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accession
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Full Name
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147
⌀
taxon
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46
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sequence
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16
2.75k
function
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5.51k
AlphaFoldDB
stringlengths
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10
Q9NTG1
PKDRE_HUMAN
Polycystic kidney disease and receptor for egg jelly-related protein
Homo
MRPGPALLLLGVGLSLSVGRLPLPPVPRGAQAAVSGAPGGLLRGAPGLGVRGGRALLSLRPSAVRAGGAVLSGRGSLCFPHGGTGRRWYCLDLRVLLSAQRLPWPAAPALALVDLQLSARGGRLSLTWSVRLPRSPGRLAWAFRLRLLGPGAARPASPAARVSPRSAAPGPRPQQGFVARTECPTDGPARVMLQAVNSSSHRAVESSVSCQINACVIQRVRINTDQKGAPVRLSMQAEATINASVQLDCPAARAIAQYWQVFSVPAVGQAPDWTQPLDLPQLEIRNSPLFIHIPNNSLQWGVYVFNFTVSITTGNPKMPEVKDSDAVYVWIVRSSLQAVMLGDANITANFTEQLILDGSTSSDPDADSPLQGLQFFWYCTTDPRNYGGDRIILGSKEVCHPEQANLKWPWASGPVLTLLPETLKGDHVYFFRMVIRKDSRTAFSDKRVHVLQGPKAIAHITCIENCERNFIVSDRFSLFLNCTNCASRDFYKWSILSSSGGEMLFDWMGETVTGRNGAYLSIKAFAFRHFLEAEFSISLYLACWSGVTSVFRHSFIINHGPQIGECKINPAKGIALITKFVVQCSNFRDKHVPLTYKIIVSDLHSVGEISSVKENTLGTILYLGPQSTVPPSFLPVGMLASQYGLKIYAQVYDSLGAFSQVTLHATAQAPTDKNSSKTVLNQLLSFTVGPSSLLSTLIQKKDFLPAGYLLYIVASVLNNMKTELPLRDDRVNLRKHLIDQSFLLPVSTLVEIGQVVMTITKLTQKPSEFTWDAQKRATMRVWQANQALQEYQQKDKRFRSEQIEIVSTGILMSLSNILKMTSPHQVVKDPFYVIESLSDTILANKVPGNKTTSMRTPNFNMYVKKVEKWGINQLFRNEKHCRNCFYPTLNVSSVPGLSANGPISTMFCDFTNDLFPWLNDQENTSVEVSGFRMTGVADNGSVLEITPDVAEVYLVRKNLTFAAFNLTVGPNSEVDGSLKKTTGGFSFQVDSTVLREVLVHIVTEVMVLFTVLVYTGSQITPTALVATFLVPHDIPPFASQSALFDPACTVKKARVVCLPVSLLQLIAQHSHSPHCTVSIVLQAPRFVMKLNDKLVRISIFSVQCLDMYGIQSEWREGYCILGEKTSWYEVHCICKNVVRARRQLGTIGLTGIHLHTHYVMAKVIVIPNPVDLRLNIIKSLHQNPVTLFTVLFIILLYVGLAFWALYRDEMDQHLRGHVIVLPDNDPYDNLCYLVTIFTGSRWGSGTRANVFVQLRGTVSTSDVHCLSHPHFTTLYRGSINTFLLTTKSDLGDIHSIRVWHNNEGRSPSWYLSRIKVENLFSRHIWLFICQKWLSVDTTLDRTFHVTHPDERLTRKDFFFIDVSSNLRKNHMWFSIFASVVAKTFNRLQRLSCCLAMLLSSLLCNIMFFNLNRQEQTESRERKYMRSMMIGIESVLITIPVQLLITFLFTCSQRKPQADLKEVSPQKHPLMSEASEHWEEYLRKWHAYETAKVHPREVAKPASKGKPRLPKASPKATSKPKHRHRKAQIKTPETLGPNTNSNNNIEDDQDVHSEQHPSQKDLQQLKKKPRIVLPWWCVYVAWFLVFATSSISSFFIVFYGLTYGYDKSIEWLFASFCSFCQSVLLVQPSKIILLSGFRTNKPKYCKNLSWSTKYKYTEIRLDGMRMHPEEMQRIHDQIVRIRGTRMYQPLTEDEIRIFKRKKRIKRRALLFLSYILTHFIFLALLLILIVLLRHTDCFYYNQFIRDRFSMDLATVTKLEDIYRWLNSVLLPLLHNDLNPTFLPESSSKILGLPLMRQVRAKSSEKMCLPAEKFVQNSIRREIHCHPKYGIDPEDTKNYSGFWNEVDKQAIDESTNGFTYKPQGTQWLYYSYGLLHTYGSGGYALYFFPEQQRFNSTLRLKELQESNWLDEKTWAVVLELTTFNPDINLFCSISVIFEVSQLGVVNTSISLHSFSLADFDRKASAEIYLYVAILIFFLAYVVDEGCIIMQERASYVRSVYNLLNFALKCIFTVLIVLFLRKHFLATGIIRFYLSNPEDFIPFHAVSQVDHIMRIILGFLLFLTILKTLRYSRFFYDVRLAQRAIQAALPGICHMAFVVSVYFFVYMAFGYLVFGQHEWNYSNLIHSTQTVFSYCVSAFQNTEFSNNRILGVLFLSSFMLVMICVLINLFQAVILSAYEEMKQPVYEEPSDEVEAMTYLCRKLRTMFSFLTSQSKAKDEPEFFIDMLYGQPEKNSHRYLGLKTRNINGKKMVYLVV
May have a central role in fertilization. May generate a Ca(2+) transporting channel directly involved in initiating the acrosome reaction of the sperm.
Q9NTG1
Q5M7C3
SP13B_XENLA
Sin3-associated polypeptide p130 B
Xenopus
MSSQQFPRQAVSMPPPQVSNSGASVGQNVQGDEVAREIDVQSRDPLGASTVLPSRDDKQEPVVVRPYPQVQMLTSHHPLQPAPSLTMTAQPAHLTSAVPLSFSENILKTPKSTMPSRPIAPAPPSALSAVPKVSGQGTVTMESGLPQTSAIPVATISGQQGHPNSLHHIMAATNVQMSIIRSGAPGPPLHIGASHLPRGAAAAAVMSSSKVTTMLRPASAQIPSAAASQSATQHIIHPPIQSRPPVTTTSVSPAVVATVSATRAQSPVITTTPAHAAEPVLRPTLAFQQHPPPAAISIQRSAQARDAATTRITLPTHPALGGQKPQLHAMTQKTLFGTGNPVAAATVAPILATNTLPSVTTSGSAPHTQVSTSTIVTMTMPTHSSHATAGTASNIPVAKVVPQQITHTSPRIQSEYGTERGNLIPIPGHRASPNPMTMEARSENRQPVPVQLQYFLPTYPPSAYPLTAHTYTPITSSVSTIRQYPVSAQAPNSAITAQSVASTVHLNPMQLINMDTSHTRHIQGIQPAPVSAQGIQPSPFSAQGIQATPISTQGIHPTPINTQAIHPATSITNQGVQTSSVSSQQASSEPKSSVVLAEGATIIANPINSSFSATPAGTTVMQSHSQSPGIGSSPAQGSSPRPSILRKKPATEGLSVRKSLIPPHPGDAVSPRHDSALRSTSASPRPAGAKPKADLHVSVAPGVTGDPGAADQPSAAASLPSSHHPTAAVPSPPSQPVSGPMPSSIHITPATIPALSAPPPLLSNAPSGAVMPEDKMKEEAEPMDILRPVSAVPPLPPNSISSPLTVLANNISGPAGELPPGASPRKKPRKQQHVISTEEGDMMETNSTDEERCHAVKPFTSRPEKRKSPPKEYIDEEGVRYVPVRPRPPITLLRHYRNPWKAAYHHFQRYTDVRVKEEKKLTLQDVANQKGITCRVQGWKTHLCAAQLLQLIKLEQDVFERLTVLQEGLVPKKKTATDDDLHRINELIQGNMQRCKLVMDQITESRDCMLKVLDHKDRVLKLLNKSGASRRLSKVKPKDKM
Acts as a transcriptional repressor.
Q5M7C3
Q09739
MCP7_SCHPO
Meiotically up-regulated gene 32 protein
Schizosaccharomyces
MPPKGLSLAEKRRRLEAIFHDSKDFFQLKEVEKLGSKKQIVLQTVKDVLQSLVDDNIVKTEKIGTSNYYWSFPSDAKRSRESVLGSLQAQLDDLKQKSKTLDENISFEKSKRDNEGTENDANQYTLELLHAKESELKLLKTQLSNLNHCNPETFELKNENTKKYMEAANLWTDQIHTLIAFCRDMGADTNQIREYCSIPEDLDDLQLPIL
Required for meiotic recombination.
Q09739
Q8AVJ1
PRR5_XENLA
Protein observed with Rictor-1
Xenopus
MRSKFMSSPTLSDLGKREATAAAALDERGTQQKRAGANATWNSIQNGVISVFQKKGLADHELYSLNEGVRQLLKTELGSFFTEYLQNQLLTKGMVILRDKIRFYEGQKLLDSLAETWDFFFSDILPMLQAIFYPVQGKEPSIRQLALLHFRNIITLNLKLDDALSRPRARVPPSIIQMLLILQGVHESKGVTEEYMNLESLIQKVVSPYLGTYGLYSNEAPFCHSSCILEKRMFRRCPKSGEILTKNPVVRSKSYNNPLLTPVAEYEMENLVANGSGIRRHSVSEMTSVLELPMGYSNLTTDSTSKLSMAGTKPPGEGERPPISNGQFPPLHNLSDSQQGLYNSQRDSPLLPAPSSSPETIVDQILESIDSDSEGIFIDFGRGCSKSPEFSMEIGRQSLV
Subunit of TORC2, which regulates cell growth and survival in response to hormonal signals.
Q8AVJ1
Q32BC8
RAPZ_SHIDS
RNase adapter protein RapZ
Shigella
MVLMIVSGRSGSGKSVALRALEDMGFYCVDNLPVVLLPDLARTLADREISAAVSIDVRNMPESPEIFEQAMSNLPDAFSPQLLFLDADRNTLIRRYSDTRRLHPLSNKNLSLESAIDKESDLLEPLRSRADLIVDTSEMSVHELAEMLRTRLLGKRERELTMVFESFGFKHGIPIDADYVFDVRFLPNPHWDPKLRPMTGLDKPVAAFLDRHTEVHNFIYQTRSYLELWLPMLETNNRSYLTVAIGCTGGKHRSVYIAEQLADYFRSRGKNVQSRHRTLEKRKP
Modulates the synthesis of GlmS, by affecting the processing and stability of the regulatory small RNA GlmZ. When glucosamine-6-phosphate (GlcN6P) concentrations are high in the cell, RapZ binds GlmZ and targets it to cleavage by RNase E. Consequently, GlmZ is inactivated and unable to activate GlmS synthesis. Under low GlcN6P concentrations, RapZ is sequestered and inactivated by an other regulatory small RNA, GlmY, preventing GlmZ degradation and leading to synthesis of GlmS.
Q32BC8
A8F7S3
PLSY_PSELT
Lysophosphatidic acid synthase
Pseudothermotoga
MNYILIGLISYFCGAIPFSYLLPKLRKIDIRRTGSGNVGGTNALRAAGPVIGFICMVLDGVKAFVPVLVFSLIFKDIHYTGISSIFAVLGHDFPVFLRFKGGKGVASTTGVFFALCPICGFTFLATWISITLLTKYVSLASIVGMYAASFVAFFFNKDYGVLFLLLSTLSTLRHSENIERLVNKSERKTDLIKIIKKRG
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
A8F7S3
Q73N16
RL25_TREDE
General stress protein CTC
Treponema
MEQRLLNANERSTYGKNAAVKMRKAGRIPAVMYDRHGKSVPIDVDEREFMKLFKLVTESTIVTLNAAGKDYEVFIKDFQHDIVSDKIKHIDFYEVERGKTLRTKVKIRLEGSPEGVRHGGILETGITELELECLPKDLPARIIVDVSALDVNQSLHVRDIKLPEAVTVLTSDDITVAAIKFAAAESTTPAATEGEETEAAAAAPEPAAEDK
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
Q73N16
A7I655
RS10_METB6
30S ribosomal protein S10
Methanoregula
MQKARIRLTGTDFNKVETVCDRIREIAERTGVNLAGPIPLPTKRLVVPIRKSPDGEGTATFDRWQMRVHKRLIDIDADERALRQLMRIQVPKDIGIEIVLES
Involved in the binding of tRNA to the ribosomes.
