium (Laverania)	MKVIKTLSIINFFIFVTFNIKNESKYSNTFINNAYNMSIRRSMAESKPPTGDGAVASAGNGAVASAGNGAVASAGNGAVASAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAVASAGNGAGNGAVASAGNGAVAERSSSTPATTTTTTTTNDAEASTSTSSENSNHNNAETNPKGNGEVQPNQANKETQNNSNVQQDSQTKSNVPRTQDADTKSPTAQPEQAENSAPTAEQTESPELQSAPENKGTGQHGHMHGSRNNHPQNTSDSQKECTDGNKENCGAATSLLNNSSNIASINKFVVLISATLVLSFAIFI	May play a role in the merozoite attachment to the erythrocyte.	Q03646
A5DZ02	RRG9_LODEL	Required for respiratory growth protein 9, mitochondrial	Lodderomyces	MLSQCFRSSLAKHCFVAKNQALHGKFVNSIMCLSSSSSNSGSSNSNSNSGSSNSNIRYNDNYRSNDDGTNFEELQLPSALKSETESLNGKGKNKLSKRPQTLLEALIESHGTLPEEVDEPKITRNVASESATSATSATSATSATSATSATSATSATSATSATSATSTTTIITTTATVPVENNVSTPYWVKRELTMKAKHSQWNPKKKLSREDMLKLRELKENFPHYKTVELAELFRVSPEAVRRILKSNWVPNDIDEDRIIARREKQKQKRQQEIQLKKLEFISNRGKKNVSSRPQQRQQQQPKQQQRQRSKVGYKNGFAFNEKYGGLGNKF	Required for respiratory activity and maintenance and expression of the mitochondrial genome.	A5DZ02
A6WJ17	CH60_SHEB8	Chaperonin-60	Shewanella	MAAKEVVFGNDARVRMLAGVNILANAVKVTLGPKGRNVVLDKSFGSPLITKDGVSVAKEIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIVVEGLKAVAAGMNPMDLKRGIDKAVIAAVAELKALSQPCADSKAIAQVATISANSDESIGEIIATAMEKVGKEGVITVEEGQALENELDVVEGMQFDRGYLSPYFINKPETGSVELDHPFVLLVDKKISNIRELLPILEGLAKTGKPLLIVAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDVAILTGGTVIAEEIGLELEKATLEDLGTAKRVVITKDNTTIIDGNGEQTQIAARVSQIKQQVEESTSDYDKEKLQERMAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVPGGGVALVRVASKIADVEVLNEDQKHGVVIALRAMEAPLRQIATNAGEEASVVANTVKNGSGNYGYNAGNDTYGDMLEMGILDPTKVTRCALQFAASIAGLMITTEAMVAEIPQNASQDMGGMGGMGGMGGMM	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.	A6WJ17
B4S8V2	SYDND_PROA2	Non-discriminating aspartyl-tRNA synthetase	Prosthecochloris	MSLAPGTETDLQNRFRSHFCGRLNTEYENKQVRLAGWIHRKRDHGGLIFIDLRDHTGIAQLIIQPEKQELFQKVERLHVESVIAVQGTVVKRSEETLNSRIPSGAIEVLVDDVQVESHAVALPFPVADELQTSEELRLTYRFLDLRREKIHQNIVFRSQLISKVRRYLEDHGFMEIQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVSGFPRYFQIAPCFRDEDARADRSPGEFYQVDMEMAFIEQDDLFEILEGMLRYLTETMSTKRITQFPFPRLSYRDVMNRFGSDKPDLRVPLEMQDVTELFVGSSFKVFASNTKEGSCIKAMVLKGRGTESRQFYDKAEKRARELGAPGLAYVQYREEGPKGPIVKFLSEAELSALQERLAIETGDVVFFGAGKWEKTCKIMGGIREYFSDLFELDRDELSFCWIVDFPLYEFDEKESRIDFSHNPFSMPQGEMDALDTMNPLDILAYQYDIVCNGIELSSGAIRNHRPDIMYRAFEIAGYSKEEVDKRFGHMIEAFKMGAPPHGGIAPGLDRLVMILRDEHNIREVIAFPMNQQAQDLMMSAPSDVSRLQLRELHLKLDLPVETAEQEPG	Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).	B4S8V2
P06799	IFNA7_MOUSE	Interferon alpha-7	Mus	MARLCAFLMVLAVMSYWPTCCLGCDLPQTHNLRNKRALTLLVKMRRLSPLSCLKDRKDFGFPQAKVDAQQIQEAQAIPVLSELTQQILNIFTSKDSSAAWNATLLDSVCNDLHQQLNDLQGCLMQEVGVQELSLTQEDSLLAVRKYFHRITVFLREKKHSPCAWEVVRAEIWRALSSSANLLARLSEKKE	Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.	P06799
Q133T3	THIC_RHOPS	Thiamine biosynthesis protein ThiC	Rhodopseudomonas	MNIRSNPDTTRPAVTTGGLPSSKKIYATPAAAPDLRVPLREIILSEGAGEPNLPIYDTSGPYTDPSVTIDVNAGLSRARTQWVKERGGVEEYQGRDVKPEDNGNVGAAHAAKSFTAYHKPLRGIGDAPITQYEFARRGIITKEMIYVAERENLGRKQQLERAEAALADGESFGASVPAFITPEFVRDEIARGRAIIPANINHGELEPMIIGRNFLTKINANIGNSAVTSSVEEEVDKMVWAIRWGADTVMDLSTGRNIHTTREWILRNSPVPIGTVPIYQALEKCEGDPVKLTWELYKDTLIEQCEQGVDYFTIHAGVRLQYIHLTANRVTGIVSRGGSIMAKWCLAHHKESFLYTHFDEICDLMRKYDVSFSLGDGLRPGSIADANDRAQFAELETLGELTKIAWAKGCQVMIEGPGHVPMHKIKINMDKQLKECGEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGCAMLCYVTPKEHLGLPDRNDVKVGVITYKIAAHAADLAKGHPAAQLRDDAVSRARFDFRWQDQFNLGLDPDTAQAFHDETLPKDAHKVAHFCSMCGPKFCSMKITQDVRDYAAGLGDNEKAALYPAGSVGMSISGVIEDGMAQMSAKFRDMGEHLYLDAEKVKESNKALS	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.	Q133T3
Q03QT7	TRUB_LEVBA	tRNA-uridine isomerase	Levilactobacillus	MNGIIPLYKERGLTSFDCVAKLRHILQTKKVGHSGTLDPSVDGVLPICIGSATKVVPYLMASGKVYRGSVTLGLATTTEDLDGDVVERQPLERPFTADQVAAAAQALTGTIQQTPPMYSAVKVNGRKLYEYARAGETVERPTRTITVDRFDLQGAGTFDATAGTQTIDFEIACSKGTYVRTLAVDLGQQLGVPAVMATLTRLKSGGFTLSQTVTLADVEAAMADDQIERTLRPIDYALQDYPHVALDEHLWALVKNGVFLSAAELNQATEPELALTYQGETKCLYRWSDEKKQYRPLKMFAVN	Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.	Q03QT7
Q66HD6	LRC18_RAT	Leucine-rich repeat-containing protein 18	Rattus	MAKGGKSPKGKKITLNVAKNCIKITFDGRKRLDLSKMGITTFPKCILRLNEIDELDLSRNMIRKIPDSISKFQNLRWLDLHSNYIDKLPESIGQMTSLLFLNVSNNRLTTNGLPVELNQLKNIRTVNLGLNHLDSVPTTLGALKELHEVGLHDNLLTSIPAGISKLPKLKKLNVKRNPFPKPDESDMFVDSIKRLENLYLVEEKDLCSSCLQKCQQARDKLNKIRSMAPSAPRKAIFSNLVSPNSTAKESQEEWSV	May be involved in the regulation of spermatogenesis and sperm maturation.	Q66HD6
Q42564	APX3_ARATH	L-ascorbate peroxidase 3	Arabidopsis	MAAPIVDAEYLKEITKARRELRSLIANKNCAPIMLRLAWHDAGTYDAQSKTGGPNGSIRNEEEHTHGANSGLKIALDLCEGVKAKHPKITYADLYQLAGVVAVEVTGGPDIVFVPGRKDSNVCPKEGRLPDAKQGFQHLRDVFYRMGLSDKDIVALSGGHTLGRAHPERSGFDGPWTQEPLKFDNSYFVELLKGESEGLLKLPTDKTLLEDPEFRRLVELYAKDEDAFFRDYAESHKKLSELGFNPNSSAGKAVADSTILAQSAFGVAVAAAVVAFGYFYEIRKRMK	Plays a key role in hydrogen peroxide removal.	Q42564
Q5NBT9	TPR1_ORYSJ	Topless-related protein 2	Oryza sativa	MSSLSRELVFLILQFLDEEKFKETVHKLEQESGFFFNMKYFEEKVHAGEWDEVEKYLSGFTKVDDNRYSMKIFFEIRKQKYLEALDRHDRAKAVDILVKDLKVFSTFNEELYKEITQLLTLENFRENEQLSKYGDTKSARSIMLIELKKLIEANPLFREKLVFPTLKASRLRTLINQSLNWQHQLCKNPRPNPDIKTLFTDHTCTPPNGARASPVSVPLAAVPKAGGTYPPLTAHTPFQPPPAGPSLAGWMANAAAATSSVPSAVVAASSLPVPPNQAVPIMKRPTITDYQSAESEQLMKRLRPSGHGVDEATYPAPIPQPLWSVEDLPRTVACTLSQGSSVTSMDFHPTRHTLLLVGSTNGEITLWEVGMRERLFSKPFKIWDIQACSPQFQSVAKESSISINRVTWSPDGDLIGVAFAKHLIHLHAYQQPNETRQVLEIDAHSGAVNDIAFSRPNKQLCVVTCGDDRLIKVWDMHGQKLFSFEGHEAPVYSICPHHKESIQFIFSTSLDGKIKAWLYDHMGSRVDYDAPGKWCTTMLYSADGTRLFSCGTSKDGDSYLVEWNESEGSIKRTYSGFRKKSAGVGVVQFDTAQNHILAAGEDNQIKFWDVDNTTMLSSTEADGGLPGLPRLRFNKEGNLLAVTTVDNGFKILANADGLRTLRAFGNRPFEAFRSQYEASSMKVSGAPVVAGISPNIGRMDHIDRNSPAKPSPIMNGGDPASRSIDIKPRISEERPDKAKPWELMEVLNAQQCRVATMPETPDQASKVVRLLYTNSGVGLLALGSNAIQRLWKWARNDQNPSGKATANVVPQHWQPNSGLVMQNDTADTNPEDAVPCIALSKNDSYVMSACGGKVSLFNMMTFKVMTTFMPPPPASTFLAFHPQDNNIIAIGMEDSTIHIYNVRVDEVKTRLKGHQRRITGLAFSNNLQILVSSGADAQLCVWATDTWEKKKSVAIQMPAGKTPSGDTWVQFNSDWSRLLVVHETQLAIYDASKMERIYQWIPQDALSAPISHASYSRNSQLVFAAFTDGNIGIFDVENLRLRCRIAPPAYLSSAAINSNPSVYPLVVAAHPQESNQFAVGLSDGSVKVIEPLESEGKWGTTPPTENGVPNGRTSTSSATSNPAADQIQR	Probable downstream regulator of strigolactones signaling.	Q5NBT9
Q9VE86	WRNXO_DROME	Werner Syndrome-like exonuclease	Sophophora	MEKYLTKMPIKSKANEVPKEEAGVKKETPKVARKATKKDTPKELKDKENAGDDNTPKQTKGRPGRPAAKRKNLDTPDVTEKLAMEEENPPKRRSSRLTRSTRSMAEDGSPSPEKEKPEKLPFIKYKGAIKYFTESQDIAASADDVLQWVEKQKDEVVPMAFDMEWPFSFQTGPGKSAVIQICVDEKCCYIYQLTNVKKLPAALVALINHPKVRLHGVNIKNDFRKLARDFPEVTAEPLIEKCVDLGLWCNEVCETGGRWSLERLTNFIAKKAMDKSKKVRMSKWHVIPLDENQLMYAAIDVYIGQVIYRELERREKVKIKNEEEFKEKNGDAAFKAMKALGETFLTKINEVTL	Has exonuclease activity on both single-stranded and duplex templates bearing overhangs, but not blunt ended duplex DNA, and cleaves in a 3'-5' direction . Essential for the formation of DNA replication focal centers . Has an important role in maintaining genome stability .	Q9VE86
Q7M8Z6	HSLV_WOLSU	ATP-dependent protease subunit HslV	Wolinella	MFEATTILAYKGENHSVIGGDGQVTFGNCVLKGNATKIRMLYNGKILSGFAGSTADAFTLFEMFERILENRKGDLVKSVIDFSKEWRKDKYLRRLEAMMIVMDRERLFILSGTGDVVEPEDGKIAAIGSGGNYALSAARALDKFADLPESELVRESLLIAGELCIYTNTNIKLLEL	Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	Q7M8Z6
C1CVC5	NUSB_DEIDV	Antitermination factor NusB	Deinococcus	MTRRREKAVQPVGTRRAAREFVFRVLFEADRGDLPLDTVFTRAEGAMREGDDTFPQLSADALTFANELVRGLEKHRADIDTTLRRTIRGWSFDQMAQTDLNVLRLATFELIYTAEPHPPVIESAVRIARKFGGDDSGRFVNGVLAGLSRSLQSAGVAKADEQADTAQD	Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.	C1CVC5
Q99KW3	TARA_MOUSE	Trio-associated repeat on actin	Mus	MSMEQDTRALLPTQGTAWATASAPVARLQGPQGDSHQACSQEPHSPSSAEAPYCDLPRCPPALQNPLRTTTCVGQSVHSLGLGLGQEPQRVWSPTTALPAEGPAAAPKNRHQDSEGIPYLEGLARSSCTDDNDNKDEDEDPNSNTSSSQDSNTPHDTSNSSSVDWDTTERPGVVPSRNRLTEMIPRRPQEGLRADSARKATRSPARGDTAGQRKENSGSGGQSAGQHWAKLRSESGYFSLERQRSGQTQASSGTPPSGPRGTTQASSAQRDVFQAAPAQEAPQTSSLPRNTQRDTQRSTPRTSSPSRVSQRDTPRVMSTQRKNTPLSSPLRATPETLKISAPEDGTHVTPSPCVQDSSLNRTSQRDSSRTPCIQWDNPRASSPNRTTQRDNPRTPCTQRDNPRASSPNRTTQRDNPRTPCTQRDNPRASSPNRTTQRDNPRTPCAQRDNPRAASPNRSTQRDSPRTPCAQRDNPRASSPNRTAQRDNPRTPCAQRDNPRTSCTSQNTPRTPSTQADKTTASCSKWEHLRSACTQRDNPRTFSQGCTQKDNPGPPSPRRATQGSNSRNPSPHRTNKDIPWASFPLRPTQSDSPRTSSPSRTKQNQVPWASISLRPTQGDKPQTSAPTRLAHNDPPQQYSPSLATTSSSSHNPGHSSASRTSSPLHAAPRGAPQTSLESSQPPCTVCIGHRDAPRASSPPRYFQYDPFPFFPDPRSSESESPHHEPPYMPPAVCIGHRDAPRATSPPRHTQFDPFPFLPDTSDADNESPQHDPPQFPPPVCIGYRDAPRASSPPRQFPEPSFFQDLPRASTESLVPSTDSMHEPPHIPTPVCIGHRDAPSFSSPPRQAPEPSLFFQDPPGTSMESLAPSIDSLHGCPLLPPQVCIGHRDAPRASSPPRHPPSDIGLLAPSPPPGSSGSRGSAPPGETRHNLEREEYTMLADLPPPRRLAQRGPEPQAQGSNEGRTRSPGRAEVERLFGQERRKSEAPGAFQTRDEGRSQRPSQAQSQLRRQSSPAPSRQVTKPSAKQAEPTRQSRTGPPHPKSPDKRPEGDRQLQRTSPPARTPARPPERKAQIERHLESGHTGPRQSLGGWQSQERLSGPQSPNRHPEKSWGSQKEGPSLGGWPELEGPSLEGIWRGPPQEHREQWGHSEAWEEPPSNGIQGAPPRGQGRLQELSRPHQPTPSSENSWAGPAECSCALQPEASTAVGWRAEGTSPHQRSAERPPDLDWRDLLGLLRAPEDGAWTRLPRLDWEGLLELLQARLPQKDPARHWHDPAKASGPEQGSSGTEDTLKTEPQTQPEGRAKATLANGHRPGQQSESPAQLPSPACTSTQWPTTKVTSGPETSPLAALEQIDHLESHSPPDLEFQPEEPEASEPSRGEDSRAVQKQADSADKRPAEGKAGSPLKGRLVTSWRMPGDRPALFNPYLLSLGVLRWQRPDLLNFKKGWMSILDEPGEWKKHWFVLTDSSLKYYRDSTAEEADELDGEIDLRSCTDVTEYAVQRNYGFQIHTKDAVYTLSAMTSGIRRNWIEALRKTVRPTSAPDVTKLSDCNKENTLHGYGTQKSSLKIGEQRTGSEVIGRGGPRKADGPRPSLDYVELSPLAPSSPQRMRTLSRSTPERPTKQEDLERDLAQRSEERRKWFESTDGRTPETPSGDGSRRGLGAPLTDDQQSRLSEEIEKKWQELEKLPLRENKRVPLTALLNQAHNDRRGPTSDSHEALEKEVQSLRAQLEAWRLRGEAPQNAPRLQEDSHIPPGYISQEACERSLAEMESSHQQVMEQLQRHHERELQRLQQEKEWLLAEETAATASAIEAMKKAYQEELSRELSKTRSLQQGPESLRKQHQLDMEALKQELQVLSERYSQKCLEIGALTRQAEEREHTLRRCQQEGQELLRHNQELHSHLSEEIDRLRSFIASQGTGNSCGRSNERSSCELEVLLRVKENELQYLKKEVQCLRDELQVIQKDKRFTGKYQDVYVELNHIKTRSEREIEQLKEHLRLAMAALQEKEAVRNSLAE	May regulate actin cytoskeletal organization, cell spreading and cell contraction by directly binding and stabilizing filamentous F-actin. The localized formation of TARA and TRIO complexes coordinates the amount of F-actin present in stress fibers. May also serve as a linker protein to recruit proteins required for F-actin formation and turnover.	Q99KW3
B1VGB7	RIMP_CORU7	Ribosome maturation factor RimP	Corynebacterium	MATPLDEKLRALAADEAMKCGLDVEKLTFTRAGAKSSVKIAVDADERPDLDLLEEASQLIGAAFDAAEEAQQIDLGPSYTLEVTTPGLDFPLREARNFQRNIGRLANLPGGGKGRIAAVENDEVAILPAAKKKAGKKSQGKKAGKKTPQAPVQIYPRAELAGSTIEVEFSPAPAAEQELLGLTMAEYHELAKSDEA	Required for maturation of 30S ribosomal subunits.	B1VGB7
P81646	LALBA_TACAC	Lactose synthase B protein	Tachyglossus	KVFEKCELSQMLKANGLDGFQGITLEEWICIAFHESGFDSRALNYYNGSSSHGLFQINRQYWCDGQDAKSTEPSVNACQISCDKLRDDDIEDDIKCVKKILKESQGITAWEAWQPFCIADLDQWKC	Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.	P81646
Q18DH0	HIS3_HALWD	Phosphoribosyl-AMP cyclohydrolase	Haloquadratum	MTDDAVTGSQDDAEIEIRFNSDGLVPAIAQDADSGEVLMLAYVSPTALKRTRETGQAHYYSRSREELWKKGETSGHTQHIREIRADCDADTILYLVEQTGGACHTGHQSCFYRTLDGTEVTERVFDPETVYE	Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.	Q18DH0
A3QGA2	EFTS_SHELP	Elongation factor Ts	Shewanella	MAITAAQVKELRERTGAGMMDCKKALTETNGDIELAIENMRKSGAAKAAKKAGNIAAEGTILIKQGEGFSVLLEVNCQTDFVAKDSNFLAFANEVLDVAAAGKVSIADLQAQFEETRVALVAKIGENINVRRVEYIDGASQASYRHGDRIGVVVTGEADEETLKHVAMHVAASKPEYVNPSDVPAEVVEKEKAVQIEIAMNEGKPQEIAEKMVAGRMKKFTGEVSLTGQAFIMEPKKTVGEILKEKGATVTNFIRLEVGEGIEKKEEDFAAEVAAQIAASKA	Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.	A3QGA2
B3E8Z1	GLGC_TRIL1	ADP-glucose synthase	Trichlorobacter	MFDGSNLGRNTIAMVLAGGKGERLMPLTLRRAKPSVTFGGKYKIIDFVLSNLFNSGIRRMYILTQYRAYSLNKHIRESWGKWTGLGEFCVAISPETSSDSEQWFKGTADAILQYLRFVETADADYVAVFGGDHIYKMDVTQMIQFHRMNRADLTIASLEVPKEEASRFGVFSVDDDNRVTAFTEKPKDPETIPGRETCFASMGNYIFPTRKLIEVLLEGKKHYEDLDFGKHVIPMMLEKGDRIYAYNFNDNLVPGMKSEERGYWKDVGTLDSYYEANMDLIHVSPQLNLYNYKWPILTNQGNLPPAKTVFDEEGRRGVNIDSYVTGGCITSGSTVRRSILGPMCKINSYSLVEDSILFEGVTVGRHVKIKKAIIDKGVVIPDGAEIGCNHEDDIKNGYTITESGIVVVPRKDR	Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.	B3E8Z1
B3EWS6	TXC12_CUPSA	CSTX-12 B chain	Cupiennius	MKVLVICAVLFLTIFSNSSAETEDDFLEDESFEADDVIPFLAREQVRSDCTLRNHDCTDDRHSCCRSKMFKDVCKCFYPSQRSDTARAKKELCTCQQDKHLKFIEKGLQKAKVLVAG	Synergistic toxin that induces or increases a cytolytic effect when combined with CSTX-1 (AC P81694) or CSTX-9 (AC P58604). When alone, has a weak insecticidal activity, with an unknown molecular target.	B3EWS6
Q4ZWV2	KAD_PSEU2	Adenylate monophosphate kinase	Pseudomonas syringae	MRVILLGAPGAGKGTQAKFITEKFGIPQVSTGDMLRAAVKAETELGLKAKSVMDSGGLVSDDLIIGLIKDRLAEPDCANGVLFDGFPRTIPQAEALLNAGLEIDHVLEIAVDDEEIVKRMSGRRVHEGSGRIYHTIFNPPKVEGIDDVTGEPLLQRKDDVEETVRHRLSVYHAQTKPLVEFYSKLEAKNGKPKCSHIPGVGSVEDITAKVLKALS	Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.	Q4ZWV2
Q8DHM0	SSRP_THEVB	Small protein B	Thermosynechococcus	MGDSIKVLSENRQARFQYEILETYECGLVLLGTEVKSIRAGKVNLRDGFARIRNGEAWLMNVHISPHESTNPSYNHDPLRDRKLLLHKQEIRKLVGKVEQKGLTLVPLKLYLKNGRVKVSLGLARGKKLHDKRQDLKQRQDKREMERAMKQR	Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.	Q8DHM0
Q2R222	C6_ORYSJ	Non-specific lipid-transfer protein C6	Oryza sativa	MAPSKSTAAAGVLLVLLVAAAGGGAEAAATTCVASLLELSPCLPFFKDKAATAAPEGCCAGLSSIVKGEAVCLCHIVNHTLERAIGVDIPVDRAFALLRDVCRLSPPADIISTCANEKGGVPPLYSCPAPSA	Lipid-transfer proteins that possesses lipid-binding activity in vitro. Involved in the development of lipidic orbicules/Ubisch bodies and pollen exine during anther development . May be regulated by the transcription factor UDT1 in developing anthers and play a role in tapetum development . Positively regulated by the transcription factor TDR in developing anthers and may play a role in tapetum programmed cell death (PCD) .	Q2R222
P61704	SYA_MYCMS	Alanyl-tRNA synthetase	Mycoplasma	MKKLSTNQIRKIWLDFFISKNHYFLETVSLIPVDDPSLLWINSGVATLKPYFDGRKTPPSPRLTNSQKAIRTNDIENVGVTARHHTMFEMLGNFSIGDYFKKEAIELAWELLTDKKYFDIDKNKLYITVFNEDTEAYNIWKDVIKIDEDHIFRLSRKTNFWDVGQGPCGPNTEIFYDRGEIWDPNKIGPRLISDDIENDRYIEVWNIVFSQFNNDGNNNYVELPRKNIDTGAGLERFASIFQNTPTNFETDIFYPTIKKVEQLTNNQFKYSIDNYFNPNKKQTRINTAFKVIADHIRATVFAISDGVFPGNKDRGYIIRRLIRRSCVFGKELGIKQAFLYKLVDSVIESMKEFYPYLIDKKTLVEQTIKDEEEKFLKTLSKGYDLLENIIKTKNTVSDKDALLLFESYGFPIEQTIEISELSNVTVDVEGFKKLLEQTKQATRNARKDLKAWDKQNELFTKLKVESEFTGWSETSRDNAKVIYMFTDQKQVESITNQEVFVILDKTPFYAEKGGQAADSGIIFNDQMKGFVIDVQQGPTHQNIHRIKVQGTLKVNDLINCRVDEEKRIYTMKNHSGTHMIHYALREVLGTSVMQSGSYNDENGLRMDFTYHRLPTNQELLKAQNLVLEKIKNKIDRQTYFCSLEESVKKHQALAFFTEKYDQIVRVIKFGDFSSELCGGTHVNNTSEIEDFIITGIESKGSGLYRIKCLTSFRAVNEYLNEQFKVYKDQAESIIDKYNQNKDLLKNDQLENIYLQIKNTTINKDNLLVIKNLLDQSKEVNKDYDKKVNDLITANKLLKYKDLTPSLNKDNINEIRLETTDLNIKDLKQLADDLRNKYNDLIVILLSSTNENTFIVVAVSQSLQNKYKAIDIFNNLEGYETKGGGNANLAQGKFVKK	Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.	P61704
P33546	ICSB_SHIFL	N-epsilon-fatty acyltransferase IcsB	Shigella	MSLKISNFIDASNTKGPIRVEDTEHGPILIAQKFNLKDLFFRTLSTINAKINSQILNEQLKNYRLENQKSLLLFLNTLASEKSAESAFAAYEAAKNSIQHSFTGRDIKLMLNTAERFHGIGTAKNLERHLVFRCWGNRGITHLGHTSISIKNNLLQEPTHTYLSWYPGGNVTKDTEINYLFEKRSGYSVDTYKQDKLNMISEQTAERLDAGQEVRNLLNSKQDQNNNKKIFFPRANQKKDPYGYWGVSADKVYIPLSGDNKTKDGKISHNLFGLDETNMSKFICKKKADAFRQLANYKLISKSENCAGMALNVLKAGNSEIYFPLPDVKLVATPNDVYAYANKVRQRIESLNQSYNEIMKYIESDFDLSRLTQLRRSYLKSFNKINLIHTPKTFKPLSISLYKHPTENVSSEDFDAVINACHSYLVKSAPSNMTRVLNELKTEATDKKEEIIEKSIKIIDYYNSLKSPDLGTKLYIHDLLQINKLLLNNSHSNI	Virulence-associated N-epsilon-fatty acyltransferase that mediates lysine-stearoylation of host Rho GTPase proteins, thereby disrupting the host actin cytoskeleton . Required at the post-invasion stage of Shigella pathogenicity .	P33546
Q7JZV0	LCP2A_DROME	Larval cuticle protein 2A	Sophophora	MKFFIAFACLLAVALANEDANVLRAEQQVNVDGFAYAVELDNSVNVQQKGDLNGEEWVVKGSQSWTSPENVPVSIQYIADANGYQVVSANPPLPTPPPIPEAIQRSLEYIAAHPPSQ	Component of the larval cuticle.	Q7JZV0
Q92LB3	PROB1_RHIME	Gamma-glutamyl kinase 1	Sinorhizobium	MTKARKALENYRRVVIKIGSALLVDRRTGLKKSWLDALCADIAALRAKGVEVLVVSSGAIALGRTVLDLPAGALKLEESQAAAAVGQIVLARAWSESLSTHAIVAGQILLTLGDTEERRRYLNARATIGQLLKLGSVPIINENDTVATTEIRYGDNDRLAARVATMVGADLLVLLSDIDGLYTAPPHLDPNARFLETVAEITPEIEAMAGGAASELSRGGMRTKIDAGKIATTAGCAMIIASGKPDHPLAAIEAGARSSWFAPSGSPVTARKTWIAGQLLPAGSLSIDAGAETALRSGKSLLPAGVRQVTGSFSRGDTIAIIGASGREIARGLAGYDADEARQIAGKKSAEIAAILGYAGRTAMVHRDDLVMTAPSGARLVEESDEGKGKLHA	Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.	Q92LB3
Q12420	SNU66_YEAST	66 kDa U4/U6.U5 small nuclear ribonucleoprotein component	Saccharomyces	MNKTENLSIEETNEIREKLGMKPIPVFQEKNTDHKESLSIEETNELRASLGLKLIPPQQNFNSSPPNVHNTSKIDELREKITKFQKKANAPLRMAHLLEETNVNDDSSWLENMDAIPSSHESKRSSTLPRKGATKEDENIDLHNVQVSYNIEALSPKKDTILTLKESSIFDDTDSTEVLENVKAAEENADREKLRLRQMNKDRRQKKKILNVSSLDIEEEEEGEKHSITTTHLIIGAEQGVMKAPNTISAKPPTGKVKVNFDSANNMSDEDGGDFKPLKIKKRKIKDPRSTKARKSKITDKMEIVKLVDEDESLSWMEEEQPVTIINPRTSSNNELKGPEDLAREIEKARDEEKRRTESILKMREISNSIVVDEKVTFLNTLDTSLSERSATENKVKVHGEGEKNIGDVTNGHTKEGSGNNTLTEAVNNEPNYEGDAENAPNFFSGLASTLGYLRKKSVFTTGDVDLKPGKDVNNSESLRRDVRNKEHTGTGTYTKDKLHGLEQFTSSDSSNANTHSKRQDHYDPDIKLVYRDEKGNRLTTKEAYKKLSQKFHGTKSNKKKRAKMKSRIEARKNTPENGSLFEFDDN	Component of the U4/U6.U5 tri-snRNP particle, one of the building blocks of the spliceosome. Required for pre-mRNA splicing.	Q12420

