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
|
|---|---|---|---|---|---|---|
Q87TQ7
|
DNAA_VIBPA
|
Chromosomal replication initiator protein DnaA
|
Vibrio
|
MSSSLWLQCLQQLQEELPATEFSMWVRPLQAELNDNTLTLFAPNRFVLDWVRDKYLNSITRLLQEYCGNDIPNLRFEVGSRPVSAPKPAPTRTPADVAAESSAPAQLQARKPVHKTWDDDPQAIAAINHRSNMNPKHKFDNFVEGKSNQLGLAAARQVSDNPGAAYNPLFLYGGTGLGKTHLLHAVGNAIVDNNPNAKVVYMHSERFVQDMVKALQNNAIEEFKRYYRSVDALLIDDIQFFANKERSQEEFFHTFNALLEGNQQIILTSDRYPKEISGVEDRLKSRFGWGLTVAIEPPELETRVAILMKKAEDHQIHLADEVAFFIAKRLRSNVRELEGALNRVIANANFTGRPITIDFVREALRDLLALQEKLVTIDNIQKTVAEYYKIKVADLLSKRRSRSVARPRQLAMALAKELTNHSLPEIGDAFGGRDHTTVLHACRKIEQLREESHDIKEDYSNLIRTLSS
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
|
Q87TQ7
|
B1YSW5
|
PRMA_BURA4
|
Ribosomal protein L11 methyltransferase
|
Burkholderia cepacia complex
|
MSYRELVVELAREHAEALSDALLELGALSVSVEDADADTPDEQPLFGEPGLVPDRTAWQHSRVIALLSPDHEPAVLLAAAVNDIGVTETPKFDVREVEEQDWVRLTQSQFEPIPIGERIWVVPSWHDAPDPDALILELDPGLAFGTGSHPTTRLCMEWLEQSVKPGQSVLDYGCGSGILAILARKCGANPVVGIDIDPQAVESARQNSERNHAEVTYGLPDACPAGEFDIVVANILSNPLKLMASMLASKVKPGGRIALSGVLARQADEVAAVYARYVDISVWREHEGWVCLAGTRRESH
|
Methylates ribosomal protein L11.
|
B1YSW5
|
Q99R07
|
CLFB_STAAM
|
Fibrinogen-binding protein B
|
Staphylococcus
|
MKKRIDYLSNKQNKYSIRRFTVGTTSVIVGATILFGIGNHQAQASEQSNDTTQSSKNNASADSEKNNMIETPQLNTTANDTSDISANTNSANVDSTTKPMSTQTSNTTTTEPASTNETPQPTAIKNQATAAKMQDQTVPQEANSQVDNKTTNDANSIATNSELKNSQTLDLPQSSPQTISNAQGTSKPSVRTRAVRSLAVAEPVVNAADAKGTNVNDKVTASNFKLEKTTFDPNQSGNTFMAANFTVTDKVKSGDYFTAKLPDSLTGNGDVDYSNSNNTMPIADIKSTNGDVVAKATYDILTKTYTFVFTDYVNNKENINGQFSLPLFTDRAKAPKSGTYDANINIADEMFNNKITYNYSSPIAGIDKPNGANISSQIIGVDTASGQNTYKQTVFVNPKQRVLGNTWVYIKGYQDKIEESSGKVSATDTKLRIFEVNDTSKLSDSYYADPNDSNLKEVTDQFKNRIYYEHPNVASIKFGDITKTYVVLVEGHYDNTGKNLKTQVIQENVDPVTNRDYSIFGWNNENVVRYGGGSADGDSAVNPKDPTPGPPVDPEPSPDPEPEPTPDPEPSPDPEPEPSPDPDPDSDSDSDSGSDSDSGSDSDSESDSDSDSDSDSDSDSDSESDSDSESDSDSDSDSDSDSDSDSESDSDSDSDSDSDSDSDSESDSDSESDSESDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSRVTPPNNEQKAPSNPKGEVNHSNKVSKQHKTDALPETGDKSENTNATLFGAMMALLGSLLLFRKRKQDHKEKA
|
Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps.
|
Q99R07
|
Q3M5C8
|
RPOC2_TRIV2
|
Transcriptase subunit beta'
|
Trichormus
|
MTNEKMIFRNRVVDKGQLRNLISWAFTHYGTARTAVMADKLKDLGFRYATRAGVSISVDDLMVPPSKRSLLEAAEEEIRATEVRYQRGEITEVERFQKVIDTWNGTSEALKDEVVTHFKQTNPLNSVYMMAFSGARGNISQVRQLVGMRGLMADPQGEIIDLPIKTNFREGLTVTEYIISSYGARKGLVDTALRTADSGYLTRRLVDVSQDVIIREIDCGTTRGIPVRPMTEGSKTLIKLSTRLLGRVVGEDVIHPKTKEVIAARNTPISDDLAKEIEKAGVAEVVVRSPLTCEAARSVCQHCYGWSLAHAKMVDLGEAVGIIAAQSIGEPGTQLTMRTFHTGGVFTGEVAQQVRSKMDGTIKLPRKLRTRTHRTRHGEDALFVESNGIMILEPRKEGSETPAPQEIHVTQGSTIYIVDGQQVKQGQLLAEVALGGRTTRTNTEKAVKDVASDLAGEVKFAEVVPEQKTDRQGNTTTTAARGGLIWILSGEVYNLPPGAELVVKNGDRVETNGVLAETKLTTIHGGVVRLPEATPGKSTREIEIITASVVLDQATVTVQSSQGRNNYLITTGNNQVFNLRATPGTKVQNGQVVAELIDDRYRTTTGGFLKFAGVEVQKKGKAKLGYEVVQGGTLLWIPEETHEVNKDISLLLVEDGQFVEAGTEVVKDIFCQNSGVVEVTQKNDILREVVVKPGELLMVDDPEAVIGRDNTLLQPGEELLGQVATELRYIQYVESPEGPALLSRPVVEFAVPSNPDVPSTTSVSQQTGRSIQMRAVQRLPYKDSERVKSVEGVELLRTQLVLEIEQEGEQEHNASPLAADIELIPDPEDADVQRLQLVILESLVLRRDIAADATQGSTQTSLEVKDGDTIVPGSVVARTQILSKEGGIVRGVQKGSEAVRRCLVLRHSDMTTLNTSAKPKVKAGDLIVAGTELAPGVFAEESGQIVAVKNAGESTTTQDAALSTQNYAVTIRAGRPYRVSPGAVLQIEDGDLVQRGDNLVLLVFERAKTGDIIQGLPRIEELLEARKPKEACILAKRGGEVKVVYGDGDEAIAIKVIESNGVVTDYPLGPGQNLAMPDGSVVPAGQPLSDGPSNPHEILEVFFSLGSEDGVYACASHALQKVQTFLVNEVQMVYQSQGIDIADKHIEVIVRQMTNKVRIDDGGDTTMLPGELVELRQVEQVNEAMAITGGARAQYTPVLLGITKASLNTDSFISAASFQETTRVLTEAAIEGKSDWLRGLKENVIIGRLIPAGTGYNTYDEPGMLEDYSTLETTSVLDETDDPLDMVLDDRTARAYNLDSPGLAETGFSNRRSILDDDELIADEIHDLVEAEVEVDDEVDDDYEDDDEDDDDYED
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q3M5C8
|
F8S101
|
PLB_CROAD
|
Phospholipase B
|
Crotalus
|
MIRFGNPSSSDKRRQRCRSWYWGGLLLLWAVAETRADIHYATVYWLEAEKSFQIKDVLDKNGDAYGYYNDAIQSTGWGILEIKAGYGNQPISNEILMYAAGFLEGYLTASHMSDHFANLFPLMIKNVIIEQKVKDFIQKQDEWTRQQIKNNKDDPFWRNAGYVIAQLDGLYMGNVEWAKRQKRTPLTDFEISFLNAIGDLLDLIPALHSELRKSDFRSMPDVSRIYQWDMGHCSALIKVLPGYENIYFAHSSWFTYAATLRIYKHLDFRITDPQTKTGRASFSSYPGLFGSLDDFYILGSGLIMLQTTNSVFNLSLLKKVVPESLFAWERVRIANMMADSGKTWAETFEKQNSGTYNNQYMILDTKKIKLQRSLEDGTLYIIEQVPKLVKYSDQTKVLRNGYWPSYNIPFDKEIYNMSGYGEYVQRHGLEFSYEMAPRAKIFRRDQGKVTDMESMKFIMRYNNYKEDPYAKHNPCNTICCRQDLDRRTPVPAGCYDSKVADISMAAKFTAYAINGPPVEKGLPVFSWVHFNKTKHQGLPESYNFDFVTMKPVL
|
May cause hemolysis or may be involved in protein folding and translation.
|
F8S101
|
P73821
|
SERA_SYNY3
|
2-oxoglutarate reductase
|
unclassified Synechocystis
|
MNLAWLQGLSLGLLSPPAPALLIFRSFTMAKVLVSDSIDQVGIDILKQVAQVDVKTGLSEAEIIDIVPEYDAIMLRSATKVTEKIIQAGSQLKIIGRAGVGVDNIDVPAATRQGIVVVNSPEGNTIAAAEHALAMMMALARHIPDANKSVKESKWERKQFIGTEVYKKTLGVVGLGKIGSHVAGVAKAMGMKLLAYDPFISQERADQIGCTLVDLDLLFSEADFITLHIPKTPETANLINAETLAKMKPTARIINCSRGGIIDEEALVTAIETAQIGGAALDVFAQEPLGESRLREFSNVILTPHLGASTEEAQVNVAVDVAEQIRDVLLGLPARSAVNIPGLTPDVMEKLRPYLKLAETLGTLVGQLAGGRIDRLTVCLQGDLAEYTNSQPLVVAAIKGLLSQALRERVNYVNAAIEAKERGIRVIETKDASVRDYSGSLHLKATGTMGEHSATGALLSNGEIRITDVDEFPINVPPNNYMLFTLHRDMPGIIGKIGSLLGSFNVNIASMQVGRKIVRGDAIMALSLDDPLPDGLLSEITKVAGIRDAYTVKL
|
Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
|
P73821
|
Q5XAD7
|
DNAJ_STRP6
|
Chaperone protein DnaJ
|
Streptococcus
|
MNNTEYYDRLGVSKDASQDDIKKAYRKMSKKYHPDINKEAGAEQKYKDVQEAYETLSDSQKRAAYDQYGAAGAQGGFGGGAGGFGGFDGGGFGGFEDIFSSFFGGGGSRNPNAPRQGDDLQYRVNLSFEEAVFGVEKEVSYNREATCGTCLGSGAKPGTAPVTCRKCHGSGVMTIDTQTPLGMMRRQVTCDICHGSGKEIKEPCQTCHGTGHEKQAHKVSVKIPAGVETGQQIRLQGQGEAGFNGGPYGDLFVILNVLPSKQFERNGSTIYYSLDISFTQAALGDTVEIPTVHGDVEMAIPAGTQTGKTFRLKGKGAPKLRGGGQGDQHVTVNIVTPTKLNDAQREALQAFAEASGDKMLHPKKKGFFDKVKDALEDI
|
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.
|
Q5XAD7
|
C7MSY6
|
MSHA_SACVD
|
N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase
|
Saccharomonospora
|
MTISGYRKAIWPRRIAVLSVHTSPLEQPGTKDAGGMNVYISQTAVEMARRGVSVEVFTRATSSDQPPAVELAPGVLVRHIPAGPFEPLERGELPSQLCAFTSGVLRTEAFQEPGYYDLIHSHYWLSGQVGWLARDRWGVPLVHTAHTLAKVKNAALASGDTPEPRTRVIGEEQVVAEADRLVVNTDVEADQLVRLYDAAPDAVRTVSPGVDLERFRPGSRAAARAALGVPADAVVLAFAGRIQPLKAPDVLLRATAALVRRDPGLRRRLVVLVAGGPSGSGLEQPRSLMDLAVELGIDDVTRFLPPQGGQDLVNVYRAADVVAVPSHNESFGLVALEAQACGTPVVAARVGGLPVAVDDEVSGLLVPTHDTEDWADALARVALRPEVRAVLSRGAREHAQRFSWRRTTDALLDIYREAMAAFRGTALEVAV
|
Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway.
