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2.75k
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5.51k
AlphaFoldDB
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B1GZJ8
PANB_ENDTX
Ketopantoate hydroxymethyltransferase
Endomicrobium
MKKKTVLTILKKKQSGEKITMLTCYDYVTAKLISSQDIDVLLVGDSLGNVKLGYENTLSVTVDDMIYHTKSVKRGNDGALLITDMPFMSYEITVEDAVKNAARIVKEGGAEAVKVEGGIEIVDRVKAISDAKVPIVGHLGLTPQSINKFGGFKVQGRTEEERGRLIADAEALEKTGAFAVVLEAVPEQLAKEVTERLKIPTIGIGSGRYCDGQVLVVDDMLGMFTDFTPKFVKKYAEIGEMVRTAVKNYIDEVKKGQFPREENTYK
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
B1GZJ8
Q97EI0
RL23_CLOAB
50S ribosomal protein L23
Clostridium
MYTNSHDIIRKPVITEKSMAEMADKKYTFIVDPHANKVQIKKAIEEVFGVKVEKVNTSNILGKTKRVGVHVGKRADYKKAIVKLTEDSKAIEFFEGMQ
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
Q97EI0
C1D1Q9
TILS_DEIDV
tRNA(Ile)-lysidine synthetase
Deinococcus
MSTLLAPLHPYAGRVVVVGVSGGADSVALLRALVQAEARPVVAHLDHALRPNSAEDAQWVHDLAEQLGAAHTSTRVDVAAVAARRGWNVEDAARRVRYEVLSRAARQHGAHTVMTAHTRRDQAETVLMGLLRGEAVLTGIPAVRGRVRRPWLDVPRSEIEAYLKALGQEWREDPTNADVTYTRAWLRTEVMPVLAARFPGVEAALGRVAKLAQQDDEALRDLAAALTPHAPRDRVPLAVLRRRVTQELKSAGLQFHVGQVDQLAEAQRTGETRHVTLLGGRGVTVTGGALHLAARAWPLPSFSWPEDWTLRTRQPGDRITLPGGTRKVSDVLTDLKIPRDQRDDVPLLVSAQGVKWIGVEPNIWAKGARAVVGQPADLLDTAMGEALGLAREAALAQEVPVGAVVLGPGGRIIGSGRNTSRADSDMTRHAELAALRAATAELGTAYLTGCTLVVTLEPCPMCLGAALEARVERIVYGASNPKAGALGGVSDLLSSHWGHVPAVTGGVRAQDAARVLRDSFQELRQRRLKSPDV
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
C1D1Q9
A5G7U4
LEUC_GEOUR
Isopropylmalate isomerase
Geotalea
MGMTIAEKIFAAHLVDEPFHGTRVLKLDVVMCHEITTPIAIADLIARGKDRVFDTSRIKAVIDHVTPSKDSKTATQAKMLRDWARRHNIKDFFDIGANGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFREPKTIRINLNGKLPKGVYAKDAILHVIGRLGVNGATDRVIEFRGAVVDAMTMESRMTLCNMAIEAGGTSGICMPDSVTVDYLWPFISEDYASKEAALVEFKKWWSDEDAVYERVLDLDISGLEPVVTFGYKPDQVKTITEMAGTPVDQVYLGSCTNGRLEDLRVAAEILKGKKIAPTVRAILSPATPKVYSDALHEGLIDIFMEAGFCVTNPTCGACLGMSNGVLAEGEVCASTTNRNFMGRMGKGGMVHLMSPATSAATAIEGKMADPRKYL
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
A5G7U4
Q9UWN5
TPIS_METFV
Triose-phosphate isomerase
Methanothermus
MDRPIIVLNFKTYKESTGENALKLAKKCEQVSEEYGVKIIVAPQHMDLRYVSENVNIPVIAQHIDPIDAGGHTGSVLLECAKEAGAKGSLVNHSEKRMKLADISKVVKKLSENDMISIVCTNNVETSAAAAALSPDFVAVEPPELIGSGIPVSKAKPEVVENTVEAVKTVNPDVRVLCGAGISSGEDVKKAVELGTEGVLLASGVILAKDQKKALEELITEM
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
Q9UWN5
P9WJY6
NARK2_MYCTO
Probable nitrate/nitrite transporter NarK2
Mycobacterium tuberculosis complex
MRGQAANLVLATWISVVNFWAWNLIGPLSTSYARDMSLSSAEASLLVATPILVGALGRIVTGPLTDRFGGRAMLIAVTLASILPVLAVGVAATMGSYALLVFFGLFLGVAGTIFAVGIPFANNWYQPARRGFSTGVFGMGMVGTALSAFFTPRFVRWFGLFTTHAIVAAALASTAVVAMVVLRDAPYFRPNADPVLPRLKAAARLPVTWEMSFLYAIVFGGFVAFSNYLPTYITTIYGFSTVDAGARTAGFALAAVLARPVGGWLSDRIAPRHVVLASLAGTALLAFAAALQPPPEVWSAATFITLAVCLGVGTGGVFAWVARRAPAASVGSVTGIVAAAGGLGGYFPPLVMGATYDPVDNDYTVGLLLLVATALVACTYTALHAREPVSEEASR
Involved in excretion of nitrite produced by the dissimilatory reduction of nitrate.
P9WJY6
A7GSN8
GCST_BACCN
Glycine cleavage system T protein
Bacillus cereus group
MITLQRTPLFDVYAKYGGKTIDFGGWELPVQFSSIKEEHEAVRTAAGLFDVSHMGEVEVTGADSLAFLQRVVTNDVSTLKVGGAQYTAMCYENGGTVDDLLIYKRGEEDYLLVINASNIEKDYEWLASHVIGDTKVVNVSNEIAQLAIQGPKAEGILQKVVSEDLKEIKFFKFKNDVLVDGIPALVSRTGYTGEDGFEIYCKSEDAIKIWEKLLEVGEEDSLKPCGLGARDTLRFEATLPLYGQELSKDITPIEAGIGFAVKTNKEADFFGKEVLKEYKENGAPRKLVGIEVIERGIPRTHYPVYVGEEKIGEVTSGTQSPTLKKSIGLALIDVKYAAIDTEVEIEIRKKRVKAVVVPTPFYKRSK
The glycine cleavage system catalyzes the degradation of glycine.
A7GSN8
Q04U69
RRF_LEPBJ
Ribosome-releasing factor
Leptospira
MASEEIISGMKTKMDKTIDLVKKDFGTVRTGRANPSLVEDIRVDYYGTLTPINQLGNISVPEPRMLVISPYDKGIMKDIEKAIQASGLGLQPSNDGVVIRIIIPELTGERRKELAKIVKSKSEEKKVAIRNIRRDAMEDLKKHTEGLSQDEIKTIQDRIQKTTDSYIDKISALTAEKEKEITTI
Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
Q04U69
Q738X4
AZOR3_BACC1
FMN-dependent NADH-azoreductase 3
Bacillus cereus group
MTKVLFITANPNSAEGSFGMAVGEAFIEAYKNEHPQDEVVTIDLFNTTVPAIDADVFAAWGKFAAGEGFEALTEAQQQKVAAMNTNLETFMHADRYVFVTPMWNFSYPPVVKAYLDNLAIAGKTFKYTENGPVGLLEGKKALHIQATGGVYSEGAYAAVDFGRNHLKTVLGFIGVNETEYIAVEGMNANPEKAQEIKEAAIANARELAKRF
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
Q738X4
P35684
RL3_ORYSJ
60S ribosomal protein L3
Oryza sativa
MSHRKFEHPRHGSLGFLPRKRSSRHRGKVKSFPKDDVSKPCHLTSFVGYKAGMTHIVREVEKPGSKLHKKETCEAVTIIETPPLVIVGLVAYVKTPRGLRSLNSVWAQHLSEEVRRRFYKNWCKSKKKAFTKYALKYDSDAGKKEIQMQLEKMKKYASIVRVIAHTQIRKMKGLKQKKAHLMEIQINGGTIADKVDYGYKFFEKEIPVDAVFQKDEMIDIIGVTKGKGYEGVVTRWGVTRLPRKTHRGLRKVACIGAWHPARVSYTVARAGQNGYHHRTEMNKKVYKIGKSGQESHAACTEFDRTEKDITPMGGFPHYGVVKGDYLMIKGCCVGPKKRVVTLRQSLLKQTSRLALEEIKLKFIDTSSKFGHGRFQTTDEKQRFFGKLKA
The L3 protein is a component of the large subunit of cytoplasmic ribosomes.