A5CSL4

MIAA_CLAM3

Isopentenyl-diphosphate:tRNA isopentenyltransferase

Clavibacter

MIPIVAVVGATGTGKSGLSLDIADRLRAQGRVAEIVNADAMQLYRGMDIGTAKLPEAARRDVPHHMLDVLDVTAEATVAGYQGEARRVITGILGRGAVPILVGGSGLYVSSVLFDYEFPGTDPEIRQRLERELAETGPGMLHRRLRELDPAAAQRIGAHNGRRLVRALEVVEITGPQPERASAEPRPWHPARILALTLPREELVPRLDARVSGMWADGLVDEVAGLLPAGLADGVTASRAIGYAQAARQLAGELTEEEAMEETRALTRRYARRQVSWFGRYADAVRLDARDERLLEHALDALPAARP

Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).

A5CSL4

P29685

ATPBM_HEVBR

ATP synthase subunit beta, mitochondrial

Hevea

MASRRLLSSLLRSSSRRSVSKSPISNINPKLSSSSPSSKSRASPYGYLLTRAAEYATSAAAAAPPQPPPAKPEGGKGGGKITDEFTGKGAIGQVCQVIGAVVDVRFDEGLPPILTSLEVLDHSIRLVLEVAQHMGEGMVRTIAMDGTEGLVRGQRVLNTGSPITVPVGRANPWTYHEVIGEPIDERGDIKTSHFLPIHREAPAFVDQATEQQILVTGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKLGDKQADSKCALVYGQMNEPPGARARVGLTGLTVAEHFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLATDLGGLQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQRFLSQPFHVAEVFTGAPGKYVELKESITSFQGVLDGKYDDLPEQSFYMVGGIDEVIAKADKIAKESAS

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

P29685

P75053

DEOD_MYCPN

Purine nucleoside phosphorylase DeoD-type

Mycoplasma

MTPHINAKKDDIAKVVLMPGDPLRAKWIAEQFMEKPRLVNEVRGMLAFTGQYKGKTITIMGHGMGIPSIGIYSYELMKFYEVNTIIRIGSCGALQGSLNLQDLIIAAKAWSESIYANDMGVEVPADKILMASPQLVELAKKTANQLQLAFHEGLVFCEDAFHQIRKDVLKLAQEKHALAVEMEAHALYANAMLLNKQALTMLTVSDSLVTHAALPAEQRQATFKNMAILSLEMASQLV

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.