|
C7MSY6
|
P33748
|
MSN2_YEAST
|
Multicopy suppressor of SNF1 protein 2
|
Saccharomyces
|
MTVDHDFNSEDILFPIESMSSIQYVENNNPNNINNDVIPYSLDIKNTVLDSADLNDIQNQETSLNLGLPPLSFDSPLPVTETIPSTTDNSLHLKADSNKNRDARTIENDSEIKSTNNASGSGANQYTTLTSPYPMNDILYNMNNPLQSPSPSSVPQNPTINPPINTASNETNLSPQTSNGNETLISPRAQQHTSIKDNRLSLPNGANSNLFIDTNPNNLNEKLRNQLNSDTNSYSNSISNSNSNSTGNLNSSYFNSLNIDSMLDDYVSSDLLLNDDDDDTNLSRRRFSDVITNQFPSMTNSRNSISHSLDLWNHPKINPSNRNTNLNITTNSTSSSNASPNTTTMNANADSNIAGNPKNNDATIDNELTQILNEYNMNFNDNLGTSTSGKNKSACPSSFDANAMTKINPSQQLQQQLNRVQHKQLTSSHNNSSTNMKSFNSDLYSRRQRASLPIIDDSLSYDLVNKQDEDPKNDMLPNSNLSSSQQFIKPSMILSDNASVIAKVATTGLSNDMPFLTEEGEQNANSTPNFDLSITQMNMAPLSPASSSSTSLATNHFYHHFPQQGHHTMNSKIGSSLRRRKSAVPLMGTVPLTNQQNNISSSSVNSTGNGAGVTKERRPSYRRKSMTPSRRSSVVIESTKELEEKPFHCHICPKSFKRSEHLKRHVRSVHSNERPFACHICDKKFSRSDNLSQHIKTHKKHGDI
|
Positive transcriptional factor that acts as a component of the stress responsive system. Recognizes and binds to the stress response element (STRE) which is involved in the response to various forms of stress (heat, oxidative, osmotic, etc.). Involved in the regulation of the CTT1, DDR2, HSP12 genes. May be regulated via WHI2-PSR1 complex phosphatase activity.
|
P33748
|
A6SXG3
|
ENO_JANMA
|
2-phosphoglycerate dehydratase
|
Janthinobacterium
|
MSAIVDIIGREVIDSRGNPTVECDVLLESGVMGRAAVPSGASTGSREAIELRDGDKSRYFGKGVLKACEHINTEISEAIMGLDANEQAFLDRTLIDLDGTENKARLGANATLAVSMAVAKAAAEESGLPLYRYFGGSGAMQMPVPMMNVINGGAHANNNLDLQEFMIIPVGAPSFREAIRYGAEVFHTLKKIINDKGLPTSVGDEGGFAPSVENHEAAIKLILQAIEQAGYEPGTQIALGLDCAASEFYKDGKYHLAGEGMTLSSADFTNLLGTWCDKYPIISIEDGMAENDWDGWATLTNALGKKVQLVGDDLFVTNTKILREGIQKNIANSILIKINQIGTLTETFAAIEMAKRAGYTAVISHRSGETEDSTIADIAVGTNSLQIKTGSMSRSDRMAKYNQLLRIEEDLGDIASYPGRGAFYNLK
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
A6SXG3
|
P58958
|
G39AC_DROME
|
Gustatory and pheromone receptor 39a, isoform D
|
Sophophora
|
MKRNAFEELRVQLRTLKWLGVLRFTIDFNKCLVRENASEERSAWLYLIGVVGITCSLIVYSTYFPSHFIMGKHNTTGNCYALINIRSCSIVTMLIYTQLYIQRFRFVALLQSILRFNQISGSHREEGRFAFYYYTHLSLLIICMLNYAYGYWTAGVRLTTIPIYLLQYGFSYLFLGQVVVLFACIQQILLSILKYYNQVVLKNIKSSKESREFYYNFCKYNQVIWLSYTEINHCFGLLLLLVTGLILLITPSGPFYLVSTIFEGRFRQNWQFSLMSFTAILWSLPWIVLLVLAMGRNDVQKEANKTAKMLTKVPRTGTGLDRMIEKFLLKNLRQKPILTAYGFFALDKSTLFKLFTAIFTYMVILVQFKEMENSTKSINKF
|
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. Plays a role in sustaining courtship behavior in males, possibly through the reception of a stimulating arrestant pheromone.
|
P58958
|
B5FTQ5
|
MUTS_SALDC
|
DNA mismatch repair protein MutS
|
Salmonella
|
MNESFDKDFSNHTPMMQQYLKLKAQHPEILLFYRMGDFYELFYDDAKRASQLLDISLTKRGASAGEPIPMAGIPHHAVENYLAKLVNQGESVAICEQIGDPATSKGPVERKVVRIVTPGTISDEALLQERQDNLLAAIWQDGKGYGYATLDISSGRFRLSEPADRETMAAELQRTNPAELLYAEDFAEMALIEGRRGLRRRPLWEFEIDTARQQLNLQFGTRDLVGFGVENASRGLCAAGCLLQYVKDTQRTSLPHIRSITMERQQDSIIMDAATRRNLEITQNLAGGVENTLAAVLDCTVTPMGSRMLKRWLHMPVRNTDILRERQQTIGALQDTVSELQPVLRQVGDLERILARLALRTARPRDLARMRHAFQQLPELHAQLETVDSAPVQALRKKMGDFAELRDLLERAIIDAPPVLVRDGGVIAPGYHEELDEWRALADGATDYLDCLEIRERERTGLDTLKVGYNAVHGYYIQISRGQSHLAPINYVRRQTLKNAERYIIPELKEYEDKVLTSKGKALALEKQLYDELFDLLLPHLADLQQSANALAELDVLVNLAERAWTLNYTCPTFTDKPGIRITEGRHPVVEQVLNEPFIANPLNLSPQRRMLIITGPNMGGKSTYMRQTALIALLAYIGSYVPAQNVEIGPIDRIFTRVGAADDLASGRSTFMVEMTETANILHNATENSLVLMDEIGRGTSTYDGLSLAWACAENLANKIKALTLFATHYFELTQLPEKMEGVANVHLDALEHGDTIAFMHSVQDGAASKSYGLAVAALAGVPKEVIKRARQKLRELESISPNAAATQVDGTQMSLLAAPEEASPAVEALENLDPDSLTPRQALEWIYRLKSLV
|
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
|
B5FTQ5
|
Q2IHP6
|
ATPF_ANADE
|
F-type ATPase subunit b
|
Anaeromyxobacter
|
MASILSPVPVLAAGGIADINPGLTLWTAITFLVMLAVLAKFAWGPIVKMLAERERSIREAIDSAKKERAEAERLLAAQKESLSKAQREAAELARRNQQEVEALRQELTAKARKEADELVAEARRQIAEELVKAKAELKAQVVDLAIDAASRLVKANLDEKSQRALVEEYIAQLPANRAA
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
Q2IHP6
|
Q49896
|
RECN_MYCLE
|
Recombination protein N
|
Mycobacterium
|
MLTEIRIESLGAISVATAEFDRGLTVLTGETGTGKTMVVTGLHLLGGARADASRVRSGANRAVVEGRFTTTDLDDVVVAQLDGILNASGSERDEDGSVIVLRSVSRDGPSRSYLGGRSVPAKSLGSFTTELLALHGQNDQLRLVRPEEQRAALDRYAAAGPSCERYRELRDAWLLARSDLIDRRNRIRELVQEADRLKFALSEIDSVDPQPGEDNALVADIVRLSELDMLREVAVNARAALSGALDDMDVSGSNAVACMGQAKAALESTDDATLRAFADQVGEVLTVVVEVGRELGEYLEELPVDASALESKLVRQAELCTLTRKYAADIDGVLQWARESRERLEQLDVSYERLAGVESRVDELERQLSQAAVDLSKLRRDAANRLAKEVTAELSALAMVDAEFTISVTTDLIPLTDYKRSAAVTLPSGGVARAGADGVDQVEFGFAAHRGMTVLPLAKSASGGELSRVMLALEVVLATSAAGTTMVFDEVDVGVGGRAAVQIGRRLARLARTHQVIVVTHLPQVAAYADVHLVVHSAGLDGASDVRRLAGDDRVAELARMLAGLGESDSGRAHARELLDAARKDKS
|
May be involved in recombinational repair of damaged DNA.
|
Q49896
|
P0CF31
|
INSB_ECOLX
|
Insertion element IS1 protein InsB
|
Escherichia
|
MPGNRPHYGRWPQHDFTSLKKLRPQSVTSRIQPGSDVIVCAEMDEQWGYVGAKSRQRWLFYAYDSLRKTVVAHVFGERTMATLGRLMSLLSPFDVVIWMTDGWPLYESRLKGKLHVISKRYTQRIERHNLNLRQHLARLGRKSLSFSKSVELHDKVIGHYLNIKHYQ
|
Absolutely required for transposition of IS1.
|
P0CF31
|
P0CY11
|
HMRA1_YEAST
|
Silenced mating-type protein A1
|
Saccharomyces
|
MDDICSMAENINRTLFNILGTEIDEINLNTNNLYNFIMESNLTKVEQHTLHKNISNNRLEIYHHIKKEKSPKGKSSISPQARAFLEQVFRRKQSLNSKEKEEVAKKCGITPLQVRVWFINKRMRSK
|
Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Silenced copy of A1 at HMR.
|
P0CY11
|
P0CAT9
|
CH60_CAUVC
|
Chaperonin-60
|
Caulobacter
|
MAAKDVYFSSDARDKMLRGVNILANAVKVTLGPKGRNVVIEKSFGAPRTTKDGVSVAKEIELADKFENLGAQMIREVASKTNDKAGDGTTTATVLAQAIVQEGLKSVAAGMNPMDLKRGIDKAVAIAIEDIKTSSKKVTTNAEIAQVGTISANGDKEVGEMIAKAMDKVGNEGVITVEEAKTAETELDVVEGMQFDRGYLSPYFITNADKMEVQLEEPLILLFEKKLSSLQPLLPVLEAVVQSGRPLLIIAEDVEGEALATLVVNKLRGGLRVAAVKAPGFGDRRKAMLEDIAILTGAQVVSEDIGIKLENVSLEMLGRAKKVSITKDDTTIVDGVGEKADIEARIAQIKRQIEDTTSDYDKEKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRVDDALNATRAAADEGIVPGGGTALLKASKALAGVVGDNDDQTAGIAIVRRALQAPIRQIAENAGVEGSIVVGKILENDNSAFGFNAQTEQYVDLVVDGVIDPAKVVRTALQNAASVAGLLITTEAAIVEAPKKGGGAPAGGGMPGGMGDMDF
|
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.
|
P0CAT9
|
A8YTZ3
|
DNLJ_LACH4
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Lactobacillus
|
MAKITLDEAKKEAASLRTKLDEWADAYYSKDAPEVEDNVYDQSYNRLLELEKAFPEIVTPDSITQRVGGEIDSDFTKVNHPIPMLSMGDVFSKDELKEFDQRMQKLVGHPVEYNVELKIDGLSLSLEYQDGKLVRASTRGNGYIGEDVTANARYIADIPQVLPEPLTIEVRGECYMGKEAFAKLNQEREDEGLSVFANPRNAAAGSLRQLDPKVTKKRQLSTFIYTWVNPPREITSQHQAIERMHELGFHTNETGRKLANLDEVFDFIDEYTAKRNSLTYGIDGIVLKVDDLSLEQQLGNTVKVPRWEIAYKFPPEEQETIVRDIVWTVGRTGVVTPTAVMDPVQLAGTTVARASLHNPDYLNEKGVRIGDTVKLHKAGDIIPEISEVVLSKRPADSVPYEIPTTCPSCGQKLVHLEDEVALRCINPSCPAQVEEGIIHFASRPAMNIAGLGPKIVKQLIAKDLVHNVADLYHLTEDDLAQLDHFKEKSINNLLTAIDNSKKNSVELLITGLGIDHVGAKAARLIAQKFKNLEKIMSLGVQDIASIDTIGMTTAESMTTYFAQPEAQKLIEELRESGLNMDYLGADEPEEAPDNPFKDKTVVLTGKLEHYTRSEFTKKLQALGAKVTGSVSHKTDYVIYGKDAGSKYNKAEQLGVPLLTEEEAIAQIE
|
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
|
A8YTZ3
|
A4VQY5
|
YBEY_PSEU5
|
Endoribonuclease YbeY
|
Pseudomonas
|
MIELDLQCASTGAAPAAADLQRWCELALRQRSGDSELTIRLVDEEEGRELNRTWRQKDYATNVLSFPADVPDEFLDIPLLGDLVICVPVVEREAAEQGKTLDAHWAHLVIHGCLHLLGYDHIEDAEAEEMEALERQLLAELGHPDPYAEDSPETGICKDS
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
A4VQY5
|
A3QJF5
|
FMT_SHELP
|
Methionyl-tRNA formyltransferase
|
Shewanella
|
MKPLKILFAGTPDFAARHLQALIDSEHQVIGVYSQPDRPAGRGKKLQASPVKALALEHDIPVYQPVSLRNEDAQAELAALGADIMVVVAYGLILPQVVLDTPRLGCINVHGSILPRWRGAAPIQRALWAGDAATGVTIMQMDIGLDTGDMLLKTHLPIEDRDTSASLYEKLAEQGPSALIQALKGLAEGSLTPEPQDEALANYAEKLSKEEAQLDWRKPAEQLWREVRAFNPWPASHFPHQDAAIKVWQASVSIEAAKQAPGTIIRADKQGIAVATGEGALVLETIQLPGKKAMAVADVLNARGDWFTPGTQLQGVTPADEAQA
|
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.
|
A3QJF5
|
Q2T9Z5
|
TF2H5_BOVIN
|
TFIIH subunit p8
|
Bos
|
MVNVLKGVLIECDPAMKQFLLYLDESNALGKKFIIQDIDDTHVFVIAELVNVLQERVGELMDQNAFSLTQK
|
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. Necessary for the stability of the TFIIH complex and for the presence of normal levels of TFIIH in the cell.