A7I655
A2CBW9
PEBB_PROM3
Phycoerythrobilin:ferredoxin oxidoreductase
Prochlorococcus
MKPLRLSSLDPVRMPEWRWAPFLSHAINALIPLKPEPYPVAPEFLQREGKTGSKSQPIKVTTCTWACRTKKFRQVRAACVEAGSSASVLNFVINPYHTFDLPFFGADLVTLPSGHLLALDLQPAITSDERHTKQVWERLMPIFEQWRVRLPEGGPIPEEAKPYFSPGFLWTRLHLGSEGNQLIDEVIMPAFRDYLNLYLDLVEMAEEVSPQRAFKLLEGQKRYLSYRGKKDPARAMLARFHGHQWTESYIHNVLFDL
Catalyzes the two-electron reduction of the C2 and C3(1) diene system of 15,16-dihydrobiliverdin.
A2CBW9
Q821E6
RECA_CHLCV
Recombinase A
Chlamydia
MNVPDRKKALEAAIAYIEKQFGAGSIMSLGKHSATHEISTIKTGALSLDLALGIGGVPKGRIVEIFGPESSGKTTLATHIVANAQKMGGVAAYIDAEHALDPGYASLIGANINDLMISQPDCGEDALSIAELLARSGAVDVIVIDSVAALVPKSELEGDIGDVHVGLQARMMSQALRKLTATLARSQTCAIFINQIREKIGVSFGNPETTTGGRALKFYSSIRMDIRRIGAIKGNESFDLGNRIKVKVAKNKLAPPFRTAEFDILFNEGISSAGCILDLAVEHNIVEKKGSWFNYQDRKLGQGREAVREELKKNKKLFDELEKRIYDISSASKVVAVEEKKEELKAQPVA
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
Q821E6
A0A443HJY8
VDTC1_BYSSP
Viriditoxin biosynthesis cluster protein C
Paecilomyces
MAEEIKLTPLETFAQAISASAKTIATYCRDSGHPQLSDDNSSGLTGDVLPPSAPQAVTAARQTILEASYRLQQLVTEPSQYLPRLTVYPQHLAALRWLCHFRIPELIPVQGTRTYYELATEAKVPLHQLQSIARMAITGSFLREPEPNIVAHSRTSAHFVENPSLRDWTLFLAEDTAPMAMKLVEATEKWGDTRSKTETAFNLALGTDLAFFKYLSSNPQFTQKFSGYMKNVTASEGTSIKHLVNGFDWASLGNAIVVDVGGSTGHASIALAESFPDLKFIVQDLPMVTSTSKDNREKTPLPETVASRISFESHDFFKPQPVQNADVYLLRMILHDWSFKEAGEILANLVPSVKQGARILIMDTVLPRHGTVPVTEEALLRVRDMTMMETFNSHEREIDEWKDLIQGVHTGLRVQQVIQPAGSSMAIIEVVRG
O-methyltransferase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity . The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-CoA units to form the heptaketide monomer backbone of viriditoxin . The product of VdtA is then O-methylated on C7 by the O-methyltransferase VdtC . The O-methyl group is important for the stereoselective coupling of the monomers at the final step of viriditoxin biosynthesis . The short-chain dehydrogenase/reductase VdtF then acts as a stereospecific reductase converting the pyrone to dihydropyrone via the reduction of the C3-C4 double bond . The FAD-binding monooxygenase VdtE then converts the ketone group into a methyl-ester group to yield semi-viriditoxin . Finally, the laccase VdtB is involved in dimerization of 2 semi-viriditoxin molecules to yield the final viriditoxin . VdtB is responsible for the regioselective 6,6'-coupling of semi-viriditoxin, which yields (M)-viriditoxin and (P)-viriditoxin at a ratio of 1:2 . The non-catalytic carboxylesterase-like protein VdtD affects the stereochemistical outcome of the coupling . The highly reducing polyketide synthase VdtX is not involved in viriditoxin synthesis, but might possibly play a role in the production of additional metabolites not identified yet .
A0A443HJY8
A6M293
SYY_CLOB8
Tyrosyl-tRNA synthetase
Clostridium
MANVLDELLERGYIKQFTHEEETRKLLENEKITFYIGFDPTADSLHVGHFIAMMFMAHMQRAGHRPIALIGGGTAMVGDPSGKTDMRKMLTKEDIQHNVDSIKKQMERFIDFSDGKAILANNADWLLNLNYVDFLREVGVHFSVNRMLTAECFKQRLEKGLSFLEFNYMLMQGYDFYELNQKYNCKMQLGGDDQWSNMIAGVELVRRKAQGEAMAMTCTLLTNSQGQKMGKTVGGALWLDPAKTSPYDFYQYWRNVDDADVEKCLALLTFLPMDEVRRLGALEGAEINGAKKVLAYEITKLVHGEEEAKKAEEAATALFAGGADMSNVPTVTIAKEEIGLPILDVMASTKIIPSKKEGRRLIEQGGLSINGVKVEGVNRILTEEDFQDGAVLIKRGKKNYNKIEIK
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
A6M293
Q9RKB5
BVMO2_STRCO
Baeyer-Villiger monooxygenase
Streptomyces albidoflavus group
MAEHEQVHEHVRVAVIGSGFGGLGAAVRLRREGITDFVVLERAGSVGGTWRDNSYPGCACDVPSHLYSFSFAPNPEWPRTFSGQEHIRAYLEHVADTFGLRPHLRFDSEVKRMAWDTEQLRWEIETVRGTLTADVVVSATGPLSDPKVPDIPGLDTFPGKVFHSARWDHDYDLAGQRVAMIGTGASAIQIVPSIQPKVDRLTLFQRTPAWVMPRVDRAISGAERALHRALPATTKLRRGLLWGIRELQVQAFTKHPNELGFVEQIAKRNMGAAIKDPALRAKLTPDYRIGCKRILLSSTYYPALAKPNVDVVASGLSEVRGSTLVAADGTEAEADAIVFGTGFHVTDMPIAERVVGADGRTLAETWKGGMEALRGGTAAGFPNFMTVIGPNTGLGNSSMILMIESQLNYLADYLRQLNVLGGRTALDPRPAAVRNWNHRVQERMKRTVWNTGGCTSWYLDASGRNTTVWPGTTAEFRRETRRVDLAEYQVLRPAPAQVGAKAAEADTGADTGADAEVSA
Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters or lactones using NADPH and/or NADH as an electron donor. Thus, can convert bicyclo[3.2.0]hept-2-en-6-one into the oxidative lactone products 2-oxabicyclo[3.3.0]oct-6-en-3-one and 3-oxabicyclo[3.3.0]oct-6-en-2-one. Is also able to catalyze the sulfoxidation of methyl phenyl sulfide (thioanisole).
Q9RKB5
Q4ZWR4
RNH2_PSEU2
Ribonuclease HII
Pseudomonas syringae
MMQTGLDFTLVEDLVAGVDEVGRGPLCGAVVTAAVILDPTRPILGLNDSKKLTEARREKLYVEIQEKALCWFIARAEVEEIDQLNILHATMLAMQRAVEGLSITPRLALIDGNRCPQLSVPSAPVVKGDSKVPAIAAASILAKVSRDREMAAFELIYPGYGIGGHKGYPTPVHLEALARLGPTPIHRRSFAPVRAAHEARATIMMGGSISPSVGLLQD
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Q4ZWR4
Q9FIQ0
AGD9_ARATH
Protein ARF-GAP DOMAIN 9
Arabidopsis
MATENLTDKNVVFRKLKSKSENKVCFDCSAKNPTWASVPYGIFLCIDCSAVHRSLGVHISFVRSTNLDSWSPEQLRTMMFGGNNRAQVFFKQHGWNDGGKIEAKYTSRAADMYRQTLAKEVAKAMAEETVLPSLSSVATSQPVESSENGFTSESPKESSLKQEAAVVSSPKASQKVVASTFKKPLVSRKSGKTGGLGARKLTTKSKDNLYEQKPEEPVPVIPAASPTNDTSAAGSSFASRFEYFDDEQSGGQSGTRVLSHVAPPKSSNFFNEFGMDSAFPKKSSSSSSKAQVEETDEARKKFSNAKSISSAQFFGNQNRDADLDSKATLQKFSGSAAISSSDLFGHGPDDSNIDITASDLINRISFQAQQDMSSIANLAEETKNKLGTFASSIFSDLQDRML
GTPase-activating protein (GAP) for ADP ribosylation factor (ARF).
Q9FIQ0
C4LJU6
RL21_CORK4
50S ribosomal protein L21
Corynebacterium
MYAIVKTGGKQYKVAEGDLVKVEKIEGEPGSSVALSPVLLVDGASITSGDDLSSVAVNAEIVEHTKGPKIRNMHYRNKTGYKRRHGHRQPLTVVKITGIK
This protein binds to 23S rRNA in the presence of protein L20.
C4LJU6
B1LQ86
CYSI_ECOSM
Sulfite reductase [NADPH] hemoprotein beta-component
Escherichia
MSEKHPGPLVVEGKLTDAERMKLESNYLRGTIAEDLNDGLTGGFKGDNFLLIRFHGMYQQDDRDIRAERAEQKLEPRHAMLLRCRLPGGVITTKQWQAIDKFAGENTIYGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVLCTSNPYESQLHAEAYEWAKKISEHLLPRTRAYAEIWLDQEKVATTDEEPILGQTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGGGLSIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVETFKAEVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDNWHLTLFIENGRILDYPGRPLKTGLLEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKIAKESGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDKIDNLMAKHGVSDEHIVMRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGIIRPVLDPARDLWD
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
B1LQ86
Q6AJ47
RSMH_DESPS
rRNA (cytosine-N(4)-)-methyltransferase RsmH
Desulfotalea
MDAEKIHISVLLEETMEFLCLQPGGIYVDGTMGLGGHTSAILERTAPDGRVVAFEWDENAIKASRERLAPYGERLTLVRRNFAEIGVGLTEAGISHIDGLLIDIGLSSLQLDTGTRGFSFQRDDDLDMRMDERGEMTAATIIATCTEEQLADLFYCYGEERQARPIAAAIVAARKLEPIQTTKQLVRVVARAIPKRFHPKKIHVATKVFQALRIAVNTELENLSKIIDDAGEFLKPGSRFCIISFHSLEDRIVKRKFRENPNFKVITNKPVKAGEEELDRNYRSRSALLRVAEKV
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Q6AJ47
F4I1I4
SAU67_ARATH
Protein SMALL AUXIN UP RNA 67
Arabidopsis
MMINAKKLMKMAKKWQQRAALHRKRISFQRSNVFTSSSSTVEKGCFVVYTADKIRFAFPISYLSNSIVQELLKISEEEFGLPTEGPITLPFDSVFLEYLIKLIQRRMDGDTEKALLMSISSAKCSLQCSLLQQEQSTQQLLVL
May promote auxin-stimulated organ elongation, such as hypocotyls, stamen filaments and petals.