P75053

Q88RX5

MNME_LACPL

tRNA modification GTPase MnmE

Lactiplantibacillus

MPTTTEFDTIAAISTPPGEGGISIIRISGDQTFNVVTQIFKGKDLSRVQSHTINYGHIVDPDTHQEVDEVMATVMRAPKTYTREDVVEINCHGGLVATNEILQLILSHGARMAEPGEFTKRAFLNGRLDLSQAEAVMDLIRAKTDKSMKVALNQLDGDLSKLIRHLRQDILDVLAQVEVNIDYPEYDAVETMTTKMLKEKATEVAQSINQLLATAKQGKVLREGLATAIIGRPNVGKSSLLNHLLHEDKAIVTDVAGTTRDVIEEYVNVRGVPLKLVDTAGIRDTEDKVEKIGVERSRKAIGAADLVLLVLDNSQPLTAEDRELLQETDQSKRIVILNKTDLPARLDQAELAQLVDLSDVLSMSVLEQSGVTQLEQRIAKMFFNEGIESSQNNVMVTNARHIGLLNQAKQALQDVQTGLAAGMPVDLVQIDMTRCWEFLGQITGDSYEDELLDQLFSQFCLGK

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.

Q88RX5

Q5FW14

CHMP7_XENTR

Chromatin-modifying protein 7

Silurana

MAALSCYPPEWDDDERMSFLFSAFKQTRDVNTSDWDGKMKFWIPLILKHARAQGLLSISLSQLERDFRRKGFAPLGLRIVIQEMMRQGTLRKESDYVSNVSSGWLSWGMRQLVIRPLRWTIGTVLGSQMGPDEPLVIPEIIKERAALVLQRYQSSPLRALPLLSEEEVRTLCAEICPNPSALNLVLLQLQGDKKICVLERAGKKLVKFVRVSVGQVDPISESDLGIYELQQSEKLLSERLQSAGEESDRLTEEARTYNRAGNKHQALRCLRKRKLLERRITELQNKQDTVQGILERIAAAETDRKVVSAYQMGVSALKLALKDVTMEKAESIVDQIQEYCDLQDDLSQTLASVSDADIDSEDLEKELNDILQNKEMIVDLPDVPSGPVVISPQRPTEWETDQDIDSEDLEKELNDILQKEEMIVDLPDVPSGPVVISPQRPTEWKTDQASRSPADGSFSRSVPEPVLQ

ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope during late anaphase. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Plays a role in the endosomal sorting pathway.

Q5FW14

Q7NF26

PSAD_GLOVI

Photosystem I reaction center subunit II

Gloeobacter

MADVKELPFGGSTPLFGGSTGGLLRKAQIEEKYLIVWNSKEEQVFEMPTGGAATMVAGTNVLYLARKEQCHALHRQLVSTFKIRDSKIYRVYPNGEQVLIFPMDGVPSEKSNPGREVVGYVPRKIGDNPNPVDVKFTGKETFDV

PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center.

Q7NF26

Q4QN00

IF1_HAEI8

Translation initiation factor IF-1

Haemophilus

MAKEDCIEMQGTILETLPNTMFRVELENGHVVTAHISGKMRKNYIRILTGDKVTVEMTPYDLSKGRIIFRSR

One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.

Q4QN00

C4LBX3

PYRI_TOLAT

Aspartate carbamoyltransferase regulatory chain

Tolumonas

MSEKKQLQVEAICNGSVIDHIPAGQGIKILKLFHLLDTRQRITVGLNLPSAALGSKDLIKVENTQLTADQANQLALFAPQATVNIIEDFKVVTKHQLELPGEIVGVFACPNSNCISHREPVRSRFGVRSTQGEVRLKCHYCEKSFTKEIVSEAF

Involved in allosteric regulation of aspartate carbamoyltransferase.

C4LBX3

P67595

SYW_STRPN

Tryptophanyl-tRNA synthetase

Streptococcus

MTKPIILTGDRPTGKLHIGHYVGSLKNRVLLQEEDKYDMFVFLADQQALTDHAKDPQTIVESIGNVALDYLAVGLDPNKSTIFIQSQIPELAELSMYYMNLVSLARLERNPTVKTEISQKGFGESIPTGFLVYPIAQAADITAFKANYVPVGTDQKPMIEQTREIVRSFNNAYNCDVLVEPEGIYPENERAGRLPGLDGNAKMSKSLNNGIYLADDADTLRKKVMSMYTDPDHIRVEDPGKIEGNMVFHYLDVFGRPEDAQEIADMKERYQRGGLGDVKTKRYLLEILERELGPIRERRIEFAKDMGEVYNMIQKGSERAREVAGQTLSEVKGAMGLHYFN

Catalyzes the attachment of tryptophan to tRNA(Trp).

P67595

P07997

HEM1_CHICK

Delta-aminolevulinate synthase 1

Gallus

MEAVVRRCPFLARVSQAFLQKAGPSLLFYAQHCPKMMEAAPPAAARGLATSASRGQQVEETPAAQPEAKKAKEVAQQNTDGSQPPAGHPPAAAVQSSATKCPFLAAQMNHKSSNVFCKASLELQEDVKEMQVDRKGKEFAKIPTNSVVRNTEAEGEEQSGLLKKFKDIMLKQRPESVSHLLQDNLPKSVSTFQYDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDYSDSLITKKEVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAKMLPGCEIYSDSGNHASMIQGIRNSRVPKHIFRHNDVNHLRELLKKSDPSTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGGIGDRDGVMHKMDIISGTLGKAFACVGGYISSTSALIDTVRSYAAGFIFTTSLPPMLLAGALESVRTLKSAEGQVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPIRVADAAKNTEICDKLMSQHSIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSYFLEKLLATWKDVGLELKPHSSAECNFCRRPLHFEVMSERERSYFSGMSKLLSVSA

Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products.

P07997

A0A411PQN2

AGN11_PAEDI

Agnestins biosynthesis cluster protein L11

Paecilomyces

MKRSFDASHGQLEKQSRPRQVPTSCHFCRTKKLKCDRRFPCSNCRARRLSCVPFSDRSQAASLDLPGAGPSSTVSNEELSENINELKARLQRLEELISVNAEEKLDSKGPTSFVTSKGGYGEDVEASKSMNSLEMDAFEHQPLHSNSEERIAQLFASSFVSIIAPAIRLVIDQPTLSLLPSRKQAERLFDYFADQVVVFYYFIHVPTVRSMLDTVYTHLENKRQPQHDHLALLSTVFALSAYFGSSSSRFPFNGAEAKMLCYRWISVAQQALCAANYIVQPTVETLQSVILIAAYLVPNLGSMSIFRVLMASALQGALQLSLHQIDSPANQRRRQNATVNWVDIESKRRIWWHLASTDWIVSFMSGPRCGTYMIHPKQMTVDLPTNVDDQDIRPAGNYAQPLENAPTDMTFSILRTRISVIFREIVDAATDSGCLQEELPYDVVLAFDHRLHGIMADAPACFRTDPRSSRAPSRSPDLRLHRLIANALNRLHRPYLARGARDPKYSYSRMVCLRTARSVIELCKEMTGANEEFQHVKMWTIVHPLFNSVLVLVMDYCLNREEPRGDERKAEILEGFRLLEACQEDSALAQRGLQQMRQLLKGSASARKDKNPIHGDTDRATPPGSSNLPQHDKSSSSSPAPPVWPCLWTDPDLAPLETMDFDVDLDESQFEVLFRDFEGRHPMY

Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of agnestins, dihydroxy-xanthone metabolites.

A0A411PQN2

A7I008

RS18_CAMHC

30S ribosomal protein S18

Campylobacter

MADKRKYTRKYCKFTEAKIEFIDYKDTALLKYCLSERFKIMPRRLTGTSKKYQEMVEKAIKRARQAALIPYIVDRDNVVVNPFEILG

Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.

A7I008

Q81VQ1

ECFA2_BACAN

Energy-coupling factor transporter ATP-binding protein EcfA2

Bacillus cereus group

MEITFQKVEHRYQYKTPFERRALYDVDVSFPSGGYYAIIGHTGSGKSTMIQHLNGLLQPTNGTVQIGEHFISAGKKEKKLKPLRKKVGVVFQFPEHQLFEETVEKDICFGPTNFGVSEEAAKQKAREAIELVGLEPELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGQNELMEMFYKLHKEKGLTVILVTHNMEDAAKYAEQIVVMHKGTVFLQGSAEEVFSHADELEKIGVDLPMSLKYKRAIEEKFGISIPKATLSLEDLTHEVVQVLRKGGHESCSS

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.

Q81VQ1

P0DJ01

P35_MALPE

Lipoprotein p35

Malacoplasma

MKIKKIKLLKALALTGAFGIVATVPVIVSSCSSTSENNGNGNGNGGTDGNTQQTEVTPAIKSEVSLTGALSKIYDTKTGTDRETTSQLIVKDIKANPENYFTNGEALKDVIASATVTVDGGFTESTFTGEAYSVWSAKADVKKGTYSQASKQLDIKSINDLQTVLGDSAAIKGICDLIPNLKLNNGTDYKVTNNGLSLSEDLLHINVTAKDGQTDVSMDLAIPVSDLNLKIDGLKISVSGTGIKTSELTTNYKFNIGIDNTVKTLTPAAVTLAEADRTNAEKVLEKLGYATVSGSTYTLDQDKLADALGLYNCKFEAVKSEKDSTNNNKYTVTLKATPNDGYFWEDGTNGAKEEISFVATFS

Major M.penetrans antigen.

P0DJ01

Q0W131

DHQS_METAR

3-dehydroquinate synthase II

Methanocella

MSDKLVWIDAQGSWNGAKEKVTGALESGANAVLVSPENVERVRELGKMTVAAAEGNPDIRVIGIGSEGDGTLFLPHDLNSSEDMATAKALKAQGTTTAAYVRLAGKEYEQFAARMGKLCDYLIIEGDDWKVIPLENLIAELGGSGTKILAKARDIDEASVALQTLEKGADGVLVDVDDPLKVREIARAVSTKQAGLGLTPVTITAVRDAGTGDRVCIDTCSLMTPGEGMLIGNQSSGLFLVQSEAEESPYVASRPFRVNAGAVHEYVLVGEKTRYLSELASGDPALIVTRDGDARKATIGRVKIERRPLLYVEAETGDRKISAILQNAETIKLVAADGSSTPVTALKPGDRVLAKLEKEARHFGMKIEETIVEK

Catalyzes the oxidative deamination and cyclization of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis.

Q0W131

O29165

ACDA1_ARCFU

ACDS complex carbon monoxide dehydrogenase subunit alpha 1

Archaeoglobus

MFELKKGALFVDEMKNVSIRIGKVVEEEEEVWEEAGPTPKPGILELRKWDHKLLERYEPFYAPMQDFCNLCTMGPCDLSMNKRGACGIDLKTAKARLVTIACCIGASAHTAHARHLVDHLIEEFGEDFPIDLGGDVNVEAPIIRTVVGIKPKTLGDLREALNWAEKEIVKVLHSTHIGNEESLLDYESKAMHVSMADHVGMEVADIAQIVAYNFPKAEPDTPLVDTGFGIVDKSKPTIVVVGHNVMYARPVADYLEEMGRIDDFELAGLCCTAHDMTRYNAKAKIFGPISYQLRVIRAGIPDVMISDEQCIRADLLEACKKMGIPLIATSDAAARGLPDVSDWPVEKIVDALVSGKLPGVFLPIPEKVGQVAPLVAEAIFKKHGGERKYKFFESDEALMEEINKCTQCMNCVFTCPHSLRVDQGMAHAQKTGDLSKLAQLEEQCLACMKCEQACPKNIKIINVIMRANYDRLYNKTGKTRVGRGPIQDTEIRKVGQPIVFGQIPGVIAAVGCINFPDEMKSIREILEEFLKRRYIVVTSGCHAMDIGMIKDEEGKTLYEKYPGNFDAGGLVNTGSCVANSHIAGAAIKIANIFAMRPLRGNYAEIADYVLNRVGAVGFSWGPYSHKAASIATGFNRLGVPVVVGPHGTKYRRAYIGKPWKKDKWWVYDIKSRQKVFIEPAPDSLLVAVETKEEAIVQLARLCIRPNDTNQGRQIKLTHYIELHQKYYGDLPDDWAVYVRSEADLPLKMRDQLLKVLEEQYGWKIDWDKKKIVEGPVRHFDAGFNPTIVEEVYEKYAGEKAPR

Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.

O29165

Q24JL3

STR2_ARATH

Sulfurtransferase 2

Arabidopsis

MKRAFSSQLRSAYPASKSTHFGRVMASSGSEAKANYAPISTNEPVVSVDWLHSNLGDADIKVLDASWYMAHEQRNPIQEYQVAHIPGALFFDLNGIADRKTNLRHMLPSEEAFAAGCSALGIENNDGVVVYDGMGLFSAARVWWMFRVFGHDKVWVLDGGLPKWRASGYDVESSVSNDAILKASAATEAIEKIYQGQTISPITFQTKFRPHLVLALDQVKENIEDKTYQHIDARSKARFDGIAPEPWKGLPSGHIPGSKCVPFPLMFDSSQTLLPAEELKKQFEQEDISLDSPIAASCGTGVTACILALGLYRLGKTNVAIYDGSWTEWATAPNLPIVGSSS

Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is 3-mercaptopyruvate > thiosulfate. Involved in embryo and seed development.

Q24JL3

A5CDC6

ATPL_ORITB

Lipid-binding protein

Orientia

MDPISFKYIAIAFMAFGMAGAALGVASIFNALMNSIARNPSAIEDLQKAALIGAGLAEAMGLFSFILAILLMFT

Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.

A5CDC6

P0C5X8

TTYH1_RAT

Protein tweety homolog 1

Rattus

MGAPPGYRPSAWVHLLHQLPRADFQLRPVPSGFAPRDQEYQQALLLVAALAGLGLGLSLIFIAVYLIRFCCCRPPEPPGAKSPPPGGGCVTWSCIAALLVGCAGIGIGFYGNSETSDGVSQLSSALQHANHTLSTIDDLVLETVERLGEAVRTELTTLEEVLSERVELVAATRGARRQAEAAAQHLQGLAFWQGVSLSPVQVAEDVTFVEEYRWLAYVLLLLLVLLVCLFTLLGLAKQSKWLVVVMTAMSLLVLVLSWGSMGLEAATAVGLSDFCSNPDTYVLNLTQEETGISSDILNYYFLCNQAVSNPFQQRLTLSQRALASIHSQLQGLEREASPQFPAAQKPLLSLEETLNVTERSFHQLVALLHCRSLHKDYGSALRGLCEDALEGLLFLMLFSLLSAGALATTLCSLPRAWALFPPSDDYDDTDDDDPFNPQESKRFVQWQSSI

Probable chloride channel. May be involved in cell adhesion.

P0C5X8

O35310

HS3S1_MOUSE

Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1

Mus

MTLLLLGAVLLVAQPQLVHSHPAAPGPGLKQQELLRKVIILPEDTGEGTASNGSTQQLPQTIIIGVRKGGTRALLEMLSLHPDVAAAENEVHFFDWEEHYSQGLGWYLTQMPFSSPHQLTVEKTPAYFTSPKVPERIHSMNPTIRLLLILRDPSERVLSDYTQVLYNHLQKHKPYPPIEDLLMRDGRLNLDYKALNRSLYHAHMLNWLRFFPLGHIHIVDGDRLIRDPFPEIQKVERFLKLSPQINASNFYFNKTKGFYCLRDSGKDRCLHESKGRAHPQVDPKLLDKLHEYFHEPNKKFFKLVGRTFDWH

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan . Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact) . This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site .