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Q2T9Z5
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C5CPT7
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PQQA_VARPS
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Pyrroloquinoline quinone biosynthesis protein A
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Variovorax
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MKWETPTATDLRFGFEITMYVSAR
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Required for coenzyme pyrroloquinoline quinone (PQQ) biosynthesis. PQQ is probably formed by cross-linking a specific glutamate to a specific tyrosine residue and excising these residues from the peptide.
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C5CPT7
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A4FZN7
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HYPA_METM5
|
Hydrogenase maturation factor HypA
|
Methanococcus
|
MHELSYATSVLNAILDAVKQQEELGRKVIKVNDINLEIGDLTLLSVDQLQFVFEVISEDTVCKGAELKAEIVKPKIFCMDCEFEGNLDTKDELEVACPKCESRNVKLKGGKEFNIVNATIEFDDEE
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Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase.
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A4FZN7
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Q6A9Q5
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MRAY_CUTAK
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UDP-MurNAc-pentapeptide phosphotransferase
|
Cutibacterium
|
MKNILLAGAVSMIGTLVGTRWFIHWLAAKGYGQFIRDDGPTTHKTKKGTPTMGGAVIIVSVLLAYLVAHLVTWTHPSISALLVLWLFSGLGFIGFLDDWTKISKQRSLGLKPKGKLLGQAFVAITFAIGVMYFPDVHGVTPGSPAISFLRDISWLYLPVWLGIVWVILLIAGSSNAVNLTDGLDGLATGASTMVFGAYTVLSIWQFNQWCSRPTTAGNHCYAVRDPHDIAVVAIAIAGACFGFLWWNAKPAQIFLGDTGSLALGGAVAGMAVVSRTELLLVIIGALFVIETVSVMLQVSVFKITGGKRVFKMAPLHHHFELKGWAEVTVVIRFWIICGLAVSAGLGIFYAEWVAGQ
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Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
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Q6A9Q5
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Q59418
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OGL_PECAS
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Oligogalacturonide lyase
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Pectobacterium
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MAKGNKIPLTFHTYQDAATGTEVVRLTPPDVICHRNYFYQKCFFNDGSKLLFGAAFDGPWNYYLLDLKEQNATQLTEGKGDNTFGGFLSPNDDALYYVKNTRNLMRVDLTTLEEKTIYQVPDDWVGYGTWVANSDCTKMVGIEIKKEDWKPLTDWKKFQEFYFTNPCCRLIRVDLVTGEAETILQENQWLGHPIYRPGDDNTVAFCHEGPHDLVDARMWFINEDGTNMRKVKEHAEGESCTHEFWVPDGSAMIYVSYLKDDTNRYIRSIDPVTLEDRQLRVMPPCSHLMSNYDGTLLVGDGSDAPVDVQDDGGYKIENDPFLYVFNLKTGKEHRIAQHNTSWEVLEGDRQVTHPHPSFTPDNKQVLFTSDVDGKPALYLAKVPDSVWN
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Involved in degradation of pectin, which causes soft-rod disease in plants.
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Q59418
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P56868
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MURI_AQUPY
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Glutamate racemase
|
Aquifex
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MKIGIFDSGVGGLTVLKAIRNRYRKVDIVYLGDTARVPYGIRSKDTIIRYSLECAGFLKDKGVDIIVVACNTASAYALERLKKEINVPVFGVIEPGVKEALKKSRNKKIGVIGTPATVKSGAYQRKLEEGGADVFAKACPLFVPLAEEGLLEGEITRKVVEHYLKEFKGKIDTLILGCTHYPLLKKEIKKFLGDVEVVDSSEALSLSLHNFIKDDGSSSLELFFTDLSPNLQFLIKLILGRDYPVKLAEGVFTH
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Provides the (R)-glutamate required for cell wall biosynthesis. Converts L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine.
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P56868
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P0DPU2
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VA543_SCODE
|
Cysteine-rich venom protein
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Scolopendra
|
MNFVIYGVIVVLTSQLYVDGWGCQMSERGLDKKMKNKILKHHNELRQKVANGQERGQPTASNMKQLRWNDELAANAQRAAERCIFQHTSDEGRKTTKYGVAGESMYAGTFSNPLKTAVDMWYEEVRDVNPSILDSYDYYPGAVIGHYIQLVWAETEAIGCGYAKSAADGESYVFCHYAPHGLFPQQSVYKRGSPASACKKGQSSRYPGLCK
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Shows trypsin inhibiting activity. The protein is highly thermally stable, since its incubation in boiling water during 10 minutes does not reduce its activity.
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P0DPU2
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Q24ZT5
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QUEC1_DESHY
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Queuosine biosynthesis protein QueC 1
|
Desulfitobacterium
|
MGKNKVVLLFSGGIDSTVLLFWLLSRNYEIFPLFINYGQKSYEGELEAINKILKDLNTKNNLLTLNMPELQLVGSGALVGEYPKNISSHNEWYASEFFPNRNMILLSIAATYGYKLQISKIAIGVVGDSYQDTTRTFLEAMEMTLAQSIARYELIAPFAGHPRQKVIEEAYRLQVPLKSTFSCNAMGNRHCLLCTSCYEREKAIQLHEQCGKERAEKSDF
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Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
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Q24ZT5
|
Q72HF4
|
GLMS_THET2
|
L-glutamine--D-fructose-6-phosphate amidotransferase
|
Thermus
|
MCGIVGYVGFRNATDVLLDGLRRLEYRGYDSAGIAVRTPEGLKVVKRSGKLSALAQAVGKTPLQGALGIGHTRWATHGAPTDPNAHPHTTEDGRIALIHNGIFENYLELKEALEARGHRFRSETDTEVLAHLLEETYRGDLLEALREALKAVRGAYAVVVAHEDHEEIVAARTVSPLVVGLGEGENFLASDVPALLPYTRRVIFLHDGDVVRLTREGVEITDLEGRPVQREAVEVDWTLEAAEKGGFPHYMLKEIYEQPWVLENTLGGRLREEEGTVELGLALDPREVDRVHVIACGTASYAGLYGKYLLETLARLPTEWDVASEYRYRDPVVDSRTLALAISQSGETIDTLEGLREAKRKGARSLGVINAKGSTLTREVEDVLYIHAGPEIGVASTKAYTAMLVAMALLAVWFGRARGALALEEAQSLLREMRRLPRLVEEVLEKRPLVAHVAEKYHQARDFLFLGRHVQAPTAYEGALKLKEISYIHAEAYPAGEMKHGPIALIDEHLPVVVLATKGPLYEKTLSNIQEVRARGGKVIAIATEGDEEIPRLAQDVIYVPEVHPLLAPIVSVVPLQLLAYEIAVLLGRDVDQPRNLAKSVTVE
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Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
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Q72HF4
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A5VWP2
|
CYOE1_PSEP1
|
Heme O synthase 1
|
Pseudomonas
|
MATLLSVRRARWRDYLELTKPKVVVLMLITSLAGMFLATRAGVSWSVLLFGNLGIGLCAGGAAVVNHVVDRRIDALMARTHKRPLAQGRVEPLPALLFALALALLGMVLLLVFTNALTAWLTLASLLGYAVLYTGFLKRATPQNIVIGGLAGAAPPLLGWVAVSGHVSAEPLLLVLIIFAWTPPHFWALAIHRKEEYAKADIPMLPVTHGERYTKLHILLYTLILLAVSLLPYAIHMSGPLYLACALGLGLRFLHWAWVLYRSSRPHAAIGTFKYSIGYLFALFIALLLDHYLLLSL
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Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
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A5VWP2
|
A4YHK0
|
ALBA_METS5
|
DNA/RNA-binding protein Alba
|
Metallosphaera
|
MSGTSPTPSNVVLVGKKPVMNYVLAALTLLNQGVPEIIIKARGRAISKAVDTVEIVRNRFLPDKIEIRAIGVGSQVVTSQDGRQSRVSTIEISIKKKA
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Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.
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A4YHK0
|
Q9BVM2
|
DPCD_HUMAN
|
Protein DPCD
|
Homo
|
MAVTGWLESLRTAQKTALLQDGRRKVHYLFPDGKEMAEEYDEKTSELLVRKWRVKSALGAMGQWQLEVGDPAPLGAGNLGPELIKESNANPIFMRKDTKMSFQWRIRNLPYPKDVYSVSVDQKERCIIVRTTNKKYYKKFSIPDLDRHQLPLDDALLSFAHANCTLIISYQKPKEVVVAESELQKELKKVKTAHSNDGDCKTQ
|
May play a role in the formation or function of ciliated cells.
|
Q9BVM2
|
Q8NGJ2
|
O52H1_HUMAN
|
Olfactory receptor OR11-45
|
Homo
|
MPSASAMIIFNLSSYNPGPFILVGIPGLEQFHVWIGIPFCIIYIVAVVGNCILLYLIVVEHSLHEPMFFFLSMLAMTDLILSTAGVPKALSIFWLGAREITFPGCLTQMFFLHYNFVLDSAILMAMAFDHYVAICSPLRYTTILTPKTIIKSAMGISFRSFCIILPDVFLLTCLPFCRTRIIPHTYCEHIGVAQLACADISINFWYGFCVPIMTVISDVILIAVSYAHILCAVFGLPSQDACQKALGTCGSHVCVILMFYTPAFFSILAHRFGHNVSRTFHIMFANLYIVIPPALNPMVYGVKTKQIRDKVILLFSKGTG
|
Odorant receptor.
|
Q8NGJ2
|
Q95KV7
|
NDUAD_BOVIN
|
NADH-ubiquinone oxidoreductase B16.6 subunit
|
Bos
|
MAASKVKQDMPPVGGYGPIDYKRNLPRRGLSGYSMFAVGIGALLFGYWSMMKWNRERRRLQIEDFEARIALMPLLQAEKDRRVLQMLRENLEEEATVMKDVPGWKVGESVFHTTRWVTPMMGELYGLRASEEVLSATYGFIWYT
|
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes.
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Q95KV7
|
A9M6P3
|
KDSB_BRUC2
|
CMP-2-keto-3-deoxyoctulosonic acid synthase
|
Brucella
|
MLQTMKTLTLIPTRLGSTRLPNKPLADICGKPMIVHVADRAAAAKLGRTVIATDSEEIFKVVAAHGHEAIMTRGDHESGSDRIYEALAKLDPSGEIDAVVNVQGDLPTIDPDTIRRALLPLEDGPADIATLGVEITVEEEKTNPNVVKIVGSPLAGNRRLRALYFTRATAPYGEGPLYHHIGLYAYRRSALERFVKLGPSPLEKREKLEQLRALEAGMRIDVEIVKTVPLGVDTQADLDRARTFCSQAGTI
|
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
|
A9M6P3
|
Q95XP9
|
ZWILC_CAEEL
|
Protein zwilch homolog
|
Caenorhabditis
|
MPLTIEQLKQYNEKMAAKGEEDDAPAPVLLLDKYRVRVLPLTSIPFVMNHSSVSQLSLSSEDVLVVDFPSKGTGSGAGKAEKKMIFKKKIEPMEDSFEDKENVNEGGPLMTSFLTLEKLRKGMVGDVEIIGYECETSFFDANPIPLSDGVSLQRYIRLNCSEHFSPSISTLPVWISTTSSKFPSICWLAAGRTNRNVQFAAATRVLGHFNNENSERVVKQLNQACGTSQLNKYRAVYEEIRKIATENRPAPGEVTIDVRWSTKSTLVLLEHPDNAADCTIKIDLGWGDKRFFVDDEIFEQLFFVLNLADVLANPDNEVIFPMAPPANFDDLVQEMDALVEASSREDNVFVSNENFRGGDITDKVWNIVRKCNDVKQVTLLFRNFLQALAYGKIKSHAQERNKSHLASLIRISKSSEFKIPVLERLSTIDMMMEIGVESLRRRVIDIFSSQLLYPSDELEFILQTCENDLPAGNGAMNSAAISLLPITMALATANRIYELLNEKDHVILPDLTRRILQKYTASMIEKSRRGETETEYTFETTLPLLRMYKEGFMSKRPCIWTCENSNTVGANVQARVLTSLELQPSLEHINRLVNDSRPVWTATEEKPAMIKDLNADYTVVHTIFSYLPKM
|
Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis . Required for chromosome segregation, the assembly of the dynein-dynactin and mdf-1-mdf-2 complexes onto kinetochores and spindle pole separation . Its function related to the spindle assembly machinery and kinetochore-microtubule attachments likely depends on its association in the mitotic RZZ complex . The RZZ complex recruits the spindly-like protein spdl-1 to kinetochores . To prevent irregular chromosome segregation, the complex also inhibits the attachment of the kinetochore-associated NDC80 complex to microtubules . The recruitment of spdl-1 to kinetochores relieves this inhibition . Required for embryonic development .