F4I1I4
Q9WZP5
THIC_THEMA
Thiamine biosynthesis protein ThiC
Thermotoga
MTQMEMARKGVVSDEMKKVAEYEGVDVEIVRQKLAEGRAVLPKNKLHRIERPMIVGEGFSVKVNANIGTSQGFSSLEEEKEKARVAIEYGADSLMVLSTWGDLREIRRAIVEMSPVPVGSVPIYDSAVRSYQMKKNVVDFSEKDFFDMVIAHAEDGIDFMTIHVGVTRRVLDRIKSSRRVLKIVSRGGAIIAGWMIKNNKENPFYEHFDELLDIAKDYDITLSLGDGMRPGAVVDASDAQQFEELFVMGELVERAREKGVQVMLEGPGHVPLNEVEMNVRLMKKIGKGAPIFLLGPLPTDRAMGYDHIACAIGGALAGYYGADFLCYVTPSEHISLPDVEDVREGVIASKIAAIVADVARGNKKAWELEKKMALARKNFDWETMFSLSLGKDVAKKKYEERPYPDKGCSMCGPFCAIKIAEEFS
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.
Q9WZP5
P43462
THCR_RHOER
Probable thc operon regulatory protein
Rhodococcus erythropolis group
MSEDPDRGNGTKTYLSDDIDEARAIGSDLYYPHEVRVLGDEHIFQMRMTAASFGPVTLGRLDYSTEVEIFTNELRDSYHVNIPMRGELVTGSGRARTVATPHRAAVYRCDQRTLLRGWASPYPTPVLALKIDRRALEDQLAARLGSEIVDPIVFGMDLDLDTVVGRQWLSLVEGLSHQLDSPEALALHPIVSTPMAECLMSGLLVAAEHDYRARLYEPKPALPGIVRLAVDYLEAHAQQPLTVAQVARNVGVSVRSLQVGFQNSLGTTPMRQLKIIRMQKARKDLLRADPASEGVTEIAQRWGFLHVGRFAGEYKQTFGVSPSEDLRTVPFR
Probably involved in the positive regulation of the thc operon for the degradation of the thiocarbamate herbicide EPTC.
P43462
Q6G080
RECO_BARQU
Recombination protein O
Bartonella
MKWKEQAVILGTRQYGETSIILEVMTRQHGRYMGIVKGGHSRRMAGLLQPGNFVEAEWWARLDEHLGLFRLEALDLYAARLILLPEALYALQLIVFHLRLLPERDPYPSLYDILHLFMQNFDESFVNAELLVRFEMRLLEELGFGLDLSRCAATGRQERLFYVSPKSGRAVCEEAGRPWKEKLLTLPQFLVRRAIRPVNFSDIINGFILTGFFLMRHVWEPRGIKQPSVRVNLIQLFERRFRM
Involved in DNA repair and RecF pathway recombination.
Q6G080
B7H1U9
LPXD_ACIB3
UDP-3-O-acylglucosamine N-acyltransferase
Acinetobacter calcoaceticus/baumannii complex
MKVQQYRLDELAHLVKGELIGEGSLQFSNLASLENAEVNHLTFVNGEKHLDQAKVSRAGAYIVTAALKEHLPEKDNFIIVDNPYLAFAILTHVFDKKISSTGIESTAQIHPSAVISETAYIGHYVVIGENCVVGDNTVIQSHTKLDDNVEVGKDCFIDSHVTITGGSKLRDRVRIHSSTVIGGEGFGFAPYQGKWHRIAQLGSVLIGNDVRIGSNCSIDRGALDNTILEDGVIIDNLVQIAHNVHIGSNTAIAAKCGIAGSTKIGKNCILAGACGVAGHLSIADNVTLTGMSMVTKNISEAGTYSSGTGLFENNHWKKTIVRLRQLADVPLTQITKRLDHIQAQIESLESTFNLRK
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
B7H1U9
A3DN21
PSB1_STAMF
Proteasome core protein PsmB 1
Staphylothermus
MVFIAVFNGVFAMSSLPGTVLGIKAVNGVVIAGEKRLTYDGYVLSKNTRKVHPITKHVGIGFAGLVGDAQFIIRALRMEAENYELQLGREIRVRGLAKILSLILYSYKLAPLMTEVVVGGFDEKGPQIYVLDPVGSLIEDKYVALGSGGPIALGIIEKEYREDIDVDEAEKLAVSAIREAIERDAVSGDGVDVLRITEEGYSLREYMFRRETS
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
A3DN21
P25713
MT3_HUMAN
Metallothionein-III
Homo
MDPETCPCPSGGSCTCADSCKCEGCKCTSCKKSCCSCCPAECEKCAKDCVCKGGEAAEAEAEKCSCCQ
Binds heavy metals. Contains three zinc and three copper atoms per polypeptide chain and only a negligible amount of cadmium. Inhibits survival and neurite formation of cortical neurons in vitro.
P25713
C6E6Z2
GATA_GEOSM
Glutamyl-tRNA(Gln) amidotransferase subunit A
unclassified Geobacter
MEIFDLTIHELHEKLKAKEVSSVEATRAMLDRIEAVDSQVNAYITVTPEQALVQAQDADRRIAAGEIAPLTGVPVGLKDIFVTKGIRTTCGSRILENFVPPYDGTAVAKLKEQGAVIVGKLNQDEFAMGSSNESSYFGPCRNPWDLSCTPGGSSGGSAAAIAARTATATLGTDTGGSIRQPASHCGCVGLKPTYGRVSRYGVIAYASSLDQVGPLTRDVTDSALLLGAVAGYDPMDSTSVNTPVPDYVAGLGKGVKGMKIGLPKQYFIEGLDPDVKRAMDEAIALYKSLGADIREVSLPNTEYAVATYYIIATAEASANLARYDGVRFGHRAENARGLAQMYSKSRAEGFGPEVKRRIMLGTYALSSGYYDAYYVKAQKVRTLIQQDFLNAFKEVDVLLTPIAPTPAFKIAEKLEDPLQMYLSDIFTIPVNLAGTCGISVPAGFSAAGLPIGLQLVGKPFGEQEILTAAYSFERETQWHLKKAPL
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
C6E6Z2
Q31EG9
HEMH_HYDCU
Protoheme ferro-lyase
Hydrogenovibrio
MEYKNYTAYQHGSEPAVGVLITNLGTPDAPTKEALRPYLKEFLMDPRVVEPPPARWLWKLILNLIILNTRPAKSAEAYQEVWGKYGDGSPLLDISNRQLMDIEEKVRAHFSGRVEFALGMRYGNPSIASALKSLQDRNVQRLIVVPLYPQYAGATTASTFDAVSAELQQWRWIPELRFVRNYHKHPGYIKALANSIREHQAEHGKPDLLVMSYHGIPQRYFDNGDPYPCECRATSRLVAEELGLNSDEYMVTFQSLFGKEEWVKPYTDATLKSLPDKGVKHLQVICPGFSADCLETIEEIDQENREYFEEAGGEKFSYIPALNDRDDHTTALTQIILQQTRGWPERDGFDAEADKEERALQAKLADQLEKKLSDEFGQ
Catalyzes the ferrous insertion into protoporphyrin IX.
Q31EG9
Q2JUT8
GATC_SYNJA
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
unclassified Synechococcus
MLTREEVQHVAHLARLELTEEEEIQFTEQLADILAYVEQLKELDTEGVEPTFHVLDAELPTRPDQVEPYPNIEGILANAPDRADMFFKVPRILEGED
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Q2JUT8
Q7VM65
SYS_HAEDU
Seryl-tRNA(Ser/Sec) synthetase
Haemophilus
MIDQNLLRTNLDDVANALKLKRNFILDVNQVKALEEQRKTLQVTTETLQAERNARSKNIGAAKARGENISQLLAEVDTMGNQLEIAKTELDKVQSEIRELLLTIPNLPAEEVPLGKDDSQNKEILRWGTPRQFDFEIKDHVTLGENLKGIDFPTGVKLTASRFVVMKDKIARLHRALAQFMLDLHSEQHGYMEVNVPLLVNHDTLYGTGQLPKFGEDLFHTQPLTGQDPNEVQRPYGLIPTAEVPLTNLVRDEIVDEDSLPIKLVAHTPCFRAEAGSYGRDTRGLIRMHQFEKVELVQIVAPEKSMEALEELTGQAEKILQLLHLPYRKVLLCTGDMGFGSAKTYDLEVWLPAQNTYREISSCSNMWDFQARRMSARCKAKGDKKTRLVHTLNGSGLAVGRTLVAVLENYQNADGSITIPEVLRPYMAGQEAITG
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).
Q7VM65
A0A061FKL9
BTS2_THECC
Theobromine synthase TCM_042578
Theobroma
MAMKVKDIVFMNKGDGENSYVKSAGLTLKVIAKTQPIVQKAVQSLFTGTHSTPLQVVNVADLGCALGPQPLESMSIVIESIVEKCGELGCEMPEIQFHLNDLAGNDFNTLFKGLSVVQEKYKNVSWFAMGAPGSFHGRLFPRNSMHLVHSCYSVHWLSKAPKITSEAGLPLNKGKIYMSKTSPPAVREGYLSQFEEDFSSVLRFRSPELAPDGRMVLILNGRQSADPTEKDICYLWDLLAEALSYLVSEGLIDEEKLDSFNVPYYNPSQEEVERVIDKEGSFTTEFSDTVVLEIGGKNAWSDPGLRIKGYRCFSEPILSHQFGEEVMDKLFDKAEEILAEDYKQGKEATKNISIVVVLKKKTNQTWT
Involved in the biosynthesis of theobromine.
A0A061FKL9
A0KPG1
SYA_AERHH
Alanyl-tRNA synthetase
Aeromonas
MYMSTSEIRTAFLEYFRSQGHQVVSSSSLVPHNDPTLLFTNAGMNQFKDVFLGADKRAYNRATTSQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKQDAIKFAWGFLTEVLQLPKERLLVTVYATDDEAFDIWEKEVGVPADRIVRIGDNKGAPYASDNFWAMGDTGPCGPCTEIFYDHGDHIWGGRPGSPEEDGDRFIEIWNVVFMQFNRQADGTMEPLPRPSVDTGMGLERISAIMQGVHSNYEIDIFQALIKKAAEIVGTSDLSNQSLRVIADHIRSCAFLVADGVMPSNEGRGYVLRRIIRRAVRHGRKLGATEVFFYKLAAELAAQMKDVAAELIAQLPLVERVLRIEEEQFVRTLDRGLLLLEDVLANLGDAKVIPGEVVFKLYDTYGFPADLTADVVREREIGIDEEGFKAEMEKQRARAKEASSFGVNYNEMLKLDFETPFTGYKTLTERTRVVGIYKGVDEVSGLIAGDEAVIVLEQTPFYAESGGQIGDSGTLKVDDGIFAVTDTVKAGKAIIHKGYMELGTLEKGAEVEAVVDGERRQAIALNHSVTHLLHAALRQALGEHVTQKGSLVGAERMRFDFSHFEGMTMATIRRVEELVNNQIRANHEITTQLMDLEAAKSAGAMALFGEKYEDDVRVVRMGDYSTELCGGTHAKRTGDIGFFKIIAESGIAAGVRRIEAVTGKAAIDFMHQVGEQIEEAAALVKGDQFCIADKVRQVLDKAKMMERELEQLKAKLAAQAGNDLLGQVIEIKGQKVLVAALEGADPKSLRGMLDELKNQMKSGVVLLATSGEGKVNLIAGVTNDLTGKVKAGELVNLVAQQVGGKGGGRPDMAQAGGTQPEAVPAALQSVHSWLEERL
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.
