accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
Q9UZP8
|
GCST_PYRAB
|
Glycine cleavage system T protein
|
Pyrococcus
|
MAKRVHLFDWHKEHAKKIEEFAGWEMPIWYSSIKEEHLAVRNAVGLFDVSHMGEIYFRGKDALKFLQYVTTNDISKPPAISGIYTLVLNERGAIKDETLIFNMGNNEYLMICDSDAFEKLYAWFTYLKKTIEQFTKLDLEIELKTYDIAMFAVQGPKARDLARDLFGIDINEMWWFQARWVELDGIKMLLSRSGYTGENGFEVYIEDANPYHPDESKRGEPEKALHVWERILEEGKKYGIKPAGLGARDTLRLEAGYTLYGNETKELQLLSTDIDEVTPLQANLEFAIYWDKDFIGKDALLKQKERGLGRKLVHFKMVDKGIPREGYKVYANGELIGEVTSGTLSPLLNVGIGIAFVKEEYAKPGIEIEVEIRGARKKAITVTPPFYDPKKYGLFRET
|
The glycine cleavage system catalyzes the degradation of glycine.
|
Q9UZP8
|
Q94819
|
TE95_TETTH
|
Telomerase component p95
|
Tetrahymena
|
MSRRNQKKPQAPIGNETNLDFVLQNLEVYKSQIEHYKTQQQQIKEEDLKLLKFKNQDQDGNSGNDDDDEENNSNKQQELLRRVNQIKQQVQLIKKVGSKVEKDLNLNEDENKKNGLSEQQVKEEQLRTITEEQVKYQNLVFNMDYQLDLNESGGHRRHRRETDYDTEKWFEISHDQKNYVSIYANQKTSYCWWLKDYFNKNNYDHLNVSINRLETEAEFYAFDDFSQTIKLTNNSYQTVNIDVNFDNNLCILALLRFLLSLERFNILNIRSSYTRNQYNFEKIGELLETIFAVVFSHRHLQGIHLQVPCEAFQYLVNSSSQISVKDSQLQVYSFSTDLKLVDTNKVQDYFKFLQEFPRLTHVSQQAIPVSATNAVENLNVLLKKVKHANLNLVSIPTQFNFDFYFVNLQHLKLEFGLEPNILTKQKLENLLLSIKQSKNLKFLRLNFYTYVAQETSRKQILKQATTIKNLKNNKNQEETPETKDETPSESTSGMKFFDHLSELTELEDFSVNLQATQEIYDSLHKLLIRSTNLKKFKLSYKYEMEKSKMDTFIDLKNIYETLNNLKRCSVNISNPHGNISYELTNKDSTFYKFKLTLNQELQHAKYTFKQNEFQFNNVKSAKIESSSLESLEDIDSLCKSIASCKNLQNVNIIASLLYPNNIQKNPFNKPNLLFFKQFEQLKNLENVSINCILDQHILNSISEFLEKNKKIKAFILKRYYLLQYYLDYTKLFKTLQQLPELNQVYINQQLEELTVSEVHKQVWENHKQKAFYEPLCEFIKESSQTLQLIDFDQNTVSDDSIKKILESISESKYHHYLRLNPSQSSSLIKSENEEIQELLKACDEKGVLVKAYYKFPLCLPTGTYYDYNSDRW
|
Ribonucleoprotein DNA polymerase that catalyzes the de novo synthesis of telomeric simple sequence repeats. Subunit p95 contains some or all of the template-independent primer DNA-binding site termed the anchor site.
|
Q94819
|
P0CS81
|
TRMB_CRYNB
|
tRNA(m7G46)-methyltransferase
|
Cryptococcus neoformans species complex
|
MEAGPSTASPGVSVSPAPALTAGEVQLLKVPQKRFYRQRAHANVFIDHELDYPKRPELMDWSTHYPAYFSQPNEDGTITQGEKKVEWADVGCGFGGLLMALAPLFPEKLMLGMEIRTSVTKYVTDRIAATRQAQSLLPADSVDTKPGGYQNVSVIKANSMKHMPNFFAKGQLEKIFFLFPDPHFKNRKHKARIITPALLAEYAYVLRPGGILYTVTDVKDLHEWMAHHLHAHPLFEYIPTETLSDDPILEAARTATEEGQKVERNKGDKWVACFRRKEDPKEEDED
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
P0CS81
|
Q332T7
|
RK22_LACSA
|
50S ribosomal protein L22, chloroplastic
|
Lactuca
|
MLNKRTTEVYALGQHISMSAHKARRVIDQIRGRSYEETLMILELMPYRACYPIFKLVYSAAANASFNMGSNEVNLVISKAEVNEGTIVKRLKPRARGRSFAIQKPTCHITIVMKDISLDEYIDTDSITWSQKPKSKKKHTTMSYYDMYSNGGTWDKK
|
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
|
Q332T7
|
Q8BJ34
|
MARF1_MOUSE
|
Meiosis arrest female protein 1
|
Mus
|
MEGKGTENPCSRTLGWFHQDNDAKPWLWKFSGCFSRPEQTLPLSSQTKEYMENKKAAVELKDIPSPLHVGSKFFPAVPLPDIRSLQQPKVQLSAIPKVSCCAHCPNEPSTSPMRFGGGSGSSGGSGSLIHTGSLLDSPSTGTVTCQVGSGFAFQSVSSLQNASTRNNLVGLSSDFPSMCVESNLPSCKHLSCCGKLHFQSCHSNVHKLHQFQNLQGCASAGYFPCSDFPSGAPGHLEERLSHSELTPHLCTNSLHLNVAPPVCLKGSLYCEDCLNKPARNSIIDAAKIWPNIPPPSTQPAPPAIPVCNGCGTKGMEKETSLLLATSLGKTASKFGSPEVAVTGQVLETLPPIGVFWDIENCSVPSGRSATTVVQRIREKFFRGHREAEFICVCDISKENKEVIQELNNCQVTVAHINATAKNAADDKLRQSLRRFANTHTAPATVVLVSTDVNFALELSDLRHRHGFHIILVHKNQASEALLHHANQLIRFEEFISDLPPRLPLKIPQCHTLLYVYNLPANKDGKSISNRLRRLSDNCGGKVLSITGCSAILRFINQDSAERAQKRMENEDVFGNRIIVSFTPKHREFFEAKSSNAIADKVKSPKKVKNTKLCLIKDTSEQSPSVKAMPGKVLQANSGSATKTTNIKSLQELCRMESKSGNRNSDHQQGHGRLAALPNSGPTASVPIVKNTGVTEPLYRSSQKKENPSSQSTVNSPVEKKKREETVFQVSYPSAFSKLIASRQVSPLLTSQSWSPRASPLAFNIANPSSGADCPDPFANGVDIQVSNVDYRLSRKELQQLLQEAFSKHGQVKSVELSPHTDYQLKAIVQMRNLHEAICAVNSLHRHKIGSKKILVSLSTGAANKSLSLLSTETMSILQDAPACCLPLFKFIDIYEKKYGHKLNVSDLYKLTDTIAIREQGNGRLVCLLPSNQARQSPLGSSQSHDGSSSNCSPVLFEELEYHEPVCKQHCSNKDFSELVFDPDSYKIPFVVLSLKVFAPQVHSLLQTHQGTVPLLSFPDCYAAEFGDLEITQDSHKGVPLEHFITCIPGVNIATAQNGVKVVKWIHNKPPPPNTDPWLLRSKSPVRNPQLIQFSREVIDLLKTQPSCILPVSNFIPSYHHHFGKQCRVSDYGYSKLIELLEAVPHVLQILGMGSKRLMTLTHRAQVKRFTQDLLKLLKSQASKQVIVRDFSQAYHWCFSKDWDVTEYGVCDLIDIISEIPDTTICLSQQDDDMVICIRKRERTQDEIERTKQFSKDVVDLLRHQPHFRMPFNKFIPSYHHHFGRQCKLAYYGFTKLLELLEAIPEILQVLECGEEKILTLTEVERFKALAAQFVKLLRSQKGNCLMMTDLFTEYAKTFGYTFRLQDYDVSSVSALTQKLCHVVKVADMESGKQIQLINRKSLRSLTAQLLVLLMSWEGDAYLPVDELRRHYETTHSTPLNPCEYGFMTLTELLKSLPYLVEVCTNDKAEEYVKLTSLYLFAKNVRSLLHTYHYQQIFLHEFSMAYNKYVGETLQPKTYGYSSVEELLGAIPQVVWIKGHGHKRIVVLKNDMKNRLSSFDLFSVNHEDQPAVSRQILAVPESHLASELQLRTGTGPSQMEQELLHLASSSPVDLLCAPVPSCLPSPQLRPDPVILKPADLIQFEEHPQEPLGVLVLNQEEKSEVPLPVQKGNLSCDSSPSSPAASPAPPGPSSEAPRPLFSKDAVESPAKKQPKNRVKLAANFSFAPVTKL
|
Essential regulator of oogenesis required for female meiotic progression to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Probably acts via some RNA metabolic process, equivalent to the piRNA system in males, which mediates the repression of transposable elements during meiosis by forming complexes composed of RNAs and governs the methylation and subsequent repression of transposons. Also required to protect from DNA double-strand breaks.
|
Q8BJ34
|
Q5R0C0
|
LOLA_IDILO
|
Outer-membrane lipoprotein carrier protein
|
Idiomarina
|
MKAVVFAMVMAVSFNVFASGDESDKQALQSLLKQTQSLSAEFEQQVKDEQGEVLQTLSGTLKLKRPANLYWHTKEPDESVMVANGKKVWYYNPFVEQVTIYAQQDMVDDSPLLLVLNSNGNQWQNYNVSFRDNRYFVEHQTNGSKLELRFTDEKLTEITMVQAQGERTELMLNNVALNETISDEQFVFDVPADVDVDDQS
|
Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).
|
Q5R0C0
|
A7IID0
|
EFP_XANP2
|
Elongation factor P
|
Xanthobacter
|
MVKVIASSLRKGNVVDIDDKLYVVLTAENIHPGKGTPVTQLDMRRISDGVKISERYRTTEQVERAFVEDRPHTFLYEDSDGYTFMNPENFDQVIVTKDVMGDSAVYLQEGMECMLSTHNGVPIAIELPARVTLEIVDTEPTVKGQTASSSYKPAKLSNGVRTMVPPHISAGTRVVIMTADNSYVERAKD
|
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
|
A7IID0
|
Q03298
|
PHHY_ACIAD
|
4-hydroxybenzoate 3-monooxygenase
|
Acinetobacter
|
MQTMKTKVAIIGSGPAGLLLGQLLYKAGIEHVIVEQRSADYVASRIRAGILEQVSVDLLEQAGVDQNLKEKGLPHSGIEILTNGQKFRVDLSALTQGKQVTVYGQTEVTKDLMQAREQAGLCSFYESNDVQIHDFYNAPKVTFESNGTHYQIECDFIAGCDGYHGVCRASVPQDKIKTFEKVYPFGWLGVLADVPPVADELIYVQSERGFALCSMRSETRSRYYIQVPLTDHVENWSDDQFWEELKNRLDPESCEKLVTGPSIEKSIAPLRSFVTEPMRFGKLFLAGDAAHIVPPTGAKGLNLAASDIAYLSSALIEFYTQGSEQGIDQYSEKCLQRVWKAERFSWWMTHLLHRFETESEFDHKIKQAELSYILGSTAGQTTLAENYVGLPYEIKSLDYLKHAS
|
Catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced FAD with oxygen to form a hydroperoxide, which then oxygenates p-hydroxybenzoate.
|
Q03298
|
A2BZG2
|
SYA_PROM1
|
Alanyl-tRNA synthetase
|
Prochlorococcus
|
MEKSSSSSINPPSLSGDEIREAFINFFVQHNHQKLASSSLIPDDPTVLLTIAGMLPFKPIFLGLKESSTPRATSSQKCIRTNDIENVGRTARHHTFFEMLGNFSFGDYFKKEAIQWAWELSTEVFRLNPQNIVISVFKEDLEAEQIWKEVVGVDANRIIRMGAADNFWSSGATGPCGPCSELYFDFKPELGSDEIDLEDDSRFIEFYNLVFMQYNRDLEGNLEPLANCHIDTGMGLERMAQILQKKSNNYETDLIFPLIKAAALLAQLEYETTNKKNKTSLKIIGDHCRAVTHLICDGVSASNLGRGYILRRLIRRMIRHGRLVGIVQPFLPQLAEMAIELMKNAYPQLLEKKKIILNELKIEESRFLETLERGEKLLAEITSHECDLISGAQAFELYDTYGFPLELTEEIANEKGISVDINGFENEMAKQRKRAKEASVSIDLTEEGSIEREISLFDETRFEGYEKLETTSTVIGIFKNNESVKQAVQGDLVKIIVNRTPFYAESGGQIGDKGIITSQDLEVSVENVRKKKNIFIHSGIVNTGVLEINSSVQMNVTPSFRQRTTSNHTATHLLQSALKLSIDSSVSQRGSLVSNHRLRFDFNAPKPLTIKELEDMEVRINQWINEDHPIQIKTMPIKEAMAAGALAMFGEKYGDVVRVVDVPGVSMELCGGTHVTRTSQLGTFKIINETGIASGIRRIEAIAGPSVLDYFNERDLVVKELSKSFKVQSYEIVERVSSLQLELKDKTKELIKVKNDLALAKALGLASYAKSVGKSKLLIRRLDGVDGSGLQSAASSLIDHLGKYSAVIFGGIPNQEIDNKLVFVAAFSPDLVSDGLHAGKFISGVAKMCGGGGGGRPNLAQAGGSQPQSLDLALEKANENLTQQLS
|
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.