|
Q95XP9
|
Q67WE2
|
CYL2_ORYSJ
|
Cyclase-like protein 2
|
Oryza sativa
|
MAHLATVVLLLVAAARQAPLAAGDHSANPRLPTCAAAPDVAAPQEHGDGGGVGGGRRILDITHAVRAELPVLGSCDGVGALVRLKKSMANGSRSNLSELRMSVHTGTHVDAPGHMWQPHFDAGLDVDTLDLGLLNGPALLVDVPRHSNVTAEVMESLNIPRGVRRVLFRTMNTDKRLMWQKESDLSFVGFTEDGAQWLVGYTDIKLVGVDYLSVASYEHMIPAHVVFLKSKEIVIVEALKLDDVEPGMYMLHCLPLRLAGAEGSPVRCILIK
|
May be involved in response to stresses.
|
Q67WE2
|
P10291
|
ITR2B_CUCSA
|
Trypsin inhibitor IIB
|
Cucumis
|
MVCPKILMKCKHDSDCLLDCVCLEDIGYCGVS
|
Inhibits trypsin.
|
P10291
|
B2SD97
|
HUTI_BRUA1
|
Imidazolone-5-propionate hydrolase
|
Brucella
|
MTKNSSTVFTHARIATLEEKAANLGLIEEAALVVKDARIVYAGPENKLPDEYASFEKIDCGNRLITPGLIDCHTHLVHAGNRAHEFELRLQGATYEEVARAGGGIVSSVRNLRAASEDDLVRETLPRLDALIAEGVTTVEVKSGYGLDRDSEIKSLKAARRLGEERDVAIRTTFLGAHALPPEMNGDKAAYIDRVINDMLPAIAEQGLADAVDGFCEGIAFLPDEIARVFDAAKAHDIPVKLHADQLSNLHGAALAASYGALSADHLEYTDADGAAAMASAGTVAVLLPGAYYFIRETQKPPVEAFRAAGTKMALATDNNPGTSPLTSLLLTMNMGATLFRMTVEECIAGVTREAARALGILDQTGTLEIGKDADLAIWDIERPAELVYRIGFNPLWKRVFKGQI
|
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
|
B2SD97
|
Q8PLG8
|
HIS5_XANAC
|
ImGP synthase subunit HisH
|
Xanthomonas
|
MTDVALIDAGGANLGSVRYALERLGVDARLVRDAAGLQGAQRVILPGVGAAPEAMSRLRAQGLVEPLRELQVPLIGICLGMQLLFEHSEEGDVECLGLLPGIVRHMTPALGIRIPHMGWNQLVPMRDSALLAGLPERASAYFVHGYAAPVTADTVAACDHGGLFTAVVQNGLRCGAQFHPERSAETGARILRNFLEMSFP
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
|
Q8PLG8
|
Q2FMT2
|
CHEB1_METHJ
|
Protein-glutamate methylesterase/protein-glutamine glutaminase 1
|
Methanospirillum
|
MIRVLVIDDSLFIRTVVQDMLSDDPDIQIVGVASDGLEALDKIRELKPDLITLDIEMPRLDGLSMLERKKEIDRFPKTLVLSSLTSEGAEMTKRAIALGADDFMLKPRGIKNIREIGGELKHKIKNICTIAYITAKPVLKDSNARNVVLIGSSAGGPPMLDTIVSKLPSDLNAAVIITQHMPKGGFTAALAARLNRISPLQIRETENGDVLKNGTVLVSRAGFHTIISSVLDKGGSQSGKIILTDSPPVHNVKPAVDKTFISAAQVFGNHCVTAILSGMGNDGGEGTEAIKKAGGVTIVCREEDCLVYGMARSALSRNCVDHVLSLQAIPEKIVETIRAMNG
|
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
|
Q2FMT2
|
A1DG68
|
LKHA4_NEOFI
|
Leukotriene A-4 hydrolase homolog
|
Aspergillus subgen. Fumigati
|
MPTVVNPPRDPNTLSNYNNWVSTHITANFDILFDQRKLAGSVIHQFRSTTHGESNHIILDTNHLDIGSVKVNGQPSEWEYLPRLEPYGTPLKIKLDQGVKLNEMIEVDISVKTTEKCTALQWLTPAQTSNKKHPYMFSQCQAIHARSIFPCQDTPDVKCTLDFNITSPLPVIASGLPVRGSSEAPKSDGKTLYKFHQKVPIPSYLFALASGDISEAPIGPRSVVATSPDKLGECQWELEADTEKFINAIEKIVYPYVWGEYNVLILPPSFPYGGMENPIFTFATPSIISKDRENIDVIAHELAHSWSGNLVTNASWEHFWLNEGWTTYLERRIVAAVHGEPYRHFSAIIGWKALTDSVEHFGPEHDFTKLITNLKGMDPDDAFSSIPYEKGFNFLFHLENLVGKSKFDLFIPHYFNKYKGKSLDSYEFKSTILDFFKDDSEASTALNELDWDSWFYAPGLPPKPDFDTSLVDVVYDLAKKWLSLPNSSFKPQPEDIRGLTANQVVVFLEQILVSERQLTPELSKLMGEIYGLAASQNIEVANLYFQVGLQAGDASVLEPTADLLGKIGRMKFVRPLYRKLAKFDRKRAVETFEKHRDFYHPICRAMVEKDLFGKKDE
|
Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro).
|
A1DG68
|
B5XNL1
|
NDK_KLEP3
|
Nucleoside-2-P kinase
|
Klebsiella
|
MAIERTFSIIKPNAVAKNVIGSIFSRFEAAGFKIVGTKMLHLTVEQARGFYAEHEGRPFFDGLVEFMTSGPIVVSVLEGENAVQRHRDLLGATNPANALAGTLRADYADSFTENGTHGSDSVESAAREIAFFFAEGEVCPRTR
|
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
|
B5XNL1
|
B6ENU6
|
GLPE_ALISL
|
Thiosulfate sulfurtransferase GlpE
|
Aliivibrio
|
MEQFQHISVTDAQEKLNQKDHNARMVDIRDPQSFGRGHVDGAFHLTNDTIVTLMNEVEFEQPVLVMCYHGHSSQGAAQYLINQGYEEVYSVDGGFEGWNKAGLPVEK
|
Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
|
B6ENU6
|
Q99490
|
AGAP2_HUMAN
|
Phosphatidylinositol 3-kinase enhancer
|
Homo
|
MSRGAGALQRRTTTYLISLTLVKLESVPPPPPSPSAAAVGAPGARGSEPRDPGSPRGAEEPGKKRHERLFHRQDALWISTSSAGAGGAEPPALSPAPASPARPVSPAPGRRLSLWAAPPGPPLSGGLSPDSKPGGAPSSSRRPLLSSPSWGGPEPEGRTGGGVPGSSSPHPGTGSRRLKVAPPPPAPKPCKTVTTSGAKAGGGKGAGSRLSWPESEGKPRVKGSKSSAGTGASVSAAATAAAAGGGGSTASTSGGVGAGAGARGKLSPRKGKSKTLDNSDLHPGPPAGSPPPLTLPPTPSPATAVTAASAQPPGPAPPITLEPPAPGLKRGREGGRASTRDRKMLKFISGIFTKSTGGPPGSGPLPGPPSLSSGSGSRELLGAELRASPKAVINSQEWTLSRSIPELRLGVLGDARSGKSSLIHRFLTGSYQVLEKTESEQYKKEMLVDGQTHLVLIREEAGAPDAKFSGWADAVIFVFSLEDENSFQAVSRLHGQLSSLRGEGRGGLALALVGTQDRISASSPRVVGDARARALCADMKRCSYYETCATYGLNVDRVFQEVAQKVVTLRKQQQLLAACKSLPSSPSHSAASTPVAGQASNGGHTSDYSSSLPSSPNVGHRELRAEAAAVAGLSTPGSLHRAAKRRTSLFANRRGSDSEKRSLDSRGETTGSGRAIPIKQSFLLKRSGNSLNKEWKKKYVTLSSNGFLLYHPSINDYIHSTHGKEMDLLRTTVKVPGKRPPRAISAFGPSASINGLVKDMSTVQMGEGLEATTPMPSPSPSPSSLQPPPDQTSKHLLKPDRNLARALSTDCTPSGDLSPLSREPPPSPMVKKQRRKKLTTPSKTEGSAGQAEAKRKMWKLKSFGSLRNIYKAEENFEFLIVSSTGQTWHFEAASFEERDAWVQAIESQILASLQCCESSKVKLRTDSQSEAVAIQAIRNAKGNSICVDCGAPNPTWASLNLGALICIECSGIHRNLGTHLSRVRSLDLDDWPRELTLVLTAIGNDTANRVWESDTRGRAKPSRDSSREERESWIRAKYEQLLFLAPLSTSEEPLGRQLWAAVQAQDVATVLLLLAHARHGPLDTSVEDPQLRSPLHLAAELAHVVITQLLLWYGADVAARDAQGRTALFYARQAGSQLCADILLQHGCPGEGGSAATTPSAATTPSITATPSPRRRSSAASVGRADAPVALV
|
GTPase-activating protein (GAP) for ARF1 and ARF5, which also shows strong GTPase activity. Isoform 1 participates in the prevention of neuronal apoptosis by enhancing PI3 kinase activity. It aids the coupling of metabotropic glutamate receptor 1 (GRM1) to cytoplasmic PI3 kinase by interacting with Homer scaffolding proteins, and also seems to mediate anti-apoptotic effects of NGF by activating nuclear PI3 kinase. Isoform 2 does not stimulate PI3 kinase but may protect cells from apoptosis by stimulating Akt. It also regulates the adapter protein 1 (AP-1)-dependent trafficking of proteins in the endosomal system. It seems to be oncogenic. It is overexpressed in cancer cells, prevents apoptosis and promotes cancer cell invasion.
|
Q99490
|
B8GNZ5
|
NUOK_THISH
|
NDH-1 subunit K
|
Thioalkalivibrio
|
MISLSHYLVLGAILFSLSIAGIFLNRKNVIILLMSIELMLLAVNMNFVAFSHFSGDLAGQVFVFFILTVAAAEAAIGLAILTLLFRNRQTINVQDLDEMKG
|
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.
|
B8GNZ5
|
P77395
|
CNOX_ECOLI
|
Trxsc
|
Escherichia
|
MSVENIVNINESNLQQVLEQSMTTPVLFYFWSERSQHCLQLTPILESLAAQYNGQFILAKLDCDAEQMIAAQFGLRAIPTVYLFQNGQPVDGFQGPQPEEAIRALLDKVLPREEELKAQQAMQLMQESNYTDALPLLKDAWQLSNQNGEIGLLLAETLIALNRSEDAEAVLKTIPLQDQDTRYQGLVAQIELLKQAADTPEIQQLQQQVAENPEDAALATQLALQLHQVGRNEEALELLFGHLRKDLTAADGQTRKTFQEILAALGTGDALASKYRRQLYALLY
|
Chaperedoxin that combines a chaperone activity with a redox-protective function . Involved in the protection against hypochlorous acid (HOCl), the active ingredient of bleach, which kills bacteria by causing protein aggregation . Functions as an efficient holdase chaperone that protects the substrates of the major folding systems GroEL/GroES and DnaK/DnaJ/GrpE from aggregation. In addition, it prevents the irreversible oxidation of its substrates through the formation of mixed disulfide complexes . After bleach stress, it transfers its substrates to the GroEL/GroES and DnaK/DnaJ/GrpE foldases . Lacks oxidoreductase activity .