O35310

Q03721

KCNC4_HUMAN

Voltage-gated potassium channel subunit Kv3.4

Homo

MISSVCVSSYRGRKSGNKPPSKTCLKEEMAKGEASEKIIINVGGTRHETYRSTLRTLPGTRLAWLADPDGGGRPETDGGGVGSSGSSGGGGCEFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELTFWGIDETDVEPCCWMTYRQHRDAEEALDIFESPDGGGSGAGPSDEAGDDERELALQRLGPHEGGAGHGAGSGGCRGWQPRMWALFEDPYSSRAARVVAFASLFFILVSITTFCLETHEAFNIDRNVTEILRVGNITSVHFRREVETEPILTYIEGVCVLWFTLEFLVRIVCCPDTLDFVKNLLNIIDFVAILPFYLEVGLSGLSSKAARDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGARPSDPRGNDHTDFKNIPIGFWWAVVTMTTLGYGDMYPKTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKRKKHVPRPAQLESPMYCKSEETSPRDSTCSDTSPPAREEGMIERKRADSKQNGDANAVLSDEEGAGLTQPLASSPTPEERRALRRSTTRDRNKKAAACFLLSTGDYACADGSVRKGTFVLRDLPLQHSPEAACPPTAGTLFLPH

This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.

Q03721

Q9KC68

RACA_HALH5

Chromosome-anchoring protein RacA

Halalkalibacterium (ex Joshi et al. 2022)

MAVQWKTKEVSEQLGVNPTTVQRWVKFFGIQCETNEHGHLLFEKEHLTVLKAIQNQLKSGKKMRDVVIEENEQLIQKPETQPMVATEQYEQRTKQFMEKIAELEKQLSQKADDVVSYQILKHRAEIDEMFKTLQSLELRMAKVEEQLEKQQEEFPLAAGDVPKRKRSFMRLFSF

Required for the formation of axial filaments and for anchoring the origin regions at the cell poles in sporulating cells, thus ensuring proper chromosome segregation in the prespore. Binds in a dispersed manner throughout the chromosome but preferentially to sites clustered in the origin portion of the chromosome, causing condensation of the chromosome and its remodeling into an elongated, anchored structure.

Q9KC68

Q31CV7

AROC_PROM9

5-enolpyruvylshikimate-3-phosphate phospholyase

Prochlorococcus

MSSSFGKIFRVSTFGESHGGGVGVILDGCPPKLKIDIKLIQNELDRRRPGQSDITTPRNEDDKIEILSGIKEGLTLGTPIAMLVRNKDQRPGDYNNLEQVFRPSHADGTYHLKYGIQAGSGGGRASARETIGRVAAGAVAKQLLKNLCNTEILSWVKRIHDIDSDVNKEKISLNKIDSNIVRCPDEKVSAEMIDRIKDLKRQGDSCGGVIECLVRNVPSGLGMPVFDKLEADLAKALMSLPATKGFEIGSGFSGTYLKGSEHNDSFIKSDDISKLRTTSNNSGGIQGGISNGENIEMKIAFKPTATIGKEQKTVNAEGKEVLMKAKGRHDPCVLPRAVPMVDAMVALVLADHLLLNNAQCGLMKN

Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.

Q31CV7

Q0AJI2

CLPP_NITEC

Endopeptidase Clp

Nitrosomonas

MQPILDWEKNELNTTGLGLIPMVIESSGRGERAYDIYSRLLRERIIFLVGPVTETSANLVIAQLLFLESENSEKDISLYINSPGGLVTAGLAVYDTMQFIKPDVSTLCIGQAASMGALLLTAGAKGKRYCLPNSRVMIHQPLGGFQGQASDIEIHAKEILALKGRLNEILAKHTSQTIRTIEKDTDRDNFLGAEAAVKYSLVDAVLTSRKVKHE

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.

Q0AJI2

Q85XC3

NDHK_HORVU

NADH-plastoquinone oxidoreductase subunit K

Hordeum

MNLIEFPLLDQTSSNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDALTKLRKKISREIVEDRTLSQNKKRCFTTSHKLYVRRSTHTGTYEQELLYQSPSTLDISSETFLKSKSPVPSYKLVN

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 translocation, and thus conserves the redox energy in a proton gradient.

Q85XC3

Q8LPR5

TCP4_ARATH

Protein MATERNAL EFFECT EMBRYO ARREST 35

Arabidopsis

MSDDQFHHPPPPSSMRHRSTSDAADGGCGEIVEVQGGHIVRSTGRKDRHSKVCTAKGPRDRRVRLSAHTAIQFYDVQDRLGFDRPSKAVDWLIKKAKTSIDELAELPPWNPADAIRLAAANAKPRRTTAKTQISPSPPPPQQQQQQQQLQFGVGFNGGGAEHPSNNESSFLPPSMDSDSIADTIKSFFPVIGSSTEAPSNHNLMHNYHHQHPPDLLSRTNSQNQDLRLSLQSFPDGPPSLLHHQHHHHTSASASEPTLFYGQSNPLGFDTSSWEQQSSEFGRIQRLVAWNSGGGGGATDTGNGGGFLFAPPTPSTTSFQPVLGQSQQLYSQRGPLQSSYSPMIRAWFDPHHHHQSISTDDLNHHHHLPPPVHQSAIPGIGFASGEFSSGFRIPARFQGQEEEQHDGLTHKPSSASSISRH

Transcription factor playing a pivotal role in the control of morphogenesis of shoot organs by negatively regulating the expression of boundary-specific genes such as CUC genes, probably through the induction of miRNA (e.g. miR164) . Required during early steps of embryogenesis . Participates in ovule develpment . Activates LOX2 expression by binding to the 5'-GGACCA-3' motif found in its promoter . Activates YUC5 transcription by binding to the 5'-GTGGGCCA-3' motif found in its promoter . Through the activation of YUC5 transcription, integrates the auxin response to a brassinosteroid-dependent molecular circuit that promotes cell elongation in hypocotyls . Activates GIS transcription by binding to the 5'-TGGTCC-3' motif found in its promoter . Involved in the regulation of trichome branching through the activation of GIS transcription . Activates CO transcription by binding to the 5'-GGACCAC-3' motif found in its promoter . Involved in the regulation of photoperiodic flowering through the activation of CO transcription . Activates TCL1 and TCL2 transcription by binding to the 5'-TGGCCA-3' and 5'-GTGGACCA-3' motifS found in their respective promoters . Involved in the suppression of trichome initiaition through the activation of TCL1 and TCL2 transcription . Activates HAT2 transcription by binding to the 5'-TGGTCCAC-3' motif found in its promoter . Through the activation of HAT2 transcription, involved in the auxin-independent reprogramming of mitotic cells to exit division and acquire differentiation competence within the transition zone .

Q8LPR5

Q8N1K5

THMS1_HUMAN

Thymocyte-expressed molecule involved in selection

Homo

MALSLEEFVHSLDLRTLPRVLEIQAGIYLEGSIYEMFGNECCFSTGEVIKITGLKVKKIIAEICEQIEGCESLQPFELPMNFPGLFKIVADKTPYLTMEEITRTIHIGPSRLGHPCFYHQKDIKLENLIIKQGEQIMLNSVEEIDGEIMVSCAVARNHQTHSFNLPLSQEGEFYECEDERIYTLKEIVEWKIPKNRTRTVNLTDFSNKWDSTNPFPKDFYGTLILKPVYEIQGVMKFRKDIIRILPSLDVEVKDITDSYDANWFLQLLSTEDLFEMTSKEFPIVTEVIEAPEGNHLPQSILQPGKTIVIHKKYQASRILASEIRSNFPKRHFLIPTSYKGKFKRRPREFPTAYDLEIAKSEKEPLHVVATKAFHSPHDKLSSVSVGDQFLVHQSETTEVLCEGIKKVVNVLACEKILKKSYEAALLPLYMEGGFVEVIHDKKQYPISELCKQFRLPFNVKVSVRDLSIEEDVLAATPGLQLEEDITDSYLLISDFANPTECWEIPVGRLNMTVQLVSNFSRDAEPFLVRTLVEEITEEQYYMMRRYESSASHPPPRPPKHPSVEETKLTLLTLAEERTVDLPKSPKRHHVDITKKLHPNQAGLDSKVLIGSQNDLVDEEKERSNRGATAIAETFKNEKHQK

Plays a central role in late thymocyte development by controlling both positive and negative T-cell selection. Required to sustain and/or integrate signals required for proper lineage commitment and maturation of T-cells. Regulates T-cell development through T-cell antigen receptor (TCR) signaling and in particular through the regulation of calcium influx and phosphorylation of Erk.

Q8N1K5

Q3UWA4

TRI40_MOUSE

Probable E3 NEDD8-protein ligase

Mus

MGSLDKDNQDICPICLDPLKEAVSTDCRHLFCRMCLTQHMDKASVSGILSCPVCRKPCSEGVLGDNYICHTHQKRVRRFCEASGHLLCEECLQSPEHQSHTELSIENAISHYKERLNRRSRKLRKDLGNLQQLKAQEKKMLQALQVDCECHRLRTDLQNQDQTKEQLKALPWHWLDQEDLPEEVAKIFSFSEAVTQLSILVSGLERMAKDLDASTLKDASDLLDRSAPQKLEGLLSRVSPAGPKLS

E3 ubiquitin-protein ligase that plays a role in the limitation of the innate immune response. Mediates inhibition of the RLR signaling pathway by ubiquitinating DDX58 and IFIH1 receptors, leading to their proteasomal degradation. Promotes also the neddylation of IKBKG/NEMO, stabilizing NFKBIA, and thereby inhibiting of NF-kappa-B nuclear translocation and activation.

Q3UWA4

Q57706

CFBE_METJA

Coenzyme F(430) synthetase

Methanocaldococcus

MVFFMLIIDVNHGALTLAEEYLNLGYEVDVWDIYQKIKKSEDFKVKYQKLKEKFGNKLNLFFEQPNFEKYDRVIAPIHCPIDVDFIPFTDAVSKILKEKFGNIHKKIINVTGVKGKTTTTSLINHILKDKYSTYLHNSNFGSIAPPTILKVLNSLDIDKYDFFIFETSLGLIKCKYGAITNVLENYKIAGGRKDALTAKFSSLKNAELSFINKRDINRYDLNINHKCLNVVDVDRAKILDKYPLKFKYFDEIFEFSKNIFGLHFVENSLFAIEICKNLVDMEEIRYRLKTFTIKNRMEIKEINKKILVKNINPGLDVKAISYAIKDFLEVFGGDIYIGGDFGIVCEEIDVKKLSEVLKRFNCRYIFVGEIGKELLNYLNGGYIKSYDENKIKRDSLVILREKIK

Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the activation the g-propionate side chain of 15,17(3)-seco-F430-17(3)-acid (seco-F430) for intramolecular C-C bond formation to yield the carbocyclic F ring of coenzyme F430.

Q57706

B6JNY0

EX7S_HELP2

Exodeoxyribonuclease VII small subunit

Helicobacter

MQDELFETEKAPPKNAKNAPKKSFEEHVHSLEQAIDRLNDPNLSLKDGMDLYKTAMQELFLAQKLLENAYLEYEKLQTTDKKA

Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.

B6JNY0

Q2YAY1

RL18_NITMU

50S ribosomal protein L18

Nitrosospira

MPNSIESRLRRARQTRAKIAELKVVRLAIHRSNSHIYAQLIDGSGSKVLASASTLEPELRKELPNGGTVTAAAVVGKRVAEKARGLGIETVAFDRSGFKYHGRVKALADAARENGLKF

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.

Q2YAY1

Q9Y9W3

SPT5_AERPE

Transcription elongation factor Spt5

Aeropyrum

MEGGVDARFYAILVTSGAEVNVATIIAERARALGLDIRSIIVPPRIKGYVILEAHDPGDVYDATRGLRHVKRRRPLILKFEEVMKLVKPEVEIPALKPGQVVEIVAGAFKGMKARVIDVNQSKGQVTVSLLEPLFRATATIPIDEVRPVEE

Stimulates transcription elongation.

Q9Y9W3

Q81F14

MTAD_BACCR

5-methylthioadenosine/S-adenosylhomocysteine deaminase

Bacillus cereus group

MKTTYVNATIVTMNEQNEVIENGYIIVENDQIIDVKSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAIMETVSRSGMRAAVSRTLFSFGTKDDEKKAIEEAEKYVKRYYNESDMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMRIATLLQKGIHQDATALPVETALSLATKGAAEVIGMKQTGSLEAGKCADFITIDPSNKPHLQPADEVLSHLVYAASGKDISDVIINGKHVVWNGECKTLDEERIIFEASRYKRGLQR

Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.

Q81F14

Q93PP9

BFR_DESDA

Bacterioferritin

Desulfovibrio

MAGNREDRKAKVIEVLNKARAMELHAIHQYMNQHYSLDDMDYGELAANMKLIAIDEMRHAENFAERIKELGGEPTTQKEGKVVTGQAVPVIYESDADQEDATIEAYSQFLKVCKEQGDIVTARLFERIIEEEQAHLTYYENIGSHIKNLGDTYLAKIAGTPSSTGTASKGFVTATPAAE

Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.

Q93PP9

Q86W28

NALP8_HUMAN

PYRIN and NACHT-containing protein 4

Homo

MSDVNPPSDTPIPFSSSSTHSSHIPPWTFSCYPGSPCENGVMLYMRNVSHEELQRFKQLLLTELSTGTMPITWDQVETASWAEVVHLLIERFPGRRAWDVTSNIFAIMNCDKMCVVVRREINAILPTLEPEDLNVGETQVNLEEGESGKIRRYKSNVMEKFFPIWDITTWPGNQRDFFYQGVHRHEEYLPCLLLPKRPQGRQPKTVAIQGAPGIGKTILAKKVMFEWARNKFYAHKRWCAFYFHCQEVNQTTDQSFSELIEQKWPGSQDLVSKIMSKPDQLLLLLDGFEELTSTLIDRLEDLSEDWRQKLPGSVLLSSLLSKTMLPEATLLIMIRFTSWQTCKPLLKCPSLVTLPGFNTMEKIKYFQMYFGHTEEGDQVLSFAMENTILFSMCRVPVVCWMVCSGLKQQMERGNNLTQSCPNATSVFVRYISSLFPTRAENFSRKIHQAQLEGLCHLAADSMWHRKWVLGKEDLEEAKLDQTGVTAFLGMSILRRIAGEEDHYVFTLVTFQEFFAALFYVLCFPQRLKNFHVLSHVNIQRLIASPRGSKSYLSHMGLFLFGFLNEACASAVEQSFQCKVSFGNKRKLLKVIPLLHKCDPPSPGSGVPQLFYCLHEIREEAFVSQALNDYHKVVLRIGNNKEVQVSAFCLKRCQYLHEVELTVTLNFMNVWKLSSSSHPGSEAPESNGLHRWWQDLCSVFATNDKLEVLTMTNSVLGPPFLKALAAALRHPQCKLQKLLLRRVNSTMLNQDLIGVLTGNQHLRYLEIQHVEVESKAVKLLCRVLRSPRCRLQCLRLEDCLATPRIWTDLGNNLQGNGHLKTLILRKNSLENCGAYYLSVAQLERLSIENCNLTQLTCESLASCLRQSKMLTHLSLAENALKDEGAKHIWNALPHLRCPLQRLVLRKCDLTFNCCQDMISALCKNKTLKSLDLSFNSLKDDGVILLCEALKNPDCTLQILELENCLFTSICCQAMASMLRKNQHLRHLDLSKNAIGVYGILTLCEAFSSQKKREEVIFCIPAWTRITSFSPTPHPPDFTGKSDCLSQINP

Involved in inflammation.

