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stringlengths 6
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stringclasses 1
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Q9VVE5 | RNA binding protein that regulates the expression of target mRNAs at the translation level. May play a role in the proliferation and maintenance of stem cells in the central nervous system | FUNCTION | MDIKIEQQQQQQQVELGPCSPSEVPNDPGKMFIGGLSWQTSPESLRDYFGRYGDISEAMVMKDPTTRRSRGFGFVTFSDPNSVDKVLTQGTHELDGKKVDPKVAFPRRAHPKMVTRTKKIFVGGLSAPTTLEDVKSYFEQFGPIEDAMLMFDKQTNRHRGFGFVTFQSEDVVDKVCEIHFHEINNKMVECKKAQPKEVMLPANLAKTRAAGRSAYDNIMWGLGTLPEGFPAAAYAAYAAGRGYSGYPSFGLPYPTVDLTNGQLTPNNNTPLLTQALSVMNNYQAAAAAAHSYGPSASPHAAAANTATRQGFPSTNSPGPTIDMYSSAAADNVGYVQATSPQPSGFPIAVSRAPLNYSPIYSLNFAMANI | 369 |
Q5NHI5 | Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits | FUNCTION | MQYKTKAKKSLGQNFLQDENIIRKIVQLANIKKHDIVVEIGPGLGALTRYLLSSSNNVSVVEFDASVIDTLIANCQKYGTPHIYNQDFLKFDISSLENSSNQKIKLIGNLPYNISSPILFKVIKDSDKIVDAHFMLQKEVVERIVSLPNSKSSGRLSVILQYHFDCSMILKIPPEVFYPQPKVDSAILRLKPKNSKELLKNYNFFEEIVKQSFAQRRKTLHNNLKSILKERKIDPSTLPVDTNLRAENLSVGDFVSLANFLS | 262 |
Q8DPS9 | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA | FUNCTION | MNKRMNELVALLNRYATEYYTSDNPSVSDSEYDRLYRELVELETAYPEQVLADSPTHRVGGKVLDGFEKYSHQYPLYSLQDAFSREELDAFDARVRKEVAHPTYICELKIDGLSISLTYEKGILVAGVTRGDGSIGENITENLKRVKDIPLTLPEELDITVRGECYMPRASFDQVNQARQENGEPEFANPRNAAAGTLRQLDTAVVAKRNLATFLYQEASPSTRDSQEKGLKYLEQLGFVVNPKRILAENIDEIWNFIQEVGQERENLPYDIDGVVIKVNDLASQEELGFTVKAPKWAVAYKFPAEEKEAQLLSVDWTVGRTGVVTPTANLTPVQLAGTTVSRATLHNVDYIAEKDIRKDDTVIVYKAGDIIPAVLRVVESKRVSEEKLDIPTNCPSCNSDLLHFEDEVALRCINPRCPAQIMEGLIHFASRDAMNITGLGPSIVEKLFAANLVKDVADIYRLQEEDFLLLEGVKEKSAAKLYQAIQASKENSAEKLLFGLGIRHVGSKASQLLLQYFHSIENLYQADSEEVASIESLGGVIAKSLQTYFAAEGSEILLRELKETGVNLDYKGQTVVADAALSGLTVVLTGKLERLKRSEAKSKLESLGAKVTGSVSKKTDLVVVGADAGSKLQKAQELGIQVRDEAWLESL | 652 |
P75064 | Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate | FUNCTION | MDLKQQYILALDEGTSSCRTIVFDKDLNQVAIAQNEFNQFFPKSGWVEQDPLEIWSVQLATMQSAKNKAQIKSNNIAAVGITNQRETIVLWNKENGLPVYNAIVWQDQRTASLCDKLNQDTKIKEFVKKHTGLPINPYFSATKIAWILENVPLAQKMLKEDKLLAGTIDTWLIWKLTGGKMHVTDVSNASRTLLFDITTMTWSQELGDIFKVPLSILPKVMPSNAHFGDIVPSHWSTSATGMVPIRGVAGDQQAALFGQLCVEPAMVKNTYGTGCFMLMNIGNELKYSQHNLLTTVAWQLENQKPVYALEGSVFVAGAALKWLRDSLKVMYSAAESDFYAKLAQKEEQEVVFVPAFTGLGAPYWDASARGAIFGIEANTKREHLVKATLEAIAFQANDLIKAMASDLNSSIKKIKADGGACNSNYLMQFQADIANLEVIIPKNVETTTMGAAFLAGLAVNYWKDTKQLEKLTGIAKQFKSQMNQTVREKKSKRWNEAVKRTLKWASLD | 508 |
A8ACS4 | Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate | FUNCTION | MANYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDIAYALRKEAIAEKRASWRKATENGFKVGTYEELIPQADLVVNLTPDKQHSDVVRSVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQYGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKTIMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVLMIAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYLFSYACVPLLKAFMTEIQPGDLGKAIAEGAVDNAQLRDVNEAIRGHAIEKVGQKLRGYMTDMKRIAVAG | 491 |
P84441 | Mediates visceral muscle contractile activity (myotropic activity) | FUNCTION | GSSSGLISMPRV | 12 |
Q97JN8 | Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate | FUNCTION | MIRVKIPATSANMGAGFDTLGMALKLYNEITIEETEGETEIKLLGGELDRNYRNNLTYISIIKVYEFFNKEFKGFKIDMSKTNIPLSRGLGSSAACIVGGIVGANALLNEKMTIKDMLKIAVDIEGHPDNVAPALLGGVIISIKDMENIIYSRINVKSQLKYAVMVPDFKVSTELSRKVLPNEYSREDALFNISRCSMLVSALNNGENEKLRYLFEDKIHQPYRKKLINNIDSIFLKAKEYGSLGEFISGSGSTLIAVLEEADENFILKMKTYLDSLKDGWRIFEVENDNNGAVII | 296 |
Q5GXV3 | Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction | FUNCTION | MAKITKTFQYGKHTVTLETGEIARQAGGAVIVKFDDTVLLVTAVAAKSAREGQDFFPLTVDYQEKFYAGGRIPGGFFKREGRATEKETLISRLIDRPIRPLFPEDYKNEVQIIATVMSMNPDIDGDIAALIGASAALSLAGTPFNGPIAAAKVGYKNGEYILNPTVTDLKDSQLELVVAGTANAVLMVESEAELLSEEVMLGAVTFGHREMQKVINIINELAVEAGTKPSDWVAPAKNDGMIAALKEAVGDQLASAFQVRDKLQRRDAISAIKKDVLGALAPRATIEGWAAGDLAKEFGELEYQTMRGSVLSTKVRIDGRALDTVRPISAKAGVLPRTHGSALFTRGETQAIVITTLGTARDGQVIDAVSGEYKENFLFHYNFPPYSVGECGRFGAPKRREIGHGRLAKRGVLAVMPSLEEFPYTIRVVSEITESNGSSSMASVCGSSLALMDAGVPIKAPVAGIAMGLVKEGNDFVVLSDILGDEDHLGDMDFKVAGTAEGVSALQMDIKIEGITEEIMKQALQQAKAGRLHILGEMAHALTTPRQELSDYAPRLLTIKIHPDKIREVIGKGGSTIQAITKETGTQIDIQDDGTIIIASVNAIAAQAAKSRIEQITSDVEPGRIYEGKVAKIMDFGAFVTILPGKDGLVHVSQISSERVEKVGDKLKEGDLVRVKVLEVDKQGRIRLSIKAVEEGEGVPASAE | 704 |
Q58670 | S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis | FUNCTION | MLILAGLGLYDENDMTLKTLKFAKKAEKIYAEFYTAVLTGTTTEKIEEVLGKKIHVLSRKDVEYNGYKLIEEAKDKDIMFLTAGDPMVATTHVDLAIEAKKKGIEVLIINAPSIYSAVGITGLQLYKFGKTTSIVFPEENYFPETPYNVIKENLERGLHTLCLLDIRIDENEKRFMTANEGLKVLLELENRKKEGIINEDTKAVVVARAGSLKPKLVYGKIKDLINYDFGEPLHCIIIPGKLHFMEEDALKYLCENI | 257 |
P0A6A1 | Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis | FUNCTION | MTPGEVRRLYFIIRTFLSYGLDELIPKMRITLPLRLWRYSLFWMPNRHKDKLLGERLRLALQELGPVWIKFGQMLSTRRDLFPPHIADQLALLQDKVAPFDGKLAKQQIEAAMGGLPVEAWFDDFEIKPLASASIAQVHTARLKSNGKEVVIKVIRPDILPVIKADLKLIYRLARWVPRLLPDGRRLRPTEVVREYEKTLIDELNLLRESANAIQLRRNFEDSPMLYIPEVYPDYCSEGMMVMERIYGIPVSDVAALEKNGTNMKLLAERGVQVFFTQVFRDSFFHADMHPGNIFVSYEHPENPKYIGIDCGIVGSLNKEDKRYLAENFIAFFNRDYRKVAELHVDSGWVPPDTNVEEFEFAIRTVCEPIFEKPLAEISFGHVLLNLFNTARRFNMEVQPQLVLLQKTLLYVEGVGRQLYPQLDLWKTAKPFLESWIKDQVGIPALVRAFKEKAPFWVEKMPELPELVYDSLRQGKYLQHSVDKIARELQSNHVRQGQSRYFLGIGATLVLSGTFLLVSRPEWGLMPGWLMAGGLIAWFVGWRKTR | 546 |
A1TM37 | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP | FUNCTION | MQAAIKGRNVVVVGTQWGDEGKGKLVDWLTESAQGVVRFQGGHNAGHTLVINGVKTALHLIPSGIMRPGVKCYIGNGVVLSAAKLFEEIEGLEKAGVEVRSRLRISEACPLILPFHAALDVAREAAREHGGSEKIGTTGRGIGPAYEDKVARRALRVQDLKHPERFAAKLKELLALHNHVLKSFLHSGSFQFGSALQPYLKDGEVQFDAVYQEAMRHAELLKPMIADVSRELNEAHKAGANLLFEGAQGTLLDVDHGTYPYVTSSNCVAGNAAAGSGVGPGLLHYVLGITKAYCTRVGGGPFPTELEWEKPGTPGYHMSTIGAEKGVTTGRSRRCGWFDAALLKRSAQVNGLTGLCITKLDVLDGLEELKLCVGYELDGERIDILPMGAEEIARCVPVYETLAGWSDSTVGVTQYDSLPANARRYLERIAEVTAVPIAMISTSPDRDHTIMMQHPYAAQ | 459 |
Q39236 | TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity | FUNCTION | MATFELYRRSTIGMCLTETLDEMVQSGTLSPELAIQVLVQFDKSMTEALESQVKTKVSIKGHLHTYRFCDNVWTFILQDAMFKSDDRQENVSRVKIVACDSKLLTQ | 106 |
Q7NHZ4 | Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine | FUNCTION | MYQPPTGVRDLLPLDVSQKLWIEQRLQRVFTRWGYQRIITPTLERMETLQASGSVDLQAILQLRDAEGVSLGLRPDPTPSLARAVATRLADAPLPVRLSYQMNVFRSTTQPQEFYQAGVELIGAGGVLADAEVLLVLAECLAELAPPDWTLILGAVAFTRSWLAQVAEPARHRLRRAMAELDRVAILAEAGIDEAVRSQLLLLFDLRGEPEMVLSKASSLPMSDAQRAELAELETLTGWLRGRSVPVVLDLSLVEAFDYYTGLIFEVSAGGRLIGRGGRYDHLLGSYGKPAPGAGFALNLEALQQVLLPTGKLPGRTVGGGFLVVPDGPDAWEAALAEADKLRCAPGERVEIELLGRTGEEAIAHGRALGAAVVRWVHPDGSTTDCDLAVIQ | 392 |
F4JHH5 | Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall | FUNCTION | MQSSKGRRKVGSTTAGAGIDSAEKLDELLISSAICNGEDLGPFVRKTFGTGKPETLLHHLKFFARSKESEIEEVCKAHYQDFIHAVDDLKSLLSDVESLKSALSDSNSKLQSVAAPLLSSLDSLVEAQTVSKNVDLAIGAVTHCVRVMELVSRANQHLQSGNFYMALKCVDSIESDFMEKTPSSTLKRMLENRIPAIRSYVERKVNKEFGDWLVEIRVVSRNLGQLAIGEASAARQREEELRIKQRQAEEQSRLSLRDCVYALNEEEDDEFGSGHEGSDGGSSGGGLLGFDLTPLYRAYHIHQTLSLGDTFKQYYYNNRDLQLTSDFQIAGFFIVEDRVLRTGGGLISKLEVETLWDTAVTKMCAVLEDQFSRMQTANHLLLIKDYVSLLGVSLRRYGYAVDSLLEVLSKHRDKYHELLLSDCRKQITEALSADKFEQMLMKKEYEYSMNVLSFQLQTSEIVPAFPFIAPFSTTVPDCCRIVRSFIEDSVSFMSHGGQLDFYDVVKKYLDRLLGEVLDEALLKLISTSVHGVSQAMQVAANMAVFERACDFFFRHAAHLSGVPLRMAERGRRHFPLTKSQNTAEDTLSGMLKKKIDGFMTLLENVNWTSDDIPQGGNEYMNEVLIYLETLVSTAQQILPAKVLKRVLRDVLAHISEKIVGTLCGDLVKRLSMAAIKGLDVDIQLLDSFTENLTPLLTDKEAREMKKAFVEIRQMINLLLSSHPENFVNPVIRERSYNALDYRKVATVSEKFRDPSDSIFGTFGTRGSRQNPKNKSLDALIKRLKDVS | 787 |