|
A2BZG2
|
Q9NRP4
|
SDHF3_HUMAN
|
Succinate dehydrogenase assembly factor 3, mitochondrial
|
Homo
|
MPGRHVSRVRALYKRVLQLHRVLPPDLKSLGDQYVKDEFRRHKTVGSDEAQRFLQEWEVYATALLQQANENRQNSTGKACFGTFLPEEKLNDFRDEQIGQLQELMQEATKPNRQFSISESMKPKF
|
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit SDHB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF1.
|
Q9NRP4
|
A5FRY5
|
RL14_DEHMB
|
50S ribosomal protein L14
|
Dehalococcoides
|
MVQQYTRLNVADNTGAKKIMCINVLGGSHKIQAKVGDVIVAAVKKSSPDAQAKSGTVVKAVVVRITKPYARPDGSYIKFDDNAAVILNDKMEPKGTRIFGPVARELRDKKFTKILSLAPEVL
|
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
|
A5FRY5
|
B9KIX1
|
NTPP_ANAMF
|
Nucleotide pyrophosphatase
|
Anaplasma
|
MLKIEGLVLASSSKYRLALLEQIGVVPGEVVSPNIDESLLKGELPRRYCMRMARTKADAVAALRSDKFVLGADTVAYCGKRVLSKTESEDCAVRYLEMLSGRRHRVCTSVCLRSPGGIVHERSVVSVVKFKSMSKGEIEYYISSGQWRGKAGGYGIQGFAGALISWIQGSYSSIAGLPLHETYCLLCGYFDLKHIP
|
Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
|
B9KIX1
|
Q73M28
|
VATA_TREDE
|
V-ATPase subunit A
|
Treponema
|
MTKTKGKVVGINGNMISVSFEGLVTLNEVGYVEVGSKKLKSEVIRIRGEVAQLQVFEITKGIKVGDIVEFTGDLLSVELGPGLLGQVYDGLQNPLPELAEQAGYFLERGIYLNALSRTAKWHFTPSAKEGDTLKRADLLGTVPEGSFTHRIMIPFNMYGTYKLKSIKPEGDYTVDDTIAEVTDERGNVIPLTMSFKWPVKRAIDCYAERLKPTETLVTKMRTMDTFFPVAKGGTYCIPGPFGAGKTVLQHATSRNADVDIVIIAACGERAGEVVETLTEFPELKDPKTGRTLMERTIIICNTSSMPVAAREASVYTGVTLAEYYRQMGLDVLLLADSTSRWAQALREMSGRLEEIPGEEAFPAYLESYIAAFYERAGIVRLSDGSKGSVTIGGTVSPAGGNFEEPVTQATLKVVGAFHGLSRERSDARKYPAIHPLDSWSKYPSVLPLEQVKYGRSFLRRGTEVEQMMKVVGEEGTSIEDFIIYLKGDLLDAVYLQQNSFDKVDDAVSVERQQHIYNILIEILGTSFKFVSKDEARSYFSKLKLMFIDYNYSPWGSDAFKSHEDGIKKHIAEKADSLDERAKKLLKQAV
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit.
|
Q73M28
|
Q4ZWE0
|
ENO2_PSEU2
|
2-phosphoglycerate dehydratase 2
|
Pseudomonas syringae
|
MKTQIQAIHAREILDSRGNPTVEVDVTLECGAMGRASVPSGASTGAHEAVELRDKDTQRYSGKGVLKAVSNVNTEILESLRGMNAIDQEQIDHLMIKLDGTSDKSRLGGNAILGVSLAVARAAASALNLPLFQYLGGEQAARMPVPMFNILNGGVHANWQGPDFQEFMIAPTGAGSFKEALRWGSEVYHELKAVLKDAGYSTAVGDEGGFAPALKKNSDAIELIIKAIERAGYTPGSQIEIAIDPASSGFYENGLYHLRSEGRKVDAQELINLYSSWVDKYPIAVLEDGLAEDDWSGWKLLNAALGDRIELVGDDLFVTNVERIQRGITENVANAVLIKPNQIGTLTETKAAIEMAYGANWGAMVSHRSGETVDSSIADLTVAMGTGHLKTGAPCRGERVEKYNQFLRIEEDLGSRAFYAGHDAFVR
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
Q4ZWE0
|
O07838
|
DCTM_RHOCA
|
C4-dicarboxylate TRAP transporter large permease protein DctM
|
Rhodobacter
|
MSALIIFGLLIALMLTGMPISISLGLTVLTFLFTMTQVPIDTVALKLFTGIEKFEIMAIPFFILAGNFLTHGGVAKRMINFATAMVGHWHGGLGLAGVIACALFAAVSGSSPATVVAIGSVILPAMVNQGFPKQFGAGVITTSGALGILIPPSIVMVMYAVATSGMVVTGPDGQPVSSASVGELFMAGVVPGLMLAGFLAFTTWNRARKFGYPRLEKASLRQRWTAFREAAWGLMLIVVVIGGIYAGIFTPTEAAAMSAVYAFFISVFVYKDLTLRDVPRVLLSSANMSAMLLYIITNAVLFSFLMAHEGIPQALGEWMVNAGLSWWMFLIIVNILLLAAGNFMEPSSIVLIMAPILFPVAVRLGIDPVHFGIMIVVNMEVGMCHPPVGLNLYVASGITKMGITELTVAVWPWLLTMLAFLVLVTYVPAISLALPNLLGM
|
Part of the tripartite ATP-independent periplasmic (TRAP) transport system DctPQM involved in C4-dicarboxylates uptake.
|
O07838
|
A1K962
|
GLPK_AZOSB
|
Glycerokinase
|
Azoarcus
|
MSYVLALDQGTTSSRAMVFDAAGRVRSVARRDFTQSFPQPGWVEHDPAEILRSQFDCARDALADAGLRAGQLAAIGIANQRETTVLWERASGRALAPAIVWQDRRTAAKCAELRARGVWSEALRERTGLELDPYFSATKLAWLLDHVPDARRRAEAGELAFGTVDSWLVWHLSGGRLHVTDHGNAARTLLLDIHRRDWDDALLALFDIPRAVLPRLVDSIGVCGESDPAVLGAAVPIAGIAGDQQAATFGQHCFAPGMAKNTYGTGCFLLMNTGATPVKSSHRLLSTVGWTQGAAHTYALEGSIFMGGATVQWLRDGLGLIREAAEVEALAARVPDSGGVVLVPAFTGLGAPYWDAAARGALFGLTRGSGPAHIARAALDAIALQTDDLVRAMTADGAGPLHELRVDGGAAANNLLMQLQADMLGVAVVRPRMLETTALGAACLAGIGAGVWRDTDALAPHWQIDRVFTPAWSEDQRGAVRARWADAVARSRAWAA
|
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
|
A1K962
|
P0DUH2
|
HSTX9_HAESL
|
Peptide HSTX-IX
|
Haemadipsa
|
MKTLLVFLLLAILVAVLIGNSQVEACNDNAQCGPLGACIMGYFLPIG
|
Leech salivary gland peptide with unknown function.
|
P0DUH2
|
D7UPN2
|
ACTS2_ALTAL
|
ACT-toxin biosynthesis protein S2
|
Alternaria alternata complex
|
MLTRRALVVQSQGEVQVEEIPLPTLRDEYITVKVKAVALNPGDWKMLYGPHATPGSILGCDYSGVVEKVGRAVNALLTPGDRVAGFAFGGCPYNHDEGGFASYVTAKGDIQAKLSDSISFEDAATLGVGITTVGQAMYQALGLPLPPAIIQEAASILVYGASTATGTLAVQYAKLTGLKVFATASPHNFDLLKKLGADEVFDYRDPECGAKIRTVTNGLLSLVFDTISEGSSPAIWAAAMGAKGGKYTALLPIKNFPRSDVKVTTILGYTALGVKVSDHLPANQKDFEFSAKFWKLSQHLLEKEKIKTHPVGVRQGGIDAIPQGLQDLKNGRVSGVKLVYKID
|
Trans-enoyl reductase; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) ACT-toxins responsible for brown spot of tangerine disease by the tangerine pathotype which affects tangerines and mandarins . ACT-toxins consist of three moieties, 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA), valine and a polyketide . ACT-toxin I is toxic to both citrus and pear; toxin II the 5''-deoxy derivative of ACT-toxin I, is highly toxic to pear and slightly toxic to citrus . On cellular level, ACT-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment . The acyl-CoA ligase ACTT1, the hydrolase ACTT2, the enoyl-CoA hydratases ACTT3 and ACTT6, and the acyl-CoA synthetase ACTT5 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety . The exact role of each enzyme, and of additional enzymes identified within the AF-toxin clusters have still to be determined . On the other hand, ACTTS1 to ACTTS4 are specific to the tangerine pathotype . The function of ACTTS3 is to elongate the polyketide chain portion of ACT-toxin that is unique to this toxin . The enoyl-reductase ACTTS2 might complement the missing enoyl-reductase (ER) domain in ACTTS3 in the synthesis of the polyketide portion of ACT-toxin . The roles of the nonribosomal peptide synthetases-related proteins ACTTS1 and ACTTS4 have also still not been elucidated .
|
D7UPN2
|
A8H3W9
|
PROQ_SHEPA
|
RNA chaperone ProQ
|
Shewanella
|
MESTEKLTDTNAILAYLYETFPLCFIAEGETKPLKIGLFQDLAERLADDSKVSKTQLRIALRRYTSSWRYLKCVKAGAQRIDLDGNACGELEQEHIDHAAATLKESQDKAKAKRVAQAKSANPAAKTAKKPVKKPVAKRPKPAQSSKPAKEPVVAENLTPAVLTELKPNQRVNVKLGKAPVAGVILDIKKEDVQVQLDSGLTIKVRAEHILL
|
RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities.
|
A8H3W9
|
Q6FT66
|
NMD4_CANGA
|
Nonsense-mediated decay protein 4
|
Nakaseomyces/Candida clade
|
MNQYNFILDASAFEKGLGNVKRWCQSNGNVDGKKNVYLRFYVPTFTLQELNFLQYRHKSFSAKEALKFIDKLETATSEGQRNHVVIGRKKEEDLRSDLELFIEFPDILDAVTWPTVLSYCTEGQATIDSLNKLPKRFKILLKSCVYKCHLEDDDRIRWILVTEDPQVRKIASQCHIPWCSIVDADSIISKDMNDRSFRDSEKFNSMMLKRGVAKSENMDGKEVIKTNFDQTVYATRGSGKLWTP
|
Involved in nonsense-mediated decay of mRNAs containing premature stop codons.
|
Q6FT66
|
P17120
|
BIMC_EMENI
|
Kinesin-like protein bimC
|
Aspergillus subgen. Nidulantes
|
MAGPQRATSGLPTRRTTTRQPTRRAGSAIPERQTSTASPAVSTKTAAISRTRTLKSPGEPASVLAKRKERDIEREINEDTSIHVVVRCRGRNEREVKENSGVVLQTEGVKGKTVELSMGPNAVSNKTYTFDKVFSAAADQITVYEDVVLPIVTEMLAGYNCTIFAYGQTGTGKTYTMSGDMTDTLGILSDNAGIIPRVLYSLFAKLADTESTVKCSFIELYNEELRDLLSAEENPKLKIYDNEQKKGHMSTLVQGMEETYIDSATAGIKLLQQGSHKRQVAATKCNDLSSRSHTVFTITVNIKRTTESGEEYVCPGKLNLVDLAGSENIGRSGAENKRATEAGLINKSLLTLGRVINALVDKSQHIPYRESKLTRLLQDSLGGRTKTCIIATISPARSNLEETISTLDYAFRAKNIRNKPQINSTMPKMTLLREFTAEIEKLKAELIATRHRNGVYMSVESYEEMKMENESRRIISEEQRAKIESMESSLRHKVQELLTLTSKFNDLKKDNDDTLAALCSTNDVLQQTDIVLQNTRAQLEEEEMLRCAHEETEHQLQDVGKGLISTLGQTVEDINSLQSKLDRKAELDATNAELWRASSTEVSDVTKRIDQRVEAFQTRHAKLLETTSVKVNEFIATEISNIERTRSDLSEYNRSLDAACNNAKAETSSAHEDMNNVLEEIKDLREEVKSKVGEGLNGLSAAAARISEEVIGEFTQLHSQLHTSFNNLGKDLKSIFETMATHLSEQKNEINRLRAELQSSNRQNIETTHKASAHLAQAIEEEHVAAEAEREILMSQIKALVEESRQKQFARLRAKIDGVRTEISASGDMLEQATTQHDRQIDEWVFKSEQFAKDVNASKDEIRTKLQNDWEAFDQRNSTIRKATESVHKETVRIVDVQVDDMGRQMEALDDFVAKARSQNGRYRDAHIATLDTIATGVRDSYSSIEGRVENLTGRMNQFQQEATHHHATLEESIAPLSNDVRKPLTDLSSSFQNRSLEEYVATGVTPKKRKYDYISVLPSTESHEVLKSRLRTTKEMEVLPFNSDDQLSGPSSSPGGSPSKGFVYNDVEDEVGTHAPTVTNVNPSNTGLREVDANVAARPLVYSTGEKSTDQDGSPVVSPDSATEAEGMNGPPSKRRRSNSVVADTKLPNKMLARRMAGMMEGRENVPPPGISNGRRLRGRPSP
|
Important role in mitotic dividing cells. Microtubule motor required for spindle body separation.