A0KPG1
B0BZK9
ATPF2_ACAM1
F-type ATPase subunit b'
Acaryochloris
MFDFNGTLPLMMFQFFLLVAVLNAVFFKPLTQAIDERDGFIRTNNTEARERLAKAKSLTEQYEQELAGTRKQSQQVLADAQAEAQKIAQTQITEAQKQVQAEVMKAQAELESQKQSAFSELEKQVDTLSQQILNKLLGSTLA
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
B0BZK9
Q2RWU7
MSRQ_RHORT
Flavocytochrome MsrQ
Rhodospirillum
MTGGSVLKDRDRLGRIAVFVACLLPLVWYGARFVGGDLGANPIEAFTRKLGEWGLIFLLASLAATPARLLWGWTFPLRRRRMVGLFAFFYVCLHLLSYIGLDQFFDWGAIWADIVKRTYITVGMAALLLLVPLAVTSTRGMVRRLGGKRWIALHRLVYPAAVLGVLHYMLMVKADLSEPLIFAGILGLLLAVRLVPAVRRRRSGRAPS
Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
Q2RWU7
Q1QMN6
EFTS_NITHX
Elongation factor Ts
Nitrobacter
MATITAAMVKDLRETTGVGMMDCKQALTENDGDMQAAIDWLRKKGLSKAAKKAGRVAAEGLIGAVTSGNKGVVVEVNSETDFVARNEQFQGLVKMVAQVALSVGADVEVIKAAKVGSATVETAISDAIATIGENMTLRRAASLEVSKGLVASYVHNAVIDGAGKMGVIVALESSGNADELAALGRQIAMHVASSNPLAIDPSGVDPAVVKREKDILADKFRQQGKPEAMIEKITESGLKTFFKEQTLLEQPFIFDDKKSVGQALKDAEGKVGAPVKLTGFVRYALGEGIEKAESDFAAEVAAAAGQG
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.
Q1QMN6
Q2RU32
NUOI_RHORT
NDH-1 subunit I
Rhodospirillum
MTSIVRTLRSLTLWELVSGMALTFRYMLKPKVTINYPFEKGYLSPRFRGEHALRRYANGEERCIACKLCEAICPAQAITIEAEPRTDGSRRTTRYDIDMTKCIYCGFCEEACPVDAIVEGPNFEFAAETREELLYNKAKLLANGDRWEPELALRLRKDAAYR
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Q2RU32
Q7U2X3
GLYA2_MYCBO
Serine hydroxymethyltransferase 2
Mycobacterium tuberculosis complex
MNTLNDSLTAFDPDIAALIDGELRRQESGLEMIASENYAPLAVMQAQGSVLTNKYAEGYPGRRYYGGCEFVDGVEQLAIDRVKALFGAEYANVQPHSGATANAATMHALLNPGDTILGLSLAHGGHLTHGMRINFSGKLYHATAYEVSKEDYLVDMDAVAEAARTHRPKMIIAGWSAYPRQLDFARFRAIADEVDAVLMVDMAHFAGLVAAGVHPSPVPHAHVVTSTTHKTLGGPRGGIILCNDPAIAKKINSAVFPGQQGGPLGHVIAAKATAFKMAAQPEFAQRQQRCLDGARILAGRLTQPDVAERGIAVLTGGTDVHLVLVDLRDAELDGQQAEDRLAAVDITVNRNAVPFDPRPPMITSGLRIGTPALAARGFSHNDFRAVADLIAAALTATNDDQLGPLRAQVQRLAARYPLYPELHRT
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Q7U2X3
Q9XH35
HOX6_ORYSI
OsHox6
Oryza sativa
MDGEEDSEWMMMDVGGKGGKGGGGGGAADRKKRFSEEQIKSLESMFATQTKLEPRQKLQLARELGLQPRQVAIWFQNKRARWKSKQLEREYSALRDDYDALLCSYESLKKEKLALIKQLEKLAEMLQEPRGKYGDNAGDDARSGGVAGMKKEEFVGAGGAATLYSSAEGGGTTTTTTAKLMPHFGSDDVDAGLFLRPSSQHHPPPPHAGAGFTSSEPAADHQSFNFHSSWPSSTEQTCSSTPWWEFESE
Probable transcription factor that binds to the DNA sequence 5'-CAAT[AT]ATTG-3'.
Q9XH35
C3JYS8
RUVA_PSEFS
Holliday junction ATP-dependent DNA helicase RuvA
Pseudomonas
MIGRLRGTLAEKQPPHLILDVNGLGYELEVPMTTLYRLPSVGEPITLHTHLVVREDAQLLYGFIGKRDRDFFRELIRLNGVGPKLALALMSSLEVDELVRAVSAQDTSALTKVPGVGKKTAERLLVELKDRFKAWEVVPSMFALVPNQPDMPAGQVASAESDAVSALISLGYKPQEASKAVSAIKDKNLSSEDMIRRALKGMI
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
C3JYS8
Q2Y9R5
SSRP_NITMU
Small protein B
Nitrosospira
MSIVQNKKAFHDYFIEEKHEAGAVLEGWEVKAIRAGRAQLKEAYVIIRNGELFLIGCHVSPLLAASTHIQPDPVRTRKLLLHAEEIKRLIGKVERAGYTLVPLDIHYKKGRIKLEIGLAKGKKQHDKRESEKQKEWERDKQRLMRPK
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.
Q2Y9R5
B6ENA3
PRMA_ALISL
Ribosomal protein L11 methyltransferase
Aliivibrio
MPWIQVKLNATSENAELISDMLVEETGALSVTFLDAKDTPIFEPLPGETRLWGETDIVALYDAETDMDLVITQLKASAVLDDNFAYKIEQLEDKDWEREWMDNFHPMKFGERLWICPSWREIPEPDAINVMLDPGLAFGTGTHATTALCLEWLESIDLTGKTVIDFGCGSGILAIAAIKLGAAKVVGIDIDPQAITASKDNATRNGVAEQLTLFLPQDQPENLVADVVVANILAAPLRELSSIITAHVKPGGALAMSGVLDTQANNVASYYSDNFTLDAIAEQQEWCRISGIKK
Methylates ribosomal protein L11.
B6ENA3
O14179
SDO1_SCHPO
Ribosome maturation protein sdo1
Schizosaccharomyces
MVISQPVGQIRLTNVSVVKYKKGGKRFEVACYKNKVTEWRNKIETDLDEVLQIHNVFNNVSKGHVASRQDLKKAFGTDDIDKIILEILQKGDFQVGEKERHHQMSSTYRDIVSHVTAMCMDPNSKRPYPASIIEKALSDCGFSVSTSKTAKSQALEAIKKLQEKNEIPIVRARMRIRIVVDVKQGKALRERLRSLADEIEEENIDDEYECIALVIPGNYKLIDELVRNETKNRGMVQVLDMSEART
Involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Together with the EF-2-like GTPase ria1, may trigger the GTP-dependent release of tif6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating tif6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export.
O14179
Q2FTV8
RLMH_METHJ
rRNA (pseudouridine-N3-)-methyltransferase RlmH
Methanospirillum
MVRIRIRAIGKIKESFIRDAIADYAKRMCSFCQVECIEYPEAPVPDTHPSTIEMACVSEGEKLCSGIDSLDYVIILDRTGKQVSSEGLAEVIRRCEIEGPYQLVFIIGGPHGLSKDCLQKGNIILSLSAMTFPHQIARLLLYEQLYRAFTIIRGLPYHR
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Q2FTV8
A1JS08
RL15_YERE8
50S ribosomal protein L15
Yersinia
MRLNTLSPAEGAKHAPKRVGRGIGSGLGKTAGRGHKGQNSRSGGGVRRGFEGGQMPLYRRLPKFGFTSRKAMITAEVRLSELALVEGDVIDLNTLKAANVVGTQIEFAKVMLSGEITRAVTLRGLRVTKGARAAIEAAGGKIEE
Binds to the 23S rRNA.
A1JS08
Q5WC42
YKUD_ALKCK
Spore protein YkuD homolog
Alkalihalobacillus
MFFHSVQQGETLSSIAADYRISLSHLIQANPTINPNQLFVGQSIVIPGLPNPNTIPYEIHVSLSQHQLTLLHNGSVVKIYPIAVGKMLTQTPTGNFVIVNKAPNPGGPFGTMWMSLSKLHYGIHGTNDPSSIGKSVSHGCIRMHNKDVEELAATVPIGTRVRIEP
Probable enzyme that may play an important role in cell wall biology.
Q5WC42
A6YGB8
PSBA_PLETE
Photosystem II Q(B) protein
Pleurastrum
MTAILERRETTSLWARFCEWVTSTENRLYIGWFGCLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAVVPTSNAIGLHFYPIWEAASLDEWLYNGGPYQLIVCHFFLGICAYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFIIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENQSANAGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVIGIWFTALGISTMAFNLNGFNFNQSVLDSQGRVLNTWADIINRANLGMEVMHERNAHNFPLDLA
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
A6YGB8
A7MJ64
CYSI_CROS8
Sulfite reductase [NADPH] hemoprotein beta-component
Cronobacter
MSEKYPGPLVVEGKLSDAERMKRESNFLRGTIAEDLHDGLTGGFNGDNFLLIRFHGMYQQDDRDIRAERAAQKLEPRHAMMLRCRLPGGIMTPQQWLAIDKFAEENTIYGSIRLTNRQTFQYHGLLKKNVKPAHQMLHSVGLDALATANDMNRNVLCTSNPVESQLHAEAYEWAKKLSEHLLPRTRAYAEIWLDQEKVATTDEEPILGATYLPRKFKTTVVVPPQNDVDLHANDMNFVAIAENGKLVGFNLLVGGGLSIEHGNKKTYARTATEFGYIPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGPDVFKAEVERRAGVTFEPVRPYEFTGRGDRIGWVKGIDDKWHLTLFIENGRILDFPDKPLKTGLKEIARIHKGDFRLTANQNLIVAGVPEGDKAKIEQIARAHGLMAGVTPQRENSMACVSFPTCPLAMAEAERFLPQFIDKVDGIMAKHGLAEEHIVLRVTGCPNGCGRAMLAELGLVGKAPGRYNLHLGGNRIGTRIPRMYRENITESEILDNIDELVGRWAQEREPGEGFGDFTVRAGIIRPVLDPARDFWE
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.
A7MJ64
Q5FW05
CTU1_XENTR
Cytoplasmic tRNA adenylyltransferase 1
Silurana
MPVNCSSCEERRAVLRRPKTGHSLCKDCFFHAFEEEIHHTIVSAKLFNPGEKVGIGASGGKDSTVLAHVLKVLNERYAYGLDLILVSVDEGISGYRDDSLETVKRNQQQYELPLKIVSYQELYGWTMDQIVKQVGLKNNCTFCGVFRRQALDRGAMMLGVNKICTGHNADDIAETVLMNFLRGDIARLRRCTSITTGSEGAIPRCKPLKYAYEKEIVLYAYFKKLDYFSTECIYSPNAYRGHARAFLKDLEAIRPSSIMDIIHSGENLSVKEDVRMPVQGTCTRCGYISSQSLCKACVLLEGLNRGLPKLGIGKHHKLHHKLLSQEPLSEQEERKLKAVDF
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated urm1 onto the uridine of tRNAs at wobble position.