|
P77395
|
A6V7S3
|
PPNP_PSEA7
|
Xanthosine phosphorylase
|
Pseudomonas
|
MFKVNEYFDGTVKSIAFDMTAGPATIGVMAAGEYEFGTSQLEVMHVIAGALTVRLPGSDEWQNFASGSQFTVPANSKFQLKVAQDTAYLCEYR
|
Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
|
A6V7S3
|
B4SR07
|
RECF_STRM5
|
DNA replication and repair protein RecF
|
Stenotrophomonas maltophilia group
|
MQIRRLALHQLRRFNAVELSPQPGLNLLTGDNGAGKTSILEALHLMAYGRSFRGRVRDGLVRQGQEALEIFVEWDEQRASHPPHRRKAGLRHSGQDWKGRLDGEDVAQLGNLCAALAVVTFEPGSHALVSGGGEPRRRFLDWGLFHVEPDFLSLWRRYSRALKQRNALLKQGGPSRMLDTWDHELAEAGEPLTSRRQHYLERLQQRTVALAAELAPQLGIQAMELSPGWRRHELPLADALLLARERDRQAGYTSVGPHRADWSVDFHNIPGRDALSRGQAKLTALACLLAQAEDYAEQRGEWPVIALDDLASELDRTHQARVLERLLGGPAQIFVTATETPAALQELTHIARFHVEHAQIVAVP
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The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
|
B4SR07
|
Q80WQ8
|
M18BP_MOUSE
|
Kinetochore-associated protein KNL-2 homolog
|
Mus
|
MIVTPLKHSGIHLSSGTLQRRNMPLDAVFIDSIPSGTLTPLKDLVKYQKSSLKVNGHKKNQLLEIRTSNNKDLFQSTMLSEATLPNSSLDISVIKPSMDRLRNEMIYESPGKIFQRMKAKVQRDKQEQLTRSSSMLGSPQGEHTKDFPPNTDKKAQLQQTYICEEKQTSVQSNDPSLGDPPILNQEQKNVSASCISKKALTRAQFGGQVLHSKESPVRITVSKKNTFVLGGIDCTYEKFENTDVNTISSLCVPIKNHSQSITSDNDVTTERTAKEDITEPNEEMMSRRTILQDPIKNTSKIKRSSPRPNLTLSGRSQRKCTKLETVVKEVKKYQAVHLQEWMIKVINNNTAICVEGKLVDMTDVYWHSNVIIERIKHNELRTLSGNIYILKGLIDSVSMKEAGYPCYLTRKFMFGFPHNWKEHIDKFLEQLRAEKKNKTRQETARVQEKQKSKKKDAEDKETYVLQKASITYDLNDNSLERTEVPTDPLNSLEQPTSGKERRHPLLSQKRAYVLITPLRNKKLIEQRCIDYSLSIEGISDFFKAKHQEESDSDIHGTPSSTSKSQETFEHRVGFEGNTKEDCNECDIITARHIQIPCPKSKQMLTNDFMKKNKLPSKLQKTENQIGVSQYCRSSSHLSSEENEVEIKSRTRARNTKERLNRERENTNHITKDILLISETEGERACYITPKRPRSCYITPKRPRSSAKESHYKSAVSKDFLTEGKASDRTSRQLLDHLPGLTDDEEWSEQELQKLHCAFTSLPKHKPGFWSDVAMAVGSRTADECQKKYTEEPQGQGSRKHGSKKKQANKVQNGEKDSADAKTIKITAKVGTLKRKRQMRDCLEHLAKDNHDDFFTATPLQKQRIQLPSFQYSQDDDFLLDMDRDPASPSSIITSPLRSTTPQCQHFSPSMLAAIERNNCDRYVYQMQKNAKKYGKSNGGLVWGNIRKKTVKTDLSSPPPTRKALFNKDLGKNTDISKYFIDDTESDEEEKDYYFSNSD
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Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis.
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Q80WQ8
|
A2BTM6
|
MUTS_PROMS
|
DNA mismatch repair protein MutS
|
Prochlorococcus
|
MQEDTIIQKNLFAIGNDINEQKKITKIPENLSLEDLKKESQKRPRQRKNSTNLINKFKTDLISNNKNVCINEESYSYKTVSKLKLTPVMKHYVTLKEENKDRLLLYRLGDFFECFFEDAVLISNLLEITLTSKDAGKEIGKIPMAGVPHHAMERYCADLIKKNYSVVICDQLEKSSGNYGTPIKRGITRIITPGTVIEEGMLIAKKNNWISAIYLSEENSDESYEWGISKADVSTGELITLEGQSLSKLFDEIIKLDSSEIIVGSNTARDLLIKGNSQITYTVSQETNFGINEANYLIKNYFQIANLEGIGLKNLNNATRSLGGLLNYLEKINPSNLDKDSSLKISLDFPQIQYGHNKLIIDYQTQKNLEIKNTQRENNYVGSLLWSIDRTYTCMGARCLRRWIDSPLLNVNEIYKRQNIITNFLESKKLRIDTQNLLRAMGDLERLAGRACAGHASPRDLIAIAEGLKKLPRLKSIIELFKYDLPDWTDQLKNIDEGLLELADTISFKLVENPPLNISEGGMIHDGVDNILDGLRNLMDDYSEWLNKEESKERKISKISNLKIQFHKNFGYYISINKSKVNLAPQHWIKRQTLTNEERYITSEIKNKENKIFQIKSRASSKEYEIFCELRNIVAEKTKQIRSIAKSIASLDALLGLSITSVENNFIKPSLIPINDSMTKNSTKIIAGRNPIVEQLLSDKKFVANDISFEDNQKLIILTGPNASGKSCFIRQLGLIQILTQIGSFVPANNAEIKIADRIFTRIGAVDDQSSGQSTFMVEMSETASILNQATSSSLVLLDEIGRGTSTFDGLSIAWSVSEYLAKKIQCNTIFATHYHELNYLKNTNKNIQNFQVLVEQNNDQLIFSHRIVKGGSNKSYGIEAAKLAGVPKEVIEKAKSVLNSLEENNKLNYDIK
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This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
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A2BTM6
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Q0AK79
|
MIAB_MARMM
|
tRNA-i(6)A37 methylthiotransferase
|
Maricaulis
|
MSTTRKRLFIKTYGCQMNVYDSDRMKDVLTPLGYESAETPEGADLVILNTCHIREKAAEKVYSELGRLRPLKDEKAASGGMTIAVAGCVAQAEGAEIMKRAPVVDLVVGPQTYHKLPELIAQAHRAKGEALDTEFEVEDKFDRLGSDRQVEGYSAFVTVQEGCDKFCTFCVVPYTRGAEWSRPVDQIVAEIRALAAKGIREVTLLGQNVNAFHGAPPSGREAEGAWGLGQLVRHVALIGGIERIRFTTSHPRDMDEVLIQAFADTPKLMPYFHLPVQAGSDKILKSMNRQHTAEEYVAIIDRLRAARPDIAISGDMIVGFPGETDADFEATLDLVRRVKFASCFSFKYSKRPGTPGAAMFNQVDEGVKSARLAVLQELLSDQQAAFNESMIGRTLPVLFEKPGRMGGQLHGRSPYLQSVHVDGPAELIGQVGEVRIEAASRNSLSGSLTGSKRSAA
|
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
|
Q0AK79
|
A8F060
|
HTPG_RICCK
|
High temperature protein G
|
belli group
|
MTQEKKKFDAEVGKILNLMIHSLYSNKEIFMRELISNASDACDKLRYLSQSNNTLVAGDSNFKITVKIDKNNGQIIIRDNGIGMNKEDLIENLGTIARSGTANFLKNLSGDSKKDNMLIGQFGVGFYSSFMVADKVTVTSRKAGEDKVYVWESDGLGEYIVSNSGKEFTRGTAIVLNIKKEEDNFLDHFRLKHIVKSYSDHIAVPIYFFDENGNSEIQLNSASALWTRPKLEITEEQYKEFYKSLSYTIDDPWITLHNKNEGAIEFTNLLFIPSSKTFDLFHPDRKRRVKLYIKRVFISDENIDLIPSYLRFLRGVVDSEDLPLNISRESLQHNSILDKIKNAITKRVLAELKKKKEESPEDYNKFWSNFGGALKEGLCESTTDHEKLLEVCIFRSALHNKMISLDEYIANFKEGQNTIYYLSGDNPDKLLSSPQIEGLLSKNIDVLLFTDTVDDFWVNVNSEYKGHAIKSATRSDIDVEQTTSSSEEKNTDSKKSDDEYKLLTDYFKETLGDLVKDVKISKKLTSSPACLAVSESAMDIRMERFLIEQKQIANASAKNLELNPKNKIIEKIFNDLKANNKNNKELVNLIFDQACILEGEPVADTGAFSKRLNDIVQKAILSL
|
Molecular chaperone. Has ATPase activity.
|
A8F060
|
B0Z4N9
|
CYF_OENAR
|
Cytochrome f
|
Oenothera
|
MKNTFSWIKKEITRSISLSLMIYIITRTSISNAYPIFAQQGYENPREATGRIVCANCHLANKPVDIEVPQAVLPDTVFEAVVRIPYDRQVKQVLANGKKGGLNVGAVLILPEGFELAPPARISPEMKERIGNPSFQSYRPTKKNILVIGPVPGQKYSEITFPILSPDPATNKDVHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNATAAGIVSKIIRKEKGGYEITITDASDGRQVVDIIPSGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEVVLQDPLRVQGLLFFLASVILAQIFLVLKKKQFEKVQLSEMNF
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
|
B0Z4N9
|
Q9UKA4
|
AKA11_HUMAN
|
Protein kinase A-anchoring protein 11
|
Homo
|
MATFRNNHMKTKASVRKSFSEDVFQSVKSLLQSQKELCSVTAEDCLQQDEHANLTEVTFLGFNEETDAAHIQDLAAVSLELPDILNSLHFCSLNENEIICMKNINKPLDISSDPLNQSHPSGMLCVMRVSPTSPRLRIDFIFSLLSKYATGIRYTLDTFLHQKHQLETTDEDDDDTNQSVSSIEDDFVTAFEHLEEEETSKPYNDGMNITVLRSQCDAASQTVTGHHLETHDLKILISSGQQKSLAKPSTSSVNVLGHKELPSVKTSVTTSISEPWTQRSFYRSSNASDKDSDLQKTFFSSSPAYSSESECSSPSPVIFLDEEGYQKSLKAKLELPKIPVMKDDIEDSDSEVSEFFDSFDQFDELEQTLETCLFNKDPVIGKSSQRKGHKHGKSCMNPQKFKFDRPALPANVRKPTPRKPESPYGNLCDAPDSPRPVKASREDSGLFSPIRSSAFSPLGGCTPAECFCQTDIGGDRIHENHDSVYYTYEDYAKSISCEVLGSVLRTHHTNTLSNINSIKHGENKTVTFKHGNLDQKNKSKNKSLMIKDSIQKFAADLVEKSFGSAFKDLQKGVSSCTNALYHLAIKLTSSVLQMAFDELRRQRAFSLKERAISGLANFLVSEALSNALKDLQYVKKQIFTNTVARFAADLAEELVFEGIMEVCQFSYPQTPASPQCGSFDFEDKVVKLYAKDLSESVIQEAFIELSQVDVTFTTKAAVSVSTDNIKYVSAESVVPSTQAVTFSPSFHNQAIMVTKPVQEYKKEYTVQQALFCTSGIVTSIPVPLAGSALLPYHISSTACQAKAHLSSDDSNSNGDSAQVHIATKNREEKAACLRNICLPSEHNPGNQNDFKPTNDDIEMQSSSKLPNDPAIISNFSAAVVHTIVNETLESMTSLEVTKMVDERTDYLTKSLKEKTPPFSHCDQAVLQCSEASSNKDMFADRLSKSIIKHSIDKSKSVIPNIDKNAVYKESLPVSGEESQLTPEKSPKFPDSQNQLTHCSLSAAKDCVPECKVSMVHGSSLETLPSCPAVTGQKSDLKESAKDQPLKKHNLNSTSLEALSFGQENPFPHSHTFSSTALTCVDGLHVEDKQKVRDRNVIPDTPPSTPLVPSRASSEWDIKKLTKKLKGELAKEFAPATPPSTPHNSSVGSLSENEQNTIEKEEFMLKLMRSLSEEVESSESGELPEVDVKSEHSGKKVQFAEALATHILSLATEMAASHLDNKIIQEPKVKNPCLNVQSQRSVSPTFLNPSDENLKTLCNFAGDLAAEVITEAEKIAKVRNCMLFKQKKNSCYADGDEDYKVEEKLDIEAVVHPREVDPFILSLPPSSCMSGLMYKYPSCESVTDEYAGHLIQILKQEGGNSELIMDQYANRLAYRSVKSGLQEAAKTTKVQCNSRMFPVPSSQVKTNKELLMFSNKEHHQEADKKRQSKRNEGYFCKNQTCERTLDPYRNEVSQLYSFSTSLVHSITKDAKEELTASLVGLPKSLTDSCLFEKSGYEEDNECHVTPELPKSLQPSSQNHRFYHSTGSLNGYGCGDNVVQAVEQYAKKVVDDTLELTLGSTVFRVSETTKSADRVTYAEKLSPLTGQACRYCDLKELHNCTGNSSQHFFRQGSLASSKPASNPKFSSRYQKSRIFHLSVPQIHVNLDKKAVLAEKIVAEAIEKAERELSSTSLAADSGIGQEGASFAESLATETMTAAVTNVGHAVSSSKEIEDFQSTESVSSQQMNLSIGDDSTGSWSNLSFEDEHQDESSSFHHLSESNGNSSSWSSLGLEGDLYEDNLSFPTSDSDGPDDKDEEHEDEVEGLGQDGKTLLITNIDMEPCTVDPQLRIILQWLIASEAEVAELYFHDSANKEFMLLSKQLQEKGWKVGDLLQAVLQYYEVMEKASSEERCKSLFDWLLENA
|
Binds to type II regulatory subunits of protein kinase A and anchors/targets them.