P35684
B6YX10
AROD_THEON
Type I dehydroquinase
Thermococcus
MIVGVVLAKNAQKAVEKIKSGEADLYEVRLDHFSSFDGLEELEPFAPNLIFTFRSYEEGGRREASDEERLRVYKRVLELYPAYVDVGLNSGIAERVVKEAREKRVGVVLSYHNFEETPDFWELLGVVKAMEALEPDVMKIVTMARSLGDNLRIARLYEGRENVVAFCMGSLGRLSRLISALLAPFTYASLDEEAAPGQLTVEELRRAIEVVGDGR
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
B6YX10
Q633N8
RNH3_BACCZ
Ribonuclease HIII
Bacillus cereus group
MSNSIVIQTNSTVIEDMKQQYKHSLSPKTPQGGIFMAKVPSCTITAYKSGKVMFQGGRAEAEAARWQTGSQTPKTAVKKAVDSHRYTPPASIGTMSIVGSDEVGTGDFFGPMTVVAVYVDAKQIPLLKELGVKDSKNLNDEQITAIAKQLLHVVPYSSLVLHNEKYNELFDKGNNQGKLKALLHNKAITNLLAKLAPTKPEGVLIDQFTQPDTYYKYLAKQKQVQRENVYFATKGESVHLAVAAASILARYSFVKQFNELSKKAGMPLPKGAGKQVDIAAAKLIQKLGKERLPEFVKLHFANTEKAFRLLK
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Q633N8
B5FJD5
ASTB_SALDC
N-succinylarginine dihydrolase
Salmonella
MTAHEVNFDGLVGLTHHYAGLSFGNEASTRHRFQMSNPRLAVKQGLLKMKALADAGFPQAVIPPHERPFIPALRQLGFTGSDEQILDKVARQAPRWLSSVSSASPMWVANAATVCPSADALDGKVHLTVANLNNKFHRALEAPVTEALLRAIFRDESQFSVHSALPQVALLGDEGAANHNRLGGEYGSAGVQLFVYGREEENEIRPARYPARQSREASEAVARLNQVNPQQVIFAQQNPEVIDQGVFHNDVIAVSNRQVLFCHEAAFARQKVLINQLRTRVDGFMAIEVPAGEVSVSDAVATYLFNSQLLSRDDGSMLLVLPRECQDHVGVWRYLNKLVAEDNPISAMQVFDLRESMANGGGPACLRLRVVLTEEERRAVNPAVMMNDALFTALNAWADRYYRDRLTAADLADPLLLREGREALDVLTRLLDLGSVYPFQQTGAADG
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
B5FJD5
B0UUS0
RNFA_HISS2
Rnf electron transport complex subunit A
Histophilus
MIDYILLIISTALINNFVLVKFLGLCPFMGVSKKIETAIGMGLATMFVLTVASLCAYLVERYLLTPLHANFLRTLIFILVIAVVVQFTEMVIHKTSPTLYRLLGIFLPLITTNCAVLGVALLNINLAHNLTQSVIYGFSASLGFSLVLVLFAALRERLTAADIPLPFRGASIALITAGLMSLAFMGFSGLVRV
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
B0UUS0
B2ULE2
MUTL_AKKM8
DNA mismatch repair protein MutL
Akkermansia
MPSIHVMSPTLASQVAAGEVVERPASVVKELVENSLDAGAKFVRVEIRRGGVGMIKVTDDGSGMSRADAELCTKRHATSKLSSLEELFEITHLGFRGEALPSIASVSRFKLCTRQQQDLEGWEIRIDGGLEHEPRSSGVSPGTAIEVADLFYNTPARRKFLKSAETEASHVEHQIRLHALAYPQVRFAYKRDDQLVFDLPATADLRVRISALTDAATAAALIPIETTIGPGISITGFLLPLSEARRTRKGQYVFMNTRPVEDQLINRAIRDGYGGFPTGLHPALFLYMEVEPALVDVNVHPAKKEVRFRRSADVVNTIVEAIANTLQKHARQEIHAAAAPEPERTLPPAHSTTAPYGEIPARSTNPGSAFPAAARPAPASSAAQPPLSSSAKQSHGAVPPPTLRAIPLKQVPATQGKLDFHRQEDEETARNAHENAALERDASAGFSYLGTLRQQFALFETPEGLVLMHPKAARERIIFERLRARREAPMPSQQLLDPVVLDLDPRDFAVIRQFAPHFDQAGMAVTPFGQNTIRIESIPALLELENARAFLLELVDRLTQSEFSRNAKRVAYETFIGEFARKSAWRERISPHRAPAILKDLLACEVPYCTPGGKPTLVNYSVPEIKRKFGLQA
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
B2ULE2
B6JB87
LEU1_AFIC5
Alpha-isopropylmalate synthase
Afipia
MTSPSTSDKDRVVIFDTTLRDGEQCPGATMTHEEKLEVAEMLDTMGVDIIEAGFPIASVGDFEAVAEIAKRANNAVIAGLARAIPADIVRAGEAVRHAKRGRIHTFVSTSPIHLAHQMRKSEEDVLGIITATVAQARNLVDDVEWSAMDSTRTPIDYLCRCVETAIAAGATTINLPDTVGYAVPEEYRRMFKVIRERVPNADKAVFSVHCHDDLGLAVANSLAGVEGGARQIECTINGIGERAGNAALEEVVMAIKTRGDVMPYWCNVESTTLTRASKVVSAATSFPVQYNKAIVGRNAFAHESGIHQDGVLKNAQTYEIMTPESVGVKQTSLVMGKHSGRHAFQHKLRELGYELADNQLQDAFVRFKALADRKKDIYDEDIEALVDQELAQTHDRLRLVSLTVIAGTHGPQRATMKVEVDGKVRIDEAEGNGPVDAVFNAVKTLVPHEAKLELYQVHAVTAGTDAQAEVSVRLSQDGRSVTARSSDPDTLVASAKAYLSALNKIISRQQREAPVAAAS
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
B6JB87
Q03EL0
ATPF_PEDPA
F-type ATPase subunit b
Pediococcus
MFSHIIVGAAHGSTLYVGDMLFYAILFIVLMALIAKFAWGPVNAMLKERADRISNDIDSAEQSRIEAEKLAKQRKEALDNSHAEATSIINNAKDSGAKERELIIGNAQNEAKSLKDKAKQDIEQERADALKSAQDDIASLSIEIASKVIKKELDENSQKDLIDSYIEGLGDSK
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Q03EL0
Q4ZJM7
OTOL1_MOUSE
Otolin-1
Mus
MWIFSSLCAVLTILAMDDVATEAKTTPYTKFTKKSEGKEMLKGLKPSSGFFLDGEETVHTETAAMAEPTTGSPALAMAESTAGPSASATTRLLPFESFSLDTTGFVLNCCHCCSFVTGQKGEPGKMGKQGPKGETGDTGSPGHPGTTGPQGPKGQKGEKGLKGDRGDQGAGGIPGYPGKPGEQGALGPKGDKGTIGPAGTKGQKGSKGELCGNGTKGEKGDPGASGAHGFIGEPGAKGEKGGVGEKGYRGDLGERGEKGQKGEKGMEGEKGSRGDVGSEGKRGSDGLPGLRGDSGPKGEKGEIGSPGFTGPAGPKGELGSKGVRGPTGKKGSRGVKGSKGEATQVPQSAFSALLSKPFPPPNVPIKFDKILSNDQGDYSPVTGKFNCSVPGTYIFSYHVTVRGRPARISLVARNRKQFKSRETLYGQQVDQASLLLILKLSAGDQVWLEVSKDWNGLYVGPEDDSIFSGFLLYPEETFSKSP
Collagen-like protein specifically expressed in the inner ear, which provides an organic scaffold for otoconia, a calcium carbonate structure in the saccule and utricle of the ear . Acts as a scaffold for biomineralization: sequesters calcium and forms interconnecting fibrils between otoconia that are incorporated into the calcium crystal structure . Together with OC90, modulates calcite crystal morphology and growth kinetics .
Q4ZJM7
Q710D6
COX5B_VULVU
fSP8
Vulpes
MKRGSAALEVRELKMQTPTASCVLSTQRANFAKGGVPTDDEQATGLEREVMMAARKGLDPYNILAPKAAAGTKEDPNLVPSITNKRIVGCICEEDNSTVIWFWLHKGEAQRCPSCGTHYKLVPHQLAH
This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport.
Q710D6
Q081N3
CMOA_SHEFN
Carboxy-S-adenosyl-L-methionine synthase
Shewanella
MNSQQDTIYAHVTDQITDFQFDQRVAGVFNDMIRRSVPGYAQIINTIGDFANRFVTPQSNIYDLGSSLGSATLSIRRQIEGRGCQIYAVDNSQSMIERCTENLAAYVSDIKVNLLCADIRDIDIKNASMVVLNFTLQFLPTHDRDALIKRIYDGMLPGGILVISEKLFFEDNHIQQLLDEQHLDFKRANGYSELEISQKRSALENVMRPDSLNVHQQRLTENGFSHFSVWFQCFNFASMVAIK
Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Q081N3
Q0B0F7
FLIW_SYNWW
Flagellar assembly factor FliW
Syntrophomonas
MKIVSTLLGELEFEEEDIIMFPAGIPAFEQEKSFLLIAMGEGVPFYYLQSALNPELCLVVANPFAFFPRYSIEIGQEELQRLDCSQREELLLYVILTVPQDFRESTANLVAPLIINQESKKGLQFIATNSDYTTRHPIFQPTQAEEQTGIAAAEEG
Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum.
Q0B0F7
P02015
HBA_AMBME
Hemoglobin alpha chain
Ambystoma
MFKLSGEDKANVKAVWDHVKGHEDAFGHEALGRMFTGIEQTHTYFPDKDLNEGSFALHSHGKKVMGALSNAVAHIDDLEATLVKLSDKHAHDLMVDPAEFPRLAEDILVVLGFHLPAKFTYAVQCSIDKFLHVTMRLCISKYR
Involved in oxygen transport from the lung to the various peripheral tissues.
P02015
O32266
SWRAA_BACSU
Swarming motility protein SwrAA
Bacillus
MKRASIVREKKYYELVEQLKDRTQDVTFSATKALSLLMLFSRYLVNYTNVESVNDINEECAKHYFNYLMKNHKRLGINLTDIKRSMHLISGLLDVDVNHYLKDFSLSNVTLWMTQER
Required for swarm cell differentiation. Plays a crucial role in regulating the degree of cell flagellation.
O32266
Q6T1W6
FDTB_ANETH
dTDP-6-deoxy-D-xylo-hex-3-ulose aminase
Aneurinibacillus
MIPFLDLRQINMRYQKEIQQAMNRVLESGWYILGGEVDDFERKFASYCGAKYCIGVANGLDALTLIIRAYDIGLGDEVIVPSNTYIASILAISANGATPVLVEPDINTYNIDPLKIEEKITSRTKAIMVVHLYGQSCDMESINLIAKKYNLKVIEDCAQAHGAIYNGKRVGSLGDAAGFSFYPGKNLGALGDGGAITTNDAELAERLNVLRNYGSHKKYENLFKGVNSRLDELQAAILSIKLSYLDDDNQRRREIAAYYLEHIKNPFIHLPTVTDDKAHVWHLFVVRVKEREAFQYYLAEQNIQTLIHYPIPPHKQKAYSEWQQESFPISEQIHSEVVSLPISPVMSREEVERVVEAVNRYGY
Specifically aminates dTDP-6-deoxy-D-xylohex-3-ulose to form dTDP-D-Fucp3N in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose, a glycan chain of the S-layer.
Q6T1W6
Q08121
CLYT_CLYGR
Phialidin
Clytia
MADTASKYAVKLRPNFDNPKWVNRHKFMFNFLDINGDGKITLDEIVSKASDDICAKLGATPEQTKRHQDAVEAFFKKIGMDYGKEVEFPAFVDGWKELANYDLKLWSQNKKSLIRDWGEAVFDIFDKDGSGSISLDEWKAYGRISGICSSDEDAEKTFKHCDLDNSGKLDVDEMTRQHLGFWYTLDPNADGLYGNFVP
Ca(2+)-dependent bioluminescence photoprotein. Displays an emission peak at 470 nm (blue light). Trace amounts of calcium ion trigger the intramolecular oxidation of the chromophore, coelenterazine into coelenteramide and CO(2) with the concomitant emission of light.
Q08121
Q7U076
RNPH_MYCBO
tRNA nucleotidyltransferase
Mycobacterium tuberculosis complex
MSKREDGRLDHELRPVIITRGFTENPAGSVLIEFGHTKVLCTASVTEGVPRWRKATGLGWLTAEYAMLPSATHSRSDRESVRGRLSGRTQEISRLISRSLRACIDLAALGENTIAIDCDVLQADGGTRTAAITGAYVALADAVTYLSAAGKLSDPRPLSCAIAAVSVGVVDGRIRVDLPYEEDSRAEVDMNVVATDTGTLVEIQGTGEGATFARSTLDKLLDMALGACDTLFAAQRDALALPYPGVLPQGPPPPKAFGT
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Q7U076
P53215
THG1_YEAST
tRNA-histidine guanylyltransferase
Saccharomyces
MANSKFGYVRQFETHDVILPQCYIVVRIDGKKFHEFSKFYEFAKPNDENALKLMNACAKNLVLKYKNDIILAFGESDEYSFILKSSTTLFNRRKDKLATLFGSFFTSNYVALWAKFFPEKPLNIKHLPYFDSRCVAYPNLQTIKDYLSWRYVDTHINNLYNTTFWQLIIKCGLTPQESEKKLCGTFSNEKQEILFSECGINYNNEPEMFKKGSLVTRKGEILHINVIAQIDELFEGY
Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage.