O28498 | Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex | FUNCTION | MAKAPKGKAKTPPLMSSAGIMRYFEEEKTQIKVSPKTILAAGIVTGVLIIILNAYYGLWP | 60 |
Q6N583 | Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate | FUNCTION | MSVQSTIRRKTAPDIRARKGGDPIVMLTSYHAHTASLVDRYCDAILVGDSLGNVMHGFETTVPVTLEMMILQGHAVMRGSQHALVVVDMPFGSYEASKEQAFHSAARILKETHCGAVKLEGGVRMAETIAFLTERGIPVMGHIGLTPQSINTLGSFRAQGREEGSWEPIEADARAVADAGAFSVVVEAVAEPLGRKITEMISIPTIGIGASAACDGQVLVLEDMLGLSPKPPKFVKRYGDLGPGIEAAIKGYAEEVRSRAFPGPEHVYGMKSKA | 274 |
Q8DI02 | Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis | FUNCTION | MIAASGPTPLVATTQRTLAGTAQWSGVGLHSGQWVALTLQPAAANTGRQFVRLDLEGQPVIPARIEAVKSTQLATELVANGASVRTVEHLLAALAIAGIDNVTIQITGPEVPVLDGSAQPWLEGIQRVGVVPQEAPRPAVILKEPVTIYEGEAFVSAIPAPELRLTYGIDFPYRAIGRQWCSFTPSELATEVAPARTFGFAEQVDYLRSQGLIQGGSLENALVCSASGWVNPPLRFADEPVRHKLLDLWGDLALLGTPPIAHYVAYRASHHLHTQLARAIAQQRV | 285 |
C1B1S4 | DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA | FUNCTION | MVSESTEAPTPAPGSVREHWNELAEDVRQHQFRYYVRDAPIISDGEFDALLGELNDLENQYPDLRTPDSPTQLVGGGFATDFASADHLERMLSLDNVFATDELRTWISRVEQETGPDLHYLCEVKIDGVALNLVYENGRLVRAATRGDGRTGEEVTLNARTIDDIPEKLTGTDKYPIPALLEVRGEVFFRLEDFAALNAALVEEGKAPFANPRNSAAGSLRQKNPAVTARRRLGMICHGLGRSEGFEPASQYDAYTALAAWGLPVSTHTVRVTGADAVVDRVQYWGEHRHDVEHEIDGLVVKVDETSLQRRLGSTSRAPRWAIAYKYPPEEATTKLLDIRVNVGRTGRVTPFAYMEPVTVAGSTVSLATLHNGSEVKRKGVLIGDTVVLRKAGDVIPEVLGPVVDARTGDEYEFVMPANCPECDTPLAPAKEGDADIRCPNQQYCPAQLRERVFHVAGRGAFDIEVLGYEAATSLLEAKAIGDEGDLFSLTEDDLLKTTLFRTKAGGLSANGRRLLDNLDSAKDKPLWRVLVALSIRHVGPTAARALAGEFGSLDRIRESSVEELAAVDGVGGTIAAAVAEWFGVDWHRQIVDKWSAAGVRMEDERDESIPRNLEGLSIVVTGSLETFSRDQAKEAILVRGGKAAGSVSKKTAFVVAGESPGSKHDKAVELGVPVLDEDGFRRLLEGGPDAVTDSGV | 697 |
B7MIM0 | Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate | FUNCTION | MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIEWAHH | 404 |
B1JUI6 | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) | FUNCTION | MTRPVRTRFAPSPTGFIHLGNIRSALYPWAFARKMKGTFVLRIEDTDVERSSQEAVDAILEGMQWLGLDFDEGPIYQMQRMDRYREVLAQMLEKGLAYPCYMSAEELDALRERQREAGLKPRYDGTWRPEPGKVLPEPPAGVKPVLRFRNPLTGTVVWDDAVKGRVEISNEELDDLVIARPDGTPIYNFCVVVDDMDMGITHVIRGDDHVNNTPRQINILNALGGEPPVYAHLPTVLNEQGEKMSKRHGAMSVMAYRDAGFLPEAVVNYLARLGWSHGDAEIFSREQFVEWFDLEHLGKSPAQYDHSKLSWLNAHYIKEADNARLAELAKPFLDALGIDDAAIATGPALDAVVGLMKDRATTVKEIAEGAAMFYRVPAPDADALAQHVTDAVRPALADLAAALKAADWTKEAVSAALKATLATHKLKMPQLAMPVRLLVAGTTHTPSIDAVLVLFGRDVVVTRIEAALA | 469 |
Q9WYC7 | Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate | FUNCTION | MGKTLAEKIFSEHVGRDVKAGEIVLARVDIAMAQDGTGPLMINEFRELGFKEVKVPKAFLFIDHASPSPRKELSNSQKMMREFGKEMGVKVFDAGDGISHQILAEKYVKPGDLVAGADSHTCTAGGLGAFGTGMGSTDVAIIFGLGQNWFKVPETIKVVVNGKLQDGVYAKDIILEIARILGSDGATYKALEFHGSCIENMNVEDRLTISNMAVEVGAKAGLMPSDEKTREFLKKMGREEDFRELKADPDAVYETEIEIDATTLEPLVSLPHYVDNVRKVSEVEKEKIKIDQVFIGTCTNGRLQDLEIALKILEKHGKHPDVRLIVGPASRKVYMDALEKGIIKKFVELGAAVIPPGCGPCVGIHMGVLGDGERVLSTQNRNFKGRMGNPNAEIYLASPATAAATAVTGYITDPRRFI | 418 |
Q9MU80 | Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits | FUNCTION | MRTNPTTSSPVVSTLEEKNLGRIAQIIGPVLDVVFPPGKMPNIYNALVVKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEKNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRVLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTSQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNLEVESKLNK | 498 |
O87384 | Acts as a chaperone | FUNCTION | MGKIIGIDLGTTNSCVAVLDGDKPRVIENAEGERTTASVIAYTDGETLVGQPGGNVNAVTNPTRYTLFAIKRLIGRRFEDEEVQRDIEIMPYKIVKADNGDAWVEAKGQKMAAPQVSAEVLKKMKKTAEDFLGEEVTGAVITVPAYFNDAQAQATKDAGRIAGLEVKRIINEPTAAALAYGLDKSGGDRTIAVYDLGGGTFDISIIEIDEVEGEKTFEVLATNGDTHLGGEDFDNRLINYLVDEFNKEQGINLKNDPLAMQRVKEAAEKAKIELSSTSQTDVNLPYVTADATGPKHMNIKVTRAKLESLVEDLVQRSLEPLKVALADADLSVNDITDVILVGGQTRMPMVQAKVAEFFGKEARRDVNPDEAVAMGAAVQGGVLAGEVKDVLLLDVTPLSLGIETMGAVMTKLVEKNTTIPTKANQVFSTAEDNQSAVTIHVLQGERKQASFNKSLGQFNLEGIQAAPRGMPQIEVTFDLDADGILHVSAKDKQTGKEQKITIQASGGLSDDDIEKMVQEAEANKEADKKFEELATARNQADQMIHGTRKQVEEAGEALPAEEKEKIEAAISELETARKGDDKEAIDAKVQALMTAAQKLMEIAQQQAQAQQAQGGYAGAQQSQEDDVVDAEFEEVKDDKK | 640 |
Q1WT04 | Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides | FUNCTION | MPVFDYEDIQLVPNKCIVKSRSEVNTKVKFGPMTFKIPVVPANMQTIIDENLAVWLAKNGYFYIMHRFYENERVDFVKNMHDKGLFASISVGVKPAEYDLIDELSQKNLVPEYITIDIAHGHSDTVINMIKHIKHKLPGVFVIAGNVGTPEAVRELENAGADATKVGIGPGKACITKLKTGFGTGGWQLAAIRACAKAASKPIVADGGIRNNGDIAKSIRFGASMCMIGSLFAGHDETPGDIIEKDGKKFKTYFGSASQYQKGEYKNVEGKKLLLPYKGKIADTLREMQEDLQSAISYAGGKELLALRKVDYVIVKNSIYNGDML | 325 |
P31273 | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis | FUNCTION | MSSYFVNPLFSKYKAGESLEPAYYDCRFPQSVGRSHALVYGPGGSAPGFQHASHHVQDFFHHGTSGISNSGYQQNPCSLSCHGDASKFYGYEALPRQSLYGAQQEASVVQYPDCKSSANTNSSEGQGHLNQNSSPSLMFPWMRPHAPGRRSGRQTYSRYQTLELEKEFLFNPYLTRKRRIEVSHALGLTERQVKIWFQNRRMKWKKENNKDKLPGARDEEKVEEEGNEEEEKEEEEKEENKD | 242 |
B4TGI5 | Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation | FUNCTION | MDNVVDRHVFYISDGTAITAEVLGHAVMSQFPVTISSITLPFVENESRARAVKDQIDAIYQQTGVRPLVFYSIVLPEIRAIILQSEGFCQDIVQALVAPLQQEMKLDPTPIAHRTHGLNPGNLNKYDARIAAIDYTLAHDDGISLRNLDQAQVILLGVSRCGKTPTSLYLAMQFGIRAANYPFIADDMDNLTLPTSLKPLQHKLFGLTIDPERLAAIREERRENSRYASLRQCRMEVAEVEALYRKNQIPCLNSTNYSVEEIATKILDIMGLNRRMY | 277 |
G5EE06 | Catalyzes the addition of fucose in alpha 1-3 linkage to GalNAc-beta-1->4-GlcNAc-beta-1->3-Gal-beta-1->4-Glc (LDNT)acceptor. Unlike fut-1, does not add fucose to Man-alpha-1->3-(Man-alpha-1->6)-Man-beta-1->4-GlcNAc-beta-1->4-GlcNAc-beta-1-Asn (M3), Man-alpha-1->3-(Man-alpha-1->6)-Man-beta-1->4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-GlcNAc-beta-1-Asn (M3F6) or GlcNAc-beta-1->2-Man-alpha-1->3-(GlcNAc-beta-1->2-Man-alpha-1->6)-Man-beta-1-4-GlcNAc-beta-1->4-(Fuc-alpha-1->6)-GlcNAc-beta-1-Asn (GnM3F6) acceptors | FUNCTION | MKHNTLRAVFQFSFFIGICTFIMIAGYSYQINYNQRMGIFYGGNITFKKVPKVVIYTATPFFDVPIENSILRDCSEKIKNSCTVTSNNKTFPIADAIVFHSRDINETKLSFFNKNRRYDIPYIMMAMENPFFAGLTVYHNFFNWTMTYRTDSDIFHPYGAFVKSYVPAEVNYSEIWNSKTKETLWMVSNGNAQNKRKELVEKLIKKGMSIDLYGQLYKKEPAECPRRRGPPGCDVKFHSPYKFAIAFENSNCKDYVTEKFWKKAGIYKTVPIVMSRKIYRDLGIPDSMYIAVDDYPNLEEFVHHIQNVTSNEEEYMKYHKWRKQFKIVDTNEGNIGFCQLCQKLAGYKRKLVPHKVYENLNSWHSTSTCDNSFATRFL | 378 |
G0HQZ5 | Involved in the production of polyhydroxyalkonic acids (PHAs), which are water-insoluble biopolymers used as intracellular energy reserve material when cells grow under conditions of nutrient limitation. PHAs are composed primarily of 3-hydroxybutyric acid (3HB) and 3-hydroxyvaleric acid (3HV). Required for the production of poly-beta-hydroxybutyrate (PHB) and poly(beta-hydroxybutyrate-co-beta-hydroxyvalerate) (PHBV) | FUNCTION | MSNTNNIQEEWTEMVEEMNNAVADSMEQNMKAQAAFVESWADAVEDTIPKEEDLADGMDGYNRAYEEWIDAAEQMVERSTDAAQGEDVDPAEFRDIWLQSANEAFKHVMGTSAFAAANGQLVESMMEMQQEADDLSQDALEQMGFPTRNDVDEVAERLIELERRQHAVEQKLDRVLEHLEE | 181 |