|
P17120
|
Q9MUU4
|
RK14_MESVI
|
50S ribosomal protein L14, chloroplastic
|
Mesostigma
|
MIQAQSYLNVADNSGAKKIMCIRVLGGSQRKYAAIGDVIIGVVKDSVPNMSLKKSEVVRAVVVRTCKGIRRENGMTIRFDDNAAVVINKDGNPKGTRVFGPVARELRDRNFTKIVSLAPEVL
|
Binds to 23S rRNA.
|
Q9MUU4
|
E7CLN5
|
SCX7_RHOJU
|
Putative beta-neurotoxin RjAa7
|
Rhopalurus
|
KEGYPVGRDGCKISCVINNNFCKVECQAKWRQSDGYCYFWGLSCYCTNLPDDAQVWDSSTNKCGG
|
Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
|
E7CLN5
|
Q5HM25
|
RPOA_STAEQ
|
Transcriptase subunit alpha
|
Staphylococcus
|
MIEIEKPRIETIEVSEDAKFGKFVVEPLERGYGTTLGNSLRRILLSSLPGAAVKYIEIEGVLHEFSAVDNVVEDVSTIIMNIKKLALKIYSEEDKTLEIDVKDEGEVTASDITHDSDVEILNPELKIATVSKGGHLKVRLVANKGRGYALAEQNNTSDLPIGVIPVDSLYSPVERVNYTVENTRVGQSSDFDKLTLDVWTNGSITPQESVSLAAKIMTEHLNIFVSLTDEAQNAEIMIEKEEDQKEKVLEMSIEELDLSVRSYNCLKRAGINSVQELADKSEADMMKVRNLGRKSLEEVKYKLEDLGLGLRKED
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q5HM25
|
Q1QYD9
|
BIOD_CHRSD
|
Dethiobiotin synthase
|
Chromohalobacter
|
MTTYFVTGTDTDAGKTLVASGLLALARRRGLTTLGLKPVASGCESTTEGLRNIDALTLQAQSMPTPPYATLNPYAYAPAIAPHLAARRAGRIPTLDALVAHVADPLAEKRDLTLIEGAGGWRVPLNDDEDLAGLAVRLELPVILVVGLELGCLNHARLSAEAIRADGLPLAGWVGNLIDPGLSFDEVADEACYRDNLATLERTLEAPCLGIVPRLAAATPDARAHAAADYLTLPGDA
|
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
|
Q1QYD9
|
P14864
|
EF1A2_MUCCL
|
Elongation factor 1-alpha
|
Mucor
|
MGKEKTHVNVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYNVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGTGEFEAGISKDGQTREHALLAFTLGFRQLIVAINKMDTTKWSQDRYNEIVKEVSGFIKKIGFNPKSVPFVPISGWHGDNMLDESTNMPWFKGWNKETKAGSKTGKTLLEAIDAIEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGTIKAGMVVNFAPAAVTTEVKSVEMHHETLTEGLPGDNVGFNVKNVSVKDIRRGNVCSDSKNDPAKESASFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFSELIEKIDRRSGKKMEDSPKFVKSGDSAIVKMVPSKPMCVEAYTDYPPLGRFAVRDMRQTVAVGVIKAVEKVDKAGKVTKAAAKASKK
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
P14864
|
Q03U68
|
SYE1_LEVBA
|
Glutamyl-tRNA synthetase 1
|
Levilactobacillus
|
MSENSTVKKNVRVRYAPSPTGFLHIGNAQSALFNYLFARHYHGTMVLRIEDTDVKRNVPHGEDSQIDNLHWLGIDWDEGPDKPNPKYAPYHQTERQDLYHRYITQLLDQGLAYKDYATEDELTTMRDQQRAAGEAPHYDGRWYGRSVADQQAAEARGLKPSIRLHLPANHEYAWDDIIKGHVAFNSDNMGGDFIIEKSNGMPTYNFAVVIDDYLMDITDVLRGDDHIANTPKQIAVYEALGLKHPNFGHITLIYNPKTRKKLSKRDKETLQFISQYKNQGYLSEAIFNFIAFLGWSPEGEDELFSREELIERYDPARMSKSPAYFDQSKLDWINAAYIKRLDLDDMTDRVLELVDEGQTDVARQVKALQLPDLRTLTSQVCKIYQTEIHQLSEIMDKVLFYVTILQEPLDYDQLRQFDRTATLAVLTAFRKHVQALPVDVATPDFKKMIQTVSQETGVTGRNLYFPLNVAFTGDHSAPQIDEVLRLFANSTIIELLTKAIAHV
|
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
|
Q03U68
|
B5QWY1
|
RHAD_SALEP
|
Rhamnulose-1-phosphate aldolase
|
Salmonella
|
MQNITDSWFVQGMIKATSDAWLKGWDERNGGNLTLRLDEADIAPFATNFHEKPRYIALSQPMPLLANTPFIVTGSGKFFRNVQLDPAANLGVVKIDSDGAGYHILWGLTHDAVPTSELPAHFLSHCERIKATHGKDRVIMHCHATNLIALTYVLENNTALITRKLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAEVLVKIYSMGGMKQTITREELVALGKRFGVTPLASAVALY
|
Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
|
B5QWY1
|
Q8XVK1
|
ZAPD_RALSO
|
Z ring-associated protein D
|
Ralstonia
|
MILYEYPFNERIRTLLRLEDLFERLDFFLTQEHPLQHHVALTTLFEIVDVAGRADLKSDLLKELDRQRQTLTVLRSNPQIDQEALDAVIAELETASGNLTATHGKAGQLIADNEWLTSIRSRAIIPGGTCEFDLPAYFAWQHHPGERRRADIVKWAQPLVPLRDATMIVLRLLRESGQSGKVIANAGSYQQMLSGRIYQLMQVRLDDVALGFIPEISANKYMLWVRFTQQDGDLRPKPVDADIPFQLKLCNF
|
Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity.
|
Q8XVK1
|
Q5F8V5
|
EX7L_NEIG1
|
Exodeoxyribonuclease VII large subunit
|
Neisseria
|
MSDFFHSDVLSVSELNAFAKSILENHLAGLWIAGEVSNLTRAASGHYYFSLKDSRAQVRCAMFKGAAARLAQPLKEGDHIEVAGKISIYEARGEFQITVNEVRLKGLGQLYEAYERLKAQLQAEGAFAAERKKPLPVRPQCIGIVTSLAAAALRDVVTTLKRRAPEIPVIVYPAAVQGAGSGFQIAQAIKTASQRAECDVLIVCRGGGSIEDLRAFNEEPVVRAIEACTIPVVSGVGHETDFTLADFVADVRAPTPTGAAELVSPNRQESLHRLVQAQGRLKTVLEQRYFDASQKLDWLARQIRHPRQKLDEQRASIGKLAQTLSYSMTQNLRAHTARFERQTQALQHCRPDVSVYRQDIVRLQTALPAAFSRLLARRRQSLTAQAALLEAVSPQHILERGFSVVKNTRGQVIRNADVLKQGQKLHITFSDGETDVRVSKEQGQQDLFDCI
|
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
|
Q5F8V5
|
Q0HSW6
|
DXS_SHESR
|
1-deoxyxylulose-5-phosphate synthase
|
Shewanella
|
MSLDISQFPVLAQANTPNELRQLPQALLPQLADELREFLLKSVGMSSGHFASGLGTVELTVALHYVYNTPFDRLIWDVGHQAYPHKILTGRRDRMHTIRQKNGLHPFPWREESEYDTFSVGHSGTSISAALAMAVAAEKEQAGRKVVAVIGDGAMTGGMVFEAMNHAGDLHNDMLMVLNDNEMSISENVGALNNHLAQLMSGRLYTTIRESSKKVLKGMPVIKEMAKRTEEHLKGMVVPGTLFEELGFNYIGPIDGHDVDALVETLRNMRSLKGPQVLHIMTKKGRGYEPAEKDPIGWHAVPKFDPSQFKKPATKPGLPTFSQVFGKWLCDIAEQDEKVLGITPAMREGSGMVEFSQRFPKQYFDAAIAEQHAVTLGAGFACEGFKPVVAIYSTFLQRGYDQLIHDVALQRLPVLFAIDRGGIVGADGPTHQGAFDLSFMRCIPNMVIMAPSDENECRQMLYTGYCYDAGPSAVRYPRGSATGATQVEAMTALPIGKGVIKRLGKRIAMLNFGTTLAAALTAAESLDATVVDMRFVKPLDVDLVKEMAQTHDVLVTVEENAIMGGAGSGVLELLQKLKMPKPVLQIGLPDEFIKHGSPEEVTHDLQLDAEGMLAQINAFLAD
|
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
|
Q0HSW6
|
Q58DX5
|
NADL2_HUMAN
|
Inactive N-acetylated-alpha-linked acidic dipeptidase-like protein 2
|
Homo
|
MGENEASLPNTSLQGKKMAYQKVHADQRAPGHSQYLDNDDLQATALDLEWDMEKELEESGFDQFQLDGAENQNLGHSETIDLNLDSIQPATSPKGRFQRLQEESDYITHYTRSAPKSNRCNFCHVLKILCTATILFIFGILIGYYVHTNCPSDAPSSGTVDPQLYQEILKTIQAEDIKKSFRNLVQLYKNEDDMEISKKIKTQWTSLGLEDVQFVNYSVLLDLPGPSPSTVTLSSSGQCFHPNGQPCSEEARKDSSQDLLYSYAAYSAKGTLKAEVIDVSYGMADDLKRIRKIKNVTNQIALLKLGKLPLLYKLSSLEKAGFGGVLLYIDPCDLPKTVNPSHDTFMVSLNPGGDPSTPGYPSVDESFRQSRSNLTSLLVQPISAPLVAKLISSPKARTKNEACSSLELPNNEIRVVSMQVQTVTKLKTVTNVVGFVMGLTSPDRYIIVGSHHHTAHSYNGQEWASSTAIITAFIRALMSKVKRGWRPDRTIVFCSWGGTAFGNIGSYEWGEDFKKVLQKNVVAYISLHSPIRGNSSLYPVASPSLQQLVVEKNNFNCTRRAQCPETNISSIQIQGDADYFINHLGVPIVQFAYEDIKTLEGPSFLSEARFSTRATKIEEMDPSFNLHETITKLSGEVILQIANEPVLPFNALDIALEVQNNLKGDQPNTHQLLAMALRLRESAELFQSDEMRPANDPKERAPIRIRMLNDILQDMEKSFLVKQAPPGFYRNILYHLDEKTSRFSILIEAWEHCKPLASNETLQEALSEVLNSINSAQVYFKAGLDVFKSVLDGKN
|
May be catalytically inactive.
|
Q58DX5
|
Q8NW49
|
THII_STAAW
|
tRNA 4-thiouridine synthase
|
Staphylococcus
|
MKYDHLLVRYGELTLKGSNRKKFVNQLRNNVNKSLKGLDGFVVKGKRDRMYIELEDHADINEITYRLSKIFGIKSISPVLKVEKTIEAMSAAAIKFAQQFEENSTFKIDVKRADKNFSMDTYELQRELGGAILKHFDNISVNVKRPDHEIRVEVRLDAIYMYEEVVPGSGGLPVGTGGKTLLMLSGGIDSPVAGMEVMRRGVTIEAIHFHSPPFTSDQAKEKVIELTRILAERVGPIKLHIVPFTELQKQVNKVVHPRYTMTSTRRMMMRVADKLVHQIGALAIVNGENLGQVASQTLHSMYAINNVTSTPVLRPLLTYDKEEIIIKSKEIGTFETSIQPFEDCCTIFTPKNPVTEPNFDKVVQYESVFDFEEMINRAVENIETLEITSDYKTIKEQQTNQLINDFL
|
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
|
Q8NW49
|
Q14I27
|
Y810_FRAT1
|
Nucleoid-associated protein FTF0810c
|
Francisella
|
MNFDMSKLMQQAQKMQEQMKKAQQERENMEVIGESGAGLVTVTMTGKYDVKSVSIDNSLMSEDKEILEDLIAAAVNSAVKKVEENSTASSDIYKMAKDAGIDLPSGINFPFK
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
Q14I27
|
Q5HPZ5
|
LSPA_STAEQ
|
Signal peptidase II
|
Staphylococcus
|
MKKKYYISISLLMTFIVLVFDQVSKWLITISMKVGDSYEIIPNFLNITSHRNNGAAWGILSGKMLFFYIITIIILIVLVIFYIKEAQFNLFMQVAISLLFAGALGNFIDRVLHGEVVDFIDTNIFGYDFPIFNIADSSLTIGVIFVIITLIKDAIINKKEV
|
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
|
Q5HPZ5
|
Q4FLS2
|
SSRP_PELUB
|
Small protein B
|
Candidatus Pelagibacter
|
MNKKANPGLKIICLNRKASFNFFFEDLIEAGIVLKGSEIKSIRDGKVNIADSYAVEKDGEIVLINSHIAAFKQASYSNHNPTDERKLLLNKKEINKLIGKMQRDGFTLVPTKMYFKKGKAKIEIAVAKGKKQFDKRATKKNRDWNREKARHIRKSS
|
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.