P53215
Q83D84
MSBA_COXBU
Lipid A export ATP-binding/permease protein MsbA
Coxiella
MKTLTSQGIRTYGRLLQATKQYWPIFLIGVVGMIAVSLSDAGFTWLIKPIINRGFIARDLVFIRWLPFIIVLVFLFRGAANFLSTYFINRVARNIVMDFRRAIFSHLLRLPAEFYDRHSSGHLLSTVIYNVEQVAQASSDALIITLQASSLVVGLLVVMFLVSWKLTLFFLVITPLIAWVMRVCSARLRHLSTSVQKSVGEVTHIASEAIEAYKIVRLYGGQKYENEKFRHATKLNQQRELKVVVTNSVGTSLVQLLIAIPIAIVLFFATQPSFHVTAGSFASIVSAMIMMLRPVRRLTMVNSYIQKGIAAAESIFKLLDEDVEKDRGERHLVRARGAIEYQGVSFAYDNSKKTILSEISFSIEPGQMVAIVGRSGAGKSTLINLLPRFYDASTGVIKIDDINIKEFRLQELRNQFGLVSQHTTLFNDTILNNIAYGQAGSIDKRKIIEAARAAHAMEFIEQLPEGLDTVIGENGVRLSGGQRQRIAIARALFKNAPIHILDEATSSLDTHSERHIQAALDNLMDQCTTLVIAHRLSTIERADWIMVLEEGRLIEKGTHQQLLTLNGAYAELYRMQFAEKPAAMTALDE
Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Q83D84
A0PPY6
LEU3_MYCUA
Beta-IPM dehydrogenase
Mycobacterium
MKLAIVAGDGIGPEVVAQAVKILDVVQPGVEKTNYDLGARRFHATGEILPDSVIAELREHDAILLGAIGDPSVPSGVLERGLLLRLRFELDYHINLRPGRLYPGVKSPLALEPGNPEIDFVVVREGTEGPYTGNGGAIRVGTANEVATEVSVNTAFGVRRVVRDAFERAMRRRKHLTLVHKNNVLTFAGSLWWRTVQEIGEEYPDVELAYQHVDAATIHMVTDPGRFDVIVTDNLFGDIITDLAAAVCGGIGLAASGNIDATRTNPSMFEPVHGSAPDIAGQGIADPTAAIMSVSLLLAHLGLDDTASRVDRAVEGYLATRGNERLATAAVGERIAAAL
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
A0PPY6
B6YS41
FABH_AZOPC
3-oxoacyl-[acyl-carrier-protein] synthase III
Candidatus Azobacteroides
MNKIHAVITGIGGYVPEYKLTNEEISTMVDTSDEWILKRIGIKERRILKPEEGKGITYLALKAIEDLKSRHDFDPLEIDAVLFATATPDYPFPNSASLIAHKVGITNAFGFDMEAACSGFIYALEVAQGFIVSGKHKKVMIIAGDVLSVFIDYSDRNTSPIFGDGCGCALVEATMEDIGLVDSIMRCDGSIPESLHVYGGGSVNPTTYETINNKLHYVWQDGKVVFRHAVSNMADTCQKLISKNNLSKDEIDWVVPHQANLRIIDAVTNHLKISRERVMINIEKYGNTGAASIPLCLCEWESKLHKGDKMIFTAFGAGFTWGATYLKWGYDSH
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
B6YS41
Q39ZN6
KUP1_GEOMG
Probable potassium transport system protein kup 1
Geobacter
MDQHKGDASLGGIVKALGLVFGDIGTSPIYTLTVIFTLTQPTRENVFGILSLVFWTMTILVTMEYAWLAMSLGRKGQGGEIVLREIIMKLVKTGRLVAFAGFLSFVGVSLLLGDGVITPAISILSAVEGLLLIPGLEGLSTGTLVAIAAAIAIGLFSVQFKGTDRVAGAFGPIMAVWFSTLAVTGVVSALSMPEIVEAINPWHAFTFFRENGLAGYFVLSEVILCSTGGEALYADMGHLGRRPIVKSWYFVFMALYLNYLGQGVFAITHPEAKNLLFGMVRDQMPTLYIPFLILTIMATIIASQSIISGVFSIVYQGITTRLLPLMRVDYTSREIKSQIYLGAVNWSLMVAVILVMLLFRKSENLAAAYGMAVTGSMTITGIMMIIVFAHTTKKWRALVALVITLIDAAYLLSTFSKIPHGAYWSLILASIPFVTIIIWTRGQRSLYHALKPLDLETFLISYEQIYAKGPIRGTGLFFTRDTDVVPPYVVHCIIRSNIIYERNVFISLVITDEPLGVETELIKGIGPGLDAFRIEAGYMEVVDIEALLKANGIQEKVIFYGVEDISTRNPLWRVFSVFKKLTPNFVQFHKLPASRLQGVVTRVEM
Transport of potassium into the cell.
Q39ZN6
A0QU81
SCMU_MYCS2
Secreted chorismate mutase
Mycolicibacterium
MLASVALAALAGVGTPHATADDASPLVPLVDAAAQRLQTADPVAASKFRSGGAIDDPDREQQVIAAVTGDATRHNIDPGYVHDVFRNQIDATSSVEHTRFAQWKLDPAAAPSSAPDLSESRQKIDTLNRTMVDEIARQWPVLHSPVCRPDLDRALDAVATARGFDPVYRHALEYATHSYCR
Catalyzes the Claisen rearrangement of chorismate to prephenate. May play some role in the pathogenicity.
A0QU81
Q7M725
TR107_MOUSE
T2R4
Mus
MLNSAEGILLCVVTSEAVLGVLGDTYIALFNCMDYAKNKKLSKIGFILIGLAISRIGVVWIIILQGYIQVFFPHMLTSGNITEYITYIWVFLNHLSVWFVTNLNILYFLKIANFSNSVFLWLKRRVNAVFIFLSGCLLTSWLLCFPQMTKILQNSKMHQRNTSWVHQRKNYFLINQSVTNLGIFFFIIVSLITCFLLIVFLWRHVRQMHSDVSGFRDHSTKVHVKAMKFLISFMVFFILHFVGLSIEVLCFILPQNKLLFITGLTATCLYPCGHSIIVILGNKQLKQASLKALQQLKCCETKGNFRVK
Putative taste receptor which may play a role in the perception of bitterness.
Q7M725
A4QDK8
GATA_CORGB
Glutamyl-tRNA(Gln) amidotransferase subunit A
Corynebacterium
MTNKYLVEGSENELTTKTAAELAGLIHSREVTSREVTQAHLDRIAAVDGDIHAFLHVGQEEALNAADDVDKRLDAGEAPASALAGVPLALKDVFTTTDAPTTAASKMLEGYMSPYDATVTRKIREAGIPILGKTNMDEFAMGSSTENSAYGPTHNPWDLERTAGGSGGGSSAALAAGQAPLAIGTDTGGSIRQPAALTNTVGVKPTYGTVSRYGLIACASSLDQGGPTARTVLDTALLHEVIAGHDGFDATSVNRPVAPVVQAAREGANGDLKGMKVGVVKQFDRDGYQPGVLEAFHASVEQMRSQGAEIVEVDCPHFDDALGAYYLILPCEVSSNLARFDGMRYGLRAGDDGTRSADEVMAYTRAQGFGPEVKRRIILGTYALSVGYYDAYYLQAQRVRTLIAQDFAKAYEQVDILVSPTTPTTAFKLGEKVTDPLEMYNFDLCTLPLNLAGLAGMSLPSGLASDTGLPVGLQLMAPAFQDDRLYRVGAAFEAGRK
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).
A4QDK8
Q9LSY8
U71B2_ARATH
Protein HYPOSTATIN RESISTANCE 1
Arabidopsis
MKLELVFIPSPGDGHLRPLVEVAKLHVDRDDHLSITIIIIPQMHGFSSSNSSSYIASLSSDSEERLSYNVLSVPDKPDSDDTKPHFFDYIDNFKPQVKATVEKLTDPGPPDSPSRLAGFVVDMFCMMMIDVANEFGVPSYMFYTSNATFLGLQVHVEYLYDVKNYDVSDLKDSDTTELEVPCLTRPLPVKCFPSVLLTKEWLPVMFRQTRRFRETKGILVNTFAELEPQAMKFFSGVDSPLPTVYTVGPVMNLKINGPNSSDDKQSEILRWLDEQPRKSVVFLCFGSMGGFREGQAKEIAIALERSGHRFVWSLRRAQPKGSIGPPEEFTNLEEILPEGFLERTAEIGKIVGWAPQSAILANPAIGGFVSHCGWNSTLESLWFGVPMATWPLYAEQQVNAFEMVEELGLAVEVRNSFRGDFMAADDELMTAEEIERGIRCLMEQDSDVRSRVKEMSEKSHVALMDGGSSHVALLKFIQDVTKNIS
Glucosyltransferase that glucosylates the cell wall inhibitor hypostatin in vivo to form a bioactive glucoside.
Q9LSY8
Q5A7Q6
LIS1_CANAL
nudF homolog
Candida
MEKLQILTERQQTELNHAIIQYLQPLCQQDNHVLLDQLSKLLNIDQSTQESNNVEKVDNYLEKRWSTVLRLQKKIIDLENEISNLNNIINSTNSDNNGIILSKDKINWIPKGAVKQSYQCENIVTTVKLHPNLPLVLNGCNDGNLYIWNISNDDNTIPEKMIKAHTRAINKICFTYKKPYYLATCSSDLTIKIWDEKFNHIRTLNGHEHTVSSIQFSPVDNSILYSVSRDKNIRVWDIFQGISLKSFVGHSEWCRDLDIISSDTYGDFVLTCSNDQSARLSHANSGAGVAMIVGHSHVVETVKFLPSLQANKILDEYITKNTEQFPTIPLELLKDKTYNQLGFKYCITASRDNTIKLWLIPPPTIAPHRPPLPSKYNNSQSWLIAELKGHSSWVKSLCVHPNGKFIISGSDDKTIKFWDLSGLLETGYVNVVKTIIGHDGFINDIDFARLKEASDVSEEDLLKQVEKRMRCLFISGSADNSIKLWN
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. Plays a central role in positioning the mitotic spindle at the bud neck during cell division. Targets cytoplasmic dynein to microtubule plus ends, thereby promoting dynein-mediated microtubule sliding along the bud cortex and consequently the movement of the mitotic spindle to the bud neck.
Q5A7Q6
O26744
RL37_METTH
50S ribosomal protein L37e
Methanothermobacter
MKGTPSFGKRNKNLHIRCRRCGKNSYHVRKKVCAACGFGRSRRIRRYSWQNKKITGQRLK
Binds to the 23S rRNA.
O26744
A8ADG3
MURR_CITK8
MurPQ operon repressor
Citrobacter
MLYLAKMRNAEGELTENEQKIASFLLAHVSELKTVSSRNLAKQLEVSQSSIVKFAQKLGAKGFTELRMALIEEYSVNREKKHDTALHLHSTITSEDSLEVIARKLNREKMFALEETCSLMDFDRLKQVINLISKARLIQITGVGGSALVGRDLSFKLMKIGYRVACEVDTHVQATIAQALQEGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLTDSPLRRLADYTLDTVSGETEWRSSSMSTRTAQNSVTDLLFVGMVQLNDVESLRMIERSSELINLLGRS
Represses the expression of the murPQ operon involved in the uptake and degradation of N-acetylmuramic acid (MurNAc). Binds to two adjacent inverted repeats within the operator region. MurNAc 6-phosphate, the substrate of MurQ, is the specific inducer that weakens binding of MurR to the operator.