Q9PI35 | Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors | FUNCTION | MAKKVVGEIKLQIAATKANPSPPVGPALGQQGVNIMEFCKAFNERTKDMAGFNIPVVITVYADKSFTFITKQPPATDLIKKAAGISKGTDNPLKNKVGKLTRAQVLEIVDKKIADLNTKDRDQAAKIIAGSARSMGVEIVD | 141 |
Q3B8E9 | As a component of IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis. Involved in retrograde ciliary transport along microtubules from the ciliary tip to the base | FUNCTION | MEDVLDLGEAPSRRTGVKMGRRARAAQETQQETADVSRNQTGREGPPKPLRQGGWADDSSGPSKSTRRMTDDVEDSRLKQQSLDESDEGEDIPVIPDLEDVQEEDLALQVASPPSVQVNRVMTYRDLDNDLMRHAAFQSLDGDVDLKLLTKVLSPEPEVREENVRWDWDLLFTEVSSELITEWDVGKMEKEDMLKPSPLVS | 201 |
Q6NAI2 | Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation | FUNCTION | MSNIDLKPKTKAKAKIKVERPKLHKVILVNDDYTPREFVVSVLKGEFRMTEDQATKVMLTAHQRGVCVVGVFTKDVAETKATRATDAGRAKGYPLLFTTEPEE | 103 |
Q9UU90 | Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences | FUNCTION | MVRFKSRYLLFEVLYPEAKEFFDYPTIPSDSSITTSSLSKIIRTMVAENFGDVGIGKVASSLTVKYFSPNTSTGILRVSRQHFRLAWAALVLIRELYGKPVIIRVVRVSGTIKKAELAAIERNKSEIHNISLMDEPIEV | 139 |
P0DJ31 | Voltage-gated potassium channel inhibitor. Selectively and irreversibly binds (K(d)=2.9 pM) and blocks hKv1.3/KCNA3 potassium channels of human T-lymphocytes. Weakly blocks hKCa3.1/KCNN4, mKv1.1/KCNA1, and hKv1.2/KCNA2 channels. In vivo, high doses (200 ug) produce no symptoms of intoxication when injected into mice | FUNCTION | AAAISCVGSPECPPKCRAQGCKNGKCMNRKCECYYC | 36 |
A2BYZ2 | Carrier of the growing fatty acid chain in fatty acid biosynthesis | FUNCTION | MSQEEILQKVCSIVSEQLSVESGEVKSDSNFQNDLGADSLDTVELVMALEEAFDIEIPDEAAEGIATVGDAVKFIEAKKG | 80 |
Q6M132 | Putative transcriptional regulator | FUNCTION | MESFLTEIQINVLNLRKRGHTQDEIANIMGTSRANISMIEKRARENIEKARNTLSIYNDIIAPSKIKIDKGTDVFSIPKIIFSKSDQEEIHVNYSSLQIMEFVNQNAQRYIKNRMVVEPFVVTILQNGDIFVHDYEESEENEKMPKKEI | 149 |
P0A735 | Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell | FUNCTION | MALLDFFLSRKKNTANIAKERLQIIVAERRRSDAEPHYLPQLRKDILEVICKYVQIDPEMVTVQLEQKDGDISILELNVTLPEAEELK | 88 |
D3JWK5 | Probable neurotoxin with unknown target. Possibly targets ion channels | FUNCTION | GRPSARYDAPYCSQEEVRECQDDCSGNAVRDSCLCAYDPAGSPACECRCVEPWRR | 55 |
Q9ZKQ9 | Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids | FUNCTION | MLKRASFVEVNTHSLRHNFNAVKNIVPKDACVMAVVKANAYGAGAIKASEIFLQEGANYLGVATLDEALELRSHFSQTPILILGYSPNTNASMLIDNDLSAMVFSLEQAEVFSQMALKSQKRLKVHLKIDTGMHRLGLEPTFKSIETIKKIRALKGLEVEGIFTHLSNADSNIKTHAKNQMKVFNAFLEQLLDQKIEFQYRHAYNSAGILSLCNGNENRLLNLYRPGIMLYGFYPSNEMKESSQTILKNVISLKARIVQIKRVKKGEFIGYGEHFYTNEETLVGVLALGYADGLVRALGNRIQVAINNQLAPLIGKVCMDQCFVKLNDIEAKEGDEVILFGDKSTKANDASEIATLLNTIPYETISTLSKRLERVYV | 377 |
Q5HFT1 | Member of the two-component regulatory system SrrA/SrrB, which is involved in the global regulation of staphylococcal virulence factors in response to environmental oxygen levels as well as biofilm formation. Also plays an essential role in host-derived nitric oxide resistance by regulating hmp/flavohemoglobin, an enzyme that detoxifies nitric oxide by converting it to nitrate. Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to SrrA. In turn, SrrA binds to the upstream promoter regions of the target genes to positively and negatively regulate their expression (Probable) | FUNCTION | MMSRLNSVVIKLWLTIILIVTTVLILLSIALITFMQYYFTQETENAIREDARRISSLVEQSHNKEEAIKYSQTLIENPGGLMIINNKHRQSTASLSNIKKQMLNEVVNNDHFDDVFDKGKSVTRNVTIKEKGSSQTYILLGYPTKAQKNSHSKYSGVFIYKDLKSIEDTNNAITIITIITAVIFLTITTVFAFFLSSRITKPLRRLRDQATRVSEGDYSYKPSVTTKDEIGQLSQAFNQMSTEIEEHVDALSTSKNIRDSLINSMVEGVLGINESRQIILSNKMANDIMDNIDEDAKAFLLRQIEDTFKSKQTEMRDLEMNARFFVVTTSYIDKIEQGGKSGVVVTVRDMTNEHNLDQMKKDFIANVSHELRTPISLLQGYTESIVDGIVTEPDEIKESLAIVLDESKRLNRLVNELLNVARMDAEGLSVNKEVQPIAALLDKMKIKYRQQADDLGLNMTFNYCKKRVWSYDMDRMDQVLTNLIDNASRYTKPGDEIAITCDENESEDILYIKDTGTGIAPEHLQQVFDRFYKVDAARTRGKQGTGLGLFICKMIIEEHGGSIDVKSELGKGTTFIIKLPKPE | 583 |
A6UQY9 | Involved in ribosome biogenesis; more specifically in 18S rRNA pseudouridylation and in cleavage of pre-rRNA | FUNCTION | MQMKKCPKCGKYTLKEYCIDCNEKAGTVKPPRFSPVDKYGKYRRMLKKSLKK | 52 |
Q9UJ37 | Catalyzes the transfer of N-acetylneuraminyl groups onto glycan chains in glycoproteins. Shows a preference for N-acetylgalactosamine (GalNAc) residues already modified by the addition of galactose or galactose followed by sialic acid in alpha-2,3 linkage | FUNCTION | MGLPRGSFFWLLLLLTAACSGLLFALYFSAVQRYPGPAAGARDTTSFEAFFQSKASNSWTGKGQACRHLLHLAIQRHPHFRGLFNLSIPVLLWGDLFTPALWDRLSQHKAPYGWRGLSHQVIASTLSLLNGSESAKLFAPPRDTPPKCIRCAVVGNGGILNGSRQGPNIDAHDYVFRLNGAVIKGFERDVGTKTSFYGFTVNTMKNSLVSYWNLGFTSVPQGQDLQYIFIPSDIRDYVMLRSAILGVPVPEGLDKGDRPHAYFGPEASASKFKLLHPDFISYLTERFLKSKLINTHFGDLYMPSTGALMLLTALHTCDQVSAYGFITSNYWKFSDHYFERKMKPLIFYANHDLSLEAALWRDLHKAGILQLYQR | 374 |
Q3YU31 | This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N'' a prepriming protein complex on the specific site of the template DNA recognized by protein N' | FUNCTION | MSSRVLTPDVVGIDALVHDHQTVLAKAEGGVVAVFANNAPAFYAVTPARLAELLALEEKLARPGSDVALDDQLYQEPQAAPVAVPMGKFAMYPDWQPDADFIRLAALWGVALREPVTTEELASFIAYWQAEGKVFHHVQWQQKLARSLQIGRASNGGLPKRDVNTVSEPDSQIPPGFRG | 179 |
Q1J0B6 | Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA | FUNCTION | MNTAPSPSDRPLSHALSHTPVLAAEVVAALAPAPGRVIVDGTLGGAGHTRLLLEAGASVIGIDQDPYALNRAREAQLPQLTVLEGNYRDMRELLAGIGVTQVDGVLLDIGVSSFQLDDAARGFSYHTDAPLDMRMAQSGESAAEVVNGYPEEELAAIIYEYGEERHSRRIARAIVQARTQAPIQSTVQLAEIIKRAYPGFSKGIHPARRTFQALRIHVNDELGALRDGLRAAEALLTPGGRLAVIAFHSLEDRIVKRFLRASPTLKSLTKRPVEASEEERGRNPRARSAKLRAAEKVAAPEGLPEVEV | 308 |
Q99N01 | Organic anion antiporter with apparent broad substrate specificity. Recognizes various substrates including thyroid hormones 3,3',5-triiodo-L-thyronine (T3), L-thyroxine (T4) and 3,3',5'-triiodo-L-thyronine (rT3), conjugated steroids such as estrone 3-sulfate and estradiol 17-beta glucuronide, bile acids such as taurocholate and prostanoids such as prostaglandin E2, likely operating in a tissue-specific manner . May be involved in uptake of metabolites from the circulation into organs such as kidney, liver or placenta. Possibly drives the selective transport of thyroid hormones and estrogens coupled to an outward glutamate gradient across the microvillous membrane of the placenta. The transport mechanism, its electrogenicity and potential tissue-specific counterions remain to be elucidated (Probable) | FUNCTION | MPQHAMGDKHFLSLPKHLFTSTSSTTDSGCDTPPSSRASPASLRSAHGALGSSSQPLFEPQVEKRSSQAACEVQYLSSGPQSTLCGWQSFTPKCLQVFNTPKGFLFFLCAASFLQGMTVNGFINTVITSIERRFDLHSYQSGLIASSYDIAACLCLTFVSYFGGNGHKPRWLGWGALVLGIGSLVFALPHFTAGRYEVEIDDEGLGTETGTCLTNQSQVECKDRASGLSSYRLIFMLGQLLHGVGATPLYTLGVTYLDENVKSSYSPIYIAIFYTAAILGPAAGYLIGGAMLNVYTEVGQRTELTTDSPLWVGAWWIGFLGAGIAAFLIAIPILGYPRQLPGSQRYVVMRAAETQQLKDHSRDNPAFGKTVRDLPLSVWILLRNPTFILLCLAGATEATLIAGMSTFGPKFFEAQFSLSASEAATLFGYLVVPAGGGGTLLGGFLVNKFKLRGSGIIRFCLFCTLTSLLAFFVFLMHCPNVHMAGVTTGYVGSLLPKGQLDLKAACNALYCCQPRHYSPLCGSDGTMYYSPCYAGCPEGAVTGPGGQKVYRGCSCILEKASSGWGNATAGKCASTCQSKPLLLVLVFVVIIFTFLSSIPALTATLRCVCDRQRSFALGIQWIVVRTLGSIPGPIAFGWVIDKACLLWQDQCGHQGSCFVYKNEAMSRYLLIAGLTFKVLGFLFFVAAYFLYKSPSVSSDGLEASLPSQSSASDSPTEQLQSNV | 723 |