|
Q4FLS2
|
B2U233
|
DNAJ_SHIB3
|
Chaperone protein DnaJ
|
Shigella
|
MAKQDYYEILGVSKTAEEREIKKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGQHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNEKQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
|
B2U233
|
Q3M546
|
MTND_TRIV2
|
Acireductone dioxygenase (Ni(2+)-requiring)
|
Trichormus
|
MATLLLEDGTIESNLDEIARELAPLGVYIKHYDPGTSILFPHLLIQDALTDKEKCHIVDLHNSVFEFIQQENGYLWCDLLNVHPGSPNLQTLIATYAKYHTHTAPEALYVLAGEMIFGFVKPDGSQVQLLVQSQDYLHIPSGVEHWCSLTASLSFKAVRYFTAADGWVPNYTGTQLNDSLNK
|
Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
|
Q3M546
|
Q1J990
|
MNMG_STRPB
|
Glucose-inhibited division protein A
|
Streptococcus
|
MTHEFTESYDVIVIGAGHAGVEASLATSRMGCKTLLATINLDMLAFMPCNPSIGGSAKGIVVREIDALGGEMGKNIDKTYIQMKMLNTGKGPAVRALRAQADKSLYAREMKHTVEKQANLTLRQTMIDDILVEDGRVVGVLTATGQKFAAKAVVVTTGTALRGEIILGELKYSSGPNNSLASVTLADNLKKLGLEIGRFKTGTPPRVKASSINYDQTEIQPGDDKPNHFSFMSKDADYLKDQIPCWLTYTNQTSHDIINQNLYRAPMFSGIVKGVGPRYCPSIEDKIVRFADKERHQLFLEPEGRDTEEVYVQGLSTSLPEDVQKDLIHSIKGLEKAEMMRTGYAIEYDIVLPHQLRATLETKLISGLFTAGQTNGTSGYEEAAGQGLIAGINAALKVQGKPELILKRSDAYIGVMIDDLVTKGTLEPYRLLTSRAEYRLILRHDNADMRLTEIGRDIGLVDDERWKAFEIKKNQFDNELKRLNSIKLKPVKATNDRVQELGFKPLTDAMTAKEFMRRPEIDYATAVSFVGPAAEDLDAKIIELLETEIKYEGYIRKALDQVAKMKRMEEKRIPANIDWDAIDSIATEARQKFKKINPETIGQASRISGVNPADISILMIYLEGNGKAHRKY
|
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
Q1J990
|
B2G7Q2
|
THIM_LIMRJ
|
4-methyl-5-beta-hydroxyethylthiazole kinase
|
Limosilactobacillus
|
MVQRQINWSLIDRVRAKNPIVLNLANLVTIDKVADAVSAVGASPIMSVEPAEADEMVMLANALSINLGTINEHQATQIRTVLRAATPLKPLVLDPVAVSAVPSRLKFAHSLLNDFHFDVIRGNASEIAALVEADNTSHGIDAGKVPNQVQIAETCARRYHSIVVLTGETDIITDGQVVYENPFSAEMLTMNVGSGDMLSSIIAAFLGITTNTWDACIVATVLVSAAGVLANRYSVGLGSWQVQFFDQLSIMDTKALLEFFDESEEDYLD
|
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
|
B2G7Q2
|
Q8ZVK6
|
AGOG_PYRAE
|
Pa-AGOG
|
Pyrobaculum
|
MAAESQLKRVIETLRRLGIEEVLKLERRDPQYRAVCNVVKRHGETVGSRLAMLNALISYRLTGKGEEHWEYFGKYFSQLEVIDLCRDFLKYIETSPFLKIGVEARKKRALKACDYVPNLEDLGLTLRQLSHIVGARREQKTLVFTIKILNYAYMCSRGVNRVLPFDIPIPVDYRVARLTWCAGLIDFPPEEALRRYEAVQKIWDAVARETGIPPLHLDTLLWLAGRAVLYGENLHGVPKEVIALFQWRGGCRPPSE
|
DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.
|
Q8ZVK6
|
Q9KUX4
|
CYSJ_VIBCH
|
Sulfite reductase [NADPH] flavoprotein alpha-component
|
Vibrio
|
MNREVVTMSTGNTLPPALAALASPLNDAQLNQLQQTVTQLNAQQLAWVSGYFWGLSQSNALSVPHISAGQTASAASGKLTIIFASQTGNAKGVAQALLKEAQAAGIQAQLFDASDYKGKDLAKETHVIFVASTNGEGEAPDNALALHEFLKSKKAPKLPNLKYGVLGLGDSSYQFFCQTGKDFDQFLENLGAQRLVERLDADVDYQAAATEWRKQVLSILKDELTGAAAVTSVATFAVSQTAESHYSKEQPYTASLSTSQKITGRDSGKDVRHIEIDLADSGITYQPGDALGVWYENRPQLVNALLDSVGLSGHEEVQVDGETLSLHSALTHHYEITAANPQLVAQFAELAQSEKLTSLAQDKEALREYATRTQVIDVLREEKVTLSAIQLLSLLRRLTPRLYSIASSQSEVGEEVHLTVGVVEYEYEGEQRLGGASSFLAHQLEEGAPVKVFVEHNNNFKLPSDDNAPLIMVGPGTGIAPFRSFIQERENRGAAGKNWLLFGDRTFTQDFLYQVEWQKYLKSGVLNRLDVAFSRDQHEKVYVQHRLLEQAELVWQWLQEGAYFYVCGDASRMAKDVHQALITVVEQQGGLNREQAEEYVSELRKAKRYQRDVY
|
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. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.
|
Q9KUX4
|
P68246
|
TNNI2_CHICK
|
Troponin I, fast-twitch isoform
|
Gallus
|
MSDEEKKRRAATARRQHLKSAMLQLAVTEIEKEAAAKEVEKQNYLAEHCPPLSLPGSMQELQELCKKLHAKIDSVDEERYDTEVKLQKTNKELEDLSQKLFDLRGKFKRPPLRRVRMSADAMLRALLGSKHKVNMDLRANLKQVKKEDTEKEKDLRDVGDWRKNIEEKSGMEGRKKMFEAGES
|
Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
|
P68246
|
Q801R4
|
CTL2A_XENLA
|
CTD small phosphatase-like protein 2-A
|
Xenopus
|
MRLRMRKGSPRSSHVAAVRTARCKRKHSEEDEEEESPLIEEDKLPKQETGLLSTIKNFIKGSTNKEDRENPAKRSKVERDLDNNLITSTPRTGDKPSKPIARVRRKSQVNGEATAYEVSQHMKQNGKLEDLPCTTSPPRTTLLGTIFSPVFNFFSPANKNGTSGSDSPGQAVEAEEIVKQLDMEKVDEFSTSTATNGASYPSLGAPVRSTAGSWLEGTEDTPERDIPPLTAPVSPESGYSSAHAEAAYEEDWEVFDPYFFIKHVPPLTEEQLNRKPALPLKTRSTPEFSLVLDLDETLVHCSLNELEDAALTFPVLFQDVIYQVYVRLRPFFREFLERMSQIYEIILFTASKKVYADKLLNILDPKKRLVRHRLFREHCVCVQGNYIKDLNILGRDLSKTIIIDNSPQAFAYQLSNGIPIESWFMDKNDKELLKLVPFLENLVELNEDVRPHVRDRFRLHDCLPPD
|
Probable phosphatase.
|
Q801R4
|
B9V973
|
MCP1A_MACPC
|
Macrocypin-1a
|
Macrolepiota
|
MGFEDGFYTILHLAEGQHPNSKIPGGMYASSKDGKDVPVTAEPLGPQSKIRWWIARDPQAGDDMYTITEFRIDNSIPGQWSRSPVETEVPVYLYDRIKAEETGYTCAWRIQPADHGADGVYHIVGNVRIGSTDWADLREEYGEPQVYMKPVPVIPNVYIPRWFILGYEE
|
Inhibits papain and cysteine cathepsin endopeptidases, and also inhibits cathepsins B and H, which exhibit both exopeptidase and endopeptidase activities.
|
B9V973
|
Q8SPU5
|
BPIA1_BOVIN
|
Palate lung and nasal epithelium clone protein
|
Bos
|
MFHIGSLVVLCGLLAPTTALLEALPTPLGQTLPLAVTPALAPSPPDLAGSLTGALSNGLLSEGLLGILENLPLLDILKTRGNAPSGLLGSLLGKVTSLTPLLNNIIELKITNPQLLELGLVQSPDGHRLYVTIPLGMILNVKTSLVGSLLKLAVKLNITVELLAVTDEQKHVHLVVGNCTHSPGSLQIFLLDGLGSLPIQSFVDNLTGILNDVLPGLVQGKVCPLVNAVLSRLDVTLVHSIVNALIHGLQFVIKV
|
Lipid-binding protein which shows high specificity for the surfactant phospholipid dipalmitoylphosphatidylcholine (DPPC). Plays a role in the innate immune responses of the upper airways. Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae. Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway surface liquid homeostasis and proper clearance of mucus. Plays a role in the airway inflammatory response after exposure to irritants. May attract macrophages and neutrophils.
|
Q8SPU5
|
Q5AB49
|
Y6200_CANAL
|
Probable pathogenesis-related protein CaO19.6200
|
Candida
|
MKFLQSFPVILAVFSFAANLVSSKLVYEYETKYVTVEIVTIVSGETTYTTERLETNGPTSTTTTIVIPSSKPSSPESKPKSDSQPMFQSPSPVQITPSTTSINNAPSPTKPETTVTASPAVIAHTSVFVVTPNSAPTTSSSPPNIVQQVKAAITPSAPKPQPQPQPQENNSGTNDDSQLSSFSRQILEAHNIKRASHGVNPLTWSNELYNYANKVASSYDCSGNLRHTSGPYGENLALGYSSGANAVSAWYSEGFNFGGAGKLNHFTQVVWKSTTQLGCAYKDCRAKGWGLYIICNYQKPGNIIGQELANILPLIRS
|
Secreted protein that acts as a virulence factor during infections.
|
Q5AB49
|
Q7F8T6
|
OMT17_ORYSJ
|
Caffeoyl-CoA 3-O-methyltransferase ROMT17
|
Oryza sativa
|
MSMACTKVWRSTMYTPRRLKRTTPASRVSSTAMAAANGDASHGANGGIQIQSKEMKTAIHSNDSPKTLLKSESLHEYMLNTMVYPRENEFMRELRLITSEHTYGFMSSPPEEGQLLSLLLNLTGAKNTIEVGVFTGCSVLATALAIPDDGKVVAIDVSREYFDLGLPVIKKAGVAHKVDFREGAAMPILDNLLANEENEGKFDFAFVDADKGNYGEYHERLLRLVRAGGVLAYDNTLWGGSVALEDDSVLEEFDQDIRRSIVAFNAKIAGDPRVEAVQLPVSDGITLCRRLV
|
Catalyzes the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers. No 3',4',5'-trimethylated ester derivatives are produced. Can use caffeoyl CoA, 5-hydroxyferulic acid, luteolin, tricetin, quercetin, myrcetin and 7,8-dihydroxyflavone as substrates, but not naringenin, apigenin or kaempferol. The 2,3-double bond and the O-dihydroxyl group of the substrate are both required for catalytic activity of the enzyme.
|
Q7F8T6
|
P0C916
|
RBL1A_ACIFR
|
Ribulose bisphosphate carboxylase large chain 1
|
Acidithiobacillus
|
MAVKTYEAGVKDYRQTYWAPEYVPLDSDILACFKITPQPGVDREEAAAAVAAESSTGTWTTVWTDLLTDMDYYKGRAYRIEDVPGDDTCFYAFVAYPIDLFEEGSVVNVFTSLVGNVFGFKAVRALRLEDVRFPLAYVKTCNGPPHGIQVERDKMNKYGRPMLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFIAWRDRFLFVADAIHTAEAETGERKGHYLNVTAPSPEEMYERAEFAKELNMPIIMHDFLTGGFCANTGLARWCRKNGVLLHIHRAMHAVVDRNPHHGIHFRVLAKALRLSGGDHLHTGTVVGKLEGDRAATQGWVDLLRESFVPEDAGRGIFFDQDWGSMPGVFAVASGGIHVWHMPALLAIFGDDAIFQFGGGTLGHPWGNAAGAAANRVALEACVEARNEGRDLEREGKDILTNAAKDSPELKIALETWKEIKFEFDTVDKLDVVNR
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.