A8ADG3
Q980V3
SYDND_SACS2
Non-discriminating aspartyl-tRNA synthetase
Saccharolobus
MFRTHLVSELNPKLDGSEVKVAGWVHNVRNLGGKIFILLRDKSGIGQIVVEKGNNAYDKVINIGLESTIVVNGVVKADARAPNGVEVHAKDIEILSYARSPLPLDVTGKVKADIDTRLRERLLDLRRLEMQAVLKIQSVAVKSFRETLYKHGFVEVFTPKIIASATEGGAQLFPVLYFGKEAFLAQSPQLYKELLAGAIERVFEIAPAWRAEESDTPYHLSEFISMDVEMAFADYNDIMALIEQIIYNMINDVKRECENELKILNYTPPNVRIPIKKVSYSDAIELLKSKGVNIKFGDDIGTPELRVLYNELKEDLYFVTDWPWLSRPFYTKQKKDNPQLSESFDLIFRWLEIVSGSSRNHVKEVLENSLKVRGLNPESFEFFLKWFDYGMPPHAGFGMGLARVMLMLTGLQSVKEVVPFPRDKKRLTP
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Q980V3
Q9PGY0
ANMK_XYLFA
AnhMurNAc kinase
Xylella
MRVHDDPCNPNPAPLYLGLMSGTSVDGIDAALVRINANAITHCELIAAQTSAWDPNLRTTLLELSQGQNTASLDQLGWLDAQVGLAFATAANTLIAKTGIKHTQIRAIGSHGQTIRHRPHGDLPFTWQLGDAHRIAELTGITTVADFRRRDVAAGGQGAPLMPAFHLAILGSANENRAVLNLGGIANLTLIPMTGPVLGFDTGPANALLDSWYQRHHHETFDQSGNFAASGKINQKLLACLLADPWFTLPPPKSTGREQFHLDWVTKQLEPTPPSPADVQATLLELTAVTVADALLRQQPKTNRLLICGGGAHNPVLMARLAAHLPNVTVESIQTYGLNPDYLEAMGFAWLAAQTLDGQPGNLPSVTGARGLRLLGAIHPA
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Q9PGY0
P81554
TRM1_PYRFU
tRNA(m(2,2)G26)dimethyltransferase
Pyrococcus
MSMELFEVHEGKAKVLVPKAKTIYDSPVFYNPRMAPNRDVVVLLLNVLKPKIVLDALSATGIRGIRFALETPAEEIWMNDINELAYELMKKNVLLNFKGTLKENAKRAIFEGEKTIVINNDDANRLMAEKHRYFHFIDLDPFGSPMEFLDTALRSVKRKGILGVTATDGAPLCGAHPKACLRKYLAVPLRGELCHEVGTRILVGVIARYAAKYDLGMEVLLAYYKDHYFRAFVKLKDGAKKGDETLENLGYVYFDEKTGRFEVEKSFLSTRPNAYGPLWLGPLKNEKVVGEMLELLVSGFEVANYREVLKLLHMLHEELDIPLFYDTHALGKRLKIEPKKLGEIIKELKSMGYEATRTHFSPTGIKTNAPYEVFVEVMRKN
Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
P81554
A7WWP0
SYS_STAA1
Seryl-tRNA(Ser/Sec) synthetase
Staphylococcus
MLDIRLFRNEPDTVKSKIELRGDDPKVVDEILELDEQRRKLISATEEMKARRNKVSEEIALKKRNKENADDVIAEMRTLGDDIKEKDSQLNEIDNKMTGILCRIPNLISDDVPQGESDEDNVEVKKWGTPREFSFEPKAHWDIVEELKMADFDRAAKVSGARFVYLTNEGAQLERALMNYMITKHTTQHGYTEMMVPQLVNADTMYGTGQLPKFEEDLFKVEKEGLYTIPTAEVPLTNFYRNEIIQPGVLPEKFTGQSACFRSEAGSAGRDTRGLIRLHQFDKVEMVRFEQPEDSWNALEEMTTNAEAILEELGLPYRRVILCTGDIGFSASKTYDIEVWLPSYNDYKEISSCSNCTDFQARRANIRFKRDKAAKPELAHTLNGSGLAVGRTFAAIVENYQNEDGTVTIPEALVPFMGGKTQISKPVK
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).
A7WWP0
B3QZG1
PNP_PHYMT
Polynucleotide phosphorylase
16SrX (Apple proliferation group)
MDLNTKNNNKKVFEIIFENNVLRIEIGEISRQANGSVMLFYKDTVILSVAVCGDKKNSLNFLPLTVNYQEKLYAAGKIPGGFLRREGKPSDQEILCSRLIDRTIRPLFSKNFKNEVQLINMVLSSDPDGNNENIALLGSSLALLISDIPFFEPVSSVCVGKIGDNLIINPTLSQRENSSFFLILAGTKDSLNMVEMSSKEISENNFLESIKFGHEIIKKLCLFQTEIANQIGKTKIKIPLHNVNNLLEVEIKDKYFSEIEMILKNKCNVNNVKKSDILKKLKENVLENYKEKFLNNKKDNFNLLDLENQKLYLNEVEIIFDFLVRTIIRETILKENIRPDGRNSSEIRSITSRIDILPRTHGSALFTRGGTQSLAIVTLGTLRESKIIDDLSDEVDKRFMLHYNFPAFAVGSVGRYLAPSRREIGHGMLAEKALECVLPSENDFPYSIRVVSEILDSNGSSSQATICASSMALMSAGVPLKSLVAGVAMGLIVDDIDKINHYTILSDIEGLEDYQGDIDFKIAGTKVGITALQLDIKIKGITLEIFEKVLEQAKKDRIKILNEMEKVINKSRNEVSKYAPKVKMILIKPEKIRDIIGSGGKIINQIIEKHDNVKIDIMQDGKIYIMHQNMEIVDLTVTYIQNFLKKIKVENVYEVKILRFVKDKMDKTFGAIAEIFPGIEGFIHISKLENYKVDKVEDVLKIGQIILVKCIKINERGQIDLSKKDVFK
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
B3QZG1
P19377
CD3D_RAT
T-cell receptor T3 delta chain
Rattus
MEHYGILVSLLLATVLPQGSPFKIEVVEYEDKVFVNCNTSIRHLDGSVERWLTKNKSLILGKGILDPRGMYMCNGTEELAKEVSTVQVYYRMCQNCVELDSATLAGVIITDLIATLLLALGVYCFAGHETGRLSGAVDTQVLLKNEQLYQPLRDRDDAQYSRLGGNWPRNKRS
Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition of this role of signal transduction in T-cell activation, CD3D plays an essential role in thymocyte differentiation. Indeed, participates in correct intracellular TCR-CD3 complex assembly and surface expression. In absence of a functional TCR-CD3 complex, thymocytes are unable to differentiate properly. Interacts with CD4 and CD8 and thus serves to establish a functional link between the TCR and coreceptors CD4 and CD8, which is needed for activation and positive selection of CD4 or CD8 T-cells.
P19377
Q88PK5
HSCB_PSEPK
Co-chaperone protein HscB homolog
Pseudomonas
MGTPCHYALFDLQPSFRLDLDKLATRYRELAREVHPDRFADASEREQRIALEKSAALNDAYQTLRSAPRRARYLLAISGHEVPQEVTVHDPDFLLQQMQWREELEELQDEADLDGVGVFKKRLKAAQDTLNEDFAGCWDAPGERDKAERLMRRMQFLDKLAQEVRQLEERLDD
Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA.
Q88PK5
A7HNY7
RSMH_FERNB
rRNA (cytosine-N(4)-)-methyltransferase RsmH
Fervidobacterium
MNRVYNDHHIPVLLNEVVENLIWKPDGVYVDCTVGEGGHTRAIAERVLPYGGRVIGIDVDSEVLQIAEHNLLSYPNVQLFKFSYVELPVLLSLLQVHKVDGLLVDLGVSTYQLKAEGRGFSFNQDEPLDMRMNLENNLTAYHIVNTYPEEKLADIIYNYGEENFSRRIARAIVQNRPIQTTRQLVEVIKRALPYKEVHNRKRHFATKTFQAIRIEVNKEIENISKFLEFAPDYLNSGGRLAIISFHSLEDRIVKHVFKNDKRLKPIGDFISPTTFEVAENPRARSAKLRLAERV
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
A7HNY7
C3P1E8
NUOB_BACAA
NDH-1 subunit B
Bacillus cereus group
MVINFEELHPNERAELERNIFFSTLEQLKGWARSNSLWPMTFGLACCAIEMMGVGSSHYDLDRFGSFFRTSPRQSDVMIVSGTVTKKMAPIVRRLYDQMPEPKWVIAMGSCATAGGPYVNSYAVVKGVDQIVPVDVYIPGCPPNPAALIYGINKLKEKIRYEAKTGKQVTNK
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
C3P1E8
P14271
UCP1_RABIT
Thermogenin
Oryctolagus
MVGTTTTDVPPTMGVKIFSAGVAACLADVITFPLDTAKVRQQIQGEFPITSGIRYKGVLGTITTLAKTEGPLKLYSGLPAGLQRQISFASLRIGLYDTVQEFFTSGEETPSLGSKISAGLTTGGVAVFIGQPTEVVKVRLQAQSHLHGLKPRYTGTYNAYRIIATTESLTSLWKGTTPNLLRNVIINCTELVTYDLMKGALVRNEILADDVPCHFVSALIAGFCTTLLSSPVDVVKTRFINSPPGQYASVPNCAMTMFTKEGPTAFFKGFVPSFLRLGSWNVIMFVCFEKLKGELMRSRQTVDCAT
Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance. Functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane. However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent transport of protons activated by LCFAs. Thereby, dissipates the mitochondrial proton gradient and converts the energy of substrate oxydation into heat instead of ATP. Regulates the production of reactive oxygen species/ROS by mitochondria.
P14271
Q8TXT7
HDRC_METKA
CoB--CoM heterodisulfide reductase iron-sulfur subunit C
Methanopyrus
MVEPRDTVIREEDLNPDFLEELSELVEPVFEEEEVLSVQACYQCGTCTGSCPSGRRTSYRTRLIMRKLQLGLVDEVIKSDELWMCTTCYTCYERCPRGVKIVDAVKAARNLAAKKGYMAKAHRMVAMFVIKTGHAVPINDEIREVRKNIGLDEVPPTTHRYEEALEEVQKLVKINEFDKLIGYDWEEGDLVD
Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B).