Q5FW05
Q1WVI7
POTA_LIGS1
Spermidine/putrescine import ATP-binding protein PotA
Ligilactobacillus
MKQPLISFKHVVKSYDDDVQVLKDVSFDIEEGKFYTLLGPSGCGKTTILNIIAGLSDATSGDVYFDGKRINDVPANKRQVNTVFQDYALFQHLNVYDNIAFGLKIKKVPADKIKEKVTEALRMVRLDGYEDRAISEMSGGQRQRVAIARAIVLDPKVLLLDEPLSALDQKLRAEMQYELRSLQKKLGITFIFITHDQEEALAMSDEIFVLNNGNIVQSGTPVDIYDEPINHYVADFIGESNIVNGIMIKDELVEFAGQQFPCVDGGMKPNEPVEVVIRPEDLVLTSPEKGQLKVKVDTQLFRGVHYEIRCTDALGNKWLVHSTKRAVPGENIGLSFGPEDIHVMRFNESEEDFDARLDSYND
Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Q1WVI7
Q98RA6
SECA_MYCPU
Protein translocase subunit SecA
Mycoplasmopsis
MIKKLKEIPFFKSTEMKIAEKTLQQINDLEPSVVNLTDEELQNKTDEFVRRIQEGETLEHIRPEVFAVSREATKRVLKKRPYDVQMLGGIILDLGSVAEMRTGEGKTITSIAPVYLNALEKKGVIVSTVNEYLAERDAAEMGEVFSFLKMTVGVNKPSMSPEEKKQIYQCDITYSIHSELGFDYLRDNMVTNINDKVQRGLNYILLDEVDSILIDEARTPLIISGGESSSSYMYEVANQFARTLQPGDYEIDEESKTIKLVDSGIDKANKFFTLSNLYDIKNSELVHRIQNALRANFIMKKDVEYIVKDEKIELIDAFTGRIMEGRAYSEGLQQAIQAKEFLEIESETKTLATITYQNFFRMFKKLSGMTGTAKTEEQEFIDIYNMRVNPIPTNLPNIRVDDEDSIYWGTRQKLNAILKEVKQVSKTGQPILIGTSQIEQSEQLHQLFDQNGIVHTVLNAKQNEQEANIISQAGQLNAITIATNMAGRGTDIKPSKEALAVGGLYVLGTDKSESRRIDNQLRGRSGRQGDIGYSKFFLSLDDQLILRFAGADKLKEIFPKSEEALNSKQLKRHFSNAQKKIEGFNYDSRKTVLNYDDVIRQQRELMYSQRDLILVSEDLLFVIERMVFRSVDDVLKNSMFLLKNGGFDYTKLTEYINDQWLKPFDFKFEESKLSHLHEKDLAEYIFQNLMEQYMIVRQRLIDSFGEDSILYHERSILISTIDSYWQNHINSMDKLRSNSNMVQYAQKNPYQVYTQKGSKKFERLIVEIALQSSVKLFNNPSAYRQDQMEEVMIEGYTQEFIDKIPESEREYFKTLPQDLKSKIVKNLIQLEQSIAMVESNDQSQDLQSITIDILPDQNLNNSSDEAK
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Q98RA6
A0A0I9QGZ2
TKT_GEOSE
Transketolase
Geobacillus
MAHSIEELAITTIRTLSIDAIEKAKSGHPGMPMGAAPMAYTLWTKFMNHNPANPNWFNRDRFVLSAGHGSMLLYSLLHLSGYDVSMDDLKQFRQWGSKTPGHPEYGHTPGVEATTGPLGQGIAMAVGMAMAERHLAATYNRDGFEIINHYTYAICGDGDLMEGVASEAASLAGHLKLGRLIVLYDSNDISLDGELNLSFSENVAQRFQAYGWQYLRVEDGNNIEEIAKALEEARADLSRPTLIEVKTTIGYGAPNKAGTSGVHGAPLGAQEAKLTKEAYRWTFAEDFYVPEEVYAHFRATVQEPGAKKEAKWNEQLAAYEQAHPELAAQLKRAIEGKLPDGWEASLPVYEAGKSLATRSSSGEVINAIAKAVPQLFGGSADLASSNKTLIKGGGNFLPDSYEGRNVWFGVREFAMGAALNGMALHGGLKVFGGTFFVFSDYLRPAIRLAALMGLPVIYVLTHDSIAVGEDGPTHEPIEHLASLRAMPNLSVIRPADANETAAAWRLALESTDKPTALVLTRQDVPTLAATAELAYEGVKKGAYVVSPAKNGAPEALLLATGSEVGLAVKAQEALAAEGIHVSVISMPSWDRFEAQPKSYRDEVLPPAVTKRLAIEMGASLGWERYVGAEGDILAIDRFGASAPGEKIMAEYGFTVDNVVRRTKALLGK
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, likely via a covalent intermediate with the cofactor thiamine pyrophosphate. Can use L-erythrulose as donor and D-ribose-5-phosphate as acceptor substrates, forming glycolaldehyde and D-sedoheptulose-7-phosphate. For synthetic purposes, is able to use hydroxypyruvate (HPA) as donor substrate, making the reaction irreversible due to the release of carbon dioxide, and various aldehydes as acceptor substrates, which leads to the corresponding ketoses. Thus, using hydroxypyruvate as donor and three different aldehydes as acceptors, i.e. glycolaldehyde, D-glyceraldehyde and butyraldehyde, the enzyme stereoselectively forms the corresponding products L-erythrulose, D-xylulose and (3S)-1,3-dihydroxyhexan-2-one, respectively.
A0A0I9QGZ2
A4TBZ0
METK_MYCGI
Methionine adenosyltransferase
Mycolicibacterium
MSEARLFTSESVTEGHPDKICDAISDSVLDALLAGDPKSRVAVETLVTTGQVHVVGEVTTNAKEAFADITNTVRERILEIGYDHSDKGFDGETCGVNIGIGRQSPDIAQGVDTAHETRVGGAADPLDSQGAGDQGLMFGYAIADTPELMPLPIALAHRLSRKLTEVRKNGTLDYLRPDGKTQVTVQYDGTTPVRLDTVVLSTQHADGIELDSQLEPEIKQHVIDAVLTELGHQTLDTSNPRILVNPTGKFVLGGPMGDAGLTGRKIIVDTYGGWARHGGGAFSGKDPSKVDRSAAYAMRWVAKNVVAAGLAERVEVQVAYAIGKAAPVGLFVETFGSETVDPVKIEKAIGEVFDLRPGAIVRDLDLLRPIYAPTAAYGHFGRTDIELPWEQLNKVDDLKSAV
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
A4TBZ0
O57690
PLIG1_PROFL
gamma-PLI
Protobothrops
MKSLHIICLLFIFVARGNSRSCDFCHNIGADCEGFQHECSSPEDECGKVFLEISSASLSVRTVHKNCFSSSVCKLRHFDVNIGHDSYIRGRINCCEKEPCEDQSFPGLPLSQPNGYYCPGSLGLFTKDSTEFEAICKGTETKCINIVGHRYEHYPGDIAYNLKGCISSCPLLSLSNATHEENRNYLEKVECKDALQFEKQ
Inhibits basic phospholipase A2 isozymes PLA-B, BP-I and BP-II.
O57690
Q91687
ITA4_XENLA
VLA-4 subunit alpha
Xenopus
MIRDLGKVGKVSLLLDHIWTGILLYTVILTPADCYNIDESSPMLFKGSPGSLFGFSVVLHSNGEGNWIVVGAPQSSWTTKNVSNPGAILKCKIQQNPNRTCDGLELGNQNGAKCGKTCKEEQDNQWLGVSLSRQPTKDGQILACGHRWKNTHFMLSDHKLPYGVCYGIPADFRTELSKRICPCYKDHVRKFGDRYGSCQAGISTFYVEDVIIMGAPGSFYWTGSIFVYNTTENTIKSYVDLNNAVKFGSYLGYSVGAGHFRTPNGYDVIGGAPQQEQTGRVYIFTYEEKQLTILFEAGGKKLGSYFGAAVCAADLNGDGLSDLLVGAPIQSTIREEGRVFVYMNTGSGAMEELKFELSGSDLYAARFGETIANLGDIDNDGFEDVAIAAPQEGDLEGAVYIYNGREKGITPSFSQRLQGSKFGYGLRMFGQSLSNVLDIDGNGYQDVAIGAFLSDSAVLLRTRPVIIIDAFLKLPSTVNKTKFECMENGVAVVCMNVTVCFAYQGLDVPGYIVMFYNITSDVRRKSGTPARFYFVSNGSSDVISGTVEIRQKSANCKTHQAFMRKDTRDIFTPIHMESSYYLGKHIVSKRSADDFQPLQPVLQQKEGKGNVITNKVYFARYCNLPNCSADLQITGKRSFPKPFESKTYLAVGGMKSLMINITLFNGGDDAFQTVLRLRLPKGLYFVKVFDLLEKEINCAVNKEENEQTRLDCSVGHFYVDAFSKQEFSFLLDSSALIRAEEDLVINATVACANELIQDTMWNNEVSFIVPTRYEIDLNVLGTVSPFSFVFGPREDKPDDSCIMEEIEYTFNVINAGSSLVPAAKLQISLPNTFAPNDIKLFNILAVKTTVGECYFDNSTRDCETPKNTRSKIGDLFAFFSRPDKRWLYCIKDDPSCLQILCLFGDMERESKATVEVQLEISHSHLERDEAMLIQFFTTAQAGFEDSFKIINLNQDHHAYVVLEALHNLKPKKHVIYMIIGISLLLGILLFSLLTYILWKVGFFRRKYQPIGTEETSRRESWNYLNKDEKEVK
Fibronectin and V-CAM adhesion receptor.
Q91687
O08601
MTP_MOUSE
Microsomal triglyceride transfer protein large subunit
Mus
MILLAVLFLCFFSSYSASVKGHTTGLSLNNERLYKLTYSTEVFLDGGKGKPQDSVGYKISSDVDVVLLWRNPDGDDDQVIQVTITAVNVENAGQQRGEKSIFQGKSTPKIIGKDNLEALQRPMLLHLVRGKVKEFYSYENEPVGIENLKRGLASLFQMQLSSGTTNEVDISGDCKVTYQAQQDKVVKIKALDTCKIERSGFTTANQVLGVSSKATSVTTYKIEDSFVTAVLAEETRAFALNFQQTIAGKIVSKQKLELKTTEAGPRMIPGKQVAGVIKAVDSKYKAIPIVGQVLERVCKGCPSLAEHWKSIRKNLEPENLSKAEAVQSFLAFIQHLRTSRREEILQILKAEKKEVLPQLVDAVTSAQTPDSLEAILDFLDFKSDSSIILQERFLYACGFATHPDEELLRALLSKFKGSFASNDIRESVMIIIGALVRKLCQNEGCKLKAVVEAKKLILGGLEKPEKKEDTTMYLLALKNALLPEGIPLLLKYAEAGEGPVSHLATTVLQRYDVSFITDEVKKTLNRIYHQNRKVHEKTVRTTAAAVILKNPSYMDVKNILLSIGELPKEMNKYMLTVVQDILHFEMPASKMIRRVLKEMAVHNYDRFSKSGSSSAYTGYVERSPRAASTYSLDILYSGSGILRRSNLNIFQYIGKAELHGSQVVIEAQGLEGLIAATPDEGEENLDSYAGMSAILFDVQLRPVTFFNGYSDLMSKMLSASGDPVSVVKGLILLIDHSQDIQLQSGLKANMEIQGGLAIDISGSMEFSLWYRESKTRVKNRVAVVITSDVTVDASFVKAGVESRAETEAGLEFISTVQFSQYPFLVCMQMDKAEAPLRQFETKYERLSTGRGYVSRRRKESLVAGCELPLHQENSEMCNVVFPPQPESDNSGGWF
Critical for the development of natural killer T (NKT) cells . Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B .
O08601
A8FFW2
LEUD_BACP2
Isopropylmalate isomerase
Bacillus
MEPLVTHKGKAAVLNRINVDTDQIIPKQFLKRIERTGYGRFAFFDWRYLADGSPNPDFELNQPIYEGSSILIAGENFGCGSSREHAPWALDDYGFKIVIAPSFADIFHQNCFKNGMLPIRLDYDVWKTFAASYENKGYEMTVDLEKQQIEDHEGNITPFDVDPHWREMLLNGYDEISLTLLLEDDIQAFEDKRSSWLRA
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
A8FFW2
Q11GV7
UVRC_CHESB
Excinuclease ABC subunit C
unclassified Chelativorans
MNAADLGNTIISAEDSTLEWDRAGTETAATGVEVIQAVVKRLPNAPGVYRMVNTEGDVLYVGKARSLKKRVTNYAQGRGHSNRIERMIRETATMEFVVTRTETEALLLEANLIKRLRPRFNVLMRDDKSFPYILLTGNHPAPGIFKHRGARSRRGDYFGPFASAGAVGRTINSLQRAFLLRTCTDSVFESRTRPCLLYQIKRCSGPCTREISVEDYATLVKEAKDFLSGRSSTVKAEIATAMQEASQALDFERAAIYRDRLAALSHVQSHQGINPQGLEEADVFAIHQEGGQTCIQVFFFRTGQNWGNRAYFPKADPALGHGEVLGSFLAQFYDDKPCPRLILLSHPVEDQDLLAEALSARAGRKVQVSVPARGEKKDLTDHALQNAREALGRRLAETSSQARLLEGLAETFGLEAAPRRIEVYDNSHIMGTNAVGAMIVAGPEGFVKNQYRKFNIRSAEITPGDDFGMMREVMQRRFARLIKEQGLPGNGSEAEDSDASFPAWPDLILIDGGQGQMSAVRQILDDLGIADLVTAIGVAKGVDRDAGRERFFMEGRPPFTLPPRDPVLYFVQRLRDEAHRFAIGSHRARRKKEMVKNPLDEIAGIGPGRKRALLHHFGTAKAVSRAAVEDLMEVGGISESIARLIYNHFHESG
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Q11GV7
B1A971
RK14_CARPA
50S ribosomal protein L14, chloroplastic
Carica
MIQPQTHLNVADNSGARELMCIRIIGASNRRYAHIGDVIVAVIKEAVPNTPLERSEVIRAVIVRTCKELKRNNGMIIRYDDNAAVVIDQEGNPKGTRIFGAIPRELRQLNFTKIVSLAPEVL
Binds to 23S rRNA.