|
P0C916
|
Q9ZVT7
|
RRP4_ARATH
|
Ribosomal RNA-processing protein 4
|
Arabidopsis
|
MVMRKLQLPLSQTQKVRFERAIERLQSLSSSANSDASVIVTDSIPVNHDDAFLKGHGTSEVDGELLATVCGVVERVDKLVYVRTLRARYKPEVGDIVVGRVIEVAQKRWRVELNFNQDGVLMLSSMNMPDGIQRRRTSVDELNMRNIFVEHDVVCAEVRNFQHDGSLQLQARSQKYGKLEKGQLLKVDPYLVKRSKHHFHYVESLGIDLIIGCNGFIWVGEHVEVRDPMAIDDQKDEEMISSSSTGKEQSHIPLETRQTICRIGNAIRVLSNLGFTVTLEVIMETVNLSNSKNIDIHDMLGSEFHVVVAENEAERRRTKRKK
|
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing, maturation and degradation events. In vitro, is an active and distributive 3'->5' exonuclease requiring a free 3'-OH on the substrate and releasing nucleoside 5'-monophosphates . Required for normal embryo development .
|
Q9ZVT7
|
A1QZN3
|
SYDND_BORT9
|
Non-discriminating aspartyl-tRNA synthetase
|
Borrelia
|
MFKTIKCNQINDKLINQKIEINAWVKKIRHHGKVTFINLRDRYDEAQVLVNDEKLLKITSQIKMEYCIKVQGKLELRPSNLVNKEMRTGAFEILAENINIISRCNELPFMIEDNNNANENAKLEYRYLDLRREEQKQKIILRSKVTHTIRNYLTKKDFLELETPTFVKSTPEGARDFLVPSRIHKGHFYALPQSPQIYKQLTMIAGLDKYFQIARCYRDEDSRGDRQPEFTQLDIEMSFIKKENIFKLMENLIFTIFKNTLNISLPKKFKRMTYKHAMNTYGSDKPDTRYELLIQDMGKYFKQSSFNVFKDILQNKGTIKALIIKNQAHNFSRSKINNLEEHAKIYKTSGLYFAKIENNEFVGGIAKFLNKIKQTLFQTYSLKNNDIIFFIADSWETACKAMGQIRIKIANELNLTNKNTFEFLWIYDFPLFEYDEDTKNYKAAHHMFSLPQQKYIDTLESNPSKVLGEVYDLVLNGMELGSGSIRVHTRELQQRIFNIVGFKDTIAEERFGFFLKALEYGAPIHGGIAIGIDRLLMIMTHSSSIKDVILFPKNSFAASPLDKAPSKVPNEQLRELNLTIEDYKN
|
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).
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A1QZN3
|
Q12TB6
|
TUSA_SHEDO
|
Sulfur carrier protein TusA
|
Shewanella
|
MTDVFSQAQHQLDALGLRCPEPVMMVRKTVRKMADGETLLIIADDPATTRDIPSFCEFMDHTLIASDTSKTPYQYLLKKGR
|
Sulfur carrier protein which probably makes part of a sulfur-relay system.
|
Q12TB6
|
Q9X4Q2
|
METK_STRST
|
Methionine adenosyltransferase
|
Streptomyces
|
MSRRLFTSESVTEGHPDKIADQISDTILDALLREDPTSRVAVETLITTGLVHVAGEVTTKAYAPIAQLVREKILEIGYDSSKKGFDGASCGVSVSIGAQSPDIAQGVDTAYESRVEGDEDELDRQGAGDQGLMFGYACDETPELMPLPIHLAHRLSRRLSEVRKNGTIPYLRPDGKTQVTIEYDGDKAVRLDTVVVSSQHASDIDLESLLAPDIREFVVEPELKALVEDGIKLETEGYRLLVNPTGRFEIGGPMGDAGLTGRKIIIDTYGGMSRHGGGAFSGKDPSKVDRSAAYAMRWVAKNVVAAGLASRCEVQVAYAIGKAEPVGLFVETFGTNTIDTDKIEQAISEVFDLRPAAIIRDLDLLRPIYSQTAAYGHFGRSLPEFTWEKTDRVDGCGRPPVWRADLLPLVH
|
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.
|
Q9X4Q2
|
O74448
|
PIN1_SCHPO
|
Peptidyl-prolyl cis-trans isomerase pin1
|
Schizosaccharomyces
|
MSNTGLPKPWIVKISRSRNRPYFFNTETHESLWEPPAATDMAALKKFIANELQESVTPTEASNSPKIRASHLLVKHRESRRPSSWKEEHITRSKEEARKLAEHYEQLLKSGSVSMHDLAMKESDCSSARRGGELGEFGRDEMQKPFEDAAFALKPGEISGVVETSSGFHIIQRHA
|
Has a role in the G1/S stage transition of mitosis where it is involved in the dephosphorylation of cdc25 and wee1.
|
O74448
|
Q00604
|
NDP_HUMAN
|
X-linked exudative vitreoretinopathy 2 protein
|
Homo
|
MRKHVLAASFSMLSLLVIMGDTDSKTDSSFIMDSDPRRCMRHHYVDSISHPLYKCSSKMVLLARCEGHCSQASRSEPLVSFSTVLKQPFRSSCHCCRPQTSKLKALRLRCSGGMRLTATYRYILSCHCEECNS
|
Activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. Plays a central role in retinal vascularization by acting as a ligand for FZD4 that signals via stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. Acts in concert with TSPAN12 to activate FZD4 independently of the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1). May be involved in a pathway that regulates neural cell differentiation and proliferation. Possible role in neuroectodermal cell-cell interaction.
|
Q00604
|
Q11HL3
|
LFTR_CHESB
|
Phenyalanyltransferase
|
unclassified Chelativorans
|
MTRPLAPGFHIPPDLLLRAYATGVFPMAEHADDPEVFWVRPEMRGIIPLDKFHVPKSLRKLLRRQPYEVRYDTDFTGVIDACAEPSAERAETWINEPIRVAYTELFKRGHCHTVEAWREGKLVGGLYGVSLGRAFFGESMFSREPNASKICLVHLVERLKAGGFLLLDTQFTTDHLRRFGAIDVPRRRYEQMLAEALEETAKF
|
Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
|
Q11HL3
|
Q15YN6
|
RL2_PSEA6
|
50S ribosomal protein L2
|
Pseudoalteromonas
|
MPLLKAKPTSAGRRHVVQVVNPDLHKGAPYAPLLEKNSKSGGRNNNGRITVRHVGGGHKQHYRVIDFKRNKDGIPAKIERLEYDPNRSANICLVLYADGERRYILAPKGAKAGDQIQSGSDAAIKAGNSLPMRNIPVGTTVHAIEMKPGKGAQIARSAGQYAQILARAEGYVTLRLRSGEVRRVLADCRATIGEIGNAEHMLRSLGKAGANRWRGIRPTVRGVAMNPVDHPHGGGEGRTSGGRHPVSPWGVPTKGKKTRSNKRTDKLIVRRRNK
|
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
|
Q15YN6
|
Q7V6I0
|
PSBD_PROMM
|
Photosystem Q(A) protein
|
Prochlorococcus
|
MTIAVGRAPQRGWFDVLDDWLKRDRFVFVGWSGLLLFPTAYLALGGWFTGTTFVTSWYTHGIASSYLEGCNFLSAAVSTPADAMGHSLLLLWGPEAQGDFVRWCQLGGLWTFVALHGSFSLIGFMLRQFEIARLVGIRPYNALAFSGPVVVFLACFLIYPLGQHSWFFAPSFGVAAIFRFILFLQGFHNWTLNPFHMMGVAGILGGALLCGIHGATVQNTLFEDGAMSNTFKGFDPTQEEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVMGMWTPSVGIVGLAVNLRAYDFVSQEVRAAEDPEFETFYTKNVLLNEGIRAWMSVADQPHENFVFPEEVMPRGNAL
|
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. D2 is needed for assembly of a stable PSII complex.
|
Q7V6I0
|
P51984
|
CREB_HYDVD
|
cAMP response element-binding protein
|
Hydra
|
MELARHSFQQPLNVAPSLSNVVNKTSVVLQQQSVIQPNQHQLQHQLQTMHDGGIDGKRREILARRPSYRRILDDLAGDGPVKMENYDDTGSSGESSPNGNNEEDINGINQSVSHQEKQYQSIHLNGIVSSVQGGENSLNQLHDSQPGDNQYIITTQGPDNKIQAYTIKGTLPIGLDNTSLASPHQLAEEATRKRELRLYKNREAARECRRKKKEYVKCLENRVAVLENQNKALIEELKSLKDLYCSKGD
|
This protein binds the cAMP response element (CRE), sequence present in many viral and cellular promoters. Could regulate the transcriptional activity of genes involved in regeneration processes.
|
P51984
|
Q8FDH4
|
GLNE_ECOL6
|
Adenylyl transferase
|
Escherichia
|
MKPLSSPLQQYWQTVVERLPEPLAEESLSAQAKSVLTFSDFVQDSVIAHPEWLTELESQPPQADEWQHYASWLQEALSNVSDEAGLMRELRLFRRRIMVRIAWAQTLALVTEESILQQLSHLAETLIVAARDWLYDACCREWGTPCNAQGEAQPLLILGMGKLGGGELNFSSDIDLIFAWPEHGCTQGGRRELDNAQFFTRMGQRLIKVLDQPTQDGFVYRVDMRLRPFGESGPLVLSFAALEDYYQEQGRDWERYAMVKARIMGDSDGVYANELRAMLRPFVFRRYIDFSVIQSLRNMKGMIAREVRRRGLTDNIKLGAGGIREIEFIVQVFQLIRGGREPSLQSRALLPTLSAIAALHLLSENDAEQLRVAYLFLRRLENLLQSINDEQTQTLPFDELNRARLAWAMDFADWPQLTGVLTAHMANVRRVFNELIGDDESETQEESLSEQWRELWQDALQEDDTTPVLAHLSEDDRKQVLMLIADFRKELDKRTIGPRGRQVLDHLMPHLLSDVCAREDAAVTLSRITALLVGIVTRTTYLELLSEFPAALKHLISLCAASPMIASQLARYPLLLDELLDPNTLYQPTATDAYRDELRQYLLRVPEDDEEQQLEALRQFKQAQLLRIAAADIAGTLPVMKVSDHLTWLAEAMIDAVVQQAWVQMVARYGKPNHLNEREGRGFAVVGYGKLGGWELGYSSDLDLIFLHDCPMDAMTDGEREIDGRQFYLRLAQRIMHLFSTRTSSGILYEVDARLRPSGAAGMLVTSAEAFADYQKNEAWTWEHQALVRARVVYGDPQLTAHFDAVRREIMTLPREGKTLQTEVREMREKMRAHLGNKHRDRFDIKADEGGITDIEFITQYLVLRYAHEKPKLTRWSDNVRILELLAQNDIMEEQEAMALTRAYTTLRDELHHLALQELPGHVSEDCFTAERELVRASWQKWLVEE
|
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
|
Q8FDH4
|
Q20303
|
ELO6_CAEEL
|
Monomethyl branched-chain fatty acid elongase 6
|
Caenorhabditis
|
MPQGEVSFFEVLTTAPFSHELSKKHIAQTQYAAFWISMAYVVVIFGLKAVMTNRKPFDLTGPLNLWNAGLAIFSTLGSLATTFGLLHEFFSRGFFESYIHIGDFYNGLSGMFTWLFVLSKVAEFGDTLFIILRKKPLMFLHWYHHVLTMNYAFMSFEANLGFNTWITWMNFSVHSIMYGYYMLRSFGVKVPAWIAKNITTMQILQFVITHFILFHVGYLAVTGQSVDSTPGYYWFCLLMEISYVVLFGNFYYQSYIKGGGKKFNAEKKTEKKIE
|
Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. Uses malonyl-CoA to add 2 carbons per cycle to the chain of long-chain fatty acids. Condensing enzyme required for the formation of isoheptadecanoate (C17iso), which plays critical roles in animal development and growth.
|
Q20303
|
Q9BZI7
|
REN3B_HUMAN
|
Up-frameshift suppressor 3 homolog on chromosome X
|
Homo
|
MKEEKEHRPKEKRVTLLTPAGATGSGGGTSGDSSKGEDKQDRNKEKKEALSKVVIRRLPPTLTKEQLQEHLQPMPEHDYFEFFSNDTSLYPHMYARAYINFKNQEDIILFRDRFDGYVFLDNKGQEYPAIVEFAPFQKAAKKKTKKRDTKVGTIDDDPEYRKFLESYATDNEKMTSTPETLLEEIEAKNRELIAKKTTPLLSFLKNKQRMREEKREERRRREIERKRQREEERRKWKEEEKRKRKDIEKLKKIDRIPERDKLKDEPKIKVHRFLLQAVNQKNLLKKPEKGDEKELDKREKAKKLDKENLSDERASGQSCTLPKRSDSELKDEKPKRPEDESGRDYREREREYERDQERILRERERLKRQEEERRRQKERYEKEKTFKRKEEEMKKEKDTLRDKGKKAESTESIGSSEKTEKKEEVVKRDRIRNKDRPAMQLYQPGARSRNRLCPPDDSTKSGDSAAERKQESGISHRKEGGEE
|
Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC) and serving as link between the EJC core and NMD machinery. Recruits UPF2 at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF2 stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA upstream of exon-exon junctions. In vitro, stimulates translation; the function is independent of association with UPF2 and components of the EJC core.