Q86W28

Q6NKS4

LIL32_ARATH

LHC-like protein 3 isoform 2

Arabidopsis

MSISMALFSPPISSSLQNPNLIPKISTSLLSTKRFSLISVPRASSDNGTTSPVVEIPKPASVAVEEVPVKSPAESSSASENGAVGGEATDSSTETVIKYQNAKWVNGTWDLKQFEKDGKTDWDSVIVSEAKRRKWLEDNPETTSNDELVVFDTSIIPWWAWMKRYHLPEAELLNGRAAMIGFFMAYFVDSLTGVGLVDQMGNFFCKTLLFVAVAGVLFIRKNEDLDKLKDLFDETTLYDKQWQAAWKEPDSSTVSSKK

Light-harvesting-like protein required for biosynthesis of phytylated chlorophylls and alpha-tocopherol in green seedlings. Functions by anchoring geranylgeranyl reductase (GGR) in the thylakoid membrane, leading to the stabilization of GGR activity . Binds chlrophyll a in the thylakoid membrane . Plays a role in the regulation of chlorophyll biosynthesis under light stress and under standard growth conditions .

Q6NKS4

A1KBD3

LEU1_AZOSB

Alpha-isopropylmalate synthase

Azoarcus

MLKNPHTKYRPANPFAGVVPGGRGLSDRTWPDNTITRPPVWMSTDLRDGNQALFEPMNSERKMRMFKMLVEIGLKEIEVAFPAASQTDFDFVRELIEGGHIPDDVTIEVLTQARPHLIERTFESVRGAKRAIVHVYNAVAPNFRRIVFDTDRAGVKQIAVDSARYFVEMAARQPGTDFTFQYSPEVFSGTELDFAVEVANAVIEVWQPTPQQKCIINLPATVEMSTPNVYADQIEWMHRHLARRDSVLLSVHPHNDRGTAVAAAELAVMAGADRVEGCLFGNGERTGNVDLVTLALNLYSQGVHPGLDFSRINEVARTVEHCTQLPIHPRHPYVGDLVFTAFSGSHQDAIKKGFAVQQPDAVWEVPYLPVDPADLGRSYESIIRVNSQSGKGGIAYLLEAEYGLVMPRRLQVEFSAAIQRITDERGTELSAGDIWRAFEEEYLAVAAPYAYVEHHLAEHGGQQGISLTVEEAGVRRVLRGVGNGPIDAALHALDAGAVLLGYEERAIGQGGDARAVAYIELADGEGGGSTFGVGIHANIVTASVLAIVSALDRLAQRRERADGVGRQVAATR

Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).

A1KBD3

B4SBV3

RS3_PELPB

30S ribosomal protein S3

Pelodictyon

MGQKVNPTGFRLGIIRDWASRWYDDSPVISEKIKQDHVIRTYVLARLKKERAGIARIIIERTTKHVKINIYAARPGAVVGRKGEEINNLSQELSRITGKEVKIDVVEVVKPEIEAQLIGDNIAYQLENRVSFRRAMKQAIQQAMRSGAEGVRIRCGGRLGGAEIARSEQYKEGKIPLHTIRANVDYASVTAHTIAGTIGIKVWVYKGEVLVQRIDAIEEDELKRIKERRNDAGARNRDSRTKRRHRTKR

Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.

B4SBV3

B1A925

RPOC2_CARPA

Plastid-encoded RNA polymerase subunit beta''

Carica

MAERANLVFHNKVIDGTAIKRLISRLIDRFGMAYTSHILDQVKTLGFQQATATSISLGIDDLLTIPSKGWLVQDAEQQSLILEKHHHYGNVHAVEKLRQSIEIWYATSEYLRQEMNPNFRVTDPFNPVHIMSFSGARGNASQVHQLVGMRGLMSDPQGQMIDLPIQSNLREGLSLTEYIISCYGARKGVVDTAVRTSDAGYLTRRLVEVVQHIVVRRTDCGTIRGISVSPKNRTMPERIFIQTLIGRVLADDIYMGPRCIAIRNQDIGIGLVNRFITFRTQSISIRTPFTCRSTSWICRLCYGRSPTHGDLVELGEAVGIIAGQSIGEPGTQLTLRTFHTGGVFTGGTAEHVRSPSNGKIKFNEDLVHPTRTRHGHPAFLCYIDLSVVIESEDIIHNVTIPPKSFLLVQNDQYVESEQVIAEIRAGTYTLNYKERVRKHIYSNSEGEMHWSTDVYHAPEFTYSNVHLLPKTSHLWILSGGSSRSSLVPFSLHKDQDQMNIHSLSVEQESISSLAVNNDQGRHKFFSSNFSDKKKCGIPDYSEFHRILDTGHCNLIYFASLHENSDLLAKRRRNRFIIPFQSIQEQEKELMPRSGISIEIPINGIFRRNSILAFFDDPRYRRKSSGILKYGTIGAHSIVKKEDVIEYRGVKKFKTKYQMKVDRFFFIPEEVHILPESSSIMVRNNSIIGVDTRITLNIRSQVGGLVRVERKKKSIELQIFSGDIHFPGKTDKISRHSGILIPPGRGKTNSKESKKLKNWIYVQRITPTKKKYFVLVRPVATYEIADGINLATLFPQDLFREKDNMQLRVVNYILYGNGKPVRGIFDTSIQLVRTCLVLNWDQDNKSSSVEEVRTFFVEVSTNSLIRDFLRIDLVKSQSHISYIRKRNDPSGSGLISDNGSDRINPFYYKERIQQSLSKNHGTIRTLLNRNKECQSLIILSSSNCFQMGPFNHVKYHNVIKQSIKKDPLIPIRNSLGPVGTAIQIANFYSIYHLITHNQISVTKYFQLDNLNQIFEVIKYYLMDETGRVYNPDPCSNIILNPFNLNWYFLYQNYHHNYCEETSTIISLGQFICENVCLAKNGPHLKSGQVLIVQVDSVVIRSAKPYLATPGATVHGHYGEILYEGDTLVTFIYEKSRSGDITQGLPKVEQVLEVRSIDSISLNLEKRVEGWNKRITRILGIPWGFLIGAELTIVQSRISLVNKIQKVYRSQGVQIHNRHIEIIVRQITSKVLVSEEGMSNVFLPGELIGLLRAERTGRALEEAICYRAILLGITRASLNTQSFISEASFQETARVLAKAALRGRIDWLKGLKENVVLGGMIPAGTGFKGLVHCSRQHTSILLETKKKNLYLFEGEMRDIFFHHRELFDSCISKNLHNTSERSFIGLNDS

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

B1A925

A9M0Q6

CH60_NEIM0

Chaperonin-60

Neisseria

MAAKDVQFGNEVRQKMVNGVNILANAVRVTLGPKGRNVVVDRAFGGPHITKDGVTVAKEIELKDKFENMGAQMVKEVASKTNDVAGDGTTTATVLAQSIVAEGMKYVTAGMNPTDLKRGIDKAVAALVEELKNIAKPCDTSKEIAQVGSISANSDEQVGAIIAEAMEKVGKEGVITVEDGKSLENELDVVEGMQFDRGYLSPYFINDAEKQIAALDNPFVLLFDKKISNIRDLLPVLEQVAKASRPLLIIAEDVEGEALATLVVNNIRGILKTVAVKAPGFGDRRKAMLQDIAILTGGVVISEEVGLSLEKATLDDLGQAKRIEIGKENTTIIDGFGDAAQIEARVAEIRQQIETATSDYDKEKLQERVAKLAGGVAVIKVGAATEVEMKEKKDRVEDALHATRAAVEEGVVAGGGVALLRARAALENLHTGNADQDAGVQIVLRAVESPLRQIVANAGGEPSVVVNKVLEGKGNYGYNAGSGEYGDMIEMGVLDPAKVTRSALQHAASIAGLMLTTDCMIAEIPEDKPAVPDMGGMGGMGGMM

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.

A9M0Q6

Q12096

GNT1_YEAST

N-acetylglucosaminyltransferase

Saccharomyces

MRLISKRRIRFIVFILFGVLTVFVVSRLVVHFQYNQEIKFYKKYFQQRKDGLHEIYNPLEIKQIPKETIDDLYTARLDKELKNGEVIEWSKFAYVNYVTNADYLCNTLIIFNDLKQEFETKAKLVLLISKDLLDPNTSSNVAYISSLLNKIQAIDEDQVVIKLIDNIVKPKDTTPWNESLTKLLVFNQTEFDRVIYLDNDAILRSSLDELFFLPNYIKFAAPLTYWFLSNSDLEKSYHETRHREKQPINLQSYTKVLTKRIGKGQMIYNHLPSLPHSLYLNSNNIAQDIISSTSSLSPLFDFQSSKKVGKLKFASNLMVINPSKEAFDEIVNVMLPKILNKKEKYDMDLINEEMYNLKKIIYKQFIFFRKVRKLFKPEVLVLPFARYGLLTGSLRNPRHYSIIYNDVLGYKTLDNDGNDIPVGLNDSVAYSKYIHFSDYPLAKPWNYPSMKEFECIVKEEDAEDSKLEHQACDLWNSVYASYIQSREICLV

N-acetylglucosaminyltransferase involved in the Golgi-specific modification of N-linked glycans.

Q12096

Q5AGW8

NUP_CANAL

Purine nucleoside permease

Candida

MKLSTLFTLATTISTLTTFTIASPVVVVEKRAINETALAEDIPTTKNNHAQTSYGKPFAIYQPKAFIISMFSLERDPWLKAMDFVHNITIPGLSPVYPDIHCTTNYTICQITTGEGEINAASSISALTLNPLFDLTKTYFLVGGIAGGEPNYTTIGGVTFAKYAVQVGLEYQLAYEDYHKTNPDWISGYIPYGTDDQNTYPGNVYGTEVFEVNEKLRDRAVELASKVHLNNGTEGNAKFRKLYNETAAQGLPKVVKCDSLTSDNYFTGNVLNDYFANFTLLMTNGSATYCSTAQEDNATLEVMTRLAKHGLVDYDRIMIMRTISDFSRPPPSMSAYEYFFNRSDGGISASLENLVIAGTPIIHDIVQNWDKIYESGEKYSSKNYVGDIFATLGGKPDFGKESFDTA

Nucleoside permease that transports adenosine and guanosine. Does not show any transport activities towards cytidine, adenine, guanine, uridine, and uracil.

Q5AGW8

P25378

RHEB_YEAST

GTP-binding protein RSG1

Saccharomyces

MEYATMSSSNSTHNFQRKIALIGARNVGKTTLTVRFVESRFVESYYPTIENEFTRIIPYKSHDCTLEILDTAGQDEVSLLNIKSLTGVRGIILCYSIINRASFDLIPILWDKLVDQLGKDNLPVILVGTKADLGRSTKGVKRCVTKAEGEKLASTIGSQDKRNQAAFIECSAELDYNVEETFMLLLKQMERVEGTLGLDAENNNKCSIM

Involved in the regulation of arginine and lysine uptake. Acts through the CAN1 permease.

P25378

Q887M0

AMPA_PSESM

Leucyl aminopeptidase

Pseudomonas

MELVVKSVSPETLKTATLVVTINESRVLIGAAQLVDIKSGGAISAVLERGDLAGKSGQTLLLTNLQNIKAERVLLVGIGKDGELSDRQLKKIAGSVLSSLKGLGGSDAVIALDDLSVKNRDTYGKARLFVEALADGEYVFDRFKTQKAEVRPLKKITLLTDKVSVADVERAANHAQAIATGMALTRDLGNLPPNICHPTYLGEEAKALGKAHKNLKVEIHDEKKLAELGMGSFLAVAQGSAQPPRLIVMNYQGGKKGDKPFVLVGKGITFDTGGISIKPAAGMDEMKFDMCGAASVFGTLRAVLELKLPINVVCILACAENMPSGTATRPGDIVTTMSGQTVEILNTDAEGRLVLCDALTYAERFKPQAVIDIATLTGACVVALGGHTSGLLGNNDALINQLLDAGKLADDRAWQLPLFDEYQEQLDSPFADIANIGGPKGGTITAACFLSRFTKAYEWAHLDIAGTAWLSGGKDKGATGRPVPLLTQYLLDRAGV

Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.

Q887M0

P84088

CPLX2_BOVIN

Synaphin-1

Bos

MDFVMKQALGGATKDMGKMLGGEEEKDPDAQKKEEERQEALRQQEEERKAKHARMEAEREKVRQQIRDKYGLKKKEEKEAEEKAALEQPCEGSLTRPKKAIPAGCGDEEEEEEESILDTVLKYLPGPLQDMFKK

Negatively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles. Also involved in mast cell exocytosis.

P84088

F4JRF4

MUTYH_ARATH

MutY homolog

Arabidopsis

MACLLRVALNPTFERSTVASQRQNPKTILSFHCKVSSFKTKTMSQSFAPREKLMRKCREKKEAEREAEREAEREAEEEEKAEEAEAEADKEEAEEESEEEEEEEEEEAEAEEEALGGDIEDLFSENETQKIRMGLLDWYDVNKRDLPWRNRRSESEKERRAYEVWVSEIMLQQTRVQTVMKYYKRWMQKWPTIYDLGQASLENLIVSRSRELSFLRGNEKKEVNEMWAGLGYYRRARFLLEGAKMVVAGTEGFPNQASSLMKVKGIGQYTAGAIASIAFNEAVPVVDGNVIRVLARLKAISANPKDRLTARNFWKLAAQLVDPSRPGDFNQSLMELGATLCTVSKPSCSSCPVSSQCRAFSLSEENRTISVTDYPTKVIKAKPRHDFCCVCVLEIHNLERNQSGGRFVLVKRPEQGLLAGLWEFPSVILNEEADSATRRNAINVYLKEAFRFHVELKKACTIVSREELGEFVHIFTHIRRKVYVELLVVQLTGGTEDLFKGQAKDTLTWKCVSSDVLSTLGLTSAVRKVPPFRLQHIKRLSLDVMVEKEQILECRCIQWLKHTSKAYLFLMSHQIEQPYRGNENSHDLLLTLFFMLLSFYSSCLALGIKFGDLGLKLNSLVSTEKSDGDV

Involved in oxidative DNA damage repair. Initiates repair of A*oxoG to C*G by removing the inappropriately paired adenine base from the DNA backbone. Possesses both adenine and 2-OH-A DNA glycosylase activities.

F4JRF4

Q9UZ56

IORB_PYRAB

Indolepyruvate ferredoxin oxidoreductase subunit beta

Pyrococcus

MKEYNIVITGVGGQGILTAANLLGWAALRAGYKVRVGEVHGMSQRFGSVIAYVRFGEDVYGAMVPEGKADVILSFEPVEALRYINYLKKGGLVFTNARPIPPVQVSMGLASYPSMEEIRKIVEEDFGGKFLAFDAEKLAIEAGNVITTNVVLIGALTQTPGFPLSAEHVKEVIRISVPPKAVDVNMRAFELGVKAAKEMLNL

Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates.

Q9UZ56

Q9SY97

LHCA3_ARATH

LHCI type III LHCA3

Arabidopsis

MAAQALVSSSLTSSVQTARQIFGSKPVASASQKKSSFVVKAAATPPVKQGANRPLWFASSQSLSYLDGSLPGDYGFDPLGLSDPEGTGGFIEPRWLAYGEIINGRFAMLGAAGAIAPEILGKAGLIPAETALPWFQTGVIPPAGTYTYWADNYTLFVLEMALMGFAEHRRLQDWYNPGSMGKQYFLGLEKGLAGSGNPAYPGGPFFNPLGFGKDEKSLKELKLKEVKNGRLAMLAILGYFIQGLVTGVGPYQNLLDHLADPVNNNVLTSLKFH

The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated, here photosystem I.

Q9SY97

Q6DI51

NDK6_DANRE

Nucleoside diphosphate kinase 6

Danio

MRCVKALQLTLAVIKPDAMAHPLILEALHQKILENFIIIRKKDLIWRKADSEMFYAEHSGRFFFQRLVEFMSSGPMRAYILAREDAITHWRTMMGPTKVFRARFSSPETLRGKYGLTDTRNTTHGSDSIESAKREISFFFPEFSAEEWMMREEPHFRLGHTEYNEESQIHTVKHT

Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.