|
Q9UKA4
|
Q606F1
|
KAD_METCA
|
Adenylate monophosphate kinase
|
Methylococcus
|
MRIMLLGSPGSGKGTQAKYLTERFGIPQISTGDMLRAAVREGTPLGMEAKKIMDAGQLVSDSIILGLIKERIAAPDCANGFLLDGFPRTIVQADALAELGVTLDHVVEIAVDDEEIVRRLSGRRVHPASGRTYHVVFNPPKVEGRDDETGEPLVQREDDKEETIRRRLEIYHVQTKPLVDYYRSKAAQGGVKFHTVPGVGSVEAIRDAVLASLA
|
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
|
Q606F1
|
Q6YK33
|
INS_GORGO
|
Insulin A chain
|
Gorilla
|
MALWMRLLPLLALLALWGPDPAAAFVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYCN
|
Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
|
Q6YK33
|
O14345
|
PFA3_SCHPO
|
Protein fatty acyltransferase 3
|
Schizosaccharomyces
|
MNLIHKVSTICQCVLVILAKYCMQIIALSLMSGVQWLAWGIYKINKNRVGIIILFLYIMIVTCYVLTNLTPPGSPSETSFDPNSTRQYMTLQNGKSRFCEKCQEYKCDRSHHCSQCNKCILRMDHHCMWFKNCVGFRNHKFFFLECFYLNLYSICVLYSTFVAITKTFTAEGANISAIYLVFWGFLFAFAVGMSIVMTAFTFYHTSLLIHNLSTLESMSSSWSRYTHSTQPFNVGWYENWCQIMGKSPFLWLLPFPNSIGEGVEYPLNANALPYLPQTEEKNDKLYKSSVPASIAGAEGWSSDEEQYAMKNRRWNPHMGQYEWIEDFLV
|
Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at one or more of its N-terminal cysteine residues, which is required for its proper membrane localization.
|
O14345
|
P0CV11
|
RLR43_PLAVT
|
Secreted RxLR effector protein 43
|
Plasmopara
|
MKVTMALAALCVALQAPCIGSESTPSNLNNRHLRHEHDSNTPLQRRDEALVPAHRVYDPVSGLACSLVGKCMVCPTSEKDESYCRETGYRQELDCPRVEDDVVHTKSVNQRTTRFRPCSFAEPARPGVAFVKFEVGNLRTLLQKL
|
Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
|
P0CV11
|
D0N0R8
|
CRE2_PHYIT
|
Core RXLR effector 2
|
Phytophthora
|
MRWLIWTAVSTLVMLLAMTEVSASIRTPEISTKGSTSATAFRARSLSSEYNSLEKRSLRDKSSSLITESEERSIAESLANKVVNRLFKTLYKKEMTPLTFRAKMMGRDNFLVGDYKVWWDKARATGTIPKWKFQRSKSYT
|
Effector that is involved in host plant infection. Contributes to virulence during the early infection stage, by inhibiting plant defense responses induced by both PAMP-triggered immunity (PTI) and effector-triggered immunity (ETI).
|
D0N0R8
|
P83255
|
VM1F_MACLB
|
VlF
|
Macrovipera
|
ERFAPRYIELVIVADHSVATKYNDNVTAILSWVHQLVNNIILFYRDLNVHFTLSAVEVWSNGDLINVQPEATVTLNLFGEWRERDLLNRRMHDNAQLLNNVALDDNTIGLAYDEGMCDPKYSVGIVKDHSAINRMVAATMAHEIGHNLGMNHDGSQCNCGGNGCVMSAVLMQQHSYQFSDCSKDEYQRYLTNHNPQCILNQP
|
Has fibrino(geno)lytic activity on the alpha and beta chains of fibrinogen (FGA and FGB). Inhibits human ADP- and collagen-induced platelet aggregation on platelet-rich plasma but does not affect the thrombin-induced aggregation of rabbit washed platelets. Slightly degrades plasminogen.
|
P83255
|
Q9UK85
|
DKKL1_HUMAN
|
Protein soggy-1
|
Homo
|
MGEASPPAPARRHLLVLLLLLSTLVIPSAAAPIHDADAQESSLGLTGLQSLLQGFSRLFLKGNLLRGIDSLFSAPMDFRGLPGNYHKEENQEHQLGNNTLSSHLQIDKMTDNKTGEVLISENVVASIQPAEGSFEGDLKVPRMEEKEALVPIQKATDSFHTELHPRVAFWIIKLPRRRSHQDALEGGHWLSEKRHRLQAIRDGLRKGTHKDVLEEGTESSSHSRLSPRKTHLLYILRPSRQL
|
Involved in fertilization by facilitating sperm penetration of the zona pellucida. May promote spermatocyte apoptosis, thereby limiting sperm production. In adults, may reduce testosterone synthesis in Leydig cells. Is not essential either for development or fertility.
|
Q9UK85
|
Q7WME6
|
TAL_BORBR
|
Transaldolase
|
Bordetella
|
MPSQLEALRRHTVVVADTGDFEAMRALRPTDATTNPSLILKAVQQEAYRPLLVQTARAHQGASPAEITDRLLVAFGRQILDIVPGRVSTEVDARLSFDTRATVERARGLIALYQAAGVPRERVLIKIASTWEGIQAARVLQAEGIRCNLTLLFCLPQAAACADAGVQLISPFVGRIYDWHKKNAGAEWVEDARRGANDPGVQSVSRIYRYYKRFGIETEIMGASFRNVDQILALAGCDLLTISPELLTRLSQTEGEVPAALSPQAGHDDADAVRLDGGEVAFRTQLNEDAMASEKLSEGIRLFVADARKLDALIESHGAA
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
Q7WME6
|
A6VJ61
|
RFCS_METM7
|
Clamp loader small subunit
|
Methanococcus
|
MQKPWVEKYRPQTLSEVVGHHEIIKRLTNYVEKKSMPHLLFSGSPGVGKTTAALALAKDLYGETWRENFLELNSSDERGIDVIRTKVKDFARTKPIGDAPFKVIFLDESDALTSDAQNALRRTMEKYSDICRFVLSCNYPSKIIPPIQSRCAIFRFSPLKTEDLVENLKEISEKENLTLEKGGIDAIIYVSEGDMRKAINVLQTAAAVSDTVTEEIVYKVASKARPDEIKKMTQLALNGKFVESREQLYNLMIDWGMSGEDILIQIFREVPNLDISEKEKVHLVEAIGECDFRIVEGSNERIQLSALLAKMGILE
|
Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA.
|
A6VJ61
|
Q90873
|
IFNB_CHICK
|
Interferon type B
|
Gallus
|
MTANHQSPGMHSILLLLLLPALTTTFSCNHLRHQDANFSWKSLQLLQNTAPPPPQPCPQQDVTFPFPETLLKSKDKKQAAITTLRILQHLFNMLSSPHTPKHWIDRTRHSLLNQIQHYIHHLEQCFVNQGTRSQRRGPRNAHLSINKYFRSIHNFLQHNNYSACTWDHVRLQARDCFRHVDTLIQWMKSRAPLTASSKRLNTQ
|
Has antiviral activities.
|
Q90873
|
Q21VL4
|
THIM_ALBFT
|
4-methyl-5-beta-hydroxyethylthiazole kinase
|
Rhodoferax
|
MAAKLSFSDLWSDVCAVRDRSPLVHSITNLVVINFNANVLLAAGASPVMAHAHEEVADMVGIAQALVLNIGTLDPYWIESMQLALRAAAKRGIPVVLDPVGAGATKYRNEAIEQLLMTSLPTVVRGNGSEIMSVAGSAAQTRGVDSSAAATDALGAAQSLVQRTQGVVCVSGQIDHILDASHRWAQLSNGHAWMTRITGVGCSATALIGAFCAVQPDAWRATVAAMALLGVVGEVAAEKVIARGKGVGSLQMALLDELQLLDQGTFEQRLKLEVAQW
|
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
|
Q21VL4
|
Q1QN30
|
RL3_NITHX
|
50S ribosomal protein L3
|
Nitrobacter
|
MRSGVIAQKVGMTRVFTDAGEHIPVTVLRLSNCQVLGHRTSEKNGYVALQLGSGARKTVYLPKAERGQFAVAKVEPKRKVAEFRVSEDSLIPVGAEIQADHFVVGQFVDVTGTSVGKGFAGGMKRWNFGGLRATHGVSVSHRSIGSTGGRQDPGKTFKNKKMPGHMGVDRVTTLNLRVVQTDVERGLILVEGAVPGSKGGWIAVRDAVKKPLPKDAPKPGKFKVAGDDKVTADAPTEKEGA
|
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
|
Q1QN30
|
Q5W270
|
PIGB_SERS3
|
Oxidoreductase PigB
|
unclassified Serratia
|
MIIQRLFGILYMLAGLAKAFPQFENVPAVLRQAAIANQGTWYAAASIWLGAHGDVINILVGVVLFGSGVILMLNPLWTTLVIYAQLLMMAVFVVILHQSQPQVMLLDGVFALAALYMLRGQYHRKPKPRTFPTTSFSLPTPSSESSFSAPLGDEYDVVIIGGGASGLTAASEFTHERVLVLEKSSTFGGNARYHTFNRLKHPTAGVCFQEPFPGSNMLRLLKKIGLEGKYKSNEKDTLVFFDTFLLLKCLGEIVVGFIKQPRYLLKLSVWGLTSQLFLHAIIGKPYVVAAKQLGDPIFADLYTFLDKFSPRGDFYPRLPWTPNGSWSKAHMELLDNISLYTYLFEPDKLGRLPEQLRPPARLGKLVENAVSTTLRVECLDIHDVSAYVGLHFLVGYLRGNLVTLPGGNGSISAGLCKYLSHQRNVTLQNHVQLTAVEPQHNGTCIQFTINGQPRQVQAQQIIWAAPKTQLATWLPGLPAKQLAAIKNIRHEDYYLANVFLSKPVLGHSFGGYMIEPDSNKDPFSWCKAGTCLVANWMDDHADVDVGVLTLLKPTTRSERQDRTAQNAFLALQQQTYAEIAKVLRNIGIGAEVIEDIQIWYWPAGLVTSVVGQQAEGVFETARQSFENIHFANQDSVGVGNIESAILSGIDAANAVKAQLMDTENVVEVAG
|
Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the oxidation of dihydro form of MAP (H2MAP) to yield MAP.
|
Q5W270
|
Q3J7Z8
|
RECR_NITOC
|
Recombination protein RecR
|
Nitrosococcus
|
MSLFGLSLGRLLEALRCLPGVGPKSAQRMAFHLLESDREGGRHLAQALLEALDKMTHCQTCRILSETDLCSLCADSRRDRGQLCVVEMPSDVQAIEQATSYSGRYFVLMGHLSPLDGVGPEALGMDLLAKRLDTDQIREVILATNLTVEGEATAYYISELAQTRGITTTRIAHGVPLGGELEFIDSNTLSHAFQSRRHL
|
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.
|
Q3J7Z8
|
B5Z947
|
RLMN_HELPG
|
tRNA m2A37 methyltransferase
|
Helicobacter
|
MKASVYDFTLKELSQLLKPSFRAKQLYLWLYAKYKTSFKDMQNNFSKDFIAYLEREFTLRTIEIAHVRKSIDGSKKYLFKSLRDNHTFEAVLLKMKDKKIDEETNAILEGEKYTVCVSCQIGCQVGCTFCFTQKGGFVRNLKASEIIQQALLIKEDNNLPIEKALNIVFMGMGEPLNNLDEVCKAIEIFNTGMQISPKRITISTSGVADKIPILAGKNLGVQLAISLHAVDDKTRSSLMPLNKKYNIECVLNEVRKWPLEQRKRVMFEYLLIKDLNDSLDCAKKLLKLLNGIKSKVNLILFNPHEGSKFERPSLESARMFADFLNSKGLLCTIRESKALDIEAACGQLREKKLSQQI
|
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
|
B5Z947
|
P44592
|
YAJC_HAEIN
|
Sec translocon accessory complex subunit YajC
|
Haemophilus
|
MEAQSPMSTLFIFVIFGLIFYFMIYRPQAKRNKEHKKLMSELAKGTEVLTAGGVIGKITKVTEGSDSIVIALNDTTEITINRNYIVSVLPKGSLKSL
|
The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions.
