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
|
|---|---|---|---|---|---|---|
A5N3V8
|
Y3826_CLOK5
|
Nucleoid-associated protein CKL_3826
|
Clostridium
|
MARGGFPNFGGGGNMNNLMKQAQKFQKQMEDMQSELENKEFSATAGGEAITVVVNGKKQIVSIKIKPEVVDPEDVEMLEDLVLTACNQALKSAEDQTASEMKKLTGGLNIPGMF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
A5N3V8
|
Q9ESN6
|
TRIM2_MOUSE
|
RING-type E3 ubiquitin transferase TRIM2
|
Mus
|
MASEGASIPSPVVRQIDKQFLICSICLERYKNPKVLPCLHTFCERCLQNYIPAHSLTLSCPVCRQTSILPEKGVAALQNNFFITNLMDVLQRTPGSNGEDSSILETVTAVAAGKPLSCPNHDGNVMEFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQLDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQDFPLHPRENDQLDFIVETEGLKKSIHNLGTILTTNAVASETVATGEGLRQTIIGQPMSVTITTKDKDGELCKTGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLSLRLYDQHIRGSPFKLKVIRSADVSPTTEGVKRRVKSPGSGHVKQKAVKRPASMYSTGKRKENPIEDDLIFRVGTKGRNKGEFTNLQGVAASTSGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSNDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSNNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ
|
UBE2D1-dependent E3 ubiquitin-protein ligase that mediates the ubiquitination of NEFL and of phosphorylated BCL2L11. Plays a neuroprotective function. May play a role in neuronal rapid ischemic tolerance.
|
Q9ESN6
|
Q1GIL9
|
TPIS_RUEST
|
Triose-phosphate isomerase
|
unclassified Ruegeria
|
MARKLAAGNWKMNGTGEHLAELENLAQGDLPEGVDVLICPPATLISRAADRAGDIAIGGQDCHAKTSGAHTGDLSADMLRDAGATYVIIGHSERRADHGEGDADVRAKTEAAQAAGLVAVVCIGETLEEREAGTTLEVVGAQLAGSLPDGVTAENTVVAYEPVWAIGTGKVPTLDQIAEVHDALRADLVARFGAAGKDLPLLYGGSVKPGNAAEIFGVSNVDGALVGGASLKAADFGPIIAALAAS
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q1GIL9
|
A4SJN2
|
TORD_AERS4
|
Chaperone protein TorD
|
Aeromonas
|
MQEFLATSERRAELYWWFATLFSAELSDKQIAEYDSYDVRSFLKSLSTLDPMRPAVTELNEAIARLLVRDERATALAADFKGLFLADTAVQPYESAHLDASSLGRMQQRLVRLAIDVSAKYPQPVDHLGVELDLMGNLIIRAAEAPSADQREQWLGEQEAVLHGHLLAWFPHFEVACRAADPFGFYGASARLLGVFLTMDANYLSLVKPASSAD
|
Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
|
A4SJN2
|
P36983
|
TX22G_PLETR
|
Plectoxin-5/6
|
Plectreurys
|
MKHLIFSSALVCALVVCTFAEEQVNVPFLPDERAVKCIGWQETCNGNLPCCNECVMCECNIMGQNCRCNHPKATNECESRRR
|
Potent toxin that may paralyze and/or kill insect pests such as H.virescens (lepidoptera), S.exigua (beet armyworm) and M.sexta (tobacco hornworm).
|
P36983
|
Q7MLQ2
|
TORA_VIBVY
|
Trimethylamine-N-oxide reductase
|
Vibrio
|
MAITRRSFLKGVATTSAASVIGPSLLASASANAVETTGTWKVSGSHWGAFRAHIYAGKVQEIKPIELDQNPTEMLNGIKGIIYSPSRVRYPMVRLDWLKKHKYSADTRGNNRFVRVTWDEALDLFYRELERVQKEYGPWALHAGQTGWNQTGSFNNCTAHMQRAVGMHGNYITKVGDYSTGAGQTILPYVLGSTEVYAQGTSWSEILENADNIILWANDPVKNLQVGWNCETHESYAYLAQLKEKVAKGEINVISVDPVKNKTQRYLENDHLYVNPMTDVPFMLAIAHVLYTENLYDKKFIETYCLGFEEFINYVQGKTKDKVEKTPEWAAPICGVKADKIREFARMLVKGRTQILMGWCIQRQEHGEQPYWAAAVVAAMIGQIGLPGGGISYGHHYSSIGVPSTGFAGPGGFPRNLDAGMKPKWDNNDFNGYSRTIPVARWIDCLLEPGKEINYNGGKVKLPDFKMMVISGCNPWHHHQDRNRMKQAFQKLQTVVTIDFAWTATCRFSDIVLPACTQWERNDIDVYGSYSSRGLIAMHRLVDPLFQSKPDFQIMKELTERFGRSEEYSRGMSEMDWIRSLYNDCKKSNEGKFEMPEFDEFWEKSVLDFGQGQPWVRHADFRQDPEINPLGTPSGFIEITSRKIGRYGYEHCQEHPMWFEKSERSHGGPGSDKHPFWLQSCHPDKRLHSQMCESEEFRATYAVKGREPVYINPLDAKAKGIKEGDLVRVFNDRGQLLAGAVLTDSYPRGVIRIEEGAWYGPLSEKVGAICTYGDPNTLTQDIGSSELAQATSANTCIVDFEKFTGKVPPVTSFGGPIEVA
|
Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions.