Q6DI51

O74095

RL23_PYRHO

50S ribosomal protein L23

Pyrococcus

MDPYKVIIRPVVTEKAISLIEKENKLTFIVDRRATKTDIKKAIEEIFNVKVEKVNTLITPKGEKKAYVKLKPEYSASEIAARLGLF

Binds to 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome.

O74095

C6DKI3

RLME_PECCP

rRNA (uridine-2'-O-)-methyltransferase

Pectobacterium

MANKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYVVTQIGGNGRIIACDILPMDPIVGVDFLQGDFRDELVLKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPKSMYLVELALGMCRDVLAPGGSFLVKVFQGEGFDEYLREIRSLFTKVKIRKPDASRARSREVYIVATGRKL

Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.

C6DKI3

Q92F41

Y266_LISIN

Putative RNase Lin0266

Listeria

MLTWVIRVCFLILGGTTGVFSLPALWVKLGIGHILLINNPYTDALIGALIFYLITFWAVKYVEAALNWLEEKLAKIAIATLIYGGLGLFVGLVIAFFASNALSQTNIPLLNSVVPVILTLVLGYLGFRIGISRRNEFGNFVNNRNAKKKTPEEEQTEEKSKKTYKILDTSVIIDGRIADILATGFLDGTVVIPLFVLAELQHIADSSDTLKRTRGRRGLDILNRIQKEDSIQVEMYEGDFEDTPEVDSKLVKLAKVMGGIVVTNDYNLNKVCEFQNVPVLNINDLANAVKPVVLPGEKMTVLMVKDGKEHNQGVAYLDDGTMIVVEDGRKFINETIQVEVTSVLQTSAGRMIFAKPS

An RNase.

Q92F41

Q8AY50

3NO22_BUNCA

Weak toxin 2

Bungarus

MKTLLLTLVVVAIVCLDLGYTLTCLICPEKDCQKVHTCRNEEKICVKRSYDKNQLGWRAQRGCAVSCPKAKPNETVQCCSTDKCNK

Binds with low affinity to muscular (alpha-1-beta-1-delta-epsilon/CHRNA1-CHRNB1-CHRND-CHRNE) and very low affinity to neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR).

Q8AY50

A0KG33

NHAA_AERHH

Sodium/proton antiporter NhaA

Aeromonas

MSDVIKKFLKLEAASGIILIMAAMLAMILANSGLAGSYQAFLDTQVQVRIAALDINKPLLLWINDGFMAVFFLLVGLEVKREMLEGALSSRVQATFPAIAAVGGMLAPALIYAFFNYSDEVARAGWAIPAATDIAFALGVMALLGKRVPVSLKVFLLALAIMDDLGVIIIIALFYTQQLSLTALAIGILATLTLLWMNRRGEDRISLYMLVGLVLWVAVLKSGVHATLAGVIVGFMIPLSGKRYASPLKQLEHALHPWSAYLILPLFAFANAGVSLEGIGLSALLSPVPLGIMLGLFIGKPLGVFTISWLAVKLGIAQLPNGVNFKQIFAVSILCGIGFTMSMFIASLAFEHGGLDYGSYSRLGILVGSTLAAIVGYLALRIALPNREADQSTEGL

Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.

A0KG33

P59733

RLMH_NITEU

rRNA (pseudouridine-N3-)-methyltransferase RlmH

Nitrosomonas

MKFHILAVGNKMPDWVRKGYTEYCQRMPKEAELLLVEIKPEKRVGSKNTRQLLQAESERIRTVLPPGCHIVVLDETGKQATTMKLAEMMDRWMGSGQDVAFIIGGADGLHQDIKQMAHEKLALSAMTLPHGLARVLLAEQLYRAFSINRNHPYHRA

Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.

P59733

P49376

ATPB_KLULA

ATP synthase subunit beta, mitochondrial

Kluyveromyces

MVLPRFYAASSRAALQAARRAVPFTGVRGYAAAASSQGKVRAVIGAIVDVQFEQGQLPAILNALEIDTPEGKLVLEVAQHLGENTVRTIAMDGTEGLVRGENVSDTGAPISVPVGRETLGRIINVIGEPIDERGPINSKMRKPIHADPPLFVEQSTAAEVLETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGDSKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVATQVQQTLQAYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGRLVRLKDTISSFKAVLDGKYDHLPENAFYMVGGIEDVVAKAEKLAAEAN

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

P49376

Q14145

KEAP1_HUMAN

Kelch-like protein 19

Homo

MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPNFLQMQLQKCEILQSDSRCKDYLVKIFEELTLHKPTQVMPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSDGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGRSGVGVAVTMEPCRKQIDQQNCTC

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting NFE2L2/NRF2 for ubiquitination . KEAP1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of NFE2L2/NRF2, a transcription factor regulating expression of many cytoprotective genes . In response to oxidative stress, different electrophile metabolites trigger non-enzymatic covalent modifications of highly reactive cysteine residues in KEAP1, leading to inactivate the ubiquitin ligase activity of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and expression of phase II detoxifying enzymes . In response to selective autophagy, KEAP1 is sequestered in inclusion bodies following its interaction with SQSTM1/p62, leading to inactivation of the BCR(KEAP1) complex and activation of NFE2L2/NRF2 . The BCR(KEAP1) complex also mediates ubiquitination of SQSTM1/p62, increasing SQSTM1/p62 sequestering activity and degradation . The BCR(KEAP1) complex also targets BPTF and PGAM5 for ubiquitination and degradation by the proteasome .

Q14145

Q953L2

NU4LM_ECHGY

NADH dehydrogenase subunit 4L

Echinosorex

MQMTMINMILAFIMATTGLLMFRSHFMSSLLCLEGMMLSIFILMSISTLNFNNSLAMMFPLVLLVFAACEAAIGLSLLVKISNTYGTDYVQNLNLLQC

Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.

Q953L2

A4XLS8

RL23_CALS8

50S ribosomal protein L23

Caldicellulosiruptor

MLPEEIIKRPIITEKSMSMIPQKKYTFEVDRRANKIEIKKAVEQLFGVEVEKVWTMNVKPKRKRVGRFEGRTKAWKKAIVKLTDKSKTIEFFDSLI

One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.

A4XLS8

Q72CG9

RL24_DESVH

50S ribosomal protein L24

Desulfovibrio

MKQFRIHKDDKVMVIAGKDKGKIGKVLKILRNKDRILVEKVNVAKRHVRPNPYRQQPGGIIEKEMPLHVSNVMVVCDACAKPTKVGYRYTEDGKKVRFCKKCNEIID

One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.

Q72CG9

Q4WAX1

FTMH_ASPFU

Fumitremorgin biosynthesis protein H

Aspergillus subgen. Fumigati

MTIPTEISCPEEDAFQLLDKFSWFPSDDQRRWWEYTGPYLLKLLRDAKYPQKDQVPCLYLLQQLLVPYLGTFPVVGQAPLPWWSNVTTYGVPFELSWNLLHNIVRIGFEPLSHLAESGVDAFNKTAPEECVSRLACLDNTIDLARFRHFQHHLLVTPEEETWLLKEKAPLAKSGRGQQTLAVEFQNGGISAKAYFFPGMKSLATGLSPGKLILDSIERLALPGLKEPVHHLRSTLGLQDDGHPTDTAIAPFLLGVDLCTPERSRLKFYVTDQVVSWDRVADMWTLRGKRLEDPQCADGLALLRKLWDLLAIPEGYRSNIRPDFAFGTPPPEDYRPVMMANWTLSPKKKFPDPQIYLLTVGMNDAVVMDALVAFYEVLGWTDLASTYKDKVASYFPGPDFTKTNYIHSGVSFSYRHSKPYLSVYYSPF

12-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities . The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA . Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B . The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively . The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B . Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties . In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).

Q4WAX1

Q4WD43

FSQB_ASPFU

Fumisoquins biosynthesis protein B

Aspergillus subgen. Fumigati

MSIPNSFIIVGSGVFGLSLAYALSLDDRFADKKIILVDRWNFEPPNATGSVHNPAAANADTSRVIRRDYPHGPYASLALEAMKHWRGKFGENNRYVNQRLLFSGEGSSLTTPPKALETVNYIKKAYAISCELTPGGRDAVQVLDSLDEVRAFLGNTPSHPPHLPVNKDPAARDLRGYVSNDCGWADAGASIEWLRQEVLRLGRVECVVGEVESLVYSDDQRAVKGVKLVDGKVLTAELTVIAAGARSSHILGIPKLCDVYSEFVAYIQLTKEEADELRRRQWPILVNCHRGVFAVGPDHDNCLKFGHFSYSGIVDVLREASIQVPTRPDGWEAQQKYWSDPRFAFGGEVKVSALGDVDDYENPAAQRALADYRLFLLELLGPTGLQGVDTLGLDQSDNLLNNIANRPFTRVRKCWYNDTPALDFVVDYHPSYGKTLFVATGGCDHAFKFLPIIGEKTLALILRNRGDSAVSLPAGVEPSLEELSELWRFPVELLQDN

Is able to convert N-methyl-3,4-dihydroxy-DL-phenylalanine (N-methyl-DOPA) directly into cyclic isoquinoline, in vitro . The absence of the meta-hydroxyl group, as in L-N-methyl-tyrosine, leads to a 25-fold lower rate of reduction and the formation of the demethylated product L-tyrosine, instead of a cyclic product . Does not accept the D-stereoisomer of N-methyltyrosine, in contrast to N-methyl-DOPA, for which both stereoisomers are oxidized with similar rates .

Q4WD43

Q21WT4

DAPE_ALBFT

N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase

Rhodoferax

MPKTLHLAEQLIARPSLTPDDAGCQQIIAERLAPLGFSCETITSGPADFRVTNLWAKRAAAPVKSAQHTTKLVVFAGHTDIVPSGPVQQWRCHPFTPTQFDGKLYGRGAADMKTSLAAFVVAVEEFLTAQPDTALAIGFLLTSDEEGPALDGTVKVCEALQARGERIDYCIVGEPTSLERTGDMIKNGRRGTLSARLTVKGVQGHIAYPHLAKNPIHLVAPALAELVGVEWDRGNAFFPPTSWQISNIHSGTGASNVIPGAVVIDFNFRFSTESTPESLQTRLAAVLERHELDYELAWTLGGTPFLTEPGTLVDAVVDAIKQETGLTTVLSTTGGTSDGRFIARICPQVIEFGPPNASIHKIDEHINVADIEPLTNIYRRVLENLSAGLSA

Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.

Q21WT4

Q661D7

RL22_BORGP

50S ribosomal protein L22

Borreliella

MLSQIKREGNRVVMLVNRRYTARGKNLPSSPKKVRPIADNIRGKSYIKAIAVLCSMPNKGAKLLEKVVKSAASNAMYHNKNLSEDMIFVKIVMVDDGRRRKKIWPRARGRADRLVNRNCHIFVEVDEKKDIKG

The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.

Q661D7

A1URW3

AROC_BARBK

5-enolpyruvylshikimate-3-phosphate phospholyase

Bartonella

MSHNTFGHLFRVTTWGESHGAALGCVIDGCPPGIAFTLTEIQAYLNKRRPGHSEYTTQRRELDQVEILSGVVSQNDGKALVTTGTPISMFIRNVDHHSEDYNAIMHKYRPGHADYTYDVKYGIRDHRGGGRASARETVVRVAAGALARKIVPGLIVRGAVTAIGPHNIDRDRWDWSEVDKNPFFSPDAQAACVFANYISQLCKTGSSVGAIVEIVAENVPAGLGAPVYAKLDQDIASFLMSINAVKGIEIGDGFAAAHLTGEENADEMRMGSDGKPVFLSNHAGGILGGISNGQPIVARFAVKPTSSILTPSRSIDIEGNDVNVMTKGRHDPCVGIRAVPVGEAMVACAIADHYLRHRGQVGCI

Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.

A1URW3

P32121

ARRB2_HUMAN

Non-visual arrestin-3

Homo

MGEKPGTRVFKKSSPNCKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTCAFRYGREDLDVLGLSFRKDLFIATYQAFPPVPNPPRPPTRLQDRLLRKLGQHAHPFFFTIPQNLPCSVTLQPGPEDTGKACGVDFEIRAFCAKSLEEKSHKRNSVRLVIRKVQFAPEKPGPQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYADICLFSTAQYKCPVAQLEQDDQVSPSSTFCKVYTITPLLSDNREKRGLALDGKLKHEDTNLASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIPLPRPQSAAPETDVPVDTNLIEFDTNYATDDDIVFEDFARLRLKGMKDDDYDDQLC

Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as signaling scaffold for the AKT1 pathway. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Increases ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Involved in CCR7-mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in p53/TP53-mediated apoptosis by regulating MDM2 and reducing the MDM2-mediated degradation of p53/TP53. May serve as nuclear messenger for GPCRs. Upon stimulation of OR1D2, may be involved in regulation of gene expression during the early processes of fertilization. Also involved in regulation of receptors other than GPCRs. Involved in endocytosis of TGFBR2 and TGFBR3 and down-regulates TGF-beta signaling such as NF-kappa-B activation. Involved in endocytosis of low-density lipoprotein receptor/LDLR. Involved in endocytosis of smoothened homolog/Smo, which also requires GRK2. Involved in endocytosis of SLC9A5. Involved in endocytosis of ENG and subsequent TGF-beta-mediated ERK activation and migration of epithelial cells. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in insulin resistance by acting as insulin-induced signaling scaffold for SRC, AKT1 and INSR. Involved in regulation of inhibitory signaling of natural killer cells by recruiting PTPN6 and PTPN11 to KIR2DL1. Involved in IL8-mediated granule release in neutrophils. Involved in the internalization of the atypical chemokine receptor ACKR3. Acts as an adapter protein coupling FFAR4 receptor to specific downstream signaling pathways, as well as mediating receptor endocytosis . During the activation step of NLRP3 inflammasome, directly associates with NLRP3 leading to inhibition of pro-inflammatory cytokine release and inhibition of inflammation .

P32121

Q2NF48

RL37_METST

50S ribosomal protein L37e

Methanosphaera

MKGTPSFGKRNKKNHIRCRRCGRNAYNPTKKYCASCGFGRSKRLRRYSWQNKKPVTGKRLK

Binds to the 23S rRNA.

Q2NF48

Q6B6N4

PCNA_HAPBU

Proliferating cell nuclear antigen

Haplochromis

MFEARLVQGSILKKVLEALKDLITEACWDVSSSGISLQSMDSSHVSLVQLTLRHDGFDSYRCDRNLAMGVNLSSMSKILKCAGNEDIITLRAEDNADTLALVFETLNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSQIGDAVMISCAKDGVKFSASGELGTGNIKLSQTSNVDKEDEAVTIEMNEPVQLIFALNYLNFFTKATPLSKTVTLSMSADIPLVVEYKIADMGHIKYYLAPKIDEEAS

This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.

Q6B6N4

Q8LG54

AGP7_ARATH

Classical arabinogalactan protein 7

Arabidopsis

MNSKIIEAFFIVALFTTSCLAQAPAPSPTTTVTPPPVATPPPAATPAPTTTPPPAVSPAPTSSPPSSAPSPSSDAPTASPPAPEGPGVSPGELAPTPSDASAPPPNAALTNKAFVVGSLVAAIIYAVVLA

Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.

Q8LG54

Q9MUX3

MATK_SORBI

Intron maturase

Sorghum

MEKFEGYSEKQKSRQHYFVYPLLFQEYIYAFAHDYGLNGSEPVEIFGCNNKKFSSILVKRLIIRMYQQNFWINSVNYPNQDRLFDHRNYFYSEFYSQILSEGFGIVVEIPLSLGQLSCPEEKEIPKFQNLQSIHSIFPFLEDKFLHLHYLSHIEIPYPIHLEILVQLLEYRIQDVPSLHLLRFFLHYYSNWNSLITSMKSIFLLKKENKRLFRFLYNSYVSEYEFFLLFLRKQSSCLRLTSSGTFLERIIFSGKMEHFGVMYPGFFRKTIWFFMDPLMHYVRYQGKAILASKGTLLLKKKWKSYLVNFSQYFFSFWTQPQRIRLNQLTNSCFDFLGYLSSVPINTLLVRNQMLENSFLIDTRMKKFDTTVPATPLVGSLSKAQFCTGSGHPISKPVWTDLSDWDILDRFGRICRNLFHYYSGSSKKQTLYRLKYILRLSCARTLARKHKSTVRTFMQRLGLVFLEEFFTEEEQVFSLMFTKTKTIHFSFHGSQSERIWYLDIIRINDLVNPLTLN

Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.