B1A971
Q8YI29
MIAA_BRUME
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Brucella
MSEDAVKNAILIAGPTASGKSALAIRMAKATGGFIVNTDSMQVYGVLDLLTARPSRANLAEAEHFLYGHVPPSSTYSTGKWFEDVEALLGRCELQGRVPIFVGGTGLYFRALLGGLSQTPEVSAQVRDHWRGRMEAEGAKALHAVLCVRDPAIAAALQPSDSQRIVRALEVLESTGKSLLEWQKVKGRALVDDQSAQKIVLRPDRAWLGVRIARRFSAMWAEGAIDEVRALLALDLDPALPAMKAIGVREVSAFLAETMSREEAIERSVIATRQYAKRQSTWFRNQLGEDWRVYASGEEVFQGGSFRDPQ
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).
Q8YI29
B5FPE7
MENH_SALDC
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
Salmonella
MMLHAQHMPGQPGTSSLVFLHGFSGDCREWQPVGEQFHGCSRLYIDLPGHGGSAAIPVGGFADVIRLLRATLISYNILKFWLVGYSLGGRVAMMAACQGIPGLCGLVVEGGHPGLQNEQARAERRLSDGRWAERFRHEPLTEVFHDWYQQPVFASLTAQQRQALTALRSQNNGETLAAMLEATSLAVQPDLREALNALAFPFYYLCGERDSKFRALAQEVAATCHVIRNAGHNAHRENPAGVVDSLAQILRL
Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).
B5FPE7
Q9V1U7
RL24_PYRAB
50S ribosomal protein L24
Pyrococcus
MRLNSKQPRKQRKFLYNAPLHLRQKMMAAPLSKELREKYKIRNLPVRVGDKVRIMRGDFKGHEGKVVEVDLKRYRIYVEGATLRKTNGTEVFYPIHPSNVMIIELNLDDERRKKIIERRAG
Located at the polypeptide exit tunnel on the outside of the subunit.
Q9V1U7
Q87VK6
RL9_PSESM
50S ribosomal protein L9
Pseudomonas
MQLILLEKVANLGNLGDKVNVKAGYGRNYLLPYGKATAATAANVAAFEERRAELEKLAADKKASAETRAAQLAELEVTITATAGDEGKLFGSIGTHDIADALTASGVEVAKSEVRLPNGTIRNVGEFDVAVHLHSDVEATVRVVVVAA
Binds to the 23S rRNA.
Q87VK6
P9WIS8
ODP1_MYCTO
Pyruvate dehydrogenase E1 component
Mycobacterium tuberculosis complex
MTTDFARHDLAQNSNSASEPDRVRVIREGVASYLPDIDPEETSEWLESFDTLLQRCGPSRARYLMLRLLERAGEQRVAIPALTSTDYVNTIPTELEPWFPGDEDVERRYRAWIRWNAAIMVHRAQRPGVGVGGHISTYASSAALYEVGFNHFFRGKSHPGGGDQVFIQGHASPGIYARAFLEGRLTAEQLDGFRQEHSHVGGGLPSYPHPRLMPDFWEFPTVSMGLGPLNAIYQARFNHYLHDRGIKDTSDQHVWCFLGDGEMDEPESRGLAHVGALEGLDNLTFVINCNLQRLDGPVRGNGKIIQELESFFRGAGWNVIKVVWGREWDALLHADRDGALVNLMNTTPDGDYQTYKANDGGYVRDHFFGRDPRTKALVENMSDQDIWNLKRGGHDYRKVYAAYRAAVDHKGQPTVILAKTIKGYALGKHFEGRNATHQMKKLTLEDLKEFRDTQRIPVSDAQLEENPYLPPYYHPGLNAPEIRYMLDRRRALGGFVPERRTKSKALTLPGRDIYAPLKKGSGHQEVATTMATVRTFKEVLRDKQIGPRIVPIIPDEARTFGMDSWFPSLKIYNRNGQLYTAVDADLMLAYKESEVGQILHEGINEAGSVGSFIAAGTSYATHNEPMIPIYIFYSMFGFQRTGDSFWAAADQMARGFVLGATAGRTTLTGEGLQHADGHSLLLAATNPAVVAYDPAFAYEIAYIVESGLARMCGENPENIFFYITVYNEPYVQPPEPENFDPEGVLRGIYRYHAATEQRTNKAQILASGVAMPAALRAAQMLAAEWDVAADVWSVTSWGELNRDGVAIETEKLRHPDRPAGVPYVTRALENARGPVIAVSDWMRAVPEQIRPWVPGTYLTLGTDGFGFSDTRPAARRYFNTDAESQVVAVLEALAGDGEIDPSVPVAAARQYRIDDVAAAPEQTTDPGPGA
Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
P9WIS8
Q5GTJ0
RL25_WOLTR
General stress protein CTC
unclassified Wolbachia
MTQQEMITINAELRDVTKTKAIRSLRKKGNIPAVVYGKGHNNVNLTLSAKEFTKQYKLGFLSAHVIELDISGKKEYALVRDIQWHVVKDTIQHVDFQFVDKGSEIKIDIPLSFVNESKSPGIKLGGVLNVLCRSITVKCSPDKIPQAIEVDLSGKMIGQSVHISDVKLPGGVKLAAHEEENFTVVTISAADSGVEESQVETTEE
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
Q5GTJ0
Q8DRS4
MNMA_STRMU
tRNA-specific 2-thiouridylase MnmA
Streptococcus
MTDNSKTRVVVGMSGGVDSSVTALLLKEQGYDVIGVFMKNWDDTDEFGVCTATEDYKDVAAVADQIGIPYYSVNFEKEYWDRVFEYFLAEYRAGRTPNPDVMCNKEIKFKAFLDYAMTLGADYVATGHYAQVSRDADGTVHMLRGADNNKDQTYFLSQLSQEQLQKVMFPLGHLQKPRVREIAEKAGLVTAKKKDSTGICFIGEKNFKEFLSSYLPAQKGRMMTIDGRDMGEHNGLMYYTIGQRGGMGIGGQKGGDNAPWFVVGKDLSQNILYVGQGFYHDALMSTSLTASQVHFTQNMPDKFTLNCTAKFRYRQPDSKVDVKVNGDKAEVIFDEPQRAITPGQAVVFYDGDECLGGGLIDNAYQEEKICQYI
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Q8DRS4
A8G4U2
COAD_PROM2
Pantetheine-phosphate adenylyltransferase
Prochlorococcus
MKILYPGTFDPLTNGHIDLIERAEKIFGNLVVAVLENTSKTPTFNLQRRIIQIKNSLSHLPNIEVISYSGLTVDCANELKANLILRGLRAMSDFEYELQIAHTNKSLNNDIETIFLSTNTNYSFLSSSLVKEVAKFGGEINHMVPPSVERDLKEYFK
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
A8G4U2
A6QNR1
RRP36_BOVIN
Ribosomal RNA processing protein 36 homolog
Bos
MRRASSCGGAVAGSPSEAQDGGEDDGSLRNDTSHMSFEELLELQSQVGTKAYKQLVTGSSTKKQSSRPPVQKGCVADKHRPLEMSAKVRVPFLRQVVPISKKVARDPRFDDLSGEYNPEVFDKTYQFLDDIRAREKELVKKQLKKHRSGEEHEKLQHLLQRMEQQEMAQKERKRQQELRLALKQERRAQAQQGHRPYFLKKSEQRQLVLAEKFKELKRSKKLESFLSRKRRRNAGKDRRHLPLSKE
Involved in the early processing steps of the pre-rRNA in the maturation pathway leading to the 18S rRNA.
A6QNR1
Q8VT59
CH10_STRGN
Chaperonin-10
Streptococcus
MLKPLGDRVVLKIEEKEEKVGGFVIAGNSHAATKTAAVVAVGQGVRTLTGELVAPSVKAGDKVLVESHAGVEVKDGEETYLLVSEANILAIVE
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
Q8VT59
B1KQ38
ATPF_SHEWM
F-type ATPase subunit b
Shewanella
MNINATLLGQTVAFIIFVWFCMKFVWPPLMNAIEERQKRIADGLADADRAVKDLELAQAKATDQLKDAKATANEIIEQANKRKAQIVDEAKAEADAERAKIIAQGQAEIEAERNRVKEDLRKQVATLAIAGAEKILERSIDEAAHSDIVNKLVAEL
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
B1KQ38
P13036
FECA_ECOLI
Iron(III) dicitrate transport protein FecA
Escherichia
MTPLRVFRKTTPLVNTIRLSLLPLAGLSFSAFAAQVNIAPGSLDKALNQYAAHSGFTLSVDASLTRGKQSNGLHGDYDVESGLQQLLDGSGLQVKPLGNNSWTLEPAPAPKEDALTVVGDWLGDARENDVFEHAGARDVIRREDFAKTGATTMREVLNRIPGVSAPENNGTGSHDLAMNFGIRGLNPRLASRSTVLMDGIPVPFAPYGQPQLSLAPVSLGNMDAIDVVRGGGAVRYGPQSVGGVVNFVTRAIPQDFGIEAGVEGQLSPTSSQNNPKETHNLMVGGTADNGFGTALLYSGTRGSDWREHSATRIDDLMLKSKYAPDEVHTFNSLLQYYDGEADMPGGLSRADYDADRWQSTRPYDRFWGRRKLASLGYQFQPDSQHKFNIQGFYTQTLRSGYLEQGKRITLSPRNYWVRGIEPRYSQIFMIGPSAHEVGVGYRYLNESTHEMRYYTATSSGQLPSGSSPYDRDTRSGTEAHAWYLDDKIDIGNWTITPGMRFEHIESYQNNAITGTHEEVSYNAPLPALNVLYHLTDSWNLYANTEGSFGTVQYSQIGKAVQSGNVEPEKARTWELGTRYDDGALTAEMGLFLINFNNQYDSNQTNDTVTARGKTRHTGLETQARYDLGTLTPTLDNVSIYASYAYVNAEIREKGDTYGNLVPFSPKHKGTLGVDYKPGNWTFNLNSDFQSSQFADNANTVKESADGSTGRIPGFMLWGARVAYDFGPQMADLNLAFGVKNIFDQDYFIRSYDDNNKGIYAGQPRTLYMQGSLKF
FecA is the outer membrane receptor protein in the Fe(3+) dicitrate transport system.