Q8TXT7
C5GAH0
UTP25_AJEDR
U three protein 25
Blastomyces
MVAPRGRDAEDEVELIDELSSGSDDDDEEDKKTSKPYNTLLQLFNAGQDTNGPARKRRKVEHSSKKTEVQIKEPEELDDEADLSESEIEDDEEDEDAEGIAVDEGEAEDSGDEDDATDPFETHFSNVDSSLLLQQINVISTKGWKTHKNELPGKFRLVLSHPDTGGDAVQLPPPAHGLQSLKLKQKLANHAGDHIAKFESLTSGLVPYIFGYQDLLFGARTLSNSAKFRDLYCLHVLNHILKTRDRVLKNNSRSQKEPDQDLELRDQGFTRPKVLIILPTRQACVRVVESITKLYHAEQQENKSRFYDTFSAADDKSWEDKPDDFRELFGGNDDDMFRLGLKFTRKTIKYFSQFYNSDIILASPLGLRMVMDKEDGKKQDFDFLSSIEVAVVDQADALLMQNWEHIEYVFSHLNLQPKESHGCDFSRVRNWYLDGQAKYVRQTLVFSSFITPEINALFSSQMHNTAGKVKVTPTYEGAILDIPLPVPVKQTFSRFNSTSPVKDPDDRFKYFTSAVLSSLVRSSTGSGGKPHASGTLIFIPSYLDFVRVRNYLATSSQTENLSFGAISEYTSVRDVARARTHFFSGRHSALLYTERTHHFRRYQIRGVKRVIMYGVPENPVFWGEIVGFLGLDPAGTAEAAEGGVRALFSKWDALKMERIVGTKRLGNMLMEKGGDTFSFV
DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2.
C5GAH0
A1VNU1
RBFA_POLNA
Ribosome-binding factor A
Polaromonas
MRKKSSTPNRGFRVADQIQRDLTELIARELKDPRVGMVTVQSVEVTPDYAHAKIYFSVLVGDPKECEIALNQAAGFLRNGLFKRLMTHTVPTLHFHFDQTTERAADLNALIAKAVSSRAQDD
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
A1VNU1
Q8EDH1
FABH_SHEON
3-oxoacyl-[acyl-carrier-protein] synthase III
Shewanella
MHTKILGTGSYVPVQVRSNQDLEKMVETSDQWIVERTGISERRIAAQDETVSTMGYLAALNALEMAGIEASDLDMIICGTTSAANAFPAAACEIQAMLGVHTIPAFDIAAACSGFVYALSVADQFVKNGTAKKVLVIGADVLSRLCEPEDRTTIILFGDGAGAAIIGASDEPGIISTHIYADGRQGDLLKCAFPPRQGETSEAVGFMTMKGNDVFKVAVTQLSHVVTETLRLNNIDKSEIDWLVPHQANFRIINATAKKLDMSLDKVVLTLAKHGNTSAASVPIALDEAVRDGRIQRGQLLLLEAFGAGFAWGSALVRF
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Q8EDH1
Q1IQ76
RECR_KORVE
Recombination protein RecR
Candidatus Koribacter
MSKFAEPMARLIDELKKLPGVGNKSAQRLAFHILRSSNDDAELLADAVRDVKAKLRLCSICNNITDVDPCTYCANPTRNQQVICVVEEPTNISAVEKTRHFNGVYHVLHGALSPLHGVGPEHLRISNLIKRVEGGKAEEVILATNPTVEGEATATYLSKILKAEGVRVTRIATGVPVGSDIEYADEVTMQKAMEGRREL
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Q1IQ76
Q8KAW9
ATPG_CHLTE
F-ATPase gamma subunit
Chlorobaculum
MPTLKDIRIRLKGVKSTQQVTKAMKMVAAAKLRRAQDRAIQARPYAGKLKEMLASLSTKVDTSVNPLLSPREEVNNVLVILVTSDRGLCGGFNANIIKMAQRLIHEEYAALHAKGGVTMICAGTKGTEFFRKRGYKLAAAYPGVFQNLSFDSAREIADKASKMYLSGEVDRVVLVYNEFKSVLAPNLRTEQLLPITPEGGDAKTASSEYLYEPSPAAIIDELVPKHLNTQLWRVMLESNAAEQAARMAAMDSATENAKELIRVLNISYNRARQAAITKELSEIVAGADALKQ
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Q8KAW9
B4T6U4
RNB_SALNS
Exoribonuclease II
Salmonella
MFQDNPLLAQLKQQLHSQTPRAEGVVKATEKGFGFLEVDAQKSYFIPPPQMKKVMHGDRIVAVIHTEKERESAEPEELIEPFLTRFVGKVQGKNDRLSIVPDHPLLKDAIPCRAARGVQHEFKEGDWAVAEMRRHPLKGDRSFYADLTQYITFADDHFVPWWVTLARHNLEKEAPNGVATEMLDEGLERQDLTALNFVTIDSASTEDMDDALYAEELADGRLQLTVAIADPTAWIAEGSKLDNTAKIRAFTNYLPGFNIPMLPRELSDDLCSLRANEVRPALACRMIIAADGTIDDDIAFFAATIESKAKLAYDNVSDWLENNGTWQPENEDIAQQIRLLHRICLSRSEWRHHHALVFKDRPDYRFVLGEKGEVLDIVAEPRRIANRIVEESMIAANLCAARVLRDKLGFGIYNVHTGFDPANADALAALLKTHGLHVDAEEVLTLEGFCKLRRELDAQPSGFLDSRIRRFQSFAEISTEPGPHFGLGLEAYATWTSPIRKYGDMINHRLLKAVIKGEAIARPQEDITQQMAERRRLNRMAERDVGDWLYARFLNDKAGTNTRFAAEIIDVSRGGMRVRLVDNGAIAFIPAPFLHAVRDELVCSQENGTVQIKGETVYKVTDVIDVTIAEVRMETRSIIARPAA
Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction.
B4T6U4
A0RMD6
NUOI_CAMFF
NDH-1 subunit I
Campylobacter
MAIKTKTIRRKKIPFLQRIYLPFIFAGMARTFRHFFRNLKDSSNIDFLEYPEQKPTDITNRYRGLHRLTKNEKGDLKCVACDMCATACPANCIFITATEIEGSKEKAPSKFTIDLLECVFCGLCVEACPKDAIRMDTGIFTKVGNTRESFLADIKTLSQREEGSF
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.
A0RMD6
I3PLR0
C82X2_PAPSO
Cytochrome P450 82X2
Papaver
MKSLMMNKLLFLQRITDSPSTTIISTFIVTIISIVFLYTVLLIRTTKNKQKIAAPKASGAWPFIGHLKLFMKQDTQFYRTLGTMSDKYGSVFTLRLGNQAILVVSNWEMVKECFTTNDKSFSNRPSTLSTKYMLNDTNSVVFSPYGTYWREMRKILVQKLLISNQRSEALKNLKTKEIDNSFVKLNDLCNNDVSGGGTKVRMDEWLADMMFNIIARITFGYQSGGGDAPGASTTSKNVERYKKTLDEMFVVLATRFAVSDIFPSLEFIDRLRGLVKDMKILGDELNSIAGCFIEEHRQKRRESLSSLLSLSNESVGDEQDFIDVLLSIMDQSRLPGDDPDFIIKIMILEAFAGGTDSLSATLTWVLSLLLNHPNVLKRAREEIDRHVENGKQVEVSDIPKLGYIDAIIKETMRLYPVGALSERYTTEECEVGRFNVPAGTRLLVNIWKIHRDPSVWENPSDFQPERFLCSDKVGVDLYGQNYELIPFGAGRRVCPAIVSSLQTMHYALARLIQGYEMKSASLDGKVNMEEMIAMSCHKMSPLEVIISPREPRRS
Cytochrome P450 involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine . Converts (S)-1-hydroxy-N-methylcanadine to (13S,14R)-1,13-dihydroxy-N-methylcanadine .
I3PLR0
C6DG59
RL6_PECCP
50S ribosomal protein L6
Pectobacterium
MSRVAKAPVVIPAGVEVKLNGQDISIKGKNGELSRKIHDAVEVKQADNALTFAPREGFVDGWAQAGTTRALLNAMVIGVTEGFTKKLQLVGVGYRAAVKGNVVNLSLGFSHPVDHALPAGITAECPSQTEIVLKGADKQVIGQVAAELRAYRRPEPYKGKGVRYADEVVRTKEAKKK
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
C6DG59
Q4ZPJ7
RNT_PSEU2
Exoribonuclease T
Pseudomonas syringae
MSEDHFDDEHEGHGGGGGSRHPMAARFRGYLPVVVDVETGGFNSATDALLEIAAVTIGMDEKGFVFPEHTYFFRVEPFEGANIEAAALEFTGIKLDHPLRMAVSEETAMNDIFRGVRKALKANGCKRAVLVGHNASFDLGFVNAAVARMDMKRNPFHPFSSFDTATLAGLAYGQTVLAKACQAAGIDFDGREAHSARYDTEKTAELFCGIVNRWKEMGGWQDFDD
Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis.
Q4ZPJ7
A1AHE9
GPMI_ECOK1
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Escherichia
MSVSKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFQADTAVAGLQAAYARDENDEFVKATVIRAEGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVGDKNVKAVEGGKLSDIAPTMLSLMGMEIPQEMTGKPLFIVE
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
A1AHE9
B1AJK7
RL19_UREP2
50S ribosomal protein L19
Ureaplasma
MALFKINKGEIMNFVNSTQLKTDIPNFDSGDTIIVHNRIVEGKKSRIQKFEGVVLRRRGSGSSETVIVRKESSGIGVEQSFNIHSPLVEKIEVIKYGKVRRAYISYMRNRSGKSARIKELNKQ
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
B1AJK7
B8HY03
RF3_CYAP4
Peptide chain release factor 3
unclassified Cyanothece
MTTDLQAELETEVERRRNFAIISHPDAGKTTLTEKLLLYGGAIHEAGAVKARRAQRHATSDWMEMEQQRGISITSTVLQFEYQGYQINLLDTPGHQDFSEDTYRTLAAADNAVMLVDAAKGLEPQTRKLFEVCKLRSLPIFTFINKLDRPGREPLDLLDEIEKELGLQTYAVNWPIGMGDRFKGVYDRRLQQIHLFERTAHGKREARDTIVDLGDPQIEALLDQDLYFQLKDDLELIEGLGPELDLEAVHQGKMTPIFFGSAMTNFGVELFLNAFLDYALKPATYRSSQGAIAPTHEDFSGFVFKLQANMDPKHRDRVAFVRVCAGKFEKDMTVNHARTGKMIRLSRPQKLFAQGRESLETAYAGDVIGLNNPGVFAIGDTIYSGQKLEYEGIPCFSPELFAYLRNPNPSKFKQFQKGVSELREEGAVQIMYSVDESKREPILAAVGQLQFEVVQFRLQNEYGVETRIELLPYTVARWVVEGWPALEAVGRIFNAVTVKDSWGRPVLLFKNEWNAQQVLADHPKLKLSGIAPVVSGQQPEAL
Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.