Q8FP92 | Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation) | FUNCTION | MSTPTNPEQPTDHPSAPFTLEARFAEEFPEMTTPWRGEDQPDPELAVLNEDLARLLGIDPDWLRSPAGVEFLLGLNPEPTTEMVAQGYAGHQFGQFVPSLGDGRALLLGEIRGTDGVLRDIHLKGSGRTRYSRGADGRAALGPALREYLVSEAMHALGVPTTRALAVVTTGRKIQRDRVLPGAVVVRVATSHIRVGSFQYANITGGIDLSRRLADHAITRHYPRLVERFPESGPERYAWFFRQVMDAQAQTVARWMRLGFVHGVLNTDNTLVSGETIDYGPCAFMDRYREDAVFSSIDTHGRYKFSNQPLILGWNLARLAETLIPLFGDTPDAGVDRAQEMINTFTDRYNDALHAELAAGLGLDADAPDTAGLIESYLELMRTHSPDVTTLNRTLSEWSVESTPPAGFEEWIPRWLAAQPDLINMQKTNPVYVPRNHLVEDALAEAVEGRWEAFTTLLGLVTDPFTRQAGMEVYERPGPDGFEDTYMTFCGT | 492 |
B2J0C5 | Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex | FUNCTION | MKLAYWMYAGPAHIGTLRIASSFKNVHAIMHAPIGDDYFNVMRSMLSRERDFTPVTTSVVDRNVLARGSQEKVVDNIVRKDAEEHPDLIVLTPTCTSSILQEDLHNFVERAQLEAKGDVMLADVNHYRYNELQAADRTLDQIVQYYIEKARKRGELAEGKTAKPSVNIIGTTTLGFHNNHDCTELKRLMADLGIKVNTLIPEGASVNDLKKMSQAWFNLVPYRELGLTTARYLEEQFGTPYIDITPMGVVETARCIRKIQQVINAQGAEVDYENFINEQTLHVSQAAWFSRSIDCQNLTGKKAVVFGDNTHAAAITKILAREMGIHVVWAGTYCKYDAGWFREQVSEYCDEVLISEDHGEIGDAIARVEPSAIFGTQMERHVGKRLDIPCGVIAAPIHVQNFPIGYKPFMGYEGTNQITDLIYNSFTLGMEDHLLEIFGGHDTKEVITRGISADSDLNWTKDGQAELNKIPGFVRGKVKRNTEKFARDRGFKEINAEVLYAAKEAVGA | 508 |
A4FH01 | Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety | FUNCTION | MVHGNSRPLEKDVVRDLRRELSYGQYLRLDRLLDAQHPVSEPEHHDELLFIIQHQTVELWLKLILHELRTAREHLARDELKPALKQLARVKHVQHTLTEQWSVLATLTPAEYVEFRGFLGRSSGFQSYQYRAIELILGNKNAEMLEVFAHDEFAHELLNGLLKEPSVYDEFVRLLHRRGHDVPAAFLQRDVSLPHTFTPELVPLFRGIYETAAENWDAYEACEELVDLEENFQFWRFRHLKTVERTIGLKHGTGGSSGVSFLRRALELTFFPELYAVRTEI | 281 |
Q6F0S4 | An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes | FUNCTION | MENKNLLSIGKIVNTFGIKGAVKIALEKSIEVNDINGIKLLFIENTNNVIIPKQVESISMQKSHLVVYFKEHNHINEVEIFKGKKVKYLNDNDAFSIFYDLTYYSVVYNKQNGKVIETMFNGNHDLVKVLLENEEKAFWVPLVDVYTNNIDDESRIITLKNIEGLK | 166 |
Q92KZ3 | Catalyzes the NADPH-specific reduction of 1,5-anhydro-D-fructose to 1,5-anhydro-D-mannitol | FUNCTION | MIRWGLIGASTIAREWVIGAIRAAGGEVVSVMSSSAERGEAYAAENGIAKAVTSVDDLVGDPDVDAVYISTTNELHHGQALAAIRAGKHVLCEKPLAMNLNDGCEMVLKACEAGVVLGTNHHLRNAATHRAMREAIAAGRIGRPIAARVFHAVYLPPHLQGWRLDKPEAGGGVILDITVHDADTLRFVLNDDPIEAVAISHSAGMGKEGLEDGVMGVLRFRSGVIAQFHDAFTTKFAETGLEVHGTAGSLIGRNVMTQRPVGTVVLRNEEGESELPLDHRNLYETAIAAFHSAIGGNGRPSASGEDGVWSLATGLAVVKAAATGGAVEIETGL | 333 |
Q7ZX83 | Acts as a transcriptional regulator. Binds DNA and RNA | FUNCTION | MAGFGAAPDFNEGSKINASKNQQDEGKMFIGGLSWDTSKKDLTEYLSRFGEVLDCTIKTDPVTGRSRGFGFVLFKDAVSVDKVLETNEHKLDGKLIDPKRAKALKGKEPPKKVFVGGLSPETTEEQIKQYFGGFGEIENIELPIDTKTNERRGFCFVTYTGEEPVKKLLESRFHQIGTGKCEIKAAQPKEVYRQQQQKQQRGGRGAVTGRGGTRGRGRGQGWNQGYNNYYDQNYGGYGNNGSYGDQDYNSYSGYDYSGYSYGYNPGYTEYSGQQSTYGKARGGGNHQNNYQPY | 293 |
Q0T5E2 | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis | FUNCTION | MKQFLDFLPLVVFFAFYKIYDIYAATAALIVATAIVLIYSWVRFRKVEKMALITFVLVVVFGGLTLFFHNDEFIKWKVTVIYALFAGALLVSQWVMKKPLIQRMLSKELTLPQPVWSKLNLAWAVFFILCGLANIYIAFWLPQNIWVNFKVFGLTALTLIFTLLSGIYIYRHMPQEDKS | 179 |
P0ABS2 | Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters. Also required for regulation of fis expression | FUNCTION | MQEGQNRKTSSLSILAIAGVEPYQEKPGEEYMNEAQLAHFRRILEAWRNQLRDEVDRTVTHMQDEAANFPDPVDRAAQEEEFSLELRNRDRERKLIKKIEKTLKKVEDEDFGYCESCGVEIGIRRLEARPTADLCIDCKTLAEIREKQMAG | 151 |
A8A9J7 | Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids | FUNCTION | MEASGKLRAYLELVRAHNLLGTVLGVIAGAALLGEVNVAAAIASASAAAVAAGGYAINDYFDVEIDKVNKPERPIPSGRVGAEEARKLALALLALGPLLGLAVGPLTGAYAALNAVLMYYYSKSLKKTGLPGNLAVSFSTASTLLYGSLATAEWAGEVARVLRTIPIILMVFLMTLAREVVKGVEDYVGDKEGGVKTLAVVKGPDFALRAALALACASLALAYLAAPLLSLGYAFLAFVTLGGLLSLASVAACLRSEDPVRCAAKPRRAMKVAMFLGLIGILVDRLVQPVFYPHVLHAGGEEG | 303 |
Q3B6L9 | IF-3 binds to the 30S ribosomal subunit and shifts the equilibrium between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins | FUNCTION | MKKQKATSQKPKITYRVNEQIRVPEVRIIFPDGTQQVMKTIDARRMAEDRNTDLIEVQPNAEPPVCKFDNLGKLLYKMAQRDKDLKKKQKTTTLKELRFHPNTDKHDFDFKTAHLEEFLRKGNRVRATIVFLGRSIIYKDKGLELADRLTERLSVVGNREGEPKFEGKKLFVYFEPDKKKIDAYERIRSKTGTPLAPLEESADAED | 206 |
Q1PE49 | Involved in intra- and inter-cellular trafficking through plasmodesmata (PD) | FUNCTION | MAATSDEQMNLLLSSFDQIYEDFKIGLNEINVYRSKSNVESSRREVLEISNKNLKEENERLKKLYTESLNNFADQLEHRTKCHSLKEELKRVNDENKSKEHEHRNALESLRQKHVTKVEELEYKIRSLLVEKATNDMVIDRLRQDLTANKSHIQAMSKKLDRVVTEVECKYELEIQDLKDCLLMEQAEKNDISNKLQSLQKELLISRTSIAEKQRDTTSNRQVETLKQKLMKLRKENEILKRKLSSS | 247 |
Q7UBT0 | Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor | FUNCTION | MSKLDLNALNELPKVDRILALAETNAELEKLDAEGRVAWALDNLPGEYVLSSSFGIQAAVSLHLVNQIHPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAWQEARYGKLWEQGVEGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAIQRGVFKVLPIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWEPGMAEEETRFFGLKRECGLHEG | 244 |
Q6CF35 | Substrate-binding subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA | FUNCTION | MKDAAQQQEPVSARQTQVHRKSSKPESPPFIFDNPRIQPNTYCMVKLPSENFRVVKLIPNQTISIGKFGSFQVNDILGLPYGYTFEIQEDKRLRIIQEGVDDHDYVVGAKGALLEPEETNQTLIDTSESQTLSMAEIEEMKKQKTLSGKDIIDHVIKGHNEFHKKTAFSKEKYLRRKEQKYLRRFTPQPMCSSLLLDFYLEKDYKKVLDMSQEMLALLLSMANVRPGGKYLVVDETTGVLTAALMERMAGEGLIVVAHENEHPNLDALKYLSMPTELQDRMIKSINWLQFFEPEGEEEVPEKTPEQIASMKPRNRGAYFRKRNRWLELQNVNDLVANQGFDGLIVASTLHPASIVDRTLHAIGGSRPVVVYSEYKEVVTEVSQLMLKDLRVLAPSIWESRVRKYQTILGRMHPSMTSRGGGGYLVHGTRVFPNEEVNATQVRNRKRKREDGDKTKSSETEGKSEESVEPDTEQSAEPEAKLETDADA | 487 |
Q2R3P9 | Confers blight susceptibility. Confers TAL effector-mediated susceptibility to Xanthomonas oryzae pv. oryzae | FUNCTION | MAGMSLQHPWAFAFGLLGNIISFMTYLAPLPTFYRIYKSKSTQGFQSVPYVVALFSAMLWIYYALLKSDECLLITINSAGCVIETIYIAVYLVYAPKKAKMFTAKLLLLVNVGVFGLILLLTLLLSAGDRRIVVLGWVCVGFSVSVFVAPLSIIRLVVRTKSVEFMPFSLSFSLTISAVVWFLYGLLIKDKYVALPNVLGFSFGVIQMGLYAMYRNSTPKAVLTKEVEAATATGDDDHSAAGVKEHVVNIAKLSAAVDVVKTREVHPVDVESPPAEAPPEEDDKAAAATAAAVAGAGEKKVAA | 303 |
Q10DV7 | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells | FUNCTION | MADAEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDMKEKLSYIALDYDQEMETAKTSSSVEKSYELPDGQVITIGAERFRCPEVLFQPSFIGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF | 377 |
Q02JW1 | Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH | FUNCTION | MNPVRKKRLIIVLAIVVGVGAAVGLALSALQQNINLFYTPTQIANGEAPTDTRIRAGGLVEKGSLQRSEDSLNVRFVVTDGAKEVTIAYHGILPDLFREGQGIVALGKLGGDGVLVADEVLAKHDENYMPPEVTKALKDSGQLKHYENGKAAGETSYNQEGK | 162 |
Q9K0U0 | Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide | FUNCTION | MKVFKQQLEQLGAQNQYRSIPDLIHQGRYITRENRKMLNMSSNDYLGLASDENLRRSFLQQYGGNFPSFTSSSSRLLTGNFPIYTDLEELVAQRFQRESALLFNSGYHANLGILPALTTTKSLILADKFVHASMIDGIRLSRCAFFRYRHNDYEHLKNLLEKNVGKFDRTFIVTESVFSMDGDVADLKQLVQLKKQFPNTYLYVDEAHAIGVYGQNGLGIAERDNLIAEIDLLVGTFGKALASVGAYAVCNQVLKECLINQMRPLIFSTALPPFNVAWTYFIFERLPQFSKERSHLEQLSAFLRREVAHRTQIMPSQTCIVPYILGGNEATLAKAEYLQRQGYYCLPIRPSTVPKNTSRIRLSLTADMTTDEVRQFAACL | 380 |