Q9MUX3

B0K9P1

DUT_THEP3

dUTP pyrophosphatase

Thermoanaerobacter

MSIILKIKKTDDAKDLPLPAYMSEGAAGMDLYANVKEEVILQPGEIKLIPTGIQIELPPNFEAQIRPRSGLALNYGITLLNTPGTIDSDYRGEIKLIVINLGKEAVKIARGQRIAQMVINQIVRPTIVEAEILSETKRDEGGFGHTGI

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.

B0K9P1

Q6GF05

MAZF_STAAR

mRNA interferase MazF

Staphylococcus

MIRRGDVYLADLSPVQGSEQGGVRPVVIIQNDTGNKYSPTVIVAAITGRINKAKIPTHVEIEKKKYKLDKDSVILLEQIRTLDKKRLKEKLTYLSDDKMKEVDNALMISLGLNAVVHQKN

Toxic component of a type II toxin-antitoxin (TA) system. Ribosome-independent, sequence-specific endoribonuclease that cleaves mRNA, thus inhibiting protein synthesis and inducing bacterial stasis. It cuts between the first and nucleotides of 5'-UACAU-3' in single-stranded RNA. Neutralized by coexpression with cognate antitoxin MazE.

Q6GF05

Q03646

MSA2_PLAF2

Merozoite surface antigen 2

Plasmodium (Laverania)

MKVIKTLSIINFFIFVTFNIKNESKYSNTFINNAYNMSIRRSMAESKPPTGDGAVASAGNGAVASAGNGAVASAGNGAVASAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAGNGAVASAGNGAGNGAVASAGNGAVAERSSSTPATTTTTTTTNDAEASTSTSSENSNHNNAETNPKGNGEVQPNQANKETQNNSNVQQDSQTKSNVPRTQDADTKSPTAQPEQAENSAPTAEQTESPELQSAPENKGTGQHGHMHGSRNNHPQNTSDSQKECTDGNKENCGAATSLLNNSSNIASINKFVVLISATLVLSFAIFI

May play a role in the merozoite attachment to the erythrocyte.

Q03646

A5DZ02

RRG9_LODEL

Required for respiratory growth protein 9, mitochondrial

Lodderomyces

MLSQCFRSSLAKHCFVAKNQALHGKFVNSIMCLSSSSSNSGSSNSNSNSGSSNSNIRYNDNYRSNDDGTNFEELQLPSALKSETESLNGKGKNKLSKRPQTLLEALIESHGTLPEEVDEPKITRNVASESATSATSATSATSATSATSATSATSATSATSATSATSTTTIITTTATVPVENNVSTPYWVKRELTMKAKHSQWNPKKKLSREDMLKLRELKENFPHYKTVELAELFRVSPEAVRRILKSNWVPNDIDEDRIIARREKQKQKRQQEIQLKKLEFISNRGKKNVSSRPQQRQQQQPKQQQRQRSKVGYKNGFAFNEKYGGLGNKF

Required for respiratory activity and maintenance and expression of the mitochondrial genome.

A5DZ02

A6WJ17

CH60_SHEB8

Chaperonin-60

Shewanella

MAAKEVVFGNDARVRMLAGVNILANAVKVTLGPKGRNVVLDKSFGSPLITKDGVSVAKEIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIVVEGLKAVAAGMNPMDLKRGIDKAVIAAVAELKALSQPCADSKAIAQVATISANSDESIGEIIATAMEKVGKEGVITVEEGQALENELDVVEGMQFDRGYLSPYFINKPETGSVELDHPFVLLVDKKISNIRELLPILEGLAKTGKPLLIVAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDVAILTGGTVIAEEIGLELEKATLEDLGTAKRVVITKDNTTIIDGNGEQTQIAARVSQIKQQVEESTSDYDKEKLQERMAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVPGGGVALVRVASKIADVEVLNEDQKHGVVIALRAMEAPLRQIATNAGEEASVVANTVKNGSGNYGYNAGNDTYGDMLEMGILDPTKVTRCALQFAASIAGLMITTEAMVAEIPQNASQDMGGMGGMGGMGGMM

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.

A6WJ17

B4S8V2

SYDND_PROA2

Non-discriminating aspartyl-tRNA synthetase

Prosthecochloris

MSLAPGTETDLQNRFRSHFCGRLNTEYENKQVRLAGWIHRKRDHGGLIFIDLRDHTGIAQLIIQPEKQELFQKVERLHVESVIAVQGTVVKRSEETLNSRIPSGAIEVLVDDVQVESHAVALPFPVADELQTSEELRLTYRFLDLRREKIHQNIVFRSQLISKVRRYLEDHGFMEIQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVSGFPRYFQIAPCFRDEDARADRSPGEFYQVDMEMAFIEQDDLFEILEGMLRYLTETMSTKRITQFPFPRLSYRDVMNRFGSDKPDLRVPLEMQDVTELFVGSSFKVFASNTKEGSCIKAMVLKGRGTESRQFYDKAEKRARELGAPGLAYVQYREEGPKGPIVKFLSEAELSALQERLAIETGDVVFFGAGKWEKTCKIMGGIREYFSDLFELDRDELSFCWIVDFPLYEFDEKESRIDFSHNPFSMPQGEMDALDTMNPLDILAYQYDIVCNGIELSSGAIRNHRPDIMYRAFEIAGYSKEEVDKRFGHMIEAFKMGAPPHGGIAPGLDRLVMILRDEHNIREVIAFPMNQQAQDLMMSAPSDVSRLQLRELHLKLDLPVETAEQEPG

Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).

B4S8V2

P06799

IFNA7_MOUSE

Interferon alpha-7

Mus

MARLCAFLMVLAVMSYWPTCCLGCDLPQTHNLRNKRALTLLVKMRRLSPLSCLKDRKDFGFPQAKVDAQQIQEAQAIPVLSELTQQILNIFTSKDSSAAWNATLLDSVCNDLHQQLNDLQGCLMQEVGVQELSLTQEDSLLAVRKYFHRITVFLREKKHSPCAWEVVRAEIWRALSSSANLLARLSEKKE

Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.

P06799

Q133T3

THIC_RHOPS

Thiamine biosynthesis protein ThiC

Rhodopseudomonas

MNIRSNPDTTRPAVTTGGLPSSKKIYATPAAAPDLRVPLREIILSEGAGEPNLPIYDTSGPYTDPSVTIDVNAGLSRARTQWVKERGGVEEYQGRDVKPEDNGNVGAAHAAKSFTAYHKPLRGIGDAPITQYEFARRGIITKEMIYVAERENLGRKQQLERAEAALADGESFGASVPAFITPEFVRDEIARGRAIIPANINHGELEPMIIGRNFLTKINANIGNSAVTSSVEEEVDKMVWAIRWGADTVMDLSTGRNIHTTREWILRNSPVPIGTVPIYQALEKCEGDPVKLTWELYKDTLIEQCEQGVDYFTIHAGVRLQYIHLTANRVTGIVSRGGSIMAKWCLAHHKESFLYTHFDEICDLMRKYDVSFSLGDGLRPGSIADANDRAQFAELETLGELTKIAWAKGCQVMIEGPGHVPMHKIKINMDKQLKECGEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGCAMLCYVTPKEHLGLPDRNDVKVGVITYKIAAHAADLAKGHPAAQLRDDAVSRARFDFRWQDQFNLGLDPDTAQAFHDETLPKDAHKVAHFCSMCGPKFCSMKITQDVRDYAAGLGDNEKAALYPAGSVGMSISGVIEDGMAQMSAKFRDMGEHLYLDAEKVKESNKALS

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.

Q133T3

Q03QT7

TRUB_LEVBA

tRNA-uridine isomerase

Levilactobacillus

MNGIIPLYKERGLTSFDCVAKLRHILQTKKVGHSGTLDPSVDGVLPICIGSATKVVPYLMASGKVYRGSVTLGLATTTEDLDGDVVERQPLERPFTADQVAAAAQALTGTIQQTPPMYSAVKVNGRKLYEYARAGETVERPTRTITVDRFDLQGAGTFDATAGTQTIDFEIACSKGTYVRTLAVDLGQQLGVPAVMATLTRLKSGGFTLSQTVTLADVEAAMADDQIERTLRPIDYALQDYPHVALDEHLWALVKNGVFLSAAELNQATEPELALTYQGETKCLYRWSDEKKQYRPLKMFAVN

Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.

Q03QT7

Q66HD6

LRC18_RAT

Leucine-rich repeat-containing protein 18

Rattus

MAKGGKSPKGKKITLNVAKNCIKITFDGRKRLDLSKMGITTFPKCILRLNEIDELDLSRNMIRKIPDSISKFQNLRWLDLHSNYIDKLPESIGQMTSLLFLNVSNNRLTTNGLPVELNQLKNIRTVNLGLNHLDSVPTTLGALKELHEVGLHDNLLTSIPAGISKLPKLKKLNVKRNPFPKPDESDMFVDSIKRLENLYLVEEKDLCSSCLQKCQQARDKLNKIRSMAPSAPRKAIFSNLVSPNSTAKESQEEWSV

May be involved in the regulation of spermatogenesis and sperm maturation.

Q66HD6

Q42564

APX3_ARATH

L-ascorbate peroxidase 3

Arabidopsis

MAAPIVDAEYLKEITKARRELRSLIANKNCAPIMLRLAWHDAGTYDAQSKTGGPNGSIRNEEEHTHGANSGLKIALDLCEGVKAKHPKITYADLYQLAGVVAVEVTGGPDIVFVPGRKDSNVCPKEGRLPDAKQGFQHLRDVFYRMGLSDKDIVALSGGHTLGRAHPERSGFDGPWTQEPLKFDNSYFVELLKGESEGLLKLPTDKTLLEDPEFRRLVELYAKDEDAFFRDYAESHKKLSELGFNPNSSAGKAVADSTILAQSAFGVAVAAAVVAFGYFYEIRKRMK

Plays a key role in hydrogen peroxide removal.

Q42564

Q5NBT9

TPR1_ORYSJ

Topless-related protein 2

Oryza sativa

MSSLSRELVFLILQFLDEEKFKETVHKLEQESGFFFNMKYFEEKVHAGEWDEVEKYLSGFTKVDDNRYSMKIFFEIRKQKYLEALDRHDRAKAVDILVKDLKVFSTFNEELYKEITQLLTLENFRENEQLSKYGDTKSARSIMLIELKKLIEANPLFREKLVFPTLKASRLRTLINQSLNWQHQLCKNPRPNPDIKTLFTDHTCTPPNGARASPVSVPLAAVPKAGGTYPPLTAHTPFQPPPAGPSLAGWMANAAAATSSVPSAVVAASSLPVPPNQAVPIMKRPTITDYQSAESEQLMKRLRPSGHGVDEATYPAPIPQPLWSVEDLPRTVACTLSQGSSVTSMDFHPTRHTLLLVGSTNGEITLWEVGMRERLFSKPFKIWDIQACSPQFQSVAKESSISINRVTWSPDGDLIGVAFAKHLIHLHAYQQPNETRQVLEIDAHSGAVNDIAFSRPNKQLCVVTCGDDRLIKVWDMHGQKLFSFEGHEAPVYSICPHHKESIQFIFSTSLDGKIKAWLYDHMGSRVDYDAPGKWCTTMLYSADGTRLFSCGTSKDGDSYLVEWNESEGSIKRTYSGFRKKSAGVGVVQFDTAQNHILAAGEDNQIKFWDVDNTTMLSSTEADGGLPGLPRLRFNKEGNLLAVTTVDNGFKILANADGLRTLRAFGNRPFEAFRSQYEASSMKVSGAPVVAGISPNIGRMDHIDRNSPAKPSPIMNGGDPASRSIDIKPRISEERPDKAKPWELMEVLNAQQCRVATMPETPDQASKVVRLLYTNSGVGLLALGSNAIQRLWKWARNDQNPSGKATANVVPQHWQPNSGLVMQNDTADTNPEDAVPCIALSKNDSYVMSACGGKVSLFNMMTFKVMTTFMPPPPASTFLAFHPQDNNIIAIGMEDSTIHIYNVRVDEVKTRLKGHQRRITGLAFSNNLQILVSSGADAQLCVWATDTWEKKKSVAIQMPAGKTPSGDTWVQFNSDWSRLLVVHETQLAIYDASKMERIYQWIPQDALSAPISHASYSRNSQLVFAAFTDGNIGIFDVENLRLRCRIAPPAYLSSAAINSNPSVYPLVVAAHPQESNQFAVGLSDGSVKVIEPLESEGKWGTTPPTENGVPNGRTSTSSATSNPAADQIQR

Probable downstream regulator of strigolactones signaling.

Q5NBT9

Q9VE86

WRNXO_DROME

Werner Syndrome-like exonuclease

Sophophora

MEKYLTKMPIKSKANEVPKEEAGVKKETPKVARKATKKDTPKELKDKENAGDDNTPKQTKGRPGRPAAKRKNLDTPDVTEKLAMEEENPPKRRSSRLTRSTRSMAEDGSPSPEKEKPEKLPFIKYKGAIKYFTESQDIAASADDVLQWVEKQKDEVVPMAFDMEWPFSFQTGPGKSAVIQICVDEKCCYIYQLTNVKKLPAALVALINHPKVRLHGVNIKNDFRKLARDFPEVTAEPLIEKCVDLGLWCNEVCETGGRWSLERLTNFIAKKAMDKSKKVRMSKWHVIPLDENQLMYAAIDVYIGQVIYRELERREKVKIKNEEEFKEKNGDAAFKAMKALGETFLTKINEVTL

Has exonuclease activity on both single-stranded and duplex templates bearing overhangs, but not blunt ended duplex DNA, and cleaves in a 3'-5' direction . Essential for the formation of DNA replication focal centers . Has an important role in maintaining genome stability .

Q9VE86

Q7M8Z6

HSLV_WOLSU

ATP-dependent protease subunit HslV

Wolinella

MFEATTILAYKGENHSVIGGDGQVTFGNCVLKGNATKIRMLYNGKILSGFAGSTADAFTLFEMFERILENRKGDLVKSVIDFSKEWRKDKYLRRLEAMMIVMDRERLFILSGTGDVVEPEDGKIAAIGSGGNYALSAARALDKFADLPESELVRESLLIAGELCIYTNTNIKLLEL

Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.

Q7M8Z6

C1CVC5

NUSB_DEIDV

Antitermination factor NusB

Deinococcus

MTRRREKAVQPVGTRRAAREFVFRVLFEADRGDLPLDTVFTRAEGAMREGDDTFPQLSADALTFANELVRGLEKHRADIDTTLRRTIRGWSFDQMAQTDLNVLRLATFELIYTAEPHPPVIESAVRIARKFGGDDSGRFVNGVLAGLSRSLQSAGVAKADEQADTAQD

Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.