|
P44592
|
B5E8U0
|
GLYA_CITBB
|
Serine hydroxymethyltransferase
|
Citrifermentans
|
MSVLETFDPAVAEVIRQETERQEYNLELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCHCVDVVENLAIDRAKELFGADHVNVQPHSGSQANMAVYFSVLKPGDTVLGMNLAHGGHLTHGSPVNFSGKLFNIVPYGVSKETQTIDYEETERLALEHKPKMIVVGASAYPRIIDFEAFRRIADKVGAVVMVDMAHIAGLVAAGLHPSPVPYAEFVTTTTHKTLRGPRGGMIMCREDWAKTLNSNIFPGIQGGPLMHVIAAKAVAFKEALTPEFKQYQGQIVKNAKALAEGLTKRGFKLTSGGTDNHLMLVDLSQTELTGKVAEEALDRAGITVNKNGIPFDTRSPFITSGIRIGTPAATSHGLKEAEMEQVAGFIAEVLGNVSDEAKLAAVKTQVNALMKRFPMYANRLV
|
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
|
B5E8U0
|
Q5E9Q7
|
2ABB_BOVIN
|
PP2A subunit B isoform beta
|
Bos
|
MEEDIDTRKINNSFLRDHSYATEADIISTVEFNHTGELLATGDKGGRVVIFQREQESKNQVHRRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQNAAYFLLSTNDKTVKLWKVSERDKRPEGYNLKDEEGRLRDPATITTLRVPVLRPMDLMVEATPRRVFANAHTYHINSISVNSDYETYMSADDLRINLWNFEITNQSFNIVDIKPANMEELTEVITAAEFHPHHCNTFVYSSSKGTIRLCDMRASALCDRHTKFFEEPEDPSNRSFFSEIISSISDVKFSHSGRYIMTRDYLTVKVWDLNMENRPIETYQVHDYLRSKLCSLYENDCIFDKFECVWNGSDSVIMTGSYNNFFRMFDRNTKRDVTLEASRENSKPRAILKPRKVCVGGKRRKDEISVDSLDFSKKILHTAWHPSENIIAVAATNNLYIFQDKVN
|
The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
|
Q5E9Q7
|
A2VDL8
|
SC23A_BOVIN
|
SEC23-related protein A
|
Bos
|
MTTYLEFIQQNEERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCSRTTCRAVLNPLCQVDYRAKLWACNFCYQRNQFPPTYAGISELNQPAELLPQFSSIEYVVLRGPQMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLITFGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKVPVTQATRGPQVQQPPPSNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIEKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGGTLEIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVNQHNAPIPQGGRGAIQFVTQYQHSSGQRRIRVTTIARNWADAQTQIQNIAASFDQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKDDPSSFRFSETFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVNPSQTHNNMYAWGQESGAPILTDDVSLQVFMDHLKKTCCVKCCLMC
|
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex. Required for the translocation of insulin-induced glucose transporter SLC2A4/GLUT4 to the cell membrane.
|
A2VDL8
|
A0PQ00
|
PPK1_MYCUA
|
Polyphosphoric acid kinase
|
Mycobacterium
|
MIGNDRWVTEIETGPVTEARPDTNAREPGDRTPAAPPAATPAATTDQLPEDRYLNRELSWLEFNARVLALAADDSMPLLERAKFLAVFASNLDEFYMVRVAGLKRRDQMGLSALSADGLTPREQLGRIGEQTQHIASRHARVFRDSVLPALGEEGIYVVTWADLDQAEREQLSTYFHEQVFPVLTPLAVDPAHPFPFVSGLSLNLAVTVRQPEDGGQHFARVKVPDNVDRFVELGGTDTDGAEGAAVHRFLPLEELIAAFLPVLFPGMEIVEHHAFRITRNADFEVEEDRDEDLLQALERELARRRFGSPVRLEVADDMTEGMLELLLRELDVHPGDVIEVPGLLDLSSLWQIYGLDRPALKDRTFVPATHPAFAERETPKSIFATLREGDVLVHHPYYSFSTSVQRFIEQAAADPNVLAIKQTLYRTSGDSPIVRALIDAAEAGKQVVALVEVKARFDEQANIRWARALEQAGVHVAYGIVGLKTHCKTALVVRREGPVIRRYCHIGTGNYNSKTARLYEDVGLLTAAPDIGADLTDLFNSLTGYSRKLSYRNLLVAPHGIRAGIIERVEREVAAHLEHGPQAGKGHIRLKMNALVDEQVTDALYRASQVGVRIEVVVRGICALRPGAEGFSENITARSILGRFLEHSRILHFRAIDEFWIGSADMMHRNLDRRVEVMAQVKDPRLTAQLDDLFESALDPATRCWELGPDGQWTASPQEGRTVRDHQVSLMERHRSP
|
Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
|
A0PQ00
|
A1WWZ4
|
PYRG_HALHL
|
UTP--ammonia ligase
|
Halorhodospira
|
MTRYLFITGGVVSSLGKGISAASLGTILQARGLSVTLIKLDPYINVDPGTMSPFQHGEVYVTDDGAETDLDLGHYERFVRAPVSRRNNFTTGRIYESVIRKERRGDYLGGTVQVIPHVTDEIKRCIQEGADDVDVALVEIGGTVGDIESLPFLEAIRQMGTELGRERCMFMHLTLVPFIGTAGEMKTKPTQHSVKELRSIGIQPDILVCRAAHPIPEEERRKIALFTNVEPRAVIAALDVPNIYQIPEELHQQGLDHIVAEKWGLELPPANLADWHRVVEIMSNPEGEVTVAMVGKYVDLTDAYMSLNEALRHAGIQTRQRVNIRYVDSESLEREGCSALEGADAILVPGGFGQRGIEGKIEAVRFARESRIPYLGICLGMQLAVIEYARHQAGLENAHSTEFVRHPHHPVIGLITEWMTDEGEVEQRDEADDLGGTMRLGGQPCRLAAGTLINQVYGKDRIVERHRHRYEFNNHYRERLAEAGLSFSGWSQDGRLVEVVELPEHPWFIGCQFHPEFTSTPRDGHPLFASFLRAAIAHRDGTAQAFNHEQH
|
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
|
A1WWZ4
|
A8G2H0
|
TRPB_PROM2
|
Tryptophan synthase beta chain
|
Prochlorococcus
|
MVSTFSRKNQNYKKDDLNQPSKDGRFGKYGGQYVPETLMPALFELETAASNAWKDKLFVKELNHLLKTYVGRETPLYEAKRLTEYYKTKKAIPKIWLKREDLNHTGAHKINNALGQALLAIRMGKKRIIAETGAGQHGVATATVCARFGLKCIIYMGAEDIKRQSLNVFRMKLLGAEVKVVNSGTATLKDATSEAIRDWVSNVESTHYILGSVAGPHPFPKIVRDFHAVIGEETKKQCLESFGSLPDILLACVGGGSNAMGLFHPFVKETSVRLIGVEAAGGGVDTDKHAATITKGSVGILHGSMSLLLQDDNGQVQEAHSISAGLDYPGVGPEHSHLKDIGRAEYGSVTDQEALDSLRLVSELEGIIPALETSHAFAWLDKLCPTLEKDTHIVINCSGRGDKDVNTVASSLDI
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
A8G2H0
|
Q9Y5K3
|
PCY1B_HUMAN
|
Phosphorylcholine transferase B
|
Homo
|
MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRLTLTAPAPFADETNCQCQAPHEKLTIAQARLGTPADRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKRYRFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLELFGPDGAWKQMFQERSSRMLQALSPKQSPVSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISSMSEGDEDEK
|
Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis.
|
Q9Y5K3
|
P73540
|
LSPA_SYNY3
|
Signal peptidase II
|
unclassified Synechocystis
|
MARSFSLAKNPLFWQVAIAGIILDQLSKLWVSQAMDPVGTTWPLWSGVFHFTYVLNTGAAFSAFRGGAGWLKWLSLAVSVGLIIFAGKVPLRKLEQLGYGCILAGAVGNGIDRFLFGHVIDFLDFRLINFPIFNLADVSINIGIAALLWASFFPVSSRKVD
|
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
|
P73540
|
Q9GR88
|
ERF1_POLMI
|
Eukaryotic peptide chain release factor subunit 1
|
Polyandrocarpa
|
MAETETTADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQVSRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTDEGKEKKVNIDFEPFKPINTSLYLCDNKFHTEALTALLSDDNKFGFIVMDGNGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEKRHNYVRKVAETAVQLFITNDRPNVTGLVLAGSADFKTELSQSDMFDQRLQVKILKLVDVSYGGENGFNQAIELSAEVLSNVKFIQEKKLIGRYFDEISQDTGKYCFGVDDTLKALEMGAVEILIVWENLDTMRYVLKNHTTDEEKILFLKPDQEKDKTHFTDKDTGVEMEMVESCSLLEWFANNYKKFGSTLEIVTDRSQEGSQFVKGFGGIGGMLRYRIDFQGMEFNDDDPDLYDDY
|
Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
|
Q9GR88
|
B0BUU8
|
KTHY_RICRO
|
dTMP kinase
|
spotted fever group
|
MNNLKQGKFITFEGGEGIGKSTQSQMLYEYLQSQNTPVILTREVGGTIVAEKMREILVHEELLPMSELFQAMAARYDHMARKIIPALQEGHIVICDRFIDSTVCYQGLELENGIDLVYNLHKTLMPSLMPDITFFIDVEPDTAIKRVNSRNMNNKFDIRGIDFYKKIYYCFKELSNRFPERIKTIKASDLSPLEVHELIKKHL
|
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
|
B0BUU8
|
Q1GI16
|
YQGF_RUEST
|
Putative pre-16S rRNA nuclease
|
unclassified Ruegeria
|
MIHDAFEDFAAALPQMTALVGLDFGEKTIGVAVSDRIGAVATPLETIRRKKFTLDSNRLLEIIAGRDINGILLGLPRNMDGSEGPRCQSTRAFARNLSRVTDLPIGFWDERLSTVAAERALLEADTSRKRRAEVIDHVAASYILQGALDRMRHIRSS
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q1GI16
|
B3EMY8
|
GATC_CHLPB
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
|
Chlorobium
|
MSVTIKDVAYIAELARLSFTDTEKEKMTSELNAILQYVEKLDEVDTDGVEPLSSIHDEVNVLRDDVRQESVPNETALLNAPDKLDRFFRVPKVIG
|
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
|
B3EMY8
|
B6ULW7
|
BTDD_PAPAN
|
BTD-7 subunit 2
|
Papio
|
MRTFALLTAMLLLVALQAQAEARQARADEAAAQQQPGADDQGMAHSFTRPENAALPLSESAKGLRCFCRRGVCQLL
|
BTD-7 has antimicrobial activity against the Gram-negative bacterium E.coli ML35, the Gram-positive bacterium S.aureus 502a, and the fungus C.albicans 16820.
|
B6ULW7
|
B4RSW4
|
RL25_ALTMD
|
General stress protein CTC
|
Alteromonas
|
MSEAIFNLDASVRTDLGKGASRRLRREDKLPGIIYGGEEAPVSITLDHNKVNNSADFEAFYSHVLTLNLDGKPVEVLVKDMQRHPYKPKIMHIDFQRVIAGEDVHTNVPLHFVNEEKSAAVKAGGIAEHHVTEIEVTCQPKDLPEFIEVDMAAVEMGQTVHLSDLTLPAGVSSVELAKNDEAHDLAVVTVKPAPKAAETDEDGEEAASEE
|
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
|
B4RSW4
|
Q02XB8
|
AROB_LACLS
|
3-dehydroquinate synthase
|
Lactococcus cremoris subsp. cremoris
|
MKLNVNLPDHPYDVIIENGALANIGNWVSSLWKKQKIVLISDNHVNGLYGQKVVEQLEKSGFEVETFEFPEGEASKNLLTAEKAWNFCAEFGLTRSDGIIAFGGGVTGDLAGFVASTYMRGIHFLQIPTSLTAQVDSSIGGKTGINSKMAKNMIGTFTQPDGVLIDPEVLKTLGQREFCEGLGEVIKCALIADKALWNLLTDLSAKDLLENFAKIEEIIYRSCEVKRKVVVDDVLDNGVRLYLNFGHTIGHAVENTAGYGKVMHGEAVAIGMVQISKIAEKKGLMPLGITDEIRKMVKKYGLPDDYQPWDEALLFKALTHDKKARGTIIKTVIVPEIGTAKINEVTFEEMKEYLKK
|
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
|
Q02XB8
|
Q5RKG6
|
TRI35_RAT
|
E3 ubiquitin-protein ligase TRIM35
|
Rattus
|
MEPGPSVSPGPSRSFKEELLCAVCYDPFRDAVTLRCGHNFCRRCVSGCWEVQTTPSCPVCKERAVPGELRTNHTLNNLVETLLREEAEGARWTGRRSPRPCRAHRAPLTLFCVEDKELLCCACQADARHQEHRVQPIKDTAQDFRAKCKNMEHVLREKAKSFWALRRTYEAIAKHNEVQTTWLEGRIRDEFDKLRDFLRVEEQATVDAMKEESRKKHLLAEEKMKQLAEQTEALAREIERLQMEMKEDDMTFLMKHKSRKRRLFCTVEPAPLQPGLLMDACKYLESLQYRVWKKMLGSVESVPFSLDPNTAAGWLKVADDLTSVINHGYRVQVENPERFSSAPCLLGSQVFSKGSHSWEVDVGGLPSWRVGVVRVQAHAQAQAQADVGGEGHSHSCYHDTRSGFWYLCRTQGVDGDHCMTSDTATAPLVQAMPRRLRVELECEEGELSFYDSERHCHLYTFHAHFGEVRPYFYLGASRGDGPPEPLRICHLRVSIKEELDI
|
E3 ubiquitin-protein ligase that participates in multiple biological processes including cell death, glucose metabolism, and in particular, the innate immune response. Mediates 'Lys-63'-linked polyubiquitination of TRAF3 thereby promoting type I interferon production via DDX58/RIG-I signaling pathway. Can also catalyze 'Lys-48'-linked polyubiquitination and proteasomal degradation of viral proteins such as influenza virus PB2. Acts as a negative feedback regulator of TLR7- and TLR9-triggered signaling. Mechanistically, promotes the 'Lys-48'-linked ubiquitination of IRF7 and induces its degradation via a proteasome-dependent pathway. Reduces FGFR1-dependent tyrosine phosphorylation of PKM, inhibiting PKM-dependent lactate production, glucose metabolism, and cell growth.