P13036
Q01N44
FAAH_ORYSI
N-acylethanolamine amidohydrolase
Oryza sativa
MGKPPRAMTPVEEVDLSAVRYQSPSLQAPHLTGFSLRAFVWLMESPLFGRLLTSVLKSQNNITRMLQDTVIPERPMYLPEYPPQEPEQGVLLLGDDRDPVDRVEEALHCLPPYDPSLRWPAGDKPPFLYWKIRDFAHAYRSGITTPSVVAEHIIAGVEEWSNKKPPMPMLVYFNADDLRKQAEASTKRFQQGNPISILDGIFIAIKDDIDCFPYPSKGATTFFDKIRSVEKDAVCVARLRKCGVLFIGKANMHELGLGVTGNNPNYGTARNPHSIDRYTGGSSSGPAALVSSGLCSAAIGTDGGGSVRIPSSLCGIIGLKTTYGRTDMTGALCDCGTVEVASPLAASVEDALLVYSAIAGSRPMDKLTLRPSPLCVPNLVSPDNNNILGSVKIGKYTEWFHDVSDRDISNTCEDALNLLCSSFGCQIEEIILPELEEMRTAHVVSIGTESFCDLNPHYRAGKRTEFTLDTRTSLALFGSFTSTDYVASQRIRRRIMYYHNEAFKKVDVIATPTTGITAPEIPQSSLKLGESNYVVSAYLMRFVIAGNLLGLPAITVPVGHDKQGLPIGLQLIGRPWGEASLLRVASAIEELCLKKRKRPSAFHDILNA
Catalyzes the hydrolysis of bioactive endogenous fatty acid amides to their corresponding acids. The hydrolysis of endogenous amidated lipids terminates their participation as lipid mediators in various signaling systems. Converts a wide range of N-acylethanolamines (NAEs) to their corresponding free fatty acids and ethanolamine.
Q01N44
Q03PV2
RS12_LEVBA
30S ribosomal protein S12
Levilactobacillus
MPTINQLVRKGRKSKSSKSDAPALNYGYNSFKKAQVKNPAPQKRGVATRVGTMTPKKPNSALRKYARVRLSNLIEVTAYIPGIGHNLQEHSVVLIRGGRVKDLPGVRYHIIRGALDTAGVTDRRQGRSKYGTKKPKG
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
Q03PV2
A3GHA4
LOC1_PICST
60S ribosomal subunit assembly/export protein LOC1
Scheffersomyces
MAPRQSKTAKRSKTQNKTRANESEVFSDASARNLMANQPKLTEKSKVKKLSKRVVKKQQAKIRLYGAKNGKEYREDQLDIPTLNKAIIPGVRAKKGKKGKKFVDDNDTLTLSRLVKSINDKYDVVNESKLEKSRRLEELRELKKKEIERKEQQKMDKLEGKKSELKNRASVARSNRRKNAKAAKKIEDEETDQPRKKTKSVSFA
Required for efficient assembly and nuclear export of the 60S ribosomal subunit.
A3GHA4
Q9PJW2
DAPF_CHLMU
PLP-independent amino acid racemase
Chlamydia
MGSFSPLMTYRYHLYSGTGNSFILGEFIPPLQHIVFLCQKEKVDGFLCVEPSEIADAKLTIFNSDGSEASMCGNGLRCVMAHVAQSLGLEDVSIETVRGVYQGKFFSMDRVLVDMTLLDWKKTKKTLTHVLPGMPEEVFFIDTGVPHVVVFVPDVNKVPVQEWGAFLRYHEDFRPNGVNVDFVQTKKEDTLLVYTYERGCERETLSCGTGMLASALVAADVFSLEQDFSLLVCSRSGNIVKIFSENGKVFLEGPVTLLNCSENIGEFAP
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Q9PJW2
P70714
CYSQ_AGGAC
3'-phosphoadenosine 5'-phosphate phosphatase
Aggregatibacter
MPILTTHLLQDVIEIAQQAGEHLRCFYQRSVTVRMKEDNTPVTEADLFVSQFLTEKLTALTPQIPILSEENCHIPLTERQTWRSYWLIDPLDGTQQFINRTGQFSVLVSLVKDHQPVLGVIHAPMLGSTYYAMQGFGAYKHHDGQHLKLAFHDIQADNALRIAVGSAAAAEKVRSILNKNLAYEFHICGSSGLKSTLVADGVCDCYIRLGCTGEWDTAASEILLAEMGGIIFDLNYQPLTYNKRESFVNPNFVMGITQDFPWDKIFHSN
Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
P70714
Q1GBK4
RS8_LACDA
30S ribosomal protein S8
Lactobacillus
MVLTDPIADFLTRIRNANMAKHDSVEIPASNIKKSLTEILKQEGFIRDYEVTEDGKQGVIKITLKYGPNGERVISGLKRISKPGLRNYVSADNLPKVLNGLGIAIVSTSAGILTDKEAREKNVGGEVIAYVW
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Q1GBK4
Q7NI67
MURC_GLOVI
UDP-N-acetylmuramoyl-L-alanine synthetase
Gloeobacter
MNMSLDPLVTGEVSHFVGIGGIGMSGLALVLRSQGKRVSGSDLKPNLQTQRLEASGISVFYGHRAENLQGVTRLVYSSAIQPDNPELLAARRGGVAVRHRAQVLAQLAEGYRMIGVSGTHGKTTTSSLIAVMLYHCGLDPTVVVGGEVDELGGNARLGSGPHLVAEVDESDGSLVLFSPEVAVVTNIEGDHLDHYANLEQIVEAFQQYANQARVVVGCLDCQAVRDRMPLTVSYSLDGHPQADYTADRVSFTAQGTTARVLERGEVLGELSLKLLGRHNLANALAAVAVGRYLGLSFEQIAAGLREFRGAHRRFERIGERDDIVFVDDYAHHPSEVRATLAAARLQGRRVVAVFQPHRYSRSQLLLDEFGTAFGDADAVVVTEIYAAGEANTLGVSGELVARRIAAHHPDVHFEATSDSLKRHLEAHLRPGDLALFLGAGNLNRIIPELLQRAEPPALAL
Cell wall formation.
Q7NI67
Q3B1B4
MNME_CHLL3
tRNA modification GTPase MnmE
Pelodictyon
MPASVVLQQPDIPIAAIATPVGVGALAIVRMSGKGVFGIADRAFRKKSGKAFSFEAAEGFTAHVGTLFDGEGMVDEVVALVFRAPSSFTMEDMVEFTCHGGPVVVRRVLAALLDGGCRLAEPGEFTRRAFLNGRIDLLQAEAIGEMIHARTDGAFRTAVTQMQGGLSRRLLEMREGLLQSCALLELELDFSEEDVEFQSREELRGEVIRLQTELSGLVDSYQHGRLLSEGVSTVIAGRPNAGKSTLLNKLLGEERSIVSHMPGTTRDYIEECFVYDKTMFRLTDTAGLRESEEDVEHEGIERSYRKISEADLILYMLDVSGEGFREEAVSAAALCAGHPEARMILLANKTDLVKDSALRIAALETAAGSPVVPMAARSGEGIEELKLLMASMVEGLDKLHEASVLVTSLRHYEALRNASDALHNALGLIEGGEATELIAFELRSALDYVGEITGKVVSEELLNTIFGQFCIGK
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.
Q3B1B4
Q5FP70
GLPK_GLUOX
Glycerokinase
Gluconobacter
MSKKDCILAIDQGTTSTRSIVFGKDAQALAISRREFPQHYPELGWVEHDVEDIWRDVLATARETIEEVGGPERIAALGITNQRETIVIWDRETGRAIHRALVWQDRRTAHECNLLRQQGKEAMVREKTGLLLDPYFSASKIAWLLDHVPDARRRAEAGELAAGTIDSFLLWRLTGGKRHATDITNACRTSLFNIHTQEWDEELLKLFNVPRALLPEVCDNSSDFGETEAKLFGEKIAIGGMAGDQHAAVIGQACFHEGMAKATYGTGCFMLLNTGEKPIMSNNRLLTTIAYRIGGKTFYALEGSIFVAGAGIKWLRDGLKLITHASQTDDMATRIPDSHGVYMVPAFVGLGAPHWDPDSRGLICGLTLGSTQAHIARAMLESVAYQTYDLIRAMREDGAMRTSILRIDGGMAVNDWFAQFLSSMLKAEVERPVNIETTALGAAFLAGLQVGLWKSLDEVTATWKQERVFAPKMDPAQRRIMIDGWHDAVRRTLTPSAPVAHSSVETTASQAA
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Q5FP70
O52399
ARGP_EDWI9
HTH-type transcriptional regulator ArgP
Edwardsiella
MKRPDYRTLQALDAVIRERGFERAAQKLCITQSAVSQRIKQLENLFGQPLLVRTVPPRPTEQGQRLLALLHQVELLEEEWLGNDNSSDGPLLLSLAVNADSLATWLLPALKPVLADSPLRLNLQVEDESRTQERLRRGEVVGAVSLQPQPLPSCLVDRLGALDYLFCASPAFAARYFPNGVTRSSLLKAPAVAFDHLDDMHQAFLQQNFELPPGSVPCHIVNSSEAFVQLALQGTTCCMLPHLQVERELRKGVLIDLTPGMVQRRMLYWHRFAPESRLMRRVTDALISHGRDVLRQD
Controls the transcription of genes involved in arginine and lysine metabolism.
O52399
B4UG41
FLGH_ANASK
Basal body L-ring protein
unclassified Anaeromyxobacter
MNPLTRVALAVAAFAALVLALSACGPAHVAGHVPKRRDYAVPDAAGQEAQAASAGSTWREGRAASMLYTDARALRVNDLVVVRIEEIADAKRSADTDLTRRSELNASIEAFLTSLDAPYALKGGATTGFKGLGSTARTERLTATVPAVVRKVLPNGNLFIEGHRVVLVNAEEQHFYISGVVRPIDIDQENGVKSSMVADAEIEFTGRGVLSDNQRQGWLSRLLGWFWPF
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
B4UG41
P54418
PCKA_BACSU
Phosphoenolpyruvate carboxykinase (ATP)
Bacillus
MNSVDLTADLQALLTCPNVRHNLSAAQLTEKVLSRNEGILTSTGAVRATTGAYTGRSPKDKFIVEEESTKNKIDWGPVNQPISEEAFERLYTKVVSYLKERDELFVFEGFAGADEKYRLPITVVNEFAWHNLFARQLFIRPEGNDKKTVEQPFTILSAPHFKADPKTDGTHSETFIIVSFEKRTILIGGTEYAGEMKKSIFSIMNFLLPERDILSMHCSANVGEKGDVALFFGLSGTGKTTLSADADRKLIGDDEHGWSDTGVFNIEGGCYAKCIHLSEEKEPQIFNAIRFGSVLENVVVDEDTREANYDDSFYTENTRAAYPIHMINNIVTPSMAGHPSAIVFLTADAFGVLPPISKLTKEQAMYHFLSGYTSKLAGTERGVTSPETTFSTCFGSPFLPLPAHVYAEMLGKKIDEHGADVFLVNTGWTGGGYGTGERMKLSYTRAMVKAAIEGKLEDAEMITDDIFGLHIPAHVPGVPDHILQPENTWTNKEEYKEKAVYLANEFKENFKKFAHTDAIAQAGGPLV
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
P54418
P04760
ACHG_MOUSE
Acetylcholine receptor subunit gamma
Mus
MQGGQRPHLLLLLLAVCLGAQSRNQEERLLADLMRNYDPHLRPAERDSDVVNVSLKLTLTNLISLNEREEALTTNVWIEMQWCDYRLRWDPKDYEGLWILRVPSTMVWRPDIVLENNVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSSCSISVTYFPFDWQNCSLIFQSQTYSTSEINLQLSQEDGQAIEWIFIDPEAFTENGEWAIRHRPAKMLLDSVAPAEEAGHQKVVFYLLIQRKPLFYVINIIAPCVLISSVAILIYFLPAKAGGQKCTVATNVLLAQTVFLFLVAKKVPETSQAVPLISKYLTFLMVVTILIVVNSVVVLNVSLRSPHTHSMARGVRKLFLRLLPQLLRMHVRPLAPAAVQDARFRLQNGSSSGWPIMAREEGDLCLPRSELLFRQRQRNGLVQAVLEKLENGPEVRQSQEFCGSLKQASPAIQACVDACNLMARARRQQSHFDSGNEEWLLVGRVLDRVCFLAMLSLFICGTAGIFLMAHYNQVPDLPFPGDPRPYLPLPD
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
P04760
Q6CRX0
BOS1_KLULA
Protein transport protein BOS1
Kluyveromyces
MNALYNHAIKQRSLLNKDLGKFEKELVTAPISLQGAIATTLVSFEKTLHQYKEQYKQYQINSSDDNDETKLKYETRLQTLTQDYEDAKEKFTELKQKYSEINARDQLFNQQASMVEETVMNKRNINAPPQTSFGIGALDQNSERMTINSAAGLPLYEGLRKENSIFERGNAHLDRILQMGQESLEDIMEQNRVLQRLQSQMTKSLHVLGVSNETIEKINKRLFKDKLIFYIGLLLLILGIYFVLKWFG
SNARE required for protein transport between the ER and the Golgi complex.