C3PKP0 | One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA | FUNCTION | MRKNAAPKRPVVKDPVYNSEQVTMLVNKILRDGKKSTAERIVYGALEVCREKTGTDPVGTLEKALGNIRPDLEVRSRRVGGATYQVPVEVKPARSNTLALRWLVTFTRQRRENSMIERLANEILDASNGLGASVKRREDTHKMAEANRAFAHYRW | 155 |
Q9VKV8 | Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. Involved in the regulation of the size and morphology of cilia. Required for sperm individualization, differentiation of the sperm flagellum and tubulin polyglycylation of axonemal microtubules | FUNCTION | MFKNTFQSGFLSILYSIGSKPLQLWDKKVRNGHIKRITDNDIQSLVLEIVGTNVSTTFITCPADPKKTLGIKLPFLVMIIKNMKKYFTFEVQVLDDKNVRRRFRASNYQSTTRVKPFICTMPMRLDEGWNQIQFNLSDFTRRAYGTNYVETLRVQIHANCRIRRVYFSDRLYSEDELPPEFKLFLPIQKPVQKSNAICS | 199 |
F5CPD7 | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission | FUNCTION | MKTLLLTLVVVTIVCLDFGHTLICYNYWTPLDKTTECCGNGVTTCFAKSWNDHRGRRTDRGCGCPNVKPGIHLNCCKTDRCNG | 83 |
A0A1F3 | Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+) | FUNCTION | MATLKDQLIQNLLKEEHVPQNKITIVGVGAVGMACAISILMKDLADEVALVDVMEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSRLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNIVKYSPNCKLLVVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWILGEHGDSSVPVWSGVNVAGVSLKNLHPELGTDADKEQWKAVHKQVVDSAYEVIKLKGYTSWAIGLSVVDLAESIMKNLRRVHPISTMIKGLYGIKEDVFLSVPCILGQNGISDVVKVTLTHEEEAYLKKSADTLWGIQKELQF | 332 |
P0DO12 | May act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway | FUNCTION | MTKISVGLQLVTRDSREKLNNIVIKSSLRLNRSNPNISELCFLKTCHLCNKQLHQDKDVYMYRGDLGFCSRECRESQMLIDDRKELEASTKMMLASYRRCNNGAGKSESRNLFDDLRRRRQLFIVP | 126 |
P25384 | Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty2 RNA and initiation of reverse transcription | FUNCTION | MESQQLHQNPRSLHGSAYASVTSKEVPSNQDPLAVSASNLPEFDRDSTKVNSQQETTPGTSAVPENHHHVSPQPASVPPPQNGQYQQHGMMTPNKAMASNWAHYQQPSMMTCSHYQTSPAYYQPDPHYPLPQYIPPLSTSSPDPIDSQNQHSEVPQAETKVRNNVLPPHTLTSEENFSTWVKFYIRFLKNSNLGDIIPNDQGEIKRQMTYEEHAYIYNTFQAFAPFHLLPTWVKQILEINYADILTVLCKSVSKMQTNNQELKDWIALANLEYDGSTSADTFEITVSTIIQRLKENNINVSDRLACQLILKGLSGDFKYLRNQYRTKTNMKLSQLFAEIQLIYDENKIMNLNKPSQYKQHSEYKNVSRTSPNTTNTKVTTRNYQRTNSSKPRAAKAHNIATSSKFSRVNNDHINESTVSSQYLSDDNELSLGQQQKESKPTHTIDSNDELPDHLLIDSGASQTLVRSAHYLHHATPNSEINIVDAQKQDIPINAIGNLHFNFQNGTKTSIKALHTPNIAYDLLSLSELANQNITACFTRNTLERSDGTVLAPIVKHGDFYWLSKKYLIPSHISKLTINNVNKSKSVNKYPYPLIHRMLGHANFRSIQKSLKKNAVTYLKESDIEWSNASTYQCPDCLIGKSTKHRHVKGSRLKYQESYEPFQYLHTDIFGPVHHLPKSAPSYFISFTDEKTRFQWVYPLHDRREESILNVFTSILAFIKNQFNARVLVIQMDRGSEYTNKTLHKFFTNRGITACYTTTADSRAHGVAERLNRTLLNDCRTLLHCSGLPNHLWFSAVEFSTIIRNSLVSPKNDKSARQHAGLAGLDITTILPFGQPVIVNNHNPDSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQDKQSKLDQFNYDTLTFDDDLNRLTAHNQSFIEQNETEQSYDQNTESDHDYQSEIEINSDPLVNDFSSQSINPLQLDKEPVQKVRAPKEVDADISEYNILPSPVRSRTPHIINKESTEMGGTVESDTTSPRHSSTFTARNQKRPGSPNDMIDLTSQDRVNYGLENIKTTRLGGTEEPYIQRNSDTNIKYRTTNSTPSIDDRSSNSESTTPIISIETKAVCDNTPSIDTDPPEYRSSDHATPNIMPDKSSKNVTADSILDDLPLPDLTHQSPTDTSDVSKDIPHIHSRQTNSSLGGMDDSNVLTTTKSKKRSLEDNETEIEVSRDTWNNKNMRSLEPPRSKKRINLIAAIKGVKSIKPVRTTLRYDEAITYNKDNKEKDRYVEAYHKEISQLLKMNTWDTNKYYDRNDIDPKKVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSDMQSNTVHHYALMTSLSIALDNDYYITQLDISSAYLYADIKEELYIRPPPHLGLNDKLLRLRKSLYGLKQSGANWYETIKSYLINCCDMQEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRSKYMKLGMEKSLTEKLPKLNVPLNPKGKKLRAPGQPGHYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH | 1,770 |
Q9SQT9 | Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death | FUNCTION | MASSILLTLITFIFLSSLSLSSPTTNTIPSSQTISPSEEKISPEIAPLLPSPAVSSTQTIPSSSTLPEPENDDVSADPDPAFAPSASPPASSLASLSSQAPGVFIYFVFAAVYCFSLRLLAVSAI | 125 |
O83270 | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates | FUNCTION | MKDIRDFDSLQIKLASPDTIRAWSYGEVKKPETINYRTLRPEREGLFCERIFGTTKEWECFCGKFKSIRYRGVICDRCGVEVTHFKVRRERMGHIELATPVSHIWYYRCVPSRMGLLLDLQVIALRSVLYYEKYIVIEPGDTDLKKNQLLTETEYNDAQERYGGGFTAGMGAEAIRTLLQNLDLDALVAQLREKMMEKGAKSDKRLLRRIEIVENFRVSGNKPEWMILSVIPVIPPDLRPMVQLDGGRFATSDLNDLYRRVIHRNSRLIRLMELKAPDIIIRNEKRMLQEAVDALFDNSKRKPAIKGASNRPLKSISDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKLWQCGLPTKMALELFKPFIMKKLVEKEIVSNIKKAKMLVEQESPKVFSVLDEVVKEHPVMLNRAPTLHRLGIQAFEPVLVEGKAIRLHPLVCKPFNADFDGDQMAVHVPLTQAAQMECWTLMLSNRNLLDPANGRTIVYPSQDMVLGLYYLTKERSLPEGARPRRFSSVEEVMMAAEKGVIGWQDQIQVRYHKCDGQLVVTTAGRLVLNEEVPAEIPFVNETLDDKRIRKLIERVFKRQDSWLAVQMLDALKTIGYTYATFFGATLSMDDIIVPEQKVQMLEKANKEVLAIASQYRGGHITQEERYNRVVEVWSKTSEELTSLMMETLERDKDGFNTIYMMATSGARGSRNQIRQLAGMRGLMAKPSGDIIELPIRSNFKEGLNVIEFFISTNGARKGLADTALKTADAGYLTRRLVDIAQDVVVNEEDCGTINGIEYRAVKSGDEIIESLAERIVGKYTLERVEHPITHELLLDVNEYIDDERAEKVEEAGVESVKLRTVLTCESKRGVCVCCYGRNLARNKIVEIGEAVGIVAAQSIGQPGTQLTMRTFHVGGTASSTTEENRITFKYPILVKSIEGVHVKMEDGSQLFTRRGTLFFHKTLAEYQLQEGDSVQVRDRARVLKDEVLYHTTDGQTVYASVSGFARIIDRTVYLVGPEQKTEIRNGSNVVIKADEYVPPGKTVATFDPFTEPILAEQDGFVRYEDIILGSTLIEEVNTETGMVERRITTLKTGIQLQPRVFISDESGNALGSYYLPEEARLMVEEGAQVKAGTVIVKLAKAIQKTSDITGGLPRVSELFEARRPKNAAVLAQISGVVSFKGLFKGKRIVVVRDHYGKEYKHLVSMSRQLLVRDGDTVEAGERLCDGCFDPHDILAILGENALQNYLMNEIRDVYRVQGVSINDQHIGLVVRQMLRKTEVVSVGDTRFIYGQQVDKYRFHEENRRVEAEGGQPAVARPMFQGITKAALNIDSFISAASFQETNKVLTNAAIAGSVDDLCGLKENVIIGHLIPAGTGMRRYRQVKLFDKNKRDLDVQMEEVIRRRKLEEEALAQAVAGMEGEPEGEA | 1,416 |
A7J391 | Inner capsid protein that self-assembles to form an icosahedral capsid with a T=2 symmetry, which consists of 120 copies of VP2, with channels at each of its five-fold vertices. This capsid constitutes the innermost concentric layer of the viral mature particle. It encapsidates the polymerase VP1, the capping enzyme VP3 and the genomic dsRNA, thereby defining the core. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels formed by VP2 N-termini. VP2 is required for the replicase activity of VP1 polymerase. Probably recruits a copy of a VP1-VP3 complex, potentially along with a segment of plus-strand RNA, as a decamer of VP2 assembles. May activate the autoinhibited VP1/RNA complex to coordinate packaging and genome replication | FUNCTION | MAYRKRGARREANLNNNDRMQEKNDEKQDSNKIQLSDKVLSKKEEVVTDSHEEVKITDEVKKSTKEESKQLLEVLKTKEEHQKEIQYEILQKTIPTFEPKETILRKLEDIKPELAKKQTKLFRIFEPKQLPIYRANGERELRNRWYWKLKKDTLPDGDYDVREYFLNLYDQVLTEMPDYLLLKDMAVENKNSRDAGKVVDSETASICDAIFQDEETEGAVRRFIAEMRQRVQADRNVVNYPSILHPIDYAFNEYFLQHQLVEPLNNDIIFNYIPERIRNDVNYILNMDRNLPSTARYIRPNLLQDRLNLHDNFESLWDTITTSNYILARSVVPDLKELVSTEAQIQKMSQDLQLEALTIQSETQFLTGINSQAANDCFKTLIAAMLSQRTMSLDFVTTNYMSLISGMWLLTVVPNDMFIRESLVACQLAIVNTIIYPAFGMQRMHYRNGDPQTPFQIAEQQIQNFQVANWLHFVNNNQFRQAVIDGVLNQVLNDNIRNGHVINQLMEALMQLSRQQFPTMPVDYKRSIQRGILLLSNRLGQLVDLTRLLAYNYETLMACITMNMQHVQTLTTEKLQLTSVTSLCMLIGNATVIPSPQTLFHYYNVNVNFHSNYNERINDAVAIITAANRLNLYQKKMKAIVEDFLKRLYIFDVSRVPDDQMYRLRDRLRLLPVEIRRLDIFNLILMNMDQIERASDKIAQGVIIAYRDMHLERDEMYGYVNIARNLEGFQQINLEELMRSGDYAQITNMLLNNQPVALVGALPFITDSSVISLIAKLDATVFAQIVKLRKVDTLKPILYKINSDSNDFYLVANYDWVPTSTTKVYKQVPQQFDFRNSMHMLTSNLTFTVYSDLLAFVSADTVEPINAVAFDNMRIMNEL | 879 |
Q1GTG6 | Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis | FUNCTION | MIALPPQPDLDLASLVRTIPDFPRPGIQFRDITTLIGDAVGFAESVRRLSACAAAYRPDLIVAVEARGFLFGAAMATAMGLGVVPVRKAGKLPGVTIGVDYELEYGTDRLELHEGAVLPGHRVVLVDDLLATGGTILATAALMRSVGAEVAAALFVIDLPDLGGSARLGAAGLRCETLIAFNGD | 184 |