|
Q9BZI7
|
A1ALL5
|
ATPA_PELPD
|
F-ATPase subunit alpha
|
Pelobacter
|
MKIRAEEISEIIKKQIREYGKEVEVSETGTIISIGDGIARIHGLSGAMAGELLEFPGGVSGMVLNLEEDNVGAAVLGEFTAIKEGHTVKRTGRIAEVPVGEALIGRVVNAIGEPIDGKGPIKTDTFSKVEIKAPGIVARKSVDQPMASGLKAVDAMVPIGRGQRELIIGDRQTGKTAVAVDTIINQKGGDVICIYVAIGQKRSTVAQVVAKLSDHGAMDYTIVVAASASESAPLQFIAPYSGVTMGEYFRDKGQHALIIYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERACKLSDECGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIYLESDLFFSGVRPAINVGLSVSRVGGKAQTKSMKQVAGTLRLNLAQYREMAAFAQFGSDLDKATQMQLARGERLVEILKQPQYRPLSNEKQVLIIFAANNGFLDELPVSTLRRYEDEMYAFFDNRQADLLSELRDKKAIDDELKKRIVAALEQFKKEFSA
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
A1ALL5
|
Q5F605
|
PYRD_NEIG1
|
Dihydroorotate oxidase
|
Neisseria
|
MYPLARRILFALDAEKAHHFTLDALNTVYKLGLIPVTDNRTKPIKLMGMDLPNPVGLAAGLDKNGEYIDALGALGFGFLEIGTVTRNPQPGNPQPRLFRVPEHQGIINRMGFNNHGIDAMIRNIEKSKYQGVLGINIGKNAVTPIQNAADDYLICLEKAYAHASYITVNISSPNTKNLRALQGGGELGALLEALKNKQAQLAAAHGKYIPLAVKIAPDLDEAQIEDIARVVKSVEMDGIIATNTTIDKSSLGSHPLAGEQGGLSGFPVREKSNRVLKKLAEHIDGALPIIGVGGIMEGGDAAEKIRLGTTAVQVYSGLIYKGPALVKECLKALAR
|
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
Q5F605
|
D4GTK4
|
SECF_HALVD
|
Protein-export membrane protein SecF
|
Haloferax
|
MVEFTVPEVDYTRYTNRQLAAVPLAVLAVALLVIGGWYVATGAPVNPGVDFTGGTELRIATDAPQSEVAAAFDSQPESIRSVAADGTYVVTFQSGSATSTELQTQAEDAGFEVRSIDAVSANFGGETQLLALGGLAVAFAGMSVLVFAMFRSFVPSIAVVLSAFSDIVIPVALMNLFGIELSLGTVAALLMLIGYSVDSDILLNNHVLRRSGDFYESTARAMRTGVTMTLTSIAAMIVMTIMATLFGIQLLAAIGTVLVFGLTADLMNTYMLNVTLLRWYKFEGVTR
|
Involved in protein export.
|
D4GTK4
|
B2IH44
|
CTAA_BEII9
|
Cytochrome aa3-controlling protein
|
Beijerinckia
|
MSALDTAPAGSLAETHAQRGTRAVAFWLWSLAVLVFLMVVLGGATRLTESGLSITEWKPISGALPPLSAEAWQAEFENYKRIPQYAALFPDMDLAGFKFIFFFEWSHRLLGRLIGVATALPLLFFWLRGRLPEGYRLKLLGLLALGGLQGFVGWWMVKSGLSDRVEVAQERLAIHLILASLTFCFIVWLAASLRKRPREISPSKASGLAWGAGLILLAILVQIGLGALVAGLRAGRAYNTWPLIEGNFLPPVESLTLLTPLWRNFVDNLLTVQFQHRMVAYLVLGLTLLQVFWTSGTLGSGRATKRAIALLGLVLAQVILGILTLVLVVPLWAGLLHQAFAMLVLGMAVAHLQALSQGR
|
Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
|
B2IH44
|
B7NSJ1
|
NORW_ECO7I
|
Flavorubredoxin reductase
|
Escherichia
|
MSNSIVIIGSGFAARQLVKNIRKQDASIPLTLIAADSMDEYNKPDLSHVISQGQRADDLTRQTAGEFAEQFNLRLFPHTWVTDIDAEAHVVKSQNNQWQYDKLVLATGASAFVPPVPGRELMLTLNSQQEYRACETQLRDARRVLIVGGGLIGIELAMDFCRAGKAVTLIDNAASILASLMLPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGILATLDRQRSIEVDAVIAATGLRPETALARRAGLTINRGVCVDSYLQTSNADIYALGDCAEINGQVLPFLQPIQLSAMVLAKNLLGNNTPLKLPAMLVKIKTPELPLHLAGETQRQDLRWQINTERQGMVARGVDDGDQLRAFVVSEDRMKEAFGLLKTLPM
|
One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase.
|
B7NSJ1
|
A4R5F6
|
ARGJ_MAGO7
|
Arginine biosynthesis bifunctional protein ArgJ beta chain
|
Pyricularia
|
MASKSTSTAVWGQLRHLAQQQTRCYSATADSIPASKKKYVPTKGVYPKGFRVSGTIVGVKPGNTTKPDLAFVTSDTPCAAAAVFTKNRFQAAPVTFSRDLLKKKGNSGVNGVIINSGCANAVTGKGGLEDAESMAREADRCLGGDGTIVMSTGVIGQRLPIKRILDNVPAAHSRLGSSHDHWLSCATAICTTDTFPKLMSRSFTLPSSPSVEYRIAGMTKGAGMIHPNMATLLGVIATDAPIAPAVLPSLLKNAVDRSFNSITIDGDTSTNDTVALLANGAAGGKEIASESSPDFAAFRDVLNVFSEDLAKLIVRDGEGATKFVTIRVVESDSEETAKKVASTIARSPLVKTALYGKDANWGRILCATGYALISEPGSAAVAEVSDKIVPEKTNVSFVPTDGTAELKLLVDGEPEQVDEVRAAEILKAEDLEILVRLGTGKAEGTYWTCDFSHEYVTINGDYRT
|
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
|
A4R5F6
|
P04712
|
SUS1_MAIZE
|
Sucrose-UDP glucosyltransferase 1
|
Zea
|
MAAKLTRLHSLRERLGATFSSHPNELIALFSRYVHQGKGMLQRHQLLAEFDALFDSDKEKYAPFEDILRAAQEAIVLPPWVALAIRPRPGVWDYIRVNVSELAVEELSVSEYLAFKEQLVDGQSNSNFVLELDFEPFNASFPRPSMSKSIGNGVQFLNRHLSSKLFQDKESLYPLLNFLKAHNYKGTTMMLNDRIQSLRGLQSSLRKAEEYLLSVPQDTPYSEFNHRFQELGLEKGWGDTAKRVLDTLHLLLDLLEAPDPANLEKFLGTIPMMFNVVILSPHGYFAQSNVLGYPDTGGQVVYILDQVRALENEMLLRIKQQGLDITPKILIVTRLLPDAAGTTCGQRLEKVIGTEHTDIIRVPFRNENGILRKWISRFDVWPYLETYTEDVSSEIMKEMQAKPDLIIGNYSDGNLVATLLAHKLGVTQCTIAHALEKTKYPNSDIYLDKFDSQYHFSCQFTADLIAMNHTDFIITSTFQEIAGSKDTVGQYESHIAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSVYYPYTETDKRLTAFHPEIEELIYSDVENSEHKFVLKDKKKPIIFSMARLDRVKNMTGLVEMYGKNARLRELANLVIVAGDHGKESKDREEQAEFKKMYSLIDEYKLKGHIRWISAQMNRVRNGELYRYICDTKGAFVQPAFYEAFGLTVIESMTCGLPTIATCHGGPAEIIVDGVSGLHIDPYHSDKAADILVNFFDKCKADPSYWDEISQGGLQRIYEKYTWKLYSERLMTLTGVYGFWKYVSNLERRETRRYIEMFYALKYRSLASQVPLSFD
|
Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways. Most active in the sink tissues where it is responsible for the breakdown of the arriving sucrose.
|
P04712
|
Q8J1Z1
|
TIM9_NEUCR
|
Mitochondrial import inner membrane translocase subunit tim9
|
Neurospora
|
MDGLTAAESRELDQRLQKRQVKEFMSVFGNLVDNCFTACVDDFTSKALSGRESGCISRCVLKSMSTQTRLGERFGELNAAMTAEMQRR
|
Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
|
Q8J1Z1
|
Q87YR0
|
FOLD1_PSESM
|
Methenyltetrahydrofolate cyclohydrolase
|
Pseudomonas
|
MTAKLIDGKAIAASLRQQIAKRVAERSQQGLRTPGLAVILVGSDPASQVYVSHKRKDCEEVGFISQAYDLPAETTQVALTNLIDRLNEDAAVDGILLQLPLPAHLDASLLLERIRPDKDVDGFHPYNVGRLAQRIPLLRPCTPKGIIALLESTGVDLYGLDAVVVGASNIVGRPMAMELLLAGCTVTVTHRFTKDLAGHVSRADLVVVAAGKPGLVKGEWIKPGAIVIDVGINRQDDGKLVGDVVYETALPRAGWITPVPGGVGPMTRACLLENTLYAAETLHD
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
Q87YR0
|
O30394
|
TYSY_BACAT
|
Thymidylate synthase A
|
Bacillus
|
SEVPILTTKKLAWKTAIKELLWIWQLKSNDVNDLNKMSVHIWDQWKQEDGTIGHAYGFQLGKKNRSLNGEKVDQVDYLLHQLKNNPSSRRHITMLWNPDELDAMALTPCVYETQWYVKHGKLHLEVRARSNDMALGNPFNVFQYNVLQRMIAQVTGYELGEYIFNIGDCHVYTRHIDNLKIQMEREQFEAPELWINPEVKDFYDFTIDDFKLINYKHGDKLLFEVRV
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
|
O30394
|
O95196
|
CSPG5_HUMAN
|
Neuroglycan C
|
Homo
|
MGRAGGGGPGRGPPPLLLFLGAALVLASGAVPAREAGSAVEAEELVKGSPAWEPPANDTREEAGPPAAGEDEASWTAPGGELAGPEEVLQESAAVTGTAWLEADSPGLGGVTAEAGSGDAQALPATLQAPHEVLGQSIMPPAIPEATEASGPPSPTPGDKLSPASELPKESPLEVWLNLGGSTPDPQGPELTYPFQGTLEPQPASDIIDIDYFEGLDGEGRGADLGSFPGSPGTSENHPDTEGETPSWSLLDLYDDFTPFDESDFYPTTSFYDDLDEEEEEEEDDKDAVGGGDLEDENELLVPTGKPGLGPGTGQPTSRWHAVPPQHTLGSVPGSSIALRPRPGEPGRDLASSENGTECRSGFVRHNGSCRSVCDLFPSYCHNGGQCYLVENIGAFCRCNTQDYIWHKGMRCESIITDFQVMCVAVGSAALVLLLLFMMTVFFAKKLYLLKTENTKLRRTNKFRTPSELHNDNFSLSTIAEGSHPNVRKLCNTPRTSSPHARALAHYDNVICQDDPSAPHKIQEVLKSCLKEEESFNIQNSMSPKLEGGKGDQADLDVNCLQNNLT
|
May function as a growth and differentiation factor involved in neuritogenesis. May induce ERBB3 activation.
|
O95196
|
B5XNE5
|
MSRQ_KLEP3
|
Flavocytochrome MsrQ
|
Klebsiella
|
MRFTVKQIAWLKVFLHLAGFLPLVWLFWAGHQGYFSADPAKDIQHFTGRMALKFLLATLLVAPLARYAKQPLLIRIRRLLGLWCFAWATLHLTSYTLLELGINNLALLGSEIINRPYLTLGMICWVILLALAATSTQAMQRKLGRRWQLLHNFVYLVAILAPIHYLWSVKIVSPQPIIYALLAVVLLACRYKKFRQWWR
|
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.
|
B5XNE5
|
Q2LR03
|
GREA_SYNAS
|
Transcript cleavage factor GreA
|
Syntrophus
|
MEKMPITKSGFENLKKELEHLKCVLIPANIKDIEIARAHGDLSENAEYTAAKEKQSFLHGKLQELENNLALSNVIDLKMLSDDRIVFGATVIIEEASTGKQTNYQLVGPFESNISENKISVTSPIGKALIGKSIGDEVKVHTPGGIRNFEVVDIYINPSEL
|
Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
|
Q2LR03
|
Q84TG3
|
PUB23_ARATH
|
U-box domain-containing protein 23
|
Arabidopsis
|
MSGGIMDEEIEIPPFFLCPISLEIMKDPVIVSTGITYDRDSIEKWLFAGKKNSCPVTKQDITDADLTPNHTLRRLIQSWCTLNASYGVERIPTPRPPICKSEIEKLIRDSASSHENQVKCLKRLRQIVSENATNKRCLEAAGVPEFLANIVSNDSENGSLTDEALNLLYHLETSETVLKNLLNNKKDNNIVKSLTKIMQRGMYESRVYATLLLKNILEVADPMQSMTLKPEVFTEVVQILDDRISQKATKAAMHILVNICPWGRNRHKAVEAGVISVIIELLMDESFTSERRGPEMAMVVLDLLCQCAEGRAEFLNHGAAIAVVCKKILRVSQTASDRAVRVLLSVGRFCATPALLHEMLQLGVVAKLCLVLQVSCGGKTKEKAKELLKLHARVWKDSPCLPKNMILAYPC
|
E3 ubiquitin-protein ligase that negatively regulates water stress response. May control in coordination with PUB23 a drought signaling pathway by ubiquitinating cytosolic RPN12a. Acts as negative regulator of the immunity triggered by the pathogen-associated molecular patterns (PAMPs), in association with PUB22 and PUB24.