B8HY03
Q2NET3
TSR3_METST
16S rRNA aminocarboxypropyltransferase
Methanosphaera
MMKIVIYHSNECDPKRCTSIKLQKQNKVAITHNMRKIPYNAIVLDAEADKAVSREDREKITKYGLSALDCSWKKLKKSSFNFKSKKNHRLLPFLVAANPVNYGKPCILSSAEALSAALYIVGYKDEARDLMNSFKWGPHFITLNENLLEAYSEAKNSTEIVEVQNEFLGGK
Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Q2NET3
P67637
XERD_MYCBO
Tyrosine recombinase XerD
Mycobacterium tuberculosis complex
MKTLALQLQGYLDHLTIERGVAANTLSSYRRDLRRYSKHLEERGITDLAKVGEHDVSEFLVALRRGDPDSGTAALSAVSAARALIAVRGLHRFAAAEGLAELDVARAVRPPTPSRRLPKSLTIDEVLSLLEGAGGDKPSDGPLTLRNRAVLELLYSTGARISEAVGLDLDDIDTHARSVLLRGKGGKQRLVPVGRPAVHALDAYLVRGRPDLARRGRGTAAIFLNARGGRLSRQSAWQVLQDAAERAGITAGVSPHMLRHSFATHLLEGGADVRVVQELLGHASVTTTQIYTLVTVHALREVWAGAHPRAR
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
P67637
A7MM89
HFQ_CROS8
RNA-binding protein Hfq
Cronobacter
MAKGQSLQDPFLNALRRERVPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPSRPVSHHSNNAGGGSNNYHHSNNAQPSSAASQDSEDAE
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
A7MM89
Q3SW78
GRPE_NITWN
HSP-70 cofactor
Nitrobacter
MTDSDGKTDKSGEPAAEVEPVVSKPYVMPDDPEDDALDALNKQLAEAKDRTLRTLAEMENLRKRTAREVSDARTYGISGFARDVLEIADNLQRALDAVPADARAAPDPGLKALIEGVELTERSLHNALEKHGVKKFDPAGEKFDPNVHQAMYEVPDPSIPVGTVAQVIQAGYMIGERVLRPALVGVAKGGAKAAAPE
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Q3SW78
Q5KMX8
HSF_CRYNJ
Heat shock factor protein
Cryptococcus neoformans species complex
MTTNLYAIAGPSKPTTPTSTPSPRSEPPSPLKSLTSLPTNPLNSHGTSTPNTLTNQLSSTGIGISKPGLSVDENGEVMKVPAFLNKLYTMVSDPEVDDLIYWGESGDSFFVPNAELFGRELLPRWFKHSNFSSFVRQLNMYGFHKVPHLQSGALKNETPIELWEFANPYFKRGQPQLLTKVTRKNNRPSNSGVGPSSSVGGSGAGGGMSTRSASAAAASGSASGQIQQAISQGHEAGNHSTSGKYLITDGTTPGSVPPSHTSAGPLIAPQTLDLSAINSGIAAIRQTQASIATDLRKLQASNEALWRQAYETQEKQRKHEETIDLIVSFLERLFGTEGEGLKGLKEAMRRGVGVRRDRDGREGRDSRDSRFAEDDDGGQKKRRRVGIDRMIEGGTGDGTGEHGEIESPTSDDRLVEIGSNSEYSIPSVKRTSSSSHPISLGQLGSSRFTALPSEDPSPSASGPGSTSYEGLHTTQTNARGAGADVNVTDPTLGMNHLSPLSDTDPLLPSSSNALAPYSSHLPFPSSNSNQSNSFNPSNPSSAWASNPSQPLLSPTSAAAAAHAYNLDPSLLQTTIGSLLQSPAAAQMFLNSLSASAQGQALASHSHPHNPSPLNPNPNGNASTSASASAHGMNTGGMGTGSGTKDVDPTLALFSPLPSHSSLTSQSNDLLKSYSDALTVGEGVDNLQESIDSLVRSMGLDLPNGGSSVGVDVGDGAGVGTETGEGDGEFNVDEFLQGLAKEGEEEGEREVEGDGGVSSSGAGAGAENGRKEDVIAQSGLKSES
DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription . Together with its coregulator SSA1, activates expression of laccase LAC1 during glucose starvation .
Q5KMX8
Q7NN81
IXTPA_GLOVI
Nucleoside-triphosphate pyrophosphatase
Gloeobacter
MMRFLILATNNQGKLQELRRLLAGTGWVVQAAPPDFAVEETGTTFAENARLKALAAAERTGEWSVGDDSGLAVDALGGAPGVYSARYGRNDGERISRLLAALAGQADRGARFICAIALAEPGRVLKEVEAECRGVILHAPRGNGGFGYDPIFLVPELDKTFAELDIVEKERHSHRGRAVRKLLSGCSRGTFIVDH
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.
Q7NN81
Q9ZEP5
CSEA_STRCO
Lipoprotein CseA
Streptomyces albidoflavus group
MRGLTDGRTPRGTRRTTQAASTAVAVFVALGVSLAGCGTGGTGARDEGPAHADAVGGAGSASPAPAAKASPSKAPDRVDAVRLVKADPKVSPEVKRELKPCVADEYPIDVSYGKVTDGSADDVVVNVLTCGDAVGVGSYVYREEDGAYQNVFKAEEPPVYAEIDRGDLVVTKQVYDKGDPVSSPSGENVITYRWASDRFTEEYRTHNDYSKAAGNAPTPAPEPDS
May be involved in the stabilization of the cell envelope or may interact with the sensor protein CseC to modulate its activity, in response to cell envelope stress.
Q9ZEP5
Q5GST9
RS12_WOLTR
30S ribosomal protein S12
unclassified Wolbachia
MPTINQLVRKGRLKLSCKKKVPALGKSNPQRRGVCTKVYTTTPRKPNSALRKVARVRISGYGEVTAYIPGEGHNLQEHSVVLIRGGRVKDLPGVRYHIIRGALDLRGVQNRKKARSKYGVKKSS
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.
Q5GST9
B6JCK6
RL20_AFIC5
50S ribosomal protein L20
Afipia
MARVKRGVTAHAKHKKVYKAAEGFRGRRKNTIRAAKAAVDKAQQYAYVGRKLKKRNFRALWIQRINAAVRPFGLTYSRFINGLAKSGVVIDRKVLSDLAIHEPAAFQAIAEKAKAALAA
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
B6JCK6
P15867
H1C2_XENLA
Clone XLHW8
Xenopus
MTETAATETTPAAPPAEPKQKKKQQPKKAAGGAKAKKPSGPSASELIVKSVSASKERGGVSLAALKKALAAGGYNVERNNSRLKLALKALVTKGTLTQVKGSGASGSFKLNKKQLETKVKAVAKKKLVAPKAKKPVAAKKKPKSPKKPKKVSAAAAKSPKKAKKPVKAAKSPKKPKAVKPKKVTKSPAKKATKPKAAKAKIAKPKIAKAKAAKGKKAAAKK
Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures.
P15867
P57105
SYJ2B_HUMAN
Mitochondrial outer membrane protein 25
Homo
MNGRVDYLVTEEEINLTRGPSGLGFNIVGGTDQQYVSNDSGIYVSRIKENGAAALDGRLQEGDKILSVNGQDLKNLLHQDAVDLFRNAGYAVSLRVQHRLQVQNGPIGHRGEGDPSGIPIFMVLVPVFALTMVAAWAFMRYRQQL
Regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction.
P57105
Q5F6X6
NQRE_NEIG1
NQR-1 subunit E
Neisseria
MEHYLSLFIKSVFIENMALSFFLGMCTFLAVSKKVSTAFGLGVAVIFVLGLSVPANQLVYSLLKDGAIVEGVDLTFLKFITFIGVIAALVQILEMFLDKFVPALYNALGIYLPLITVNCAIFGAVSFMAQREYDFGESVVYGFGAGLGWMLAIVALAGITEKMKYSDAPKGLKGLGITFIAAGLMAMAFMSFSGIQL
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Q5F6X6
Q84GJ9
TRPB_NEIGO
Tryptophan synthase beta chain
Neisseria
MKNYHAPDEKGFFGEHGGLYVSETLIPALKELEQAYNEAKNDPEFWAEFRRDLKHYVGRPSPVYHAARLSEHLGGAQIWLKREDLNHTGAHKVNNTIGQALLARRMGKKRVIAETGAGQHGVASATVAARFGMTSDVYMGADDIQRQMPNVFRMKLLGANVIGVDSGSRTLKDAMNEAMREWVARVDDTFYIIGTAAGPAPYPEMVRDFQCVIGNEAKAQMQEATGRQPDVAVACVGGGSNAIGLFYPYIEEENVRLVGVEAGGLDVDTPDHAAPITSGAPIGVLHGFRSYLMQDENGQVLGTHSVSAGLDYPGIGPEHSHLHDIKRVEYTVAKDDEALEAFDLLCRFEGIIPALESSHVVGSGDKTRRKMGKDQVILVNLSGRGDKDINTVAKLKGIEL
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Q84GJ9
A5VZN0
RAPA_PSEP1
ATP-dependent helicase HepA
Pseudomonas
MAQQYQPGQRWISDSEAELGLGTILAQDGRLLTVLYPATGDTRQYSLRNAPLTRVRFSPGDQITHFEGWKLTVREVEDIDGLMVYHGLDGQNQPRTLPETQLSNFIQFRLASDRLFAGQIDPLSWFSLRYNTLQHTSKQMQSALWGLGGCRAQPIAHQLHIAREVADRSAPRVLLADEVGLGKTIEAGLVIHRQLLSGRASRVLILVPENLQHQWLVEMRRRFNLQVALFDAERFIESDASNPFEDAQLALVALEWLVDDEKAQDALFAAGWDLMVVDEAHHLVWHEDQVSAEYGLVEQLAQVIPGVLLLTATPEQLGQDSHFARLRLLDPNRFHDLAAFRAESEHYRPVAEAVQELLDEGRLSPKAHATILGFLGAEGEALLAAVSDGDTQASARLIRELLDRHGTGRVLFRNTRAAIQGFPERQLHPYPLATPEQYRNLPAGEHAELYPEVAFQAQGEVADDERWWRFDPRVDWLIDTLKMLKRTKVLVICAHAETAMDLEDALRVRSGIPASVFHEGMSILERDRAAAYFADEEFGAQVLICSEIGSEGRNFQFAHHLVMFDLPAHPDLLEQRIGRLDRIGQKHTIQLHIPYLQDSPQERLFQWYHEGLNAFLNTCPTGNALQHQFGPRLLPLLEGGDHKAWDTLVADARSERERLEAELHTGRDRLLELNSGGAGEGQALVEAILEQDDQFALPIYMETLFDAFGIDSEDHSENALILKPSEKMLDASFPLGDDEGVTITYDRGQALSREDMQFLTWEHPMVQGGMDLVLSGSMGNTAVALIKNKALKPGTVLLELLFVSEVVAPRSLQLGRYLPPAALRCLLDANGNDLASRVAFETLNDQLESVPRASANKFVQAQRDVLAKRISGGEEKILPAHNERVAEAQRRLTAEADEELARLVALQAVNPSVRDSEIDALRKRREDGLAMLEKAALRLEAIRVLVAG
Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair.