B3CV38 | Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine | FUNCTION | MNKMLYIKTYGCQMNVYDSNRMVDLLETQGYNIVANMADASVIILNTCHIREKASEKMYSELGRIKKLQQSRLKAGKSKAKIIVAGCVGQAEGEEIFIREPAVNIIVGPQSYYNLPTMLEKLDSGTENHLIDLDFVEAAKFNKLPEVLKSPTVSGLVSVQEGCDKFCTFCVVPYTRGAEFSRPLEQVYREVLNIAQQGAKEVVLVGQNVSAYHGKDENGKECSLADLIKYVAKIDKIKRIRYITSHPNDMTDQLLSLHATEEKLMPFLHLPVQSGSNKILKLMNRRHSRERYLEIIQQLRELRPDIVISSDIIVGFPGEDDEDFEATLSLAKEARFGQCYSFKYSQRPGTPAAVKQQISEEVKQHRLSILQAQLMQQQLECNQKLIGKVVPVLFDRDGKYDGQIIGKTPYMQSVCIMNEKDNNLYGKIVNVKILTASASSLFGEVYADS | 449 |
B2TTU8 | Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate | FUNCTION | MQKRAIYPGTFDPITNGHIDIVTRATQMFDHVILAIAASPSKKPMFTLEERVALAQQATAHLGNVEVVGFSDLMANFARNQHATVLIRGLRAVADFEYEMQLAHMNRHLMPELESVFLMPSKEWSFISSSLVKEVARHQGDVTHFLPENVHQALMAKLA | 159 |
P20867 | Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis | FUNCTION | MGGKWSKHSVPGWSTVRERMRRAEPATDRVRQTEPAAVGVGAVSRDLEKHGAITSSNTAATNADCAWLEAYEDEEVGFPVRPQVPLRPMTYKAAIDLSHFLKEKGGLEGLIYSQKRQDILDLWIYHTQGYFPDWQNYTAGPGVRFPLTFGWCFKLVPVDPEKVEEANEGENNCLLHPMSQHGMDDPEKEVLVWKFDSKLALHHVARELHPEYYKDC | 216 |
B5F9T8 | Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC) | FUNCTION | MSKSFTFKQFHIDIGSCGMPVSTDGVLLGAWTNISECSQILDIGAGTGLLSLMSAQRNSNAHIDAIELMPIAAEVARLNFSQSPWKERLVLIHQDFLSYQTAYEYDAIICNPPYFNNGEQSLKGERSTARHTDSLPFDKLLQHCKTLISSTGRASFILPVFEGEIFIKIAKGCDFHLTKITKVKTTEKKSPTRLLIELSLFPHIYQESTLTIHDGNGYSDDFIKLTRMFYLNMG | 234 |
A1WBD4 | Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) | FUNCTION | MLDILLLRKDLASAVARLETRKKPQAFLNVEAFQALESERKTIQMRTEELQSQRNQLSKQIGMLMGKGEKDAAEAAKAQVAAIKAELDGSATRLDQIQGELQTMLAAVPNLPHESVPVGSDESANVEVRRWSPDGQQPRSLGFTPKDHVDLGEPLGLDFDMGVKLSGSRFTVMKGGIARLHRALAQFMLDVQTQEHGYTECYVPYVVNADSLKGTGQLPKFEGDLFAAQKGGQDAEPVPDNAQLYLIPTSEVPLTNFVRDEVLAEAQLPLKLTAHTPCFRSEAGSYGRDTRGMIRQHQFDKVEMVQIVHPDKSYEALEEMTRHAEAVLQKLGLPYRVMSLCTGDMGFGAAKTYDLEVWLPAQNTYREISSVSNCEAFQARRLQARFKNAQGKNELVHTLNGSGLAVGRTLVAVLENYQNEDGSVTIPEVLRPYMGGQATLSV | 442 |
C1CRV9 | Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis | FUNCTION | MSKGFLVSLEGPEGAGKTSVLEALLPILEEKGVEVLTTREPGGVLIGEKIREVILDPSHTQMDAKTELLLYIASRRQHLVEKVLPALEAGKLVIMDRFIDSSVAYQGFGRGLDIEAIDWLNQFATDGLKPDLTLYFDIEVEEGLARIAANSDREVNRLDLEGLDLHKKVRQGYLSLLDKEGNRIVKIDASLPLEQVVETTKSVLFDGMGLAK | 212 |
A0ZZ78 | Probable ATPase of unknown function. Its presence in a non-photosynthetic plant (Epifagus virginiana) and experiments in tobacco indicate that it has an essential function which is probably not related to photosynthesis | FUNCTION | MKGHQFKSWIFELREILREIKNSHYFLDSWTQFNSVGSFIHIFFHQERFIKLLDPRIWSILLSRNSQGSTSNRYFTIKGVVLFVVAVLIYRINNRNMVERKNLYLTGLLPIPMNSIGPRNDTLEESFGSSNINRLIVSLLYLPKGKKISESCFLDPKESTWVLPITKKCIMPESNRDSRWWRNWIGKKRDSSCKISNETVAGIEISFKEKDIKYLEFLFVYYMDDSIRKDHDWELFDRLSPSKRRNIINLNSGQLFEILVKDWICYLMFAFREKIPIEVEGFFKQQGAGSTIQSNDIEHVSHLFSRGKWAISLQNCAQFHMWQFRQDLFVSWGKNPHESDFLRNISRENWIWLDNVWLVNRDRFFSKVRNVSSNIQYDSTRSSFVQVTDSRQLKGSSDQSRDRFDSISNEDSEYHTLINQREIQQLKERSILWDPSFLQTERTEIESDRFPKCLSGYSSMSRLFTEREKRMNNHLLPEEIEEFLGNPTRSIRSFFSDRWSELHQGSNPTERSTRDQKLLKKEQDVSFVPSRRSENKEIVNIFKIITYLQNTVSFHPISSDPGCDMVPKDELGSSNKISFLNKNPFFDLFHLFHDQNRRGYTLHHDFESEERFQEMADLFTLSITEPDLVYYKGFAFSIDSYGLDQKQFLNEVFNSRDESKKKSLSALPPIFYEENESFYRRIRKKWVRISCGNELEDPKPKIVVFASNNIMEAVNQDRLIRNLIQIQYSTYGYIRNVLNRFIKKNRSDRNFEYGILRDQIGNDTLNHRTIMKYTINQHLSNLKKSQKKWFDPLILISRTERSMNRDPNAYRYKWSNGSKNFQEHLEHFVSEQKSRFQVVFVRLRINQYSIDWSEVIDKKDLSKSLRFFLSKLLLFLSKLLLFLSNSLPFFFVSFGNIPIHRSEIHIYELKGPNDQLCNQLLESIGLQIVHLKKLKPFLLDDHNTSQKPKFLINGGTISPFLVNKIPKWMIDSFHTRNNRRKSFDNMDFSMISHDQDNWLNPVKPFHRSSLISSFYKANRLRFLNNPHHFCFYCNKRFPFYVEKARINNYDFTYGQFLNILFIRNKIFSLCGGKKKHAFLGRDTISPSPIESQVSNIFISNDFPQSGDERYNLYKSFQFAIRSDPLVRRAIYSIADISGTPLTEGQIVNFERTYCQPLSDMNPSDSEEKNLHQYLNFNSNMGLIHTPCSEKYLPSEKRKKRSLCLKKCVEKGWMYRTFQRDSAFSTLSKRNLFQTYMPWFLTSTGYKYLNLIFLDTFSDLLPILSSSQKFVSIFHDIMHGSDISWRILQKKLCLPQWNLISEISSKCLHNFLLSEEMIHRNNESPLISTHLRSPNVQEFLYSILFLLLVAGYLVRTHLLFVSRAYSELQTEFEKVKSLMIPSYMIELRKLLDRYPTSELNSFWLKNLFLVALEQLGDSLEEIRGSAFGGNMLWGGGPAYGVKSIRSKKKYLNINLIDIIDLISIIPNPINRIIFSRNTRHLSHTSKEIYSLIRKRKNVSGDWIDEKIESWVANSDSIDDKEREFLVQFSTLTTEKRIDQILLSLTHSDHLSKNDSGYQMIEQPGPIYLRYLVDIHKKYLMNYEFNTSCLAERRIFLAHYQTITYSQTSCGANSFHFPSRGKPFSLRLALSPSRGILVIGSIGTGRSYLFKYLATNSYVPFITVFLNKFLDNKLKGFLIDDIDIDDSDDIDASDDIDASDAIDDSDAIDRDLDTELELLTMMNALTMDMMSEIDRFYITLQFELAKAMSPCIIWIPNIHDLDVNEANYLSLGLLVNYLSKDCERCSTRNILVIASTHIPQKVDPTLIAPNKLNTCIKIRRLLIPQQRKHFFTLSYTRGFHLEKKMFHTNGFGSITVGSNARDLVALTNEALSISITQKKSIIDTNTIRSALHRQTWDLRSQVRSVQDHGILFYQIGRAVVQNVLLSNCPLDPISIYMKKKSCNEGDSYLYKWYFELGTSMKKLTILLYLLSCSAGSVAQDLWSLPGPDEKNGITSYGFVENDSDLVHGLLEVEGALVGSSRTEKDCGQFDNDRVTLLLRSEPGNPLYMMQNGSCSIVDQRNLYEKYESEFEEGEGEGVLDPQQIEEDLFNHIVWAPRIWRPWGFLFDCIERPNELGFPYWAGSFRGKRIIYDEKDELQENDSAFLQSGTMQYQARDRSSKEQGFFRISQFIWDPADPLFFLFKDQPFVSVFSHREFFADEEMSKGLLTSQTDPPTSIYKRWFIKNTQEKHFELLIHRQRWLRTNSSLSNANGFFRSNTPSESYQYLSNLFLSNGRLLDQMTKTLLRKRWLFPDEMKIGFM | 2,298 |
Q7M4T0 | Partially degrades N.crassa cell wall beta-D-glucan, liberating small amounts of oligosaccharides | FUNCTION | MYPPALTLLLTPGLVAAAIQPQAYASSADGRYKLSSYSAPVRGTGTPGSNSTWKLTIDDTPSGRKQTIKGFGAAVTDSTVSVFNALPSAQRTALLNTLMTTAGANFAMMRHTIASSDLSANPAYSYDDSNGQTDLSLSNFNLGGRGNAMASLLAEMRRLQPGLTILGSPWSPPGWMKLNRAIQGTTVNNNLDHAYASQFAQYFVKYLQAYQAKGATIDAITIQNEPLNSRAQMPTMYIYADEAGDLIQNNIGPALRNAGLDTKIWAYDHNTDQPSYPSTVLSRAGGYVPAVAWHCYASSLDWSVLTTFHNAHPGVEQYMTECWTSAKQPTPWNWAASFTMGPLQNWASGVTAWVLGTDTNDGPHLTGSDACDKCTGLVTVDAAAGTYNLRGDYYMMAQFSKFMKKGAVVMSGTGSWTYGDGSGLESVAATNADDGSRVVVIENKFGNEIYVTVEAKSGEVWSGLVYRNSVVTWVLPAAGA | 480 |
Q40158 | Metallothioneins have a high content of cysteine residues that bind various heavy metals | FUNCTION | MSCCGGNCGCGSSCKCGNGCGGCKMYPDMSYTESSTTTETLVLGVGPEKTSFGAMEMGESPVAENGCKCGSDCKCNPCTCSK | 82 |
P63641 | Provides the (R)-glutamate required for cell wall biosynthesis | FUNCTION | MDNRPIGFLDSGVGGLTVVRELMRQLPHEEIVYIGDSARAPYGPRPAEQIREYTWQLVNFLLTKDVKMIVIACNTATAVVWEEIKAQLDIPVLGVILPGASAAIKSSQGGKIGVIGTPMTVQSDIYRQKIHDLDPDLQVESLACPKFAPLVESGALSTSVTKKVVYETLRPLVGKVDSLILGCTHYPLLRPIIQNVMGPKVQLIDSGAECVRDISVLLNYFEINRGRDAGPLHHRFYTTASSQSFAQIGEEWLEKEIHVEHVEL | 264 |
Q5HHE4 | Alternative, nonproton pumping NADH:quinone oxidoreductase that delivers electrons to the respiratory chain by oxidation of NADH and reduction of quinones, and contributes to the regeneration of NAD(+) | FUNCTION | MAQDRKKVLVLGAGYAGLQTVTKLQKAISTEEAEITLINKNEYHYEATWLHEASAGTLNYEDVLYPVESVLKKDKVNFVQAEVTKIDRDAKKVETNQGIYDFDILVVALGFVSETFGIEGMKDHAFQIENVITARELSRHIEDKFANYAASKEKDDNDLSILVGGAGFTGVEFLGELTDRIPELCSKYGVDQNKVKITCVEAAPKMLPMFSEELVNHAVSYLEDRGVEFKIATPIVACNEKGFVVEVDGEKQQLNAGTSVWAAGVRGSKLMEESFEGVKRGRIVTKQDLTINGYDNIFVIGDCSAFIPAGEERPLPTTAQIAMQQGESVAKNIKRILNGESTEEFEYVDRGTVCSLGSHDGVGMVFGKPIAGKKAAFMKKVIDTRAVFKIGGIGLAFKKGKF | 402 |
A7FZH1 | Binds together with bS18 to 16S ribosomal RNA | FUNCTION | MRKYETVFILNPTLDEEGYKANVEKFKGVIENAGGTVDNVDLWGKRKLAYEVKKVSEGYYTLMNFTADTELPKELDRVFRITDTVIRHMIITQE | 94 |