Q6CRX0
Q6C443
OXR1_YARLI
Oxidation resistance protein 1
Yarrowia
MDSSDRPSLRQRLSNWGRTDTKPAATDLTAPPNDPSENMELPPLPPVELLGYSHSTRTKIMTTELADEIRNLVPERIKLYRSWQLQYSLEQHGTSLTTLYHRNIPPHGDTARNGFVLAVKNSRGQVFGAYTDQHYHVGGKKFYGNGDCFLWKVKNADSFQAFPYTGENNFVVYCNPHFLSLGGGDGKYGLWLDDALKTGVTYPCATFGNEPLGDEKFDVVAVEVWRVGE
May be involved in protection from oxidative damage.
Q6C443
B1I9B4
TGT_STRPI
tRNA-guanine transglycosylase
Streptococcus
MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFPGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCKNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFREYFVEKYGYNKSGRNF
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).
B1I9B4
Q5QVT8
EFP_IDILO
Elongation factor P
Idiomarina
MANYSTSEFKGGLKIMQDGEPCSIVENEMVKPGKGQAFNRVKIRKLISGKVVEKTFKSGESVEGADVIELELSYLYNDGEFWHFMNNETFEQVPADEKAVGEAEKWLVEQDVCTLTLWEGKPINVQPPNFVELEITETDPGLKGDTAGTGGKPATLSTGAVVRVPLFVQIGEVIKVDTRSGEYVSRVQK
Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation.
Q5QVT8
Q3SWY3
IMDH2_BOVIN
IMPDH-II
Bos
MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPRDRVRDVFEAKARHGFCGIPITDTGRMGSHLVGIISSRDIDFLKEEEHDRLLGEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNENDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLSQAGVDVVVLDSSQGNSIFQINMIKYIKEKYPSIQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.
Q3SWY3
B2I3B3
IXTPA_ACIBC
Nucleoside-triphosphate pyrophosphatase
Acinetobacter calcoaceticus/baumannii complex
MSTPHWFDQGSLVLASNNKGKVAEFEKLFEQLKLPVEIIPQGHLNIPDAIEDGLSFIENAIIKARHASKISGKPAMADDSGICVPVLGGAPGIYSARYAGEHGDDAANNAKLLNDLLPFRKNGEAIEGMFVCVLALVTHAEDPLPQIFQGIWHGEILEAPRGENGFGYDPLFWLPELQVSSAELSKEEKNKISHRGQAMQLFRESLQK
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
B2I3B3
Q6D7W3
MENH_PECAS
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
Pectobacterium
MTHGAVAPIQPWLVCLHGLFGSGEDWSPVLPFFRDWPMLLVDLPGHGASRAITTADFAEVSRQLTATLLEQGIERYWLLGYSLGGRIAMYHACEGHHDGMLGLLVEGGHPGLATPEQRTERIHHDARWAQRFRQDPLPEALQDWYQQAVFADIDSVQREQLIARRSANHGASVAAMLEATSLGRQPFLAARLQHLSIPFIYLCGASDVKFQTLAAQYGLPLLSVALAGHNAHQANPAAYAERVRTFLSHPVKD
Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).
Q6D7W3
B9MRY0
ARGR_CALBD
Arginine repressor
Caldicellulosiruptor
MKSERQQKILEIIQNEDIETQEELVERLKALGYDVTQATVSRDIKELRLTKVLTETGKYKYAVLSGPEANITEKLIKVFSESIVKYDTADNLVIIKTITGAAQGAAAAIDSLSWPEVVGTIAGDDTIFIATKGSAAADKIVERIKAIISQGE
Regulates arginine biosynthesis genes.
B9MRY0
P0DJ80
VKT22_CYRSC
Kunitz-type serine protease inhibitor HWTX-XI-IS22
Cyriopagopus
MGTARFLSAVLLLSVPLMVTFPALLSAEYHDGRVDICSLPSDSGDCLRFFEMWYFDGTTCTKFVYGGYGGNDNRFPTEKACMKRCAKA
Dual-function toxin that inhibits both serine proteases and voltage-gated potassium channels (Kv).
P0DJ80
B6JNM7
PSD_HELP2
Phosphatidylserine decarboxylase beta chain
Helicobacter
MVALSNALSRVFGSVAGYKFPSFIQKGINALYAKIFKVDLSEFEPLENYKSLNALFTRSLKKERPFDKAPNICIAPCDALITECAFLDNDSALQIKGMPYKAHELVGEINPLSPSFFYVNFYLSPKDYHHYHAPCDLEILETRYFAGKLLPVNKPSLHKNKNLFVGNERVALVTKDIQGNRLYFVAVGALNVGKMRFNFDKNIQTNAKARFTQTYSYNPPIKVKKGDNLGNFEMGSTIVLFVQNTAFKDLKEKSVKFGESIGEFHAN
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
B6JNM7
O86062
NUDC_PSEAE
NADH pyrophosphatase
Pseudomonas
MAGEFRWQAGRPATAQVGGWVLAHCQQRFLQDDNGLLFPREWLKRQELPLLAEHGVGHWQGEPVYVLELDEPIELPGMAWAPLRQFMLHGDFDQFCMLGYASQIGIWARHNRFCGNCGTRMQAQDHERVMQCPQCGLHQYPRLSPSMIVLVTRGDEVLLARSPRFVPGVYSTLAGFVEAGESVEQCVVREVREEVGVEVANLEYIGSQNWPFPHSLMLGFHAEYVSGEIVPQEDEIEDAQWFSLDALPPLPAQRSIARHLIDLYLARRSGAAEPVLPG
mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.
O86062
Q8EJW1
PRPB_SHEON
(2R,3S)-2-methylisocitrate lyase
Shewanella
MTQSAGLRFRQALANSKPLQIVGTTNAYFALMAEQTGFQALYLSGAGVANASYGLPDLGMTSMNDVLIDAGRITSATQLPLLVDIDTGWGGAFNIARTIKEFEKIGVAAVHMEDQVSQKRCGHRPNKAVVSTEEMVDRIKAAVDARTDPNFVIMARTDAVAVEGLEAGIERAKAYIAAGADMIFAEALTELDQYRHFKAQVKAPILANMTEFGQTQLFNKEELAQAGADMVLYPLGTFRAANQAALKVMQALMNDGHQRNVLDTMQTRADLYKYLGYHAFEDKLDQLFSQDK
Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-carbanion intermediate.
Q8EJW1
A7X347
DTD_STAA1
Gly-tRNA(Ala) deacylase
Staphylococcus
MKVVVQRVKEASVTNDTLNNQIKKGYCLLVGIGQNSTEQDADVIAKKIANARLFEDDNNKLNFNIQQMNGEILSVSQFTLYADVKKGNRPGFSNSKNPDQAVKIYEYFNDALRAYGLTVKTGEFGTHMNVSINNDGPVTIIYESQDGKIQ
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
A7X347
Q0I9S4
ISPE_SYNS3
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
unclassified Synechococcus
MTATVRVTAPAKINLHLEVLGQRSDGFHELAMVMQSIDLADQLDCSNRADGLIQLSCDQPGLSCGNDNLVFRAAALLRQRSGFHELGAQIHLRKRIPIGAGLAGGSSDGAAALLALNTLWGLGHTHDHLCAMAAELGSDMPFCLAGGIQLCFGRGECLESVPAAEQSLGVVLVKNPTVSVSTPWAYGECRRLKGDHYLSDEVAFAQRRQDLRAASWLNPLRAAEPPPLRNDLQDVVEPQTASVQMALRLLQDLPGQLRTAMSGSGPSCFALFPNRLDADQALDVARDSFAQAGFDAWSCSFVGHGAKLMP
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
Q0I9S4
A1S6N9
RUVA_SHEAM
Holliday junction ATP-dependent DNA helicase RuvA
Shewanella
MIGRLKGILVEKHAPEVLIDVGGVGYELQMPLTSFYELPLPGAEVIVYTHFVVREDAQLLYGFIHKEERSLFRLLIKANGVGPKLALTILSGMTAKEFIGCLERDDIATLIKLPGVGKKTAERLLVEMRDKLKSLMEASMGAEREFVLKSNFTPAPVAATVEEDAIAALLSLGYKPQQASKAVSSAFQEGMDPEQLIKAALKSML
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
A1S6N9
Q03156
ALBU2_SALSA
Albumin 2
Salmo
MQWLSVCSLLVLLSVLSRSQAQNQICTIFTEAKEDGFKSLILVGLAQNLPDSTLGDLVPLIAEALAMGVKCCSDTPPEDCERDVADLFQSAVCSSETLVEKNDLKMCCEKTAAERTHCFVDHKAKIPRDLSLKAELPAADQCEDFKKDHKAFVGRFIFKFSKSNPMLPPHVVLAIAKGYGEVLTTCCGEAEAQTCFDTKKATFQHAIAKRVAELKSLCIVHKKYGDRVVKAKKLVQYSQKMPQASFQEMAGMVDKIVATVAPCCSGDMVTCMKERKTLVDEVCADESVLSRAAGLSACCKEDAVHRGSCVEAMKPDPKPDGLSEHYDVHADIAAVCQTFTKTPDVAMGKLVYEISVRHPESSQQVILRFAKEAEQALLQCCDMEDHAECVKTALAGSDIDKKITDETDYYKKMCAAEAAVSDDNFEKSMMVYYTRIMPQASFDQLHMVSETVHDVLHACCKDEPGHFVLPCAEEKLTDAIDATCDDYDPSSINPHIAHCCNQSYSMRRHCILAIQPDTEFTPPELDASSFHMGPELCTKDSKDLLLSGKKLLYGVVRHKTTITEDHLKTISTKYHTMKDKCCAAEDQAACFTEEAPKLVSESAELVKV
Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood.
Q03156
Q8K348
ACV1C_MOUSE
Activin receptor-like kinase 7
Mus
MTPARGSALSLALLLVALAADLAAGLKCVCLLCDSSNFTCQTEGACWASVMLTNGKEQVIKSCVSLPELNAQVFCHSSNNVTKTECCFTDFCNNITLHLPTASPNAPRLGPTELTVVITVPVCLLSIAAMLTIWACQDRQCTYRKTKRHNVEEALAEYSLVNAGKTLKDLIYDATASGSGSGLPLLVQRTIARTIVLQEIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSLYDYLNRNIVTVAGMVKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCDTCAIADLGLAVKHDSIMNTIDIPQNPKVGTKRYMAPEMLDDTMNLSIFESFKRADIYSVGLVYWEIARRCSVGGVVEEYQLPYYDMVPSDPSIEEMRKVVCDQKLRPNLPNQWQSCEALRVMGRIMRECWYANGAARLTALRVKKTISQLCVKEDCKA
Serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in cell differentiation, growth arrest and apoptosis.
Q8K348
Q4R836
F118B_MACFA
Protein FAM118B
Macaca
MASTGSQASDIDEIFGFFSDGAPPTKKPRKLLPSLKTKKPRELVLVIGTGISAAVAPQVPALKSWKGLIQALLDAAIDFDLLEDEESKKFQKCLHEDKNLVHVAHDLIQKLSPRTSNVRSTFFKDCLYEVFDDLESKMEDSGKQLLQSVLHLMENGALVLTTNFDNLLELYAADQGKQLESLDLTDEKKVLEWAQEKRKLSVLHIHGVYTNPSGIVLHPAGYQNVLRNTEVMREIQKLYENKSFLFLGCGWTVDDTTFQALFLEAVKHKSDLEHFMLVRRGDVDEFKKLRENMLDKGIKVISYGNDYADLPEYFKRLTCEISTRGRSGMVREGQLNGSSAAHSEIRGCST
May play a role in Cajal bodies formation.
Q4R836