A5VZN0
P0DB62
GLMU_STRP3
Glucosamine-1-phosphate N-acetyltransferase
Streptococcus
MTNYAIILAAGKGTRMTSDLPKVLHKVSGLTMLEHVFRSVKAINPEKAVTVIGHKSEMVRAVLADQSAFVHQTEQLGTGHAVMMAETQLEGLEGHTLVIAGDTPLITGESLKSLIDFHVNHKNVATILTATAPDPFGYGRIVRNKDGEVIKIVEQKDANEYEQQLKEINTGTYVFDNKRLFEALKCITTNNAQGEYYLTDVVAIFRANKEKVGAYILRDFNESLGVNDRVALATAETVMRQRITQKHMVNGVTFHNPETVYIESDVTIAPDVLIEGNVTLKGRTHIGSGTVLTNGTYIVDSEIGDNCVVTNSMIESSVLAAGVTVGPYAHLRPGTTLDREVHIGNFVEVKGSHIGEKTKAGHLTYIGNAQVGSSVNVGAGTITVNYDGQNKYETVVGDHAFIGSNSTLIAPLEIGDNALTAAGSTISKTVPADSIVIGRSRQVTKEGYAKRLAHHPSRSK
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
P0DB62
Q50382
CH60_MYCSC
Chaperonin-60
Mycobacterium
PYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVKEGLRNVAAGANPLSLKRGIEKAVEKVTETLLKSAKEVETKDQIAATAAISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGL
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Q50382
Q2TA11
CF107_BOVIN
Cilia- and flagella-associated protein 107
Bos
MQFLTAVSPQSSSTPSWKIETKYSTRVLTGNWTEERRKFIKATEKTPQTIYRKEYVPFPGHRPDQISRWYSKRTVEGLPYKYLITHHQEPSQRYLISTYDDHYNRHNYHPGLPELRTWNRHKLLWLPEKADFPLLGPPTNYGLYEQLKQKWLPPPEATLRESIYTSSYPRPPAGAMSRREHAIPVPPPRLQPVPHF
Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Q2TA11
Q5E5I3
RL20_ALIF1
50S ribosomal protein L20
Aliivibrio
MPRVKRGVQARARHKKVLKQAKGYYGARSRVYRVAFQAVTKAGQYAYRDRRNKKRVFRQLWIARINAAARQNEMSYSRFINGLKKASIEIDRKILADIAVFDKVAFAALVEKAKAAL
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
Q5E5I3
O83986
RECX_TREPA
Regulatory protein RecX
Treponema
MGTRPTDEQYGAVCFACRCYEAECVAVRLLARSETSAQQLGFKLLKRGFEKRVVESVFPVLKRYSWLDDTRFARAWLRNRVDSRPASRAQLLGELKRRGVSHADAEGALDLLFQEQDEETLCLRLLEKLRRRGYGPHTLQRALQRRQFSPSLVRRCLAVETEGA
Modulates RecA activity.
O83986
A5I4X1
AROE_CLOBH
Shikimate dehydrogenase (NADP(+))
Clostridium
MYTTGLIGKNINYSESPEIHNNYYKKNNIPFFYKIFNLKQDQIDDFIKNLHKNNIKGFNVTIPYKETILQYLNDIVYPADKIGAVNTVAVQEDKLIGYNTDYIGFIKSLQYYNIQVKNFKCLIIGSGGSAKCIYYALKELNARDICIVSRNPEKARLKFEKKVKILNIKDENKLDRYDLIVNCTPIGGPNLKEQKPIELKEIKKNCVVYDLNYTPKRSKLLKEAKENGAFIINGEKMLIFQAYSAIGLWCLNGIKGGR
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
A5I4X1
B4UIA9
NUOD2_ANASK
NDH-1 subunit D 2
unclassified Anaeromyxobacter
MSEAKGVGGIDPRATPGSAGAGERPPMGTLSPRAGEGELYAPMPSKHMVINLGPSHPAMHGVTRAVVELNGEIIEGMKLDIGFLHRGFEKSCENVTWGQVFPYTDRLNYVSSIMNNVGFALAVEKLAKLEIPERARYLRVITSEIHRICDHLTLVGAMAMELGAMTVFLYGIEARDLLWDRLAELCGARLTSNYARIGGVARDIPEGWQEKTLKVLDRVVAIREEIGQLLNRNRIFIDRCLNTGKVSREDALELGFTGPCLRASGEPYDVRKAAPYLVYDRLDFDIPVGSNGDNFDRYLMRMEEMRQSDKIIRQCFEQMAPGEIIVQDFRYALPPKPLVYGTIEGVMAHFKLVMEGIKVPAGEVYSYTEAANGELGFYVVSDGGGRPYKLGLRAPGWPMLAALPVMTKGSLLSDLIPTFDSINMIGGEVEQ
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.
B4UIA9
B3QCH2
FMT_RHOPT
Methionyl-tRNA formyltransferase
Rhodopseudomonas
MPLRLVFMGTPEFAVPTLLALAAHGHDIAAVYTREPKPAGRGMKLQETPVALAAHRLQAPVLTPKTLRTDEALANFRAHEADAAVVVAYGMILPQAILDAPELGCYNLHGSLLPRWRGAAPLNRAIMAGDAETGVMVMKMDAGLDTGDVAMAERIAITDAMTVTDVHDQLARLGADLMVRAMAALERGGLQLTKQSEDGVTYAAKIDKAEAKIDFAKPAWAVLRHIHGLSPFPGAWCELPIEGQPVRIKVLRCAIADGRGEPGEVIDDHLTIACGDGAIRVSQLQRAGKQPMTAEEFLRGTPIAKGVRVG
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
B3QCH2
Q9ASV6
RR20_ARATH
30S ribosomal protein S20, chloroplastic
Arabidopsis
MATIVQCLSSCATLESQFKVLSLKGISCSSPSSSFSNRRGASATLSSSLSFSQSVSQCVAFSTGNLWVQKPMRQLIVCEAAAPTKKADSAAKRARQAEKRRVYNKSKKSEARTRMKKVLEALEGLKKKTDAQADEIVTVEKLIGEAYSAIDKAVKVKALHKNTGARRKSRLARRKKAVEIHHGWYVPDAAAAAPSEAVPMAA
Binds directly to 16S ribosomal RNA.
Q9ASV6
Q8R9R0
LSPA_CALS4
Signal peptidase II
Caldanaerobacter
MAIVIVAFVVFLDQFTKYLAAKYLMPIGSYPVIKHFFHLTYVENRGAAFGMLQNKTLFFIVITVVVGIVLIYSMIKLPENSLYNYTLAMILGGAIGNLIDRVRLGYVVDFIDFKFFPAVFNVADSFIVVGAIILGYLMIFKGGIR
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Q8R9R0
Q8LFR2
DRE2C_ARATH
Dehydration-responsive element-binding protein 2C
Arabidopsis
MPSEIVDRKRKSRGTRDVAEILRQWREYNEQIEAESCIDGGGPKSIRKPPPKGSRKGCMKGKGGPENGICDYRGVRQRRWGKWVAEIREPDGGARLWLGTFSSSYEAALAYDEAAKAIYGQSARLNLPEITNRSSSTAATATVSGSVTAFSDESEVCAREDTNASSGFGQVKLEDCSDEYVLLDSSQCIKEELKGKEEVREEHNLAVGFGIGQDSKRETLDAWLMGNGNEQEPLEFGVDETFDINELLGILNDNNVSGQETMQYQVDRHPNFSYQTQFPNSNLLGSLNPMEIAQPGVDYGCPYVQPSDMENYGIDLDHRRFNDLDIQDLDFGGDKDVHGST
Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates high salinity- and abscisic acid-inducible transcription.
Q8LFR2
Q1GCQ5
TSAD_RUEST
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
unclassified Ruegeria
MTQTLTLLGLESSCDDTAAAVVRQTTGAKAEILSSIVFGQTELHSAYGGVVPEIAARAHAEKLDSCVRDALAEAGLTLGDLDAIAVTAGPGLIGGVMSGVMCAKGISAATGLPLIGVNHLAGHALTPRLTDDITYPYLMLLVSGGHCQYLIARGPETFSRLGGTIDDAPGEAFDKTARLLGLPQPGGPSVQAEAEHGDPERFRFPRPLLDRPDCNLSFSGLKTALMRMRDQIIAEKGGLTRQDRADLCAGFQAAIVDTLVEKTRRALRLYLEDKPQHPTLAVAGGVAANTEIRNGLMALCFELETDFLAPPLALCTDNAAMIAYAGLERYKTGARDGMSLSARPRWPLDKTSPALIGSGKKGAKA
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Q1GCQ5
P87017
AFLH_ASPPU
Aflatoxin biosynthesis protein H
Aspergillus
MEVLDTTVDLGTLQGKSALITGGASGIGLATARAWAAAGMYVTIADIQPLETGQNILADLAGGHVHYVCCDVTSWESQITAFKEAIQFTPSKALDIVAAFAGVSFAGGNQVDHVLAAGDPRLDVNPSPPDIRNIQVNLIGVYYTSWLGLYYLRLSPTNKAANPSPDKSLILMGSIGSYMDSPKASTYPASKFGVRGLFRSTRARTRELGVRCNLLAPWFIDTPLIAPMKKAMAARGIDMAQRLTFASVDACVEAATTCAANPQLHGTPPIRYAYCLKT
5'-hydroxyaverantin dehydrogenase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) . The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits aflA and aflB, as well as the PKS aflC . AflC combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR . The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase aflA/aflB . The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin . The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN . The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) . The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway . The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA) . VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL) . Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen . Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA) . A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2 . Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST) . AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring . The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST) . Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively . Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 .
P87017
Q7VKR5
PURA_HAEDU
IMP--aspartate ligase
Haemophilus
MGKSVAILGAQWGDEGKGKIVDLLTDRVKYVVRYQGGHNAGHTLIINGEKTVLRLIPSGILRENVTCLIGNGVVLSPEALMKEMGELEACGINVRERLKISEACPLILPYHVAMDHAREAALGKNKIGTTGRGIGPAYEDKVARRGLRVSDLFDKEAFATKLKDILDLYNFQLVHYYKVEPVDFQKTLDDVFAVADVIKGMVADVTTLLHQARKEGVNILFEGAQGTMLDIDHGTYPFVTSSNTTAGGVATGAGFGPRNLDYVLGIIKAYCTRVGSGPFTTELFNEEGETIARKGNEFGAVTGRPRRCGWFDAVAVRRAVQINSISGFCMTKLDVLDGFETLKICTAYKMPNGEIVEYAPMAAKDWEGVEPIYETMPGWSENTFGVIKYEALPQAALDYIKRIEELVGVPVDILSTGPDRIETMILRDPFVA
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.