Q85WL2 | Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns | FUNCTION | MEELQGYFKKARSLQQHFLYPLLLQEFIYTLAYDDGLKGSIFYEPIEFFGYDNKSSLVLIKRLITRMYQQNFLIYSVNDSNQNGLRGHINYFYSHFFYSHIVSEGFSVIVEIPFSLRLVSSPKEKEIPKSQNLRSIHSIFPFLEDKLSHLNNVSDILIPHPIHLEILVPILQYWIQDVPSLHLLRFFLHKYHNLNSFIQNNKTIYVFSKENKRLFWFLYNSYVSECEFLLVFLRKQSCYLRSTSSVAFLERSHFYGKMEHIIIVCCNNFQKTLWPFKDPFMHYVRYQGKAILASRGAHLLMKKWRYYLVNFWQYYFHFWSQPYRMHINPLLNYSFYFLGYLSSVLINPYAVKNKMLENSFLIDTVFKKFDTIIPIIPLIGSLSKAKFCTVSGHPISKPVWGDLSDFDIIDRFGRICRNLSHYHSGSSKKQSLYRIKYILRLSCARTLARKHKSTARALLQRLGSGLLEEFFTEEEQVLSFIFPKTTPFPLHGSHKERIWSLDIIRVNDLVNQII | 514 |
B4SMH9 | Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr) | FUNCTION | MNTSITARELFEQQRERLGLRWAAGKSGEKRELEAGNTVSRRPSLAGYLNAIYPNKVQILGTEELSWLDALEPRQRWETIEKIMQSHPLALVLTRNQPCPEDLRAAADESGTPLWLSPKRGHELLNHLSYHLARTLAPRVILHGVFMEIYSIGVLITGEAGSGKSELALELLSRGHRLVADDAPEFTQIAPDVLDGTCPELLQDLLEVRGLGVLNVREMFGDTAVKKNKYLRLIVHLTKPMTEPTPHGYERLTGDSGTRHVLDLDVPLITLPVMPGRNLAVLTEAATRLHILRTKGIDPAAMFIARHSNLLERRTP | 316 |
P9WJG1 | This subunit may be involved in monitoring complementarity of crRNA and target RNA | FUNCTION | MSVIQDDYVKQAEVIRGLPKKKNGFELTTTQLRVLLSLTAQLFDEAQQSANPTLPRQLKEKVQYLRVRFVYQSGREDAVKTFVRNAKLLEALEGIGDSRDGLLRFCRYMEALAAYKKYLDPKDK | 124 |
B7MPG7 | Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) | FUNCTION | MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD | 375 |
B8GP32 | Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides | FUNCTION | MAVTDRDIFTVTRLNQAVQGLLEGTFPLIWVEGELSSVSRPASGHLYFTLKDSGAQVRCALFRNRAQLMRFRPADGMQVLVRARVGLYAPRGDYQLIVEHMEEAGDGALRRAFEELKQRLEREGLFDAERKRPLPRFPRRLGVITSPTGAAIRDILSVLRRRFPGLPALIYPVPVQGAAAAPAIAEALRTASARKDCDVLILARGGGSLEDLWAFNEEIVARAIHDCEIPVVSGVGHEVDVTIADLAADLRAATPSAAAELVSPLRDEWLLHVERQRRLLVERMQRGLQHQALKLDNLERRLRQQHPERRLQNQAQRVDELERRLALAMQHRLRHRESRLARLQDRLQHRSPARALERLEAREAQLRLRLDSALRRRLDRFEARLAAAGRALHSVSPLATLGRGYSILTTAEGQVIRDASQVQVNDRVEARLGKGRLSCTVVTRYEG | 447 |
A0A482ATU4 | Acts as a suppressor component of the dual wtf meiotic drive system, and can suppress but not confer meiotic drive by compatible poisons. Wtf meiotic drive systems promote unequal transmission of alleles from the parental zygote to progeny spores by encoding a poison and an antidote from the same locus; the poison is trans-acting and forms toxic aggregates in all spores within an ascus, wherease the antidote is spore-specific and targets aggregates for degradation by the vacuole. Meiotic drive by wtf systems therefore lead to poisoning of all progeny that do not inherit the dual poison/antidote allele, or express a compatible antidote | FUNCTION | MKNNYTSLKSSIDKEDELKSVHEIDLEKGLLPEYNSDEESTLPPYSDHARVSNPPNTHRENHSSGTTDNSSPFLIKLLISFTSIILFNAPAVCYLKYKDAFFKNYGAAEWTLIGFWCASSLIIFTFSWYFYETWTKAVGKGIKHFLKKWRNIPMAFSEVFLFNILVGSPRVTLRHISGERWGLKCSLADHIIFAILSILVFIVETVEPGSSKINIMKRLRGDNARDATQHVNEYTAVPLREMNPESEA | 248 |
Q6MMZ9 | Binds directly to 16S ribosomal RNA | FUNCTION | MANHKSAAKRARQSIRKTAVNNARKSTVKTAEKKLVKAIEAKDLKALPELLKNFSSQVMKAAKTGVIKKETASRKISRLSTRASATK | 87 |
P31936 | Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes adhesion and migration of various cells via the alpha-V/beta-3 integrin receptor (ITGAV:ITGB3) | FUNCTION | FSMKNFHRRAKLEDPEENGVFKYRPRYYLYKHAYFYPPLKRFPVQSSSDSSEENGNGDSSEEEEEEEENSNEEENNEENEDSDGNEDEDSEAENITLSTTTLGYGGDVTPGTASIGLAALQLPKKAGDIGKKSAKEEESDEDEEEEEENEENEAEVDDNEQGTNGTSTNSTEVDSGNGHSGGDNGEEGDQESVTEAQGTTVAGEQDNGGAKTTTSPNGGLEPTPPPQDISGTTLPPSGKTTTPEYEGEYEQTGAHEYDNGYEIYESENGEPRGDSYRAYEDEYSYYKGRSYNSYGGHDYY | 300 |
P33761 | Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP-independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication | FUNCTION | MLHNTFFICETNQIMNEIEKAKGIILNRNMNDIWSALLIEVKKSNLIIKSTDRNIFFESTISIVSETDFKVLINASNFYDAVKAFNFYKKIKIVFNENNSKLEIMGELNDEKEEYEDHLKEPTFSYEEIENYNYDMVNEDYTFGIEIKQKSFKKVINRIAFSAHLDESKNVLNGVYFSKDEDSKLLLVSTNGHRMSICKTEVIVEEDVNFIVPVKIFNFLKHLMSGEGMVKIKFSDKKFYVEFDNYKIACSLINGNYPDYKSIIPKEQKNKSLVSLGILKDRLARVNLYVDKSRKLVLTFSELQLKLLGEDLITGRKGEFFIKDPNYLYDGADEVMAINISYFVEAISVFETSKIEIQFNSGNVLKLSEPENFNFTHLIMPMSLG | 385 |
B0KGD9 | Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate | FUNCTION | MLIVADENIPLLDAFFQGFGEIRRYPGRSLDAASVKDADILLVRSVTKVDRQLLEGSRVRFVGTCTIGTDHLDLDYFAQASISWSSAPGCNARGVVDYVLGSLLTLAELDGVALAERVYGVVGAGEVGGRLVRVLHGLGWKVLVCDPLRQAAEGGDYVSLETIVQQCDVISLHTPLQRGGEHPTWHLLGPAQLAQLRPGAWLVNASRGPVVDNIALRELLLDREDVHAVLDVWEGEPQVDLQLADLCTLASPHIAGYSLDGRQRGTAQIYQALCRFLGVDEQVQLADLLPRPALAQVELDASTDPAWALATLCRAVYDPRRDDADFRRSLSDDPQLQRAAFDQLRKHYPPRREIEGLAVRLRGESPQLAQLVSALGGALV | 380 |
A6ZQI5 | Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses | FUNCTION | MKFDNDSEKQVFDKLKKAIPGIIKEKCAGYDELYGYKLNPEGLTQEEVDKYYDEKIADRLTYKLCKAYQFEYSTIVQNLIDILNWRREFNPLSCAYKEVHNTELQNVGILTFDANGDANKKAVTWNLYGQLVKKKELFQNVDKFVRYRIGLMEKGLSLLDFTSSDNNYMTQVHDYKGVSVWRMDSDIKNCSKTVIGIFQKYYPELLYAKYFVNVPTVFGWVYDLIKKFVDETTRKKFVVLTDGSKLGQYLKDCPYEGYGGKDKKNNLTKQNVTNVHPTEYGLYILQKQIIEDVE | 294 |
Q57CK0 | Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A | FUNCTION | MNDETTPANKNPEKAELRCGWTTGACATAATKAALTALITGEFPDPVGIILPKGEVPYFQLAYEGLGEGYAMAGIVKDAGDDPDVTHGATIISTVYPAPPGTGIIFRAGEGVGTVTREGLAIPPGEAAINPVPRRMMTEICEAICAEYGLPADLVITISVPGGEEIAQKTWNPRLGIIGGISILGTTGVVHPFSCSAWIHSIHRGIDVARAAGQKHVLGATGSTSEDAAQALYNLPDFAILDMGDFAGGVLKYLREHPIDRLTIAGGFAKLTKLAQGALDLHSSRSQVDKGFLWQIAERAGAPAGMKERILLANTAMEVLELTQSIGIDIAGPIALEARQTALKTLRGAPVEVEIIVTDRKGNILARV | 368 |
O32143 | Oxidizes hypoxanthine and xanthine to uric acid | FUNCTION | MDIKEAGPFPVKKEQFRMTVNGQAWEVAAVPTTHLSDLLRKEFQLTGTKVSCGIGRCGACSILIDGKLANACMTMAYQADGHSITTIEGLQKEELDMCQTAFLEEGGFQCGYCTPGMIIALKALFRETPQPSDKDIEEGLAGNLCRCTGYGGIMRSACRIRRELNGGRRESGF | 173 |
Q8EUD7 | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates | FUNCTION | MEKFLRYNIQIGKDQNKDADYGVFVFKPLERGFGHTLGNSLRRVLLSNIIGHSLFAIKIPNVSHEFQSIKGVKEDLTQIILNLKRLVVKIDQEIFGEEEQKETSLEKWPTLKIDFSKGGVLKASDIETPVGFEIINKDMYIATIESGVKFKMELFVKTGRGFTTFSENKELINAINVIAVDSNFSPVLKVGYKVSDIKTTKNEINDVLELEVATNGAVSAAEAVAMSAKILLEHYKPIVTELFDNYNDLRIINEEATVSSSKSSLAISIDELELSVRSYNCLKRAGIHTITQLTDKTKGEIEKIRNLGKKSFKEIIKKIQDRNLKLKEEQN | 331 |
Q2NEH4 | Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) | FUNCTION | MLVNIRIDFKIADIETMEKSYAKLDMINAELHEKLDILEEVTLKTCNRYEIYLLIDEEVNIPTTTFIVEKNDMAINHLLRLASGLESMIMGEDQILGQIKTARKNAIKNKTIGPKLEKVFTKAIHVGQTIRKNTHINEGGVSVGSGAVELIEEKYGSLKGKNVLIIGAGEMGTVVSKALLEKETNTIVVANRTYDKARQLAQELDGEAIKFDEMNNELVNIDIVISSTGAPHSIISKERIAFLPEEHLHDMIMLDLANPHDIENDVQELGVKLYNLDDLRYVTDKNKERRNKEAIKAEAIIEDETLLLKESLKQMEITPILSSLNIEAEKIRKQELDKTLHMLDLDKKSSKKVDYLTRSITDKLLYNIINNLKEAAANNDKDTIRNAKKILLEYN | 395 |
Q0VSK3 | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit | FUNCTION | MAIGVIGRKCGMTRVFTEEGVSVPVTVIEVGPNRVSQVKTEESDGYQAVQVTVGERRASRVTKAQAGHFAKAGVEAGRGVWEFRAEAGEFEAGSSVTVEGFEAGQMIDVTGTSKGKGFAGGVKRWNFSTQDATHGNSLSHRAPGSIGQNQTPGRVFKGKKMAGHLGAERVTVQNLEVVRVDADKNLLLVKGAVPGATGGDVIVRLAVKAKA | 211 |