|
Q84TG3
|
Q7M8E4
|
RL24_WOLSU
|
50S ribosomal protein L24
|
Wolinella
|
MVKFQIKKGDKVQVIAGDDKGKVAEVIKVMPKSSQVIVAGCKVAKKSVKPSEQNPKGGFVNKEMPIHISNVKKVEA
|
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
|
Q7M8E4
|
Q0I5I2
|
FTSB_HAES1
|
Cell division protein FtsB
|
Histophilus
|
MRLFILSLFALLVMFQYDFWFGKNGYLDYQDIKAEIIQRKQENKKLSQRNQTIFAEIQDLKNGIEAIEERARMEHEMIKQNEVFYRIVKNKNR
|
Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
|
Q0I5I2
|
Q7TPS5
|
C2CD5_MOUSE
|
138 kDa C2 domain-containing phosphoprotein
|
Mus
|
MPGKLKVKIVAGRHLPVMDRASDLTDAFVEVKFGNTTFKTDVYLKSLNPQWNSEWFKFEVDDEDLQDEPLQITVLDHDTYSANDAIGKVYIDIDPLLYSEAATVISGWFPIYDTIHGIRGEINVVVKVDLFNDSNRFRQSSCGVKFFCTTSIPKCYRAVVIHGFVEELVVNEDPEYQWIDRIRTPRASNEARQRLISLMSGELQRKIGLKVLEMRGNAVVGYLQCFDLEGESGLVVRAIGTACTLDKLSSPAAFLPACSSPSRELKEIPFNEDPNPNTHSSGPSTPLKNQTYSFSPSKSYSRQSSSSDTDLSLTPKTGMGSGSAGKEGGPFKALLRQQTQSALEQREFPFLTLTAFPPGLLVHVGGVVSARSVKLLDRIHNPDEPETRDAWWAEIRQEIKSHAKALGCHAVVGYSESTSICEEVCILSASGTAAVLNPRFLQEGTVEGCLEQRIEENLPVGCGFCHIPYDELNMPFPAHLTYCYNCRKQKVPDVLFTTIDLPTDAVVVGKGCLIQARLCRLKKKAQAEANATAISNLLPFMEYEVHTQLMNKLKLKGMNALFGLRIQITVGETMLMGLASATGVYLAALPTPGGIQIAGKTPNDGSYEQHISHMQKRINDTIAKNKELYEITPPEVSEEMIGSPIPEPRQRSRLLRSQSESSDEVTELDLSHGKKDAFVLEIDDTDAMEDVHSLLTDAPPPSGFYSCNTEIMPGINNWTSEIQMFTSVRVVRLSSLNLTNQALNKNFNGLCENLLKSLYFKLRSMTPCCLCHVNFTVSLPEDELIQVTVTAVAITFDKNQALQTTKPHVEKSLQRASTDNEELLQFPLELCSDSLPPHPFPAAKEHLESANSNSGIPAAQRAVTVEKASAMGDGNFRNRSAPPCASPTVGVVKMTPLSFIPGAKITKYLGIINMFFIRETTSLREEGGVSGFLHAFIAEVFAMVRAHVAALGGNAVVSYIMKQCVFMENPSKNQAQCLINVSGDAVVFVRDSDLEVMSSQQPAANCQPSCTGEVTT
|
Required for insulin-stimulated glucose transport and glucose transporter SLC2A4/GLUT4 translocation from intracellular glucose storage vesicle (GSV) to the plasma membrane (PM) in adipocytes. Binds phospholipid membranes in a calcium-dependent manner and is necessary for the optimal membrane fusion between SLC2A4/GLUT4 GSV and the PM.
|
Q7TPS5
|
Q91ZB5
|
MRGRG_MOUSE
|
Evolutionary breakpoint transcript 2 protein
|
Mus
|
MFSIFNIWGTFNKVLFFLSLTVSLAGLVGNALLLWHLGLHIKKGPFNTYLLHLAAADFLFLSCQVGFSIATIVSGHEDTLYFPVTFLWFAVGLWLLAAFSVDCCLAYMFPSFCSPNRRPRFTSVVLCLVIWALTMPAVLLPANACGLLKNGMSLLVCLKYHWTSVTWLAVLSGMACGASKFLLIFGNCCSSQPPPKFCKLAQCSGILLFFCRLPLVVYWCLRPVLKFLLPFFFPLATLLACIDSSAKPLLYYMKGRQLRKDPLQVALNRALGEESQSGLGGLSLPMHQV
|
Orphan receptor. May regulate nociceptor function and/or development, including the sensation or modulation of pain.
|
Q91ZB5
|
B8EAU2
|
THII_SHEB2
|
tRNA 4-thiouridine synthase
|
Shewanella
|
MKFIVKLYPEIMMKSKPVRMRFTKMLETNIRNVLKKVDEDAKVQRQWDRIMVMVPKDKPELAQAFGERLACIPGIAHVVQVDEYSFESVDDIYQQVLPVYRDQLAGKTFCVRVKRTGDHDFNSIEVERYVGGGLNQFTDALGVRLKNPDITVNLEIERDNLYMVTKRIEGLGGFPMATQEDVLSLISGGFDSGVSSYQFIKKGARTHYCFFNLGGAQHEIGVKQVAYHLWKTYGESHKVKFISVPFEPVVAEILERIDNGQMGVVLKRMMMRTAARIADRMGIQALVTGESLGQVSSQTLTNLNVIDRCTELLILRPLIAMDKQDIINESRKIGTEDFAKSMPEYCGVISQKPTVKAVLAKVEAEEKKFSEDLIDQIIAQSVTIDIREIAEQMDTRITETETVASIDTNQVVIDIRAPEEEESKPLQIEGIEIKRIPFFKLATQFADLDKQKTYLLYCERGVMSKLQALYLIEQGYTNVKVYRP
|
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
|
B8EAU2
|
Q1D7Z0
|
ENGB_MYXXD
|
Probable GTP-binding protein EngB
|
Myxococcus
|
MIKVLDARFVTTAVEPKGYPTDHTAEVAFVGRSNVGKSSMINALTGRRKLVRVSNTPGRTRTLNFFDVDLERGGVRHQIRLADLPGYGFAKASKADKAQWEKMITTYLEKRHRLEAVVSIVDVEVGPTPDDLTTLDYLQAHNRRVLVVATKVDRLTKARLKPRLVELSKLMDLPLEVILPFSSTEKLGVDEVWGALLDTFGKSARV
|
Necessary for normal cell division and for the maintenance of normal septation.
|
Q1D7Z0
|
Q5HJ89
|
ESSA_STAAC
|
ESAT-6 secretion machinery protein EssA
|
Staphylococcus
|
MLMNSVIALTFLTASSNNGGLNIDVQQEEEKRINNDLNQYDTTLFNKDSKAVNDAIAKQKKERQQQIKNDMFQNQASHSTRLNETKKVLFSKSNLEKTSESDKSPYIQNKQEKKIFPYILMSVGAFLTLGFVIFSIHKGRRTKNESARKSNI
|
Component of the ESAT-6 secretion system (Ess). Required for the secretion of EsxA and EsxB.
|
Q5HJ89
|
Q8U9L5
|
PAL_AGRFC
|
Outer membrane lipoprotein Omp16 homolog
|
Agrobacterium tumefaciens complex
|
MSRTNISALSPMQKLARNPAVIAMTLALALAGCANKKNMPNSAGELGLGGAGSATPGSQQDFTVNVGDRIFFDTDSTSIRADAQQTLQRQAQWLSRYPNYAITVEGHADERGTREYNLALGARRAAATRDFLASQGVPASRMKTISYGKEKPVAVCDDISCWSQNRRAVTVLGGAGM
|
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
|
Q8U9L5
|
Q9N2D1
|
TRYT_PIG
|
Tryptase
|
Sus
|
MLNLLVLALPLLVSLVHTAPAPGQALERAGIVGGKEAPGHKWPWQVSLRCLDQYWKHFCGGSLIHPQWVLTAAHCFGPEKADPLYIRVQLGEQHLYYQDRLLLVSRIIVHPNYYDEVNGADIALLELEDPVNLSSHVQPVTLPPASETFPKGTRCWVTGWGDVHSGWPLPPPYPLKQVRVPIVENSECDMQYHLGLSTGDNIPIVRDDMLCAGSEGHDSCQGDSGGPLVCRVNGTWLQAGVVSWGEGCALPNRPGIYTRVTHYLDWIHQCIPRES
|
Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type.
|
Q9N2D1
|
Q53LQ0
|
PDI11_ORYSJ
|
Endosperm storage protein 2
|
Oryza sativa
|
MAISKAWISLLLALAVVLSAPAARAEEAAAAEEGGDAAAEAVLTLDADGFDEAVAKHPFMVVEFYAPWCGHCKKLAPEYEKAAQELSKHDPPIVLAKVDANDEKNKPLATKYEIQGFPTLKIFRNQGKNIQEYKGPREAEGIVEYLKKQVGPASKEIKSPEDATNLIDDKKIYIVGIFSELSGTEYTNFIEVAEKLRSDYDFGHTLHANHLPRGDAAVERPLVRLFKPFDELVVDSKDFDVTALEKFIDASSTPKVVTFDKNPDNHPYLLKFFQSSAAKAMLFLNFSTGPFESFKSVYYGAAEEFKDKEIKFLIGDIEASQGAFQYFGLREDQVPLIIIQDGESKKFLKAHVEPDQIVSWLKEYFDGKLSPFRKSEPIPEVNDEPVKVVVADNVHDFVFKSGKNVLVEFYAPWCGHCKKLAPILDEAATTLKSDKDVVIAKMDATANDVPSEFDVQGYPTLYFVTPSGKMVPYESGRTADEIVDFIKKNKETAGQAKEKAESAPAEPLKDEL
|
Probable protein disulfide isomerase that plays an essential role in the segregation of proglutelin and prolamin polypeptides within the ER lumen of endosperm. Required to retain proglutelin in the cisternal ER lumen until ER export and, thereby, indirectly prevents heterotypic interactions with prolamin polypeptides.
|
Q53LQ0
|
P24711
|
INVO_CEPBA
|
Involucrin
|
Cephalopachus
|
MSQQQTLPVTLPPALSQELLKTVPPPANTQQDQMKQPTPSPAPCQKGPSELPVEKHPAPVKQVPEQECEPQQQDHQEPELQLGRKQQEPQEQEVHPGKQQQKPQEQEAHLGKKQEPQGQEVHLGKQQQKTQEQEVHLGKQQQELQEQEVHLEKQLQEPQEVHLEKQLQEQEVHLEKQLQEPEPELNLGKQQQEPQEQEAYLGKQQQELPEPQDPELHLGKQQQEPQEQEVQLEKQQEAQEQELHLGKQQQESQEQELHLRKLQQVPQEPQDQELHLGKQQQELQEQEVHLGKQLQEPQEQELHLGRQQQELQEEEVHLGMKEEQLLKHVEQQEGQLEQQEGQLKQPVCIPTPGQVQDIQPAQPPKGEVLLPTEKQQKQEVQWPLKQE
|
Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia.
|
P24711
|
P0DPK3
|
NT2NB_HUMAN
|
Notch homolog 2 N-terminal-like protein B
|
Homo
|
MPALRPALLWALLALWLCCATPAHALQCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGICLNLPGSYQCQCLQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPETVRRGTELWERDREVWNGKEHDEN
|
Human-specific protein that promotes neural progenitor proliferation and evolutionary expansion of the brain neocortex by regulating the Notch signaling pathway . Able to promote neural progenitor self-renewal, possibly by down-regulating neuronal differentiation genes, thereby delaying the differentiation of neuronal progenitors and leading to an overall final increase in neuronal production . Acts by enhancing the Notch signaling pathway via two different mechanisms that probably work in parallel to reach the same effect . Enhances Notch signaling pathway in a non-cell-autonomous manner via direct interaction with NOTCH2 . Also promotes Notch signaling pathway in a cell-autonomous manner through inhibition of cis DLL1-NOTCH2 interactions, which promotes neuronal differentiation .