Q7VKR5
P42285
MTREX_HUMAN
TRAMP-like complex helicase
Homo
MADAFGDELFSVFEGDSTTAAGTKKDKEKDKGKWKGPPGSADKAGKRFDGKLQSESTNNGKNKRDVDFEGTDEPIFGKKPRIEESITEDLSLADLMPRVKVQSVETVEGCTHEVALPAEEDYLPLKPRVGKAAKEYPFILDAFQREAIQCVDNNQSVLVSAHTSAGKTVCAEYAIALALREKQRVIFTSPIKALSNQKYREMYEEFQDVGLMTGDVTINPTASCLVMTTEILRSMLYRGSEVMREVAWVIFDEIHYMRDSERGVVWEETIILLPDNVHYVFLSATIPNARQFAEWICHLHKQPCHVIYTDYRPTPLQHYIFPAGGDGLHLVVDENGDFREDNFNTAMQVLRDAGDLAKGDQKGRKGGTKGPSNVFKIVKMIMERNFQPVIIFSFSKKDCEAYALQMTKLDFNTDEEKKMVEEVFSNAIDCLSDEDKKLPQVEHVLPLLKRGIGIHHGGLLPILKETIEILFSEGLIKALFATETFAMGINMPARTVLFTNARKFDGKDFRWISSGEYIQMSGRAGRRGMDDRGIVILMVDEKMSPTIGKQLLKGSADPLNSAFHLTYNMVLNLLRVEEINPEYMLEKSFYQFQHYRAIPGVVEKVKNSEEQYNKIVIPNEESVVIYYKIRQQLAKLGKEIEEYIHKPKYCLPFLQPGRLVKVKNEGDDFGWGVVVNFSKKSNVKPNSGELDPLYVVEVLLRCSKESLKNSATEAAKPAKPDEKGEMQVVPVLVHLLSAISSVRLYIPKDLRPVDNRQSVLKSIQEVQKRFPDGIPLLDPIDDMGIQDQGLKKVIQKVEAFEHRMYSHPLHNDPNLETVYTLCEKKAQIAIDIKSAKRELKKARTVLQMDELKCRKRVLRRLGFATSSDVIEMKGRVACEISSADELLLTEMMFNGLFNDLSAEQATALLSCFVFQENSSEMPKLTEQLAGPLRQMQECAKRIAKVSAEAKLEIDEETYLSSFKPHLMDVVYTWATGATFAHICKMTDVFEGSIIRCMRRLEELLRQMCQAAKAIGNTELENKFAEGITKIKRDIVFAASLYL
Catalyzes the ATP-dependent unwinding of RNA duplexes with a single-stranded 3' RNA extension . Central subunit of many protein complexes, namely TRAMP-like, nuclear exosome targeting (NEXT) and poly(A) tail exosome targeting (PAXT) . NEXT functions as an RNA exosome cofactor that directs a subset of non-coding short-lived RNAs for exosomal degradation. NEXT is involved in surveillance and turnover of aberrant transcripts and non-coding RNAs . PAXT directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor ZCCHC8, which links to RNA-binding protein adapters . Associated with the RNA exosome complex and involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA . May be involved in pre-mRNA splicing. In the context of NEXT complex can also in vitro unwind DNA:RNA heteroduplexes with a 3' poly (A) RNA tracking strand . Can promote unwinding and degradation of structured RNA substrates when associated with the nuclear exosome and its cofactors. Can displace a DNA strand while translocating on RNA to ultimately degrade the RNA within a DNA/RNA heteroduplex . Plays a role in DNA damage response .
P42285
B6J1I6
FABH_COXB2
3-oxoacyl-[acyl-carrier-protein] synthase III
Coxiella
MTYARIQGVGSYIPQQILSNADLEKMVNTTDEWIMQRVGVRERHVIANSPDNTTTMAVDAAKRAIEMAEIDPAVIDMIIVGTATAEYYFPSTACLVQKHLNLREDIPAFDINAACAGFVYALSIADQYIRNEGAKHILVIGVDSLTKVVDWKDRSTCILFGDGAGAVILQAHKEPGILNTILHANGDYSDLITAKSGVWERESVPHLHMYGKEVFKLAVTKLGEIVDEIIEKSGLKQSDIDWLIPHQANLRIIEATAKRLGLPRERVILTIEQHGNTSAASIPLALDAAVRAGKIKRGDTLLLEAFGAGLAWGAALLKL
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
B6J1I6
A9WGS4
ATPB_CHLAA
F-ATPase subunit beta
Chloroflexus
MPAKGVIQEIIGVVIRAKFPEDEVPEIYNAIEIPLGNGDRLVCEVQQQLGNGVVKAVAMGSTDGLRRGLEVIDTGRPIAVPVGPATLGRVFNVLGDPIDGMGPIGPEVERRPIHRDPPSFEEQNTQAQIFETGIKVIDLIAPFTRGGKTAIFGGAGVGKTVVIQELIANIAKEQSGFSVFAGVGERSREGNDLIHEMKEARIDENTTVFDKTVMVFGQMNEPPGARLRVGLTALTMAEYFRDEGRDILLFIDNIFRFVQAGSEVSSLLGRMPSQVGYQPTLGTEMGELQERITSTKRGSITSMQAVYVPADDYTDPAPATVFSHLDATISLERSIAERAIFPAVDPLASTSRILDPNIVGEEHYRVAQEVKRVLQRYKDLKDIIAILGMEELSDEDKLTVQRARKIELFFSQPFTVAQQFTGRPGKYVPVKKTVESFARLLNGEGDHIPESFFYMQGDFDDVLAAYEASQK
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
A9WGS4
A6RT94
UTP25_BOTFB
U three protein 25
Botrytis
MAFGQRNTSRGGRGGGGGGSSFRGRGGSRGGPRGRGGMRGGRGRGRGRPVFDSARLAQKEEDEESDSESEEPSQDEASEEESSDDDDDDEPVPAVKSYTALMQSFTRDSAPQAKRRKLNVDKEEKEDEDADLMDEDTNEADLVEEEEEGPETATDGILEDDEEDKADPFEAHFANPDDNILSRRLQHLEKGQWALRMSSLAKVGTAITSIPGDGEPRAMKAMTIGSPEGLKLKQKLANVIKKQRPTFDALEKSIAPLVFGYQDLLFTERNTSNAESLRRLTCLHAVNHVFKTRDRVIKNNSRLAREDSSDDLELRDQGFTRPKVLMLLPTRESCVRMVDMITSLCEPEQQENRKRFNDSFVDKEENYSTDKPEDFRELFAGNDDDMFRLGLKFTRKTIKYFSQFYNSDIIFASPLGLRMAIGDEDAKKVDHDFLSSIEIVIVDQADALLMQNWEHVEFIFDHLNLQPKEAHGCDFSRVRSWYLDNNAKYFRQNIALAGFNTPELQTMFYTQSQNWEGKAKVSSTYPGAIQELGLKVKQTFSRIDTESIASDPQSRFEYFTSAIIPTLTRRSKDSSGTLLFIPSYMDFVKVRNYFSTSATTSSLSFGSISEYTTPKEVARARSHFFSGRHNVLLYTERAHHFRRYQIRGVKKVIMYGIPENPIFYKEIVAGYLGRSVREGDLEPGNGSLRAVFSKWDSMKLERIAGTERVNKMIKEKGDTFDFL
DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2.
A6RT94
Q81LS1
GRPE_BACAN
HSP-70 cofactor
Bacillus cereus group
MEERNEQVVEEVKEAQVEEAVTPENSEETVEEKSEAALLQEKVDELQAKLTETEGRTLRLQADFENYKRRVQMDKQAAEKYRAQSLVSDILPALDNFERAMQVEATDEQTKSLLQGMEMVHRQLLEALNKEGVEVIEAVGKQFDPNEHQAIMQVEDSEFESNAVVEEFQKGYKLKDRVIRPSMVKVNQ
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Q81LS1
B3RNT0
QTRT2_TRIAD
Queuine tRNA-ribosyltransferase domain-containing protein 1
Trichoplax
MNFKVRVIDLAGSCCRLGALQFGTKVVETPGCLIYNRSGVVPHLTPDILETLDNVPPIMHTPLASIIEEPGLIKLRGYGKGLASFIGYKDNSVYISASDYQGEAMYQYNENKSISVWTKTGRTKVTPDDYSKFVEVCRPSWYQSLCDTVPANASIKRTRKSVDRTLEFLDQCLKYREKHDSLKTSELWAAVEGGGLVDERQRSAKESATRPVFGFTLEGFGSDQMNVETIFELLPLTTQNLPVEKPRLIHAIGSPTINSLSRSSKLTEVEEENGNDSSNDQDRTATFSLLNLREDRYNEDFSPLVSGCKCFVCSNHTRAYIHHLIINNEMLGGVLLMTHNLFQYIEFFRCIRTSLKNNKWKELRKLFDA
Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
B3RNT0
A7FZD1
RLMH_CLOB1
rRNA (pseudouridine-N3-)-methyltransferase RlmH
Clostridium
MNISIISVGKIKEKFLKAAIDEYSKRLSKYCKLNIIEVADEKTPDNASLKEENIIKEKEGNLILKHIKDNSFVIALDLKGKSITSEEFSDLIENCRLTGNSTIAFVIGGSLGLSQQVLSRANYKLSFSKMTFPHQLFRVMLLEQVYRAFRILCREPYHK
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
A7FZD1
Q02ET8
DTD_PSEAB
Gly-tRNA(Ala) deacylase
Pseudomonas
MKALLQRVGAARVEVGGEIVGSIDRGLLVLVGVEPEDGERCAAKMLHKLLNYRVFGDDEGKMNRSLLDVQGGLLLVSQFTLAANTRSGLRPSFSSAAPPAQGETVFEHLVKLAREAYPQVATGRFGADMQVHLVNDGPVTFLLES
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.
Q02ET8
Q5UAW9
GP157_HUMAN
G-protein coupled receptor 157
Homo
MQPSPPPTELVPSERAVVLLSCALSALGSGLLVATHALWPDLRSRARRLLLFLSLADLLSAASYFYGVLQNFAGPSWDCVLQGALSTFANTSSFFWTVAIALYLYLSIVRAARGPRTDRLLWAFHVVSWGVPLVITVAAVALKKIGYDASDVSVGWCWIDLEAKDHVLWMLLTGKLWEMLAYVLLPLLYLLVRKHINRAHTALSEYRPILSQEHRLLRHSSMADKKLVLIPLIFIGLRVWSTVRFVLTLCGSPAVQTPVLVVLHGIGNTFQGGANCIMFVLCTRAVRTRLFSLCCCCCSSQPPTKSPAGTPKAPAPSKPGESQESQGTPGELPST
Orphan receptor that promotes neuronal differentiation of radial glial progenitors (RGPs). The activity of this receptor is mediated by a G(q)-protein that activates a phosphatidylinositol-calcium second messenger.
Q5UAW9
Q9C469
GRT1_SCHPO
Zinc finger protein grt1
Schizosaccharomyces
MVLSKRPVRISKACENCRKRKVKCSGGDVCFECQKYNENCVYRQFYRKIKRLKYNNDNSKIDNFSNEQMNIPEFISVRNLNDDSSSIEFFGPASNISFVNQLNHYLRKAERNGYDFLSEGQNDITPEEERKGLEKFGMKLMVLKDNANNFDFSLSNITTEKMNGLLIAYLETWHIPCPIFKAEDLFNLSVRTWKNPSASVHDKALLYLILSIGSAASYFDLQSNSSTLPLARGFFNLALRTVPHIFTELSLDAIRIVFFMSVSAGNLGDTALSYLYSGTAVRMSLAIGLHKCKNFSNDLSDKYQNIRLWVSVWQWEGYWSFCVGRPSCSRQDIPIPAVPNEAFSFSGYGEHGRFLINHEHMRLRVFFSSCCSKIQSEIYSTNRNLLSVLQTVEQISKEVDKEYFSSTNHQLIRSEIGEYCKTLDINSCREWFWIRIYYLYLKLMIFRPFLIFLAYVNISKTSAPDDIIEGLKRGSDQCVQEAIDISKFIVQLNRKVRMLQPIFFICTYLESACTVLLFYIASNSAKIQGQLATEIWAVLRDTCSFLQGSSGPYVGSVSTIAKDALESLNNILVSKKYQDNSVNNTYFDKVMQHVLVHSPAFDDSSDPKFETNRSETPTQYTLDDSANDELMIPDLQGFWEQTLDWINN
May be involved in the facilitation of anaphase progression in mitosis.
Q9C469