P0C6W4 | Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium | FUNCTION | MSFVAGVAPQGARGKYRAELNTEKRTDHVSLKASLCDAGDLVLKISPWFMDGESAYKHVSEQLSKGSKLLFVPQTLKGFIRHLPGPRVYLVERLTGGTYSDPFMVNQLAYQNAAGEGVIGTTLQGKRVGMFFPFDADLVTGEFQFLLRKKGFGGNRFRDAPWDYNWTPYSDLMDALEADPCGKYSQSLLKKLVGGDFTPIDQYMCGKNGKPIAEFAALMASEGITKLADVEAEVKSRTDSDRYIVFKNKLYRIVWNVQRKDVAYSKQSAFTMNSIVQLDTMEDVPRHSFTIGSEIQVIAPSTAVQANGHLNLKQRLLYAFYGKQAVSEPNYIYHSAYVDCTSCGKGSWLTGNAVQGFACDCGAHYCANDVDLQSSGLVRKNAVLLTTCPCNKDGECKHTLPQLVSMMTDKCDVEVVGKTFILTYGGVIYAYMGCSGGTMHFIPRAKSCVSKIGDAIFTGCTGTWSKVCETANLFLERAQHAINFVNEFVLTETVVALLSGTTSSIEELRDLCRNATFEKVRDYLTPRGWIVTMGSYIEGVINVGAAGVCNAALNAPFIVLSGLGESFKKVAATPWKLCSSLRETLDHYADSITYRVFPYDIPCDVTDYTALLLDCAVLTGASAYFVARYVDEKVEQLTNLVFSSCQSAVAAFVQACMSTYKATAKFISDMFTLIKVVSERLYVYTSVGFVVVGDYSSQLLKQFMHILSKAMQLLHTTVSWAGSKLPSVVYNGRDSLVFPSGTYYCVSTQGRSLQDQFDLVIPGDLSKKQIGILEPTPNSTTVDKKINTNVVEVVVGQLEPTKEHSPELVVGDYVIISNKIFVRSVEDSETVFYPLCTDGKIVPTLFRLKGGAPPKGVKFGGEQTKEITAVRSVSVDYDVHPVLDALLAGSELATFTVEKDLPVKDFVDVVKDEVIELLSKLLRGYNVDGFDLEDFADTPCYVYNAEGDLAWSSTMTFSVNPVEEVEEECDDDYVEDEYLSEEMLVEEDENSWAAAVEAVIPMEDVQLDTLVAEIDVSEPADDVAEQASTEEVEVPSACVLEASQVANAAEVESCEAEVSSSIPLHEDANAAKANDCAEGMPALDSTETVSKLSVDTPVGDVTQDDATSSNATVISEDVHTATHSKGLVAVPEVVPEKALGTSVERMRSTSEWTVVETSLKQETAVIVKNDSSAKPQRVKKPKAENPLKNFKHIVLNNDVTLVFGDAIAVARATEDCILVNAANTHLKHGGGIAAAIDRASGGLVQAESDDYVNFYGPLNVGDSTLLKGHGLATGILHVVGPDARANQDIQLLKRCYKAFNKYPLVVSPLISAGIFCVEPRVSLEYLLSVVHTKTYVVVNSEKVYNDLAAPKPPTGLTYSHEGWRGIIRNAKSFGFTCFICTDQSANAKLLKGRGVDLTKKTQTVDGVKYYLYSSKDPLTDIITAANACKGICAMPIGYVTHGLDLAQAGQQVKKITVPYVCLLASKDQVPILNSDVAVQTPEQSFINTVIANGGYHCWHLVTGELIVKGVSYRKLLNWSDQTICYADNKFYVVKGQIALPFDSLEKCRTYLTSRAAQQKNVDVLVTIDGVNFRTVVLNNTTTYRVQLGSVFYKGSDISDTIPTEKMSGEAVYLADNLSEAEKAVLSEVYGTADTAFLHRYYSLLALVKKWKYTVHDGVKSLKLNSNNCYVNVTMLMLDMLKEIKFIVPALQAAYLKHKGGDSTEFIALIMAYGDCTYGEPDDASRLLHTILSKAELTTQAKMVWRQWCNVCGVQDTTTTGLKACIYVGMNSLDELHATHEECCQCGDVRKRQLVEHNAPWLLLSGLNEAKVMTPTSQSAGPDYTAFNVFQGVETSVGHYLHVRVKDNLLYKYDSGSLSKTSDMKCKMTDVYYPKQRYSADCNVVVYSLDGNTWADVDPDLSAFYMKDGKYFTKKPVIEYSPATILSGSVYTNSCLVGHDGTIGSDAISSSFNNLLGFDNSKPVSKKLTYSFFPDFEGDVILTEYSTYDPIYKNGAMLHGKPILWVNNSKFDSALNKFNRATLRQVYDIAPVTLENKYTVLQDNQIQQVEVEAPKEDAKPQSPVQVAEDIDNKLPIIKCKGLKKPFVKDGYSFVNDPQGVNVIDTLGIDDLRALYVDRNLRLIVLKENNWSALFNIHTVEKGDLSVIAASGSITRRVKILLGASSLFAQFASVTVNVTTAMGKALGRMTRNVITNTGIIGQGFALLKMLLILPFTFWKSKNQSTVKVEVGALRTAGIVTTNVVKQCASAAYDVLVVKFKRIDWKSTLRLLFLICTTGLLLSSLYYLFLFHQVLTSDVMLDGAEGMLATYRELRSYLGIHSLCDGMVEAYRNVSYDVNDFCSNRSALCNWCLIGQDSLTRYSAFQMIQTHVTSYVINIDWVWFVMEFALAYVLYTSTFNVLLLVVSSQYFFSYTGAFVNWRSYNYLVSGYFFCVTHIPLLGLVRIYNFLACLWFLRRFYNHVINGCKDTACLLCYKRNRLTRVEASTVVCGSKRTFYIVANGGTSFCCRHNWNCVDCDTAGIGNTFICEEVANDLTTSLRRLVKPTDKSHYYVESVTVKDSVVQLHYSREGASCYERYPLCYFTNLDKLKFKEVCKTPTGIPEHNFLIYDSSDRGQENLARSACVYYSQVLSKPMLLVDSNMVTTVGDSREIASKMLDSYVNSFISLFGVNRDKLDKLVATARDCVKRGDDFQTVIKTFTDAARGPAGVESDVETSSIVDALQYAYKHDLQLTTEGFNNYVPSYIKPDSVATADLGCLIDLNAASVNQTSIRNANGACIWNSSDYMKLSDSLKRQIRIACRKCNIPFRLTTSRLRSADNILSVKFSATKLSGGAPKWLLKLRDFTWKSYCVVTLVVFAMAVLSYLCLPAFNMSQVSFHEDRILTYKVVENGIIRDITPSDTCFANKYQSFSKWFNEHYGGLFNNDISCPVTVAVIAGVAGARVPNLPANVAWVGRQIVLFVSRVFASSNNVCYTPTAEIPYERFSDSGCVLASECTLFRDAEGKINPYCYDPTVLPGASAYDQMKPHVRYDMYDSDMYIKFPEVVFESTLRITKTLATRYCRFGSCEDANEGVCITTNGSWAIYNDHYANKPGVYCGDNYFDIVRRLGLSLFQPVTYFQLSTSLALGVMLCIFLTIAFYYVNKVKRALADYTQCAVVAVAAALLNSLCLCFVVSNPLLVLPYTALYYYATFYLTGEPAFVMHVSWFVMFGTVVPIWMVFAYIVGVCLRHLLWVMAYFSKKHVEVFTDGKLNCSFQDAAANIFVINKDTYVALRNSITQDSYNRYLSMFNKYKYYSGAMDTASYREASAAHLCKALQVYSETGSDVLFQPPNCSVTSSVLQSGLVKMAAPSGVVENCMVQVTCGSMTLNGLWLDNYVWCPRHVMCPADQLSDPNYDALLVSKTNLSFIVQKNVGAPANLRVVGHTMVGTLLKLTVESANPQTPAYTFTTVKPGASFSVLACYNGRPTGVFMVNMRQNSTIKGSFLCGSCGSVGYTQEGNVINFCYMHQMELSNGTHTGCAFDGVMYGAFEDRQVHQVQLSDKYCTINIVAWLYAAILNGCNWFVKPNKTGIATFNEWAMSNQFTEFIGTQSVDMLAHKTGVSVEQLLYAIQTLHKGFQGKTILGNSMLEDEFTPDDVNMQVMGVVMQSGVKRISYGLVHWLFTTLLLAYVATLQLTKFTIWNYLFEVIPLQLTPLVLCVMACVMLTVKHKHTFLTLFLLPTAICLTYANIVYEPQTPVSSALIAVANWLNPASVYMRTTHTDLGVYLSLCFALAVVVRRLYRPNASNLALALGSAMVWFYTYTTGDCSSPLTYLMFLTTLTSDYTVTVFLAVNVAKFFARVVFLYAPHAGFIFPEVKLVLLMYLAVGYFCTVYFGVFSLLNLKLRVPLGVYDYTVSTQEFRYLTGNGLHAPRNSWEALRLNMKLIGIGGTPCIKIASVQSKLTDLKCTSVVLLSVLQQLHLEANSKAWAHCVKLHNDILAATDPTEAFDNFVCLFATLMSFSANVDLEALASDLLDHPSVLQATLSEFSHLASYAELEAAQSSYQKALNSGDASPQVLKALQKAVNIAKNAYEKDKAVARKLERMAEQAMTSMYKQARAEDKKAKIVSAMQTMLFGMIKKLDNDVLNGVISNARNGCVPLSVVPLCASNKLRVVIPDITIWNKVVTWPSLSYAGALWDISLINNVDGEVVKSSDVTETNESLTWPLVLECTRAASSAVTLQNNEIRPSGLKTMVVSAGIDHANCNTSSLAYYEPVEGRKMLMGILSENAHLKWAKVEGRDGFVNIELQPPCKFLIAGPKGPEVRYLYFVKNLNNLHRGQLLGHIAATVRLQAGSNTEFAINSSVLSAVTFSVDPGKAYLDFVNAGGAPLTNCVKMLTPKTGTGIAVSVKPEANADQDTYGGASVCLYCRAHIEHPDVTGVCKFKGKFVQVPLHIRDPVGFCLQNTPCNVCQFWIGHGCNCDALRGTTIPQSKDSNFLNRVRGSIVNARIEPCASGLTTDVVFRAFDICNYKAKVAGIGKYYKTNTCRFVEVDDEGHRLDSFFVVKRHTMENYELEKRCYDLVKDCDAVAVHDFFIFDVDKVKTPHIVRQRLTEYTMMDLVYALRHFDQNNCEVLKSILVKYGCCDASYFDNKLWFDFVENPNVISVYHKLGERIRQAVLNTVKFCDQMVKSGLVGVLTLDNQDLNGKWYDFGDFVITQPGAGVAIVDSYYSYLMPVLSMTNCLAAETHRDCDLTKPLIEWPLLEYDYTDYKIGLFEKYFKXWDQQYHPNCVNCTDDRCVLHCANFNVLFSMTLPGTSFGPIVRKIFVDGVPFVISCGYHYKELGLVMNMDVSLHRHRLSLKELMMYAADPAMHIASASALWDLRTPCFSVAALTTGLTFQTVRPGNFNKDFYDFVVSKGFFKEGSSVTLRHFFFAQDGHAAITDYSYYAYNLPTMCDIKQMLFCMEVVDRYFEIYDGGCLNASEVIVNNLDKSAGHPFNKFGKARVYYESLSYQEQDELFAMTKRNVLPTITQMNLKYAISAKNRARTVAGVSILSTMTNRQYHQKMLKSMAATRGSTCVIGTTKFYGGWDFMLKTLYKDVDNPHLMGWDYPKCDRAMPNMCRIFASLILARKHSTCCTNTDRFYRLANECAQVLSEYVLCGGGYYVKPGGTSSGDATTAYANSVFNILQATTANVSALMGANGNTIVDEEVKDMQFELYVNVYRKSQPDPKFVDRYYAFLNKHFSMMILSDDGVVCYNSDYATKGYIASIQNFKETLYYQNNVFMSEAKCWVETDLKKGPHEFCSQHTLFIKDGDDGYFLPYPDPSRILSAGCFVDDIVKTDGTLMVERFVSLAIDAYPLTKHDDPEYQNVFWVYLQYIEKLYKDLTGHMLDSYSVMLCGDNSAKFWEESFYRDLYTAPTTLQAVGSCVVCHSQTSLRCGTCIRRPFLCCKCCYDHVIATPHKMVLSVSPYVCNAPGCDVADVTKLYLGGMSYFCIDHRPVCSFPLCANGLVFGLYKNMCTGSPSVTEFNRLATCDWTESGDYTLANTTTEPLKLFAAETLRATEEASKQSYAIATIKEIVGERELLLVWEAGKAKPPLNRNYVFTGYHITKNSKVQLGEYVFERIDYSDAVSYKSSTTYKLAVGDIFVLTSHSVATLQAPTIVNQERYVKITGLYPTLTVPEEFANHVANFQKAGFSKFVTVQGPPGTGKSHFAIGLAIYYPTARVVYTACSHAAVDALCEKAFKYLNIAKCSRIIPAKARVECYDQFKVNETNSQYLFSTINALPETSADILVVDEVSMCTNYDLSVINARIKAKHIVYVGDPAQLPAPRTLLTRGTLEPENFNSVTRLMCNLGPDIFLSVCYRCPEEIVNTVSALVYNNKLVAKKPASGQCFKILYKGSVTHDASSAINRPQLNFVKSFIAANPNWSKAVFISPYNSQNAVARSVLGLTTQTVDSSQGSEYPYVIFCQTADTAHANNINRFNVAVTRAQKGILCVMTSQALFDSLEFAEVSLNNYKLQSQIVTGLYKDCSRESSGLHPAYAPTYVSVDDKYKTSDELCVNLNVPANVPYSRVISRMGFKLDASIPNYPKLFITRDEAIRQVRSWIGFDVEGAHASRNACGTNVPLQLGFSTGVNFVVQPVGVVDTEWGSMLTSIAARPPPGEQFKHLVPLMNKGAAWPIVRRRIVQMLSDTLDKLSDYCTFVCWAHGFELTSASYFCKIGKEQRCCMCNRRASTYSSPLHSYACWSHSSGYDYVYNPFFVDVQQWGYIGNLATNHDRYCSVHQGAHVASNDAVMTRCLAIHDCFIERVEWDITYPYISHEKRLNSCCRAVERNVVRAALLAGRFERVYDIGNPKGIPIVDDPVVDWHYYDAQPLSKKVQQLFYTEDCAKNFSDGLCLFWNCNVPRYPNNAIVCRFDTRVHSEFNLPGCDGGSLYVNKHAFHTPAYDASAFRDLKPLPFFYYSTTPCEVHGNGNMLEDIDYVPLKSAVCITACNLGGAVCRKHAAEYRDYMEAYNLVSASGFRLWCYKTFDVYNLWSTFTKIQGLENIAYNVIKQGHFTGVEGELPVAVVNDKIYTKSDVNDVCIFENKTTLPTNIAFELYAKRAVRSHPDFNLLRNLEVDVCYKFVLWDYERSNIYGSATIGVCKYTDIDVNSALNICFDIRDNGSLERFMSLPNGILISDRKVKNYPCIVSSNYAYFNGTLIRDNTGNSQSSDGEVKQPVTFYIYKKVNNEFVQFTDTYYTLGRTVSDFTPVSEMEKDFLALDSDVFIKKYKLEAYAFEHVVYGDFSRTTLGGLHLLIGLYKKHQEGHIIMEEMLKERATVHNYFVTESNTASFKAVCSVIDLKLDDFVDIIKAMDLSVVSKVVKIPIDLTMIEFMLWCKDGQVQTFYPRLQAINDWKPGLAMPSLFKVQNSNLEPCMLPNYKQSIPMPQGVHMNIAKYMQLCQYLNTCTIAVPANMRVMHFGAGSDKGVAPGSSVLRQWLPTDAILIDNDLNEYVSDADITLFGDCVTVRVGQQVDLLISDMYDPSTKVVGETNEAKALFFVYLCNFIKNNLALGGSVAIKITEHSWSAELYELMGRFAWWTVFCTNANASSSEGFLIGINYLGELKEVIDGNVMHANYIFWRNTTLMNLSTYSLFDLSRFPLKLKGTPVLQLKESQINELVISLLSQGKLIIRDNDTLSVSTDVLVNFYRKPHKRSKC | 7,182 |
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