|
Q7MLQ2
|
Q0A5L6
|
UBID_ALKEH
|
Polyprenyl p-hydroxybenzoate decarboxylase
|
Alkalilimnicola
|
MKYRDLRDFISKLEADGELRRVDVEVDPRLEMTEVCDRTLRAEGPAILFQKPKGYRMPVLGNLFGTPRRVALGMGAEDVSALREIGELLAFLRQPEPPKGLRDAWSQLPVFRKVLDMGPKKVRRAACQEVVVEGDDVDLGRLPVQTCWPGDAGPLITWALVVTRGPEKERQNLGIYRNQVIGRNRTIMRWLAHRGGALDFRDWQRERPGEPFPVAIALGADPATILGAVTPVPDSLSEYGFAGLLRGSKTELVKCLGPDLQVPASAEIVLEGHIHPDDTAPEGPFGDHTGYYNEVDHFPVFTVDRITHRRDPIYHSTYTGRPPDEPAILGVALNEVFVPILRKQFPEISDFYLPPEGCSYRMAVVTMKKQYPGHAKRVMLGVWSFLRQFMYTKFVIVTDDDVNARDWKDVIWAMTTRMDPKRDTVMIDNTPIDYLDFASPVSGLGSKIGFDATHKWPGETDREWGRPIVMDDETRARVDALWPKLGLD
|
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
|
Q0A5L6
|
A1W450
|
TATA_ACISJ
|
Sec-independent protein translocase protein TatA
|
unclassified Acidovorax
|
MGSFSIWHWLIVLLIVVMVFGTKKLKNIGSDLGGAVKGFKDGMKDGASTDDSATTSAPAGQVTNNSTAADKTTIDVEAKHKS
|
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
|
A1W450
|
B7JGI9
|
TAGU_BACC0
|
Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU
|
Bacillus cereus group
|
MKKKILFWVLGILGVLIIGGGIYAYNVYSSVSNTLKEVHQPLKRDQNNSNVGEKVSKSEPVSILLLGADERGDDKGRSDSLMVITLNPKNNSMKTVSIPRDTYTEIVGKGKSDKINHAYAFGGVDMSVATVEKFLDVPINYYIEVNMEGFKDIVDAVGGVDVTNDLEFTQDGHHFAKGNIHLTGDQALAFTRMRKQDPRGDFGRQMRQRQVMQGVIKKGASFSSLTGYGDVLAAIQKNVKTNLTQDQMFDMQKNYKDCLKNSEDIQIPGDGHKAADGIWYYYVPDAAKQDLTNKLRSHLEVTK
|
May catalyze the final step in cell wall teichoic acid biosynthesis, the transfer of the anionic cell wall polymers (APs) from their lipid-linked precursor to the cell wall peptidoglycan (PG).
|
B7JGI9
|
C4K8L9
|
TRHO_HAMD5
|
tRNA hydroxylation protein O
|
Candidatus Hamiltonella
|
MPVLHNRISNQKLKEKMLAETQERQTLSFYKYFALDNPSMFRDKLYTQWNQLSVFGRVYIAKEGINAQISVPIDHYNDFKASLFNAHPALDQIRLNTALEDNGRSFWVLRMKVRQRIVADGIEDETFNPAHTGQYLKAHEVNEMIKDPDALFVDMRNHYEYEVGHFKNAIKVPSDTFREQLPMAVDMLKEDKEKKMVLYCTGGIRCEKASAYLLHHGFKNVYHVEGGIIEYVRTAKKKDLPLHFIGKNFVFDERMGERVSEEVIAHCHQCEQFCDTHVNCHNSACHLLFIQCAICSEKFSGCCSAICQEELELSPEEQRLRRSARGNKIKIFNKSKDVLETIMNKSIIDQGNKEG
|
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
|
C4K8L9
|
Q9BQ50
|
TREX2_HUMAN
|
3'-5' exonuclease TREX2
|
Homo
|
MSEAPRAETFVFLDLEATGLPSVEPEIAELSLFAVHRSSLENPEHDESGALVLPRVLDKLTLCMCPERPFTAKASEITGLSSEGLARCRKAGFDGAVVRTLQAFLSRQAGPICLVAHNGFDYDFPLLCAELRRLGARLPRDTVCLDTLPALRGLDRAHSHGTRARGRQGYSLGSLFHRYFRAEPSAAHSAEGDVHTLLLIFLHRAAELLAWADEQARGWAHIEPMYLPPDDPSLEA
|
Exonuclease with a preference for double-stranded DNA with mismatched 3' termini. May play a role in DNA repair.