|
Q5RKG6
|
P70936
|
TRPD_PRIM1
|
Anthranilate phosphoribosyltransferase
|
Priestia
|
MFKELLKKCLRGESLSAEEAEKIMNDIMNGKVPAAQIASVLTILTYRGETVDEIVGFVRGMKNNMNAISLEELNVVDTCGTGGDGASTFNISTASAIVASAAGVKVAKHGNRAVSSKSGSADVLEHLDIWIQGNEKEVKNAVADLNMSFLFAPLYHPAMKHVAATRKELGFRTVFNALGPLANPTNCTKQVIGVYSIELARKLAEALVVLGANHVLLVAGRDGLDEISATDVTDVVEVQGNVITEYTLAPEDVHLQRGKLEDLVVEDAKSSAELIESLFLNKSNVTAKNAVVLNSAAAIYVSGNVSTFEEGVAVALETIESGAAYTQLQRLKSKKVVEHAQ
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
P70936
|
Q9M568
|
PAL1_RUBID
|
RiPAL1
|
Rubus
|
MEFYKNGNGAVESFCEGHDPLNWNMAAESLKGSHVDELKRMVSDYRKPVVKLGGETLTIGQVAAIASHDGGVRVELSEEKRAGVKASSDWVMDSMGKGTDSYGVTTGFGATSHRRTKNGGALQRELIRFLNAGIFGSSLDSTHKLPHTATRAAMLVRFNTLLQGYSGIRFEILEAITKFLNGNITPCLPLRGTITASGDLVPLSYIAGLLIGRPNSKSVGPKGETLSPAEGFKLAGIDGGFFELQPKEGLALVNGTAVGSGMASMVLFDANTLAVLSEVMSAIFAEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILEGSSYVKEAKKVHEMDPLQKPKQDRYALRTSPQWLGPQIEVIRAATKMIEREINSVNDNPLIDVSRNKALHGGNFQELPIGVAMDNTRLAIASIGKLIFAQFSELVNDYYNNGLPSILTGSSNPSLDYGFKGAEIAMASYCSELQFLANPVTNHVQSAEQHNQDVNSLGLISSRKTSEAVDILKLMSSTFLVALCQAIDLRHLEENLKIVVKTTVSNVAKRTLTVSPNGELHPSRFSEKDLLTVVDREYLFSYIDDPCLATYPLMQKLRAELVEHALKNGERERSANTSIFHKIAAFEEELKTILPKEVDNARIEIENGKSEIPNRIKECRSYPLYRFVREELGTSLLTGEKIKSPGEECYKVFNAICAGKLVDPLLECLKEWNGAPLPIS
|
This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
|
Q9M568
|
B0UVZ8
|
DAPA_HISS2
|
4-hydroxy-tetrahydrodipicolinate synthase
|
Histophilus
|
MTTHRPLFYGSITALITPMDNHGEVDFNALKKLVEYHIASGTHAIVSVGTTGESATLSIAENVKTILKTLEFADGRIPVIAGTGANATSEAITMTKLLNDSGVAGCLSVVPYYNKPTQEGMYQHFKAIAECTDIPQILYNVPSRTGSDLLPETVGRLAQISNIIGIKEATGDVSRVAKIKQAAGDDFIFLSGDDATGLESMKLGGQGVISVTNNIAAADMAKMCELALAGKFDEAEIINDKLSALHKDLFIESNPIPVKWAAYKLGLIPEPILRLPLTTLSEQSQPKVIEALKNAGLL
|
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
|
B0UVZ8
|
A1W573
|
NDK_ACISJ
|
Nucleoside-2-P kinase
|
unclassified Acidovorax
|
MAIERTLSIIKPDAVAKNVIGQIYARFEAAGLKIAAARMIHLSRAEAEQFYAVHKERPFFKDLVDFMISGPVMVQALEGENAVLKNRELMGATDPKKAAPGTIRADFADSIDANAVHGSDAAETAQVEVAFFFPGLNIYSR
|
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
|
A1W573
|
Q39XZ0
|
RL18_GEOMG
|
50S ribosomal protein L18
|
Geobacter
|
MSPLAQKKVAHLKRKTRVRKKIRGTTDRPRLNVYKSARHIYAQIIDDVTGVTLVSASTVQDESDALKYTGNVEAAKCVGAMVAKKALEKNITSVVFDRNGFLYHGRVKALADSARENGLSF
|
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
|
Q39XZ0
|
Q8AXS4
|
PLIAL_ELAQU
|
Phospholipase A2 inhibitor alpha-like protein
|
Elaphe
|
MQLILLSSLLLLGLSLANGHETDPEGQILNSLVETVGRLEKKIDKVENAFLTVHRARSFGSGSERLYVTNKQVGNFEAVRNTCVQAGGHIPSPQLLNENKAFASVLERHNKAAYLVVQNSAKFTNWAAGEPNNADGNKLCVKADAQGAWHSASCDEDLLVVCEFSFI
|
Does not show any inhibitory activity against various snake venom PLA2s. Does not inhibit the endogenous PLA2 activities in various tissue homogenates prepared from this snake.
|
Q8AXS4
|
Q2K302
|
EFP_RHIEC
|
Elongation factor P
|
Rhizobium
|
MVKVIASSVRKGNVLDVDGKLYVVLTAQNFHPGKGTPVTQVDMRRIVDGVKVSERWRTTEQVERAFVEDVNFQYLYEDGEGFHFMNPATYDQVVVSAETMGDQKAYLQEGMTCILSIHEGVPLALELPRHVTLEIVETEPVVKGQTASSSYKPAMLSNGIRTSVPPHIDAGTRVVIATEDNSYVERAKD
|
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.
|
Q2K302
|
A0L3K8
|
AROE_MAGMM
|
Shikimate dehydrogenase (NADP(+))
|
Magnetococcus
|
MLSKALNINGETGLLAVIGDPVSHSLSPKMHNLALRHCQLNYCYVALPVKPHNLVRAVQGFAAMGMRGFNATIPHKENLLPLMHTLSEEASHIGAVNTVVIDDDGKMTGHNTDAYGFITGLKEAWRSDLSGLTAIMLGSGGAARAILYGLIQAKAARVIIANRTIERAQALIEAMQPYAPNTQLMVAPTQADQLPLESCDLLINTTSMGLKGETIPYIDLARLPHHAFVSDIVYGAHPTPLLRATAQHQLGGQDGLPMLIHQGAKAFELWTGHSMPVELVEHTLRQ
|
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).
|
A0L3K8
|
Q1CRI0
|
YIDD_HELPH
|
Putative membrane protein insertion efficiency factor
|
Helicobacter
|
MRNNKTPFLSAIFTASIRGYQRFFSAFTPSSCRFYPTCSNYALWLLCFENPLSAMGKIAIRILSCNPFCSGGIAYPTTRLKRPSLLQSHKDFNRNFKTITFWLVPTTKSRTTYYIIKV
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
Q1CRI0
|
B8CLC5
|
TGT_SHEPW
|
tRNA-guanine transglycosylase
|
Shewanella
|
MKFELDTTQGRARRGRLVFERGTVETPAFMPVGTYGTVKGMTPEEVRETGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQDSLGSDVVMIFDECTPYPATEDEARKSMQMSLRWAQRSRDEFDRLENPNSLFGIIQGGVYEGLRDESLKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHTCPQIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVVKIRNARHRDDTSTLDDKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQRLMEGLRGAIETGTLDDFVTEFYTSQGREVPEVPELTD
|
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
|
B8CLC5
|
P37829
|
SCRK_SOLTU
|
Fructokinase
|
Solanum
|
MAVNGSALSSGLIVSFGEMLIDFVPTVSGVSLAEAPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQADGINFDKGARTALAFVTLRADGEREFMFYRNPSADMLLTPDELNLDLIRSAKVFHYGSISLIVEPCRSAHLKAMEVAKEAGALLSYDPNLRLPLWSSEAEARKAIKVSDVELEFLTGSDKIDDESAMSLWHPNLKLLLVTLGEKGCNYYTKKFHGSVGGFHVKTVDTTGAGDSFVGALLTKIVDDQAILEDEARLKEVLRFSCACGAITTTKKGAIPALPTESEALTLLKGGA
|
May play an important role in maintaining the flux of carbon towards starch formation.
|
P37829
|
A6TG45
|
MNMG_KLEP7
|
Glucose-inhibited division protein A
|
Klebsiella
|
MFYQDPFDVIIIGGGHAGTEAAMAAARMGQQTLLLTHNIDTLGQMSCNPAIGGIGKGHLVKEVDALGGLMAKAIDQAGIQFRILNASKGPAVRATRAQADRVLYRQAVRTALENQPNLMIFQQAVEDLIVENDRVVGAVTQMGLKFRAKAVVLTVGTFLDGKIHIGLDNYSGGRAGDPPSIPLSRRLRELPLRVSRLKTGTPPRIDARTIDFSVLAQQHGDNPMPVFSFMGSADQHPRQVPCYITHTNEKTHDVIRNNLDRSPMYAGVIEGIGPRYCPSIEDKVMRFADRNQHQIFLEPEGLTSNEIYPNGISTSLPFDVQMQIVRSMQGMENARIVRPGYAIEYDFFDPRDLKPTLESKFIQGLFFAGQINGTTGYEEAAAQGLLAGLNAARFSAEKEGWAPRRDQAYLGVLVDDLCTLGTKEPYRMFTSRAEYRLMLREDNADLRLTEQGRELGLVDDERWARYNEKLESIERERQRLKSTWVNPQAESANEVNAHLTAPLSREASGEDLLRRPEMTYEQLVQLSPFTPGLEDRQAAEQVEIQVKYEGYIARQQDEIEKQQRNENTLLPATLDYRQVTGLSNEVIAKLNDHKPSSIGQASRISGITPAAISILLVWLKKQGMLRRSA
|
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.
|
A6TG45
|
Q5T4D3
|
TMTC4_HUMAN
|
Transmembrane and TPR repeat-containing protein 4
|
Homo
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MAVLDTDLDHILPSSVLPPFWAKLVVGSVAIVCFARSYDGDFVFDDSEAIVNNKDLQAETPLGDLWHHDFWGSRLSSNTSHKSYRPLTVLTFRINYYLSGGFHPVGFHVVNILLHSGISVLMVDVFSVLFGGLQYTSKGRRLHLAPRASLLAALLFAVHPVHTECVAGVVGRADLLCALFFLLSFLGYCKAFRESNKEGAHSSTFWVLLSIFLGAVAMLCKEQGITVLGLNAVFDILVIGKFNVLEIVQKVLHKDKSLENLGMLRNGGLLFRMTLLTSGGAGMLYVRWRIMGTGPPAFTEVDNPASFADSMLVRAVNYNYYYSLNAWLLLCPWWLCFDWSMGCIPLIKSISDWRVIALAALWFCLIGLICQALCSEDGHKRRILTLGLGFLVIPFLPASNLFFRVGFVVAERVLYLPSVGYCVLLTFGFGALSKHTKKKKLIAAVVLGILFINTLRCVLRSGEWRSEEQLFRSALSVCPLNAKVHYNIGKNLADKGNQTAAIRYYREAVRLNPKYVHAMNNLGNILKERNELQEAEELLSLAVQIQPDFAAAWMNLGIVQNSLKRFEAAEQSYRTAIKHRRKYPDCYYNLGRLYADLNRHVDALNAWRNATVLKPEHSLAWNNMIILLDNTGNLAQAEAVGREALELIPNDHSLMFSLANVLGKSQKYKESEALFLKAIKANPNAASYHGNLAVLYHRWGHLDLAKKHYEISLQLDPTASGTKENYGLLRRKLELMQKKAV
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Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases dedicated primarily to the cadherin superfamily, each member seems to have a distinct role in decorating the cadherin domains with O-linked mannose glycans at specific regions. Also acts as O-mannosyl-transferase on other proteins such as PDIA3.
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Q5T4D3
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