|
P0DPK3
|
A7ZSB6
|
NANE_ECO24
|
ManNAc-6-P epimerase
|
Escherichia
|
MSLLAQLDQKIAANGGLIVSCQPVPDSPLDKPEIVAAMALAAEQAGAVAIRIEGVANQQATRAVVSVPIIGIVKRDLEDSPVRITAYIEDVDALAQAGADIIAIDGTDRPRPVPVETLLARIHHHGLLAMTDCSTPEDGLACQKLGAEIIGTTLSGYTTPETPEEPDLALVKTLSDAGCRVIAEGRYNTPAQAADAMRHGAWAVTVGSAITRLEHICQWYNTAMKKAVL
|
Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
|
A7ZSB6
|
P22458
|
VTNC_RABIT
|
Serum-spreading factor
|
Oryctolagus
|
MAPLRPIFTLALLLWVVLADQESCKDRCTEGFNANRKCQCDELCSYYQSCCADYAAECKPQVTRGDVFTMPEDEYGPYDYIEQTKDNASVHAQPESPTVGQEPTLSPDLQTEGGAEPTHEVPLEPEMETLRPEGEDLQAGTTELGTSASPAEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDETAVRPGYPKLIQDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGILDPDYPRNISEGFSGIPDNVDAAFALPAHSYSGRERVYFFKGDKYWEYQFQQQPSQEECEGSSLSAVFEHFAMLHRDSWEDIFKLLFWGRPSGGARQPQFISRDWHGVPGKVDAAMAGRIYISGLTPSPSAKKQKSRRRSRKRYRSRYGRGRSQNSRRLSRSISRLWFSSEEVSLGPYNYEDYETSWLKPATSEPIQSVYFFSGDKYYRVNLRTQRVDTVNPPYPRSIAQYWLGCPAPGGQ
|
Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.
|
P22458
|
Q02020
|
FIBB_CHICK
|
Fibrinogen beta chain
|
Gallus
|
ASVEYDNEEDSPQIDARAHRPLDKRQEAAPTLRPVAPPISGTGYQPRPPKQDKQAMKKGPIIYPDAGGCKHPLDELGVLCPTGCELQTTLLKQEKTVKPVLRDLKDRVAKFSDTSTTMYQYVNMIDNKLVKTQKQRKDNDIILSEYNTEMELHYNYIKDNLDNNIPSSLRVLRAVIDSLHKKIQKLENAIATQTDYCRSPCVASCNIPVVSGRECEDIYRKGGETSEMYIIQPDPFTTPYRVYCDMETDNGGWTLIQNRQDGSVNFGRAWDEYKRGFGNIAKSGGKKYCDTPGEYWLGNDKISQLTKIGPTKVLIEMEDWNGDKVSALYGGFTIHNEGNKYQLSVSNYKGNAGNALMEGASQLYGENRTMTIHNGMYFSTYDRDNDGWLTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGTYSWDMAKHGTDDGIVWMNWKGSWYSMKKMSMKIKPYFPD
|
Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots.
|
Q02020
|
Q9NYT6
|
ZN226_HUMAN
|
Zinc finger protein 226
|
Homo
|
MNMFKEAVTFKDVAVAFTEEELGLLGPAQRKLYRDVMVENFRNLLSVGHPPFKQDVSPIERNEQLWIMTTATRRQGNLGEKNQSKLITVQDRESEEELSCWQIWQQIANDLTRCQDSMINNSQCHKQGDFPYQVGTELSIQISEDENYIVNKADGPNNTGNPEFPILRTQDSWRKTFLTESQRLNRDQQISIKNKLCQCKKGVDPIGWISHHDGHRVHKSEKSYRPNDYEKDNMKILTFDHNSMIHTGQKSYQCNECKKPFSDLSSFDLHQQLQSGEKSLTCVERGKGFCYSPVLPVHQKVHVGEKLKCDECGKEFSQGAHLQTHQKVHVIEKPYKCKQCGKGFSRRSALNVHCKVHTAEKPYNCEECGRAFSQASHLQDHQRLHTGEKPFKCDACGKSFSRNSHLQSHQRVHTGEKPYKCEECGKGFICSSNLYIHQRVHTGEKPYKCEECGKGFSRPSSLQAHQGVHTGEKSYICTVCGKGFTLSSNLQAHQRVHTGEKPYKCNECGKSFRRNSHYQVHLVVHTGEKPYKCEICGKGFSQSSYLQIHQKAHSIEKPFKCEECGQGFNQSSRLQIHQLIHTGEKPYKCEECGKGFSRRADLKIHCRIHTGEKPYNCEECGKVFRQASNLLAHQRVHSGEKPFKCEECGKSFGRSAHLQAHQKVHTGDKPYKCDECGKGFKWSLNLDMHQRVHTGEKPYKCGECGKYFSQASSLQLHQSVHTGEKPYKCDVCGKVFSRSSQLQSHQRVHTGEKPYKCEICGKSFSWRSNLTVHHRIHVGDKSYKSNRGGKNIRESTQEKKSIK
|
May be involved in transcriptional regulation.
|
Q9NYT6
|
P78795
|
EIF3G_SCHPO
|
Translation initiation factor eIF3 p33 subunit homolog
|
Schizosaccharomyces
|
MSSSKSLDWADDEDYGTGLPSIQTFDNPDGTKTMIEFRIDDNGKKVKVTRVIRKTVITERVQHAVAERKKWKKFGKEAGKNSGVDARTTSVGENVQLRLQLGWTTTKEEEQDEAALAAAKVKAKGSSVVRCRACKGNHFTAQCPYKSIIGPVDEPPLDASPVSSRASGALGEKGRYIAPHLRAGSGRESGDSMFKRERDDSATLRVTNLSDDTREEELRDLFRRFGGIQRVYLAKDKETGRAKGFAFVSYYDRDCAIKARDRLDGYGWNNLILRCEFSKPRD
|
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. This subunit can bind 18S rRNA.
|
P78795
|
Q8IZ08
|
GP135_HUMAN
|
G-protein coupled receptor 135
|
Homo
|
MEEPQPPRPPASMALLGSQHSGAPSAAGPPGGTSSAATAAVLSFSTVATAALGNLSDASGGGTAAAPGGGGLGGSGAAREAGAAVRRPLGPEAAPLLSHGAAVAAQALVLLLIFLLSSLGNCAVMGVIVKHRQLRTVTNAFILSLSLSDLLTALLCLPAAFLDLFTPPGGSAPAAAAGPWRGFCAASRFFSSCFGIVSTLSVALISLDRYCAIVRPPREKIGRRRALQLLAGAWLTALGFSLPWELLGAPRELAAAQSFHGCLYRTSPDPAQLGAAFSVGLVVACYLLPFLLMCFCHYHICKTVRLSDVRVRPVNTYARVLRFFSEVRTATTVLIMIVFVICCWGPYCFLVLLAAARQAQTMQAPSLLSVVAVWLTWANGAINPVIYAIRNPNISMLLGRNREEGYRTRNVDAFLPSQGPGLQARSRSRLRNRYANRLGACNRMSSSNPASGVAGDVAMWARKNPVVLFCREGPPEPVTAVTKQPKSEAGDTSL
|
Orphan receptor. Has spontaneous activity for beta-arrestin recruitment . Shows a reciprocal regulatory interaction with the melatonin receptor MTNR1B most likely through receptor heteromerization .
|
Q8IZ08
|
W3X7K0
|
PFMAD_PESFW
|
Conidial pigment biosynthesis cluster protein D
|
Pestalotiopsis
|
MWTARLSSIAVLTQVVGTWADTITLNWEITWVNAAPDGFHRPVIGVNGKWPCPPIHATVGDTVVINMKNSLGNQTTGLHFHGINQLDTNYMDGASMVNSCPVVPGSSMTYSFTADEPGTYWYHSHNMAQYPDGLRGPLIIHDDNDPFDGEFDNEVILTISDWYHQQTLTLVQNMLVSSNDQWRPPLPDGMIVNEGGNTDIELDIGTTTRVRILNFGALTAFMLRFGSRDMDVIMTDASYVQRETIHQLRIAPGQRYDVLVSATKKDKGKNIPYLISMDLNRDFTVSGTWTFNQTGYLITDAKAPCTAKEVVQQWRPFDEALFTPLDEMPLLGPLDRTWTLNFALCKDMNNIPRMCFNDQTYVMQKTPTLYTAATVGNANTDPSVYGAVLPFIIEYGDVLEIVINNLDPAIHPFHLHGHQFQVVERPESGSGSFDGSSTANPVPPRRDVISINGGSYARLRITADNPGVFLFHCHIEWHVEMGLTATLIEAPEMLDGYDIPQAMIDSCKAQGYPVAGNAAGDTINVWDDSGYLTDPPSTYSGSQWPVPKGGNSQKSRPRRKPSGQSSQTRQISNMSGEFQHRITW
|
Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment forming a dark layer in the conidial wall that protects the conidia from UV radiations . The first step of the pathway is the production of the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN or T4HN) by the polyketide synthase PfmaE though condensation of acetyl-CoA with malonyl-CoA. T4HN is not stable and easily oxidizes into the stable form flaviolin . T4HN is also substrate of the hydroxynaphthalene reductase PfmaG to yield scytalone . The scytalone dehydratase PfmaJ then reduces scytalone to 1,3,8-THN . 1,3,8-THN is then substrate of the hydroxynaphthalene reductase PfmaI to yield vermelone (Probable). Vermelone is further converted by the multicopper oxidase PfmaD to 1,8-DHN (Probable). Finally the laccase PFICI_06862 transforms 1,8-DHN to DHN-melanin (Probable). The roles of the 5-oxoprolinase PfmaA and the proline iminopeptidase PfmaB within the cluster have not been elucidated yet (Probable).
|
W3X7K0
|
Q9PTQ7
|
DMRT1_CHICK
|
Doublesex- and mab-3-related transcription factor 1
|
Gallus
|
MPGDSPVVSKRAAPKPRRAAMPGDSPVVSKPPDGAGPGDKAGGLGKAAAQMAAAPAAGKKLPRLPKCARCRNHGYSSPLKGHKRFCMWRDCQCKKCSLIAERQRVMAAQVALRRQQAQEEELGISHPVPLPSAPEPVVKKSSSSSSCLLQDSSSPAHSTSTVAAAAASAPPEGRMLIQDIPSIPSRGHLESTSDLVVDSTYYSSFYQPSLYPYYNNLYNYSQYQMAVATESSSSETGGTFVGSAMKNSLRSLPATYMSSQSGKQWQMKGMENRHAMSSQYRMCSYYPPTSYLGQGVGSPTCVTQILASEDTPSYSESKARVFSPPSSQDSGLGCLSSSESTKGDLECEPHQEPGAFAVSPVLEGE
|
Transcription factor that plays a key role in male sex determination. Acts both as a transcription repressor and repressor.
|
Q9PTQ7
|
A5VR03
|
RL2_BRUO2
|
50S ribosomal protein L2
|
Brucella
|
MALKHFNPITPGQRQLVIVDRSELYKGKPVKSLTEGLSKKGGRNNTGRITVRFQGGGHKRSYRFIDFKRRKLDVVGTVERLEYDPNRTAFIALIRYTDGELAYILAPQRLAVGDQVVAGNFVDVKPGNAMPLSSMPVGTIIHNVELKPGKGGQIARSAGTYAQLVGRDQGMAILRLNSGEQRLVSGACFASVGAVSNPDHGNINDGKAGRSVWRGKRPHVRGVAMNPVDHPHGGGEGRTSGGRHPVTPWGKPTKGKKTRSNKATDKFIMRSRHQRKK
|
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
|
A5VR03
|
Q6MSP3
|
RL15_MYCMS
|
50S ribosomal protein L15
|
Mycoplasma
|
MKLNELKYTPGSKTKATIVGRGMASGKGKTATRGHKGQNSRSGGGVRPGFEGGQTPLFRRLPKVGFTSLNQKQYTILNLSDLETLGLEKIDHESLINSKIIKNNASLIKILANGTLTKKVDVKVNKISKAAKDAIEKLGGKVEVI
|
Binds to the 23S rRNA.
|
Q6MSP3
|
Q21SF4
|
RL1_ALBFT
|
50S ribosomal protein L1
|
Rhodoferax
|
MTQLTKKQKSFQGKVDSNKLYPLADALGLVKECATAKFDESIDVAVQLGIDAKKSDQVVRGAVVLPNGTGKTKRVAVFAQGAKAEEAKAAGADIVGMDDLAAMIKAGDMPFDIVIAAPDAMRVVGTLGQILGPRGLMPNPKVGTVTPDVATAVKNAKAGQVQFRVDKAGIVHSTIGRRSFDTDKLQGNLAALVDALTKAKPATSKGVYLKKVAVSSTMGVGIRVDLQSIAA
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
Q21SF4
|
Q39E95
|
NTPPA_BURL3
|
Nucleotide pyrophosphatase
|
Burkholderia cepacia complex
|
MPSSTPPALFPTLYLASQSPRRQELLQQIGVRFELLLPRPDEDAEALEAELPGEAADAYVRRVTIAKAEAARARLVASGKPASPVLVADTTVTIDGAILGKPANADDALSMLTRLAGREHAVLTAVAVIDADGELLPPALSRSSVRFAPASRDAYARYVESGEPFGKAGAYAIQGRAAEFIERIDGSHSGIMGLPLFETAALLRAARVAF
|
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
|
Q39E95
|
Subsets and Splits
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