C1CVC5

Q99KW3

TARA_MOUSE

Trio-associated repeat on actin

Mus

MSMEQDTRALLPTQGTAWATASAPVARLQGPQGDSHQACSQEPHSPSSAEAPYCDLPRCPPALQNPLRTTTCVGQSVHSLGLGLGQEPQRVWSPTTALPAEGPAAAPKNRHQDSEGIPYLEGLARSSCTDDNDNKDEDEDPNSNTSSSQDSNTPHDTSNSSSVDWDTTERPGVVPSRNRLTEMIPRRPQEGLRADSARKATRSPARGDTAGQRKENSGSGGQSAGQHWAKLRSESGYFSLERQRSGQTQASSGTPPSGPRGTTQASSAQRDVFQAAPAQEAPQTSSLPRNTQRDTQRSTPRTSSPSRVSQRDTPRVMSTQRKNTPLSSPLRATPETLKISAPEDGTHVTPSPCVQDSSLNRTSQRDSSRTPCIQWDNPRASSPNRTTQRDNPRTPCTQRDNPRASSPNRTTQRDNPRTPCTQRDNPRASSPNRTTQRDNPRTPCAQRDNPRAASPNRSTQRDSPRTPCAQRDNPRASSPNRTAQRDNPRTPCAQRDNPRTSCTSQNTPRTPSTQADKTTASCSKWEHLRSACTQRDNPRTFSQGCTQKDNPGPPSPRRATQGSNSRNPSPHRTNKDIPWASFPLRPTQSDSPRTSSPSRTKQNQVPWASISLRPTQGDKPQTSAPTRLAHNDPPQQYSPSLATTSSSSHNPGHSSASRTSSPLHAAPRGAPQTSLESSQPPCTVCIGHRDAPRASSPPRYFQYDPFPFFPDPRSSESESPHHEPPYMPPAVCIGHRDAPRATSPPRHTQFDPFPFLPDTSDADNESPQHDPPQFPPPVCIGYRDAPRASSPPRQFPEPSFFQDLPRASTESLVPSTDSMHEPPHIPTPVCIGHRDAPSFSSPPRQAPEPSLFFQDPPGTSMESLAPSIDSLHGCPLLPPQVCIGHRDAPRASSPPRHPPSDIGLLAPSPPPGSSGSRGSAPPGETRHNLEREEYTMLADLPPPRRLAQRGPEPQAQGSNEGRTRSPGRAEVERLFGQERRKSEAPGAFQTRDEGRSQRPSQAQSQLRRQSSPAPSRQVTKPSAKQAEPTRQSRTGPPHPKSPDKRPEGDRQLQRTSPPARTPARPPERKAQIERHLESGHTGPRQSLGGWQSQERLSGPQSPNRHPEKSWGSQKEGPSLGGWPELEGPSLEGIWRGPPQEHREQWGHSEAWEEPPSNGIQGAPPRGQGRLQELSRPHQPTPSSENSWAGPAECSCALQPEASTAVGWRAEGTSPHQRSAERPPDLDWRDLLGLLRAPEDGAWTRLPRLDWEGLLELLQARLPQKDPARHWHDPAKASGPEQGSSGTEDTLKTEPQTQPEGRAKATLANGHRPGQQSESPAQLPSPACTSTQWPTTKVTSGPETSPLAALEQIDHLESHSPPDLEFQPEEPEASEPSRGEDSRAVQKQADSADKRPAEGKAGSPLKGRLVTSWRMPGDRPALFNPYLLSLGVLRWQRPDLLNFKKGWMSILDEPGEWKKHWFVLTDSSLKYYRDSTAEEADELDGEIDLRSCTDVTEYAVQRNYGFQIHTKDAVYTLSAMTSGIRRNWIEALRKTVRPTSAPDVTKLSDCNKENTLHGYGTQKSSLKIGEQRTGSEVIGRGGPRKADGPRPSLDYVELSPLAPSSPQRMRTLSRSTPERPTKQEDLERDLAQRSEERRKWFESTDGRTPETPSGDGSRRGLGAPLTDDQQSRLSEEIEKKWQELEKLPLRENKRVPLTALLNQAHNDRRGPTSDSHEALEKEVQSLRAQLEAWRLRGEAPQNAPRLQEDSHIPPGYISQEACERSLAEMESSHQQVMEQLQRHHERELQRLQQEKEWLLAEETAATASAIEAMKKAYQEELSRELSKTRSLQQGPESLRKQHQLDMEALKQELQVLSERYSQKCLEIGALTRQAEEREHTLRRCQQEGQELLRHNQELHSHLSEEIDRLRSFIASQGTGNSCGRSNERSSCELEVLLRVKENELQYLKKEVQCLRDELQVIQKDKRFTGKYQDVYVELNHIKTRSEREIEQLKEHLRLAMAALQEKEAVRNSLAE

May regulate actin cytoskeletal organization, cell spreading and cell contraction by directly binding and stabilizing filamentous F-actin. The localized formation of TARA and TRIO complexes coordinates the amount of F-actin present in stress fibers. May also serve as a linker protein to recruit proteins required for F-actin formation and turnover.

Q99KW3

B1VGB7

RIMP_CORU7

Ribosome maturation factor RimP

Corynebacterium

MATPLDEKLRALAADEAMKCGLDVEKLTFTRAGAKSSVKIAVDADERPDLDLLEEASQLIGAAFDAAEEAQQIDLGPSYTLEVTTPGLDFPLREARNFQRNIGRLANLPGGGKGRIAAVENDEVAILPAAKKKAGKKSQGKKAGKKTPQAPVQIYPRAELAGSTIEVEFSPAPAAEQELLGLTMAEYHELAKSDEA

Required for maturation of 30S ribosomal subunits.

B1VGB7

P81646

LALBA_TACAC

Lactose synthase B protein

Tachyglossus

KVFEKCELSQMLKANGLDGFQGITLEEWICIAFHESGFDSRALNYYNGSSSHGLFQINRQYWCDGQDAKSTEPSVNACQISCDKLRDDDIEDDIKCVKKILKESQGITAWEAWQPFCIADLDQWKC

Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.

P81646

Q18DH0

HIS3_HALWD

Phosphoribosyl-AMP cyclohydrolase

Haloquadratum

MTDDAVTGSQDDAEIEIRFNSDGLVPAIAQDADSGEVLMLAYVSPTALKRTRETGQAHYYSRSREELWKKGETSGHTQHIREIRADCDADTILYLVEQTGGACHTGHQSCFYRTLDGTEVTERVFDPETVYE

Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.

Q18DH0

A3QGA2

EFTS_SHELP

Elongation factor Ts

Shewanella

MAITAAQVKELRERTGAGMMDCKKALTETNGDIELAIENMRKSGAAKAAKKAGNIAAEGTILIKQGEGFSVLLEVNCQTDFVAKDSNFLAFANEVLDVAAAGKVSIADLQAQFEETRVALVAKIGENINVRRVEYIDGASQASYRHGDRIGVVVTGEADEETLKHVAMHVAASKPEYVNPSDVPAEVVEKEKAVQIEIAMNEGKPQEIAEKMVAGRMKKFTGEVSLTGQAFIMEPKKTVGEILKEKGATVTNFIRLEVGEGIEKKEEDFAAEVAAQIAASKA

Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.

A3QGA2

B3E8Z1

GLGC_TRIL1

ADP-glucose synthase

Trichlorobacter

MFDGSNLGRNTIAMVLAGGKGERLMPLTLRRAKPSVTFGGKYKIIDFVLSNLFNSGIRRMYILTQYRAYSLNKHIRESWGKWTGLGEFCVAISPETSSDSEQWFKGTADAILQYLRFVETADADYVAVFGGDHIYKMDVTQMIQFHRMNRADLTIASLEVPKEEASRFGVFSVDDDNRVTAFTEKPKDPETIPGRETCFASMGNYIFPTRKLIEVLLEGKKHYEDLDFGKHVIPMMLEKGDRIYAYNFNDNLVPGMKSEERGYWKDVGTLDSYYEANMDLIHVSPQLNLYNYKWPILTNQGNLPPAKTVFDEEGRRGVNIDSYVTGGCITSGSTVRRSILGPMCKINSYSLVEDSILFEGVTVGRHVKIKKAIIDKGVVIPDGAEIGCNHEDDIKNGYTITESGIVVVPRKDR

Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.

B3E8Z1

B3EWS6

TXC12_CUPSA

CSTX-12 B chain

Cupiennius

MKVLVICAVLFLTIFSNSSAETEDDFLEDESFEADDVIPFLAREQVRSDCTLRNHDCTDDRHSCCRSKMFKDVCKCFYPSQRSDTARAKKELCTCQQDKHLKFIEKGLQKAKVLVAG

Synergistic toxin that induces or increases a cytolytic effect when combined with CSTX-1 (AC P81694) or CSTX-9 (AC P58604). When alone, has a weak insecticidal activity, with an unknown molecular target.

B3EWS6

Q4ZWV2

KAD_PSEU2

Adenylate monophosphate kinase

Pseudomonas syringae

MRVILLGAPGAGKGTQAKFITEKFGIPQVSTGDMLRAAVKAETELGLKAKSVMDSGGLVSDDLIIGLIKDRLAEPDCANGVLFDGFPRTIPQAEALLNAGLEIDHVLEIAVDDEEIVKRMSGRRVHEGSGRIYHTIFNPPKVEGIDDVTGEPLLQRKDDVEETVRHRLSVYHAQTKPLVEFYSKLEAKNGKPKCSHIPGVGSVEDITAKVLKALS

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.

Q4ZWV2

Q8DHM0

SSRP_THEVB

Small protein B

Thermosynechococcus

MGDSIKVLSENRQARFQYEILETYECGLVLLGTEVKSIRAGKVNLRDGFARIRNGEAWLMNVHISPHESTNPSYNHDPLRDRKLLLHKQEIRKLVGKVEQKGLTLVPLKLYLKNGRVKVSLGLARGKKLHDKRQDLKQRQDKREMERAMKQR

Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.

Q8DHM0

Q2R222

C6_ORYSJ

Non-specific lipid-transfer protein C6

Oryza sativa

MAPSKSTAAAGVLLVLLVAAAGGGAEAAATTCVASLLELSPCLPFFKDKAATAAPEGCCAGLSSIVKGEAVCLCHIVNHTLERAIGVDIPVDRAFALLRDVCRLSPPADIISTCANEKGGVPPLYSCPAPSA

Lipid-transfer proteins that possesses lipid-binding activity in vitro. Involved in the development of lipidic orbicules/Ubisch bodies and pollen exine during anther development . May be regulated by the transcription factor UDT1 in developing anthers and play a role in tapetum development . Positively regulated by the transcription factor TDR in developing anthers and may play a role in tapetum programmed cell death (PCD) .

Q2R222

P61704

SYA_MYCMS

Alanyl-tRNA synthetase

Mycoplasma

MKKLSTNQIRKIWLDFFISKNHYFLETVSLIPVDDPSLLWINSGVATLKPYFDGRKTPPSPRLTNSQKAIRTNDIENVGVTARHHTMFEMLGNFSIGDYFKKEAIELAWELLTDKKYFDIDKNKLYITVFNEDTEAYNIWKDVIKIDEDHIFRLSRKTNFWDVGQGPCGPNTEIFYDRGEIWDPNKIGPRLISDDIENDRYIEVWNIVFSQFNNDGNNNYVELPRKNIDTGAGLERFASIFQNTPTNFETDIFYPTIKKVEQLTNNQFKYSIDNYFNPNKKQTRINTAFKVIADHIRATVFAISDGVFPGNKDRGYIIRRLIRRSCVFGKELGIKQAFLYKLVDSVIESMKEFYPYLIDKKTLVEQTIKDEEEKFLKTLSKGYDLLENIIKTKNTVSDKDALLLFESYGFPIEQTIEISELSNVTVDVEGFKKLLEQTKQATRNARKDLKAWDKQNELFTKLKVESEFTGWSETSRDNAKVIYMFTDQKQVESITNQEVFVILDKTPFYAEKGGQAADSGIIFNDQMKGFVIDVQQGPTHQNIHRIKVQGTLKVNDLINCRVDEEKRIYTMKNHSGTHMIHYALREVLGTSVMQSGSYNDENGLRMDFTYHRLPTNQELLKAQNLVLEKIKNKIDRQTYFCSLEESVKKHQALAFFTEKYDQIVRVIKFGDFSSELCGGTHVNNTSEIEDFIITGIESKGSGLYRIKCLTSFRAVNEYLNEQFKVYKDQAESIIDKYNQNKDLLKNDQLENIYLQIKNTTINKDNLLVIKNLLDQSKEVNKDYDKKVNDLITANKLLKYKDLTPSLNKDNINEIRLETTDLNIKDLKQLADDLRNKYNDLIVILLSSTNENTFIVVAVSQSLQNKYKAIDIFNNLEGYETKGGGNANLAQGKFVKK

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.

P61704

P33546

ICSB_SHIFL

N-epsilon-fatty acyltransferase IcsB

Shigella

MSLKISNFIDASNTKGPIRVEDTEHGPILIAQKFNLKDLFFRTLSTINAKINSQILNEQLKNYRLENQKSLLLFLNTLASEKSAESAFAAYEAAKNSIQHSFTGRDIKLMLNTAERFHGIGTAKNLERHLVFRCWGNRGITHLGHTSISIKNNLLQEPTHTYLSWYPGGNVTKDTEINYLFEKRSGYSVDTYKQDKLNMISEQTAERLDAGQEVRNLLNSKQDQNNNKKIFFPRANQKKDPYGYWGVSADKVYIPLSGDNKTKDGKISHNLFGLDETNMSKFICKKKADAFRQLANYKLISKSENCAGMALNVLKAGNSEIYFPLPDVKLVATPNDVYAYANKVRQRIESLNQSYNEIMKYIESDFDLSRLTQLRRSYLKSFNKINLIHTPKTFKPLSISLYKHPTENVSSEDFDAVINACHSYLVKSAPSNMTRVLNELKTEATDKKEEIIEKSIKIIDYYNSLKSPDLGTKLYIHDLLQINKLLLNNSHSNI

Virulence-associated N-epsilon-fatty acyltransferase that mediates lysine-stearoylation of host Rho GTPase proteins, thereby disrupting the host actin cytoskeleton . Required at the post-invasion stage of Shigella pathogenicity .

P33546

Q7JZV0

LCP2A_DROME

Larval cuticle protein 2A

Sophophora

MKFFIAFACLLAVALANEDANVLRAEQQVNVDGFAYAVELDNSVNVQQKGDLNGEEWVVKGSQSWTSPENVPVSIQYIADANGYQVVSANPPLPTPPPIPEAIQRSLEYIAAHPPSQ

Component of the larval cuticle.

Q7JZV0

Q92LB3

PROB1_RHIME

Gamma-glutamyl kinase 1

Sinorhizobium

MTKARKALENYRRVVIKIGSALLVDRRTGLKKSWLDALCADIAALRAKGVEVLVVSSGAIALGRTVLDLPAGALKLEESQAAAAVGQIVLARAWSESLSTHAIVAGQILLTLGDTEERRRYLNARATIGQLLKLGSVPIINENDTVATTEIRYGDNDRLAARVATMVGADLLVLLSDIDGLYTAPPHLDPNARFLETVAEITPEIEAMAGGAASELSRGGMRTKIDAGKIATTAGCAMIIASGKPDHPLAAIEAGARSSWFAPSGSPVTARKTWIAGQLLPAGSLSIDAGAETALRSGKSLLPAGVRQVTGSFSRGDTIAIIGASGREIARGLAGYDADEARQIAGKKSAEIAAILGYAGRTAMVHRDDLVMTAPSGARLVEESDEGKGKLHA

Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.

Q92LB3

Q12420

SNU66_YEAST

66 kDa U4/U6.U5 small nuclear ribonucleoprotein component

Saccharomyces

MNKTENLSIEETNEIREKLGMKPIPVFQEKNTDHKESLSIEETNELRASLGLKLIPPQQNFNSSPPNVHNTSKIDELREKITKFQKKANAPLRMAHLLEETNVNDDSSWLENMDAIPSSHESKRSSTLPRKGATKEDENIDLHNVQVSYNIEALSPKKDTILTLKESSIFDDTDSTEVLENVKAAEENADREKLRLRQMNKDRRQKKKILNVSSLDIEEEEEGEKHSITTTHLIIGAEQGVMKAPNTISAKPPTGKVKVNFDSANNMSDEDGGDFKPLKIKKRKIKDPRSTKARKSKITDKMEIVKLVDEDESLSWMEEEQPVTIINPRTSSNNELKGPEDLAREIEKARDEEKRRTESILKMREISNSIVVDEKVTFLNTLDTSLSERSATENKVKVHGEGEKNIGDVTNGHTKEGSGNNTLTEAVNNEPNYEGDAENAPNFFSGLASTLGYLRKKSVFTTGDVDLKPGKDVNNSESLRRDVRNKEHTGTGTYTKDKLHGLEQFTSSDSSNANTHSKRQDHYDPDIKLVYRDEKGNRLTTKEAYKKLSQKFHGTKSNKKKRAKMKSRIEARKNTPENGSLFEFDDN

Component of the U4/U6.U5 tri-snRNP particle, one of the building blocks of the spliceosome. Required for pre-mRNA splicing.

Q12420