|
Q9BQ50
|
A2Q9P2
|
TVP38_ASPNC
|
Golgi apparatus membrane protein tvp38
|
Aspergillus subgen. Circumdati
|
MPADYSSTARALSVSTSSPEPLSPSEDEAYPPWSRRAPGRRNSASISGGRSATLRDQIIDRATKTYHQILESWRKMNFWQRVGAVAAFLLANLLGIGFLVFTGKVFIWLQPVAAQWEHSPLAYGVLWLCVFFVSFPPLVGWSTFGTMAGYIFGIWKGWLLYASATVLGSTCSFIVSRTILSKFVHRLMERDKRFAALSLTLKYDGLKLLCMIRLCPLPYSVCNGAVSTFPTVQPLMYGLATALISPKLLVPAFIGNRLRVLSENNEEMSAGSKAVNICSIIVSICIGIFTGLYIYRRTLARAKELEAKEREDIRRSLQADHAAHRPHDAFSEDPEVNSAAALLARDEEERIGFGDLDDDHVDLAIDDESGSETSPHRTQASPYRDEFTDNDSDVFKDGDGTHEEMYTLHTHVRRP
|
Golgi membrane protein involved in vesicular trafficking and spindle migration.
|
A2Q9P2
|
A1RSQ1
|
TBP_PYRIL
|
TATA-box factor
|
Pyrobaculum
|
MESGGPTYRIENIVATVNLGVELDLEKLAERLAMAEYNPDQFPGLILRLTKPRISALIFRTGKMVCTGAKNEEDLKNAVRALVKLLRDHGAEVPFDPEVQVQNIVASGNLHAEVDLEQAVLMLENAMYEPEQFPGLIYRMSSPRVVMLIFGSGKIVCTGAKSERDVATAVQKLYNQLKDLGVLYIEEGGGEEEEELEEL
|
General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation.
|
A1RSQ1
|
Q5R4H0
|
ZNT9_PONAB
|
Solute carrier family 30 member 9
|
Pongo
|
MLPGLAAAAAAHRCSWSSLCRLRPRCRAAACNPSDCQEWQNLVTFGSFSNMVPCSHPYIGTLSQVKLYSTDVQKEGQGSQTLRVEKVPSFETAEGIGAELKAPLKQEPLQVRVKAVLKKREYGSKYTQNNFITGVRAINEFCLKSSDLEQLRKIRRRSPHEDTESFTVYLRSDVEAKSLEVWGSPEALAREKKLRKEAEIEYRERLFRNQKILREYRDFLGNTKPRSRTASVFFKGPGKVVMVAICINGLNCFFKFLAWIYTGSASMFSEAIHSLSDTCNQGLLALGISKSVQTPDPSHPYGFSNMRYISSLISGVGIFMMGAGLSWYHGVMGLLHPQPIESLLWAYCILAGSLVSEGATLLVAVNELRRNARAKGMSFYKYVMESRDPSTNVILLEDTAAVLGVIIAATCMGLTSITGNPLYDSLGSLGVGTLLGMVSAFLIYTNTEALLGRSIQPEQVQRLTELLENDPSVRAIHDVKATDLGLGKVRFKAEVDFDGRVVTRSYLEKQDFDQMLQEIQEVKTPEELETFMLKHGENIIDTLGAEVDRLEKELKKRNPEVRHVDLEIL
|
Acts as a zinc transporter involved in intracellular zinc homeostasis. Functions as a secondary coactivator for nuclear receptors by cooperating with p160 coactivators subtypes. Plays a role in transcriptional activation of Wnt-responsive genes.
|
Q5R4H0
|
Q94572
|
TBA3_HOMAM
|
Alpha-III tubulin
|
Homarus
|
MRECISIHVGQAGAQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFCETGAGKHVPRAVFVDLEPTVIDEIRTGVYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDIVLDRIRKLADNCAGLQGFLIFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFAIYPAPQVATAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPVISAEKAYHEQLSVSEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTAVPGGDLAKVSRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFTEAREDLAALEKDYEEVGVDSADAEGEEEGEEY
|
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
Q94572
|
A2QPT2
|
YPI1_ASPNC
|
Type 1 phosphatases regulator ypi1
|
Aspergillus subgen. Circumdati
|
MSRTRQIPSEPASSSQLELTEEHTETSSAVPVPATLRLRGADEPAANRLELNEGNSRRIRWSEDVIDNEGMGKKSSKVCCIYHKSRPIGDSSSESESSDSSTSNSDTDSDDEAACHRRTGHRPPTAQGENYASSGQRLSSNSEERTCRSSHRARKTKRKPSPNAYEKMPKTTKGR
|
Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control.
|
A2QPT2
|
Q08224
|
THI20_YEAST
|
Hydroxymethylpyrimidine phosphate kinase
|
Saccharomyces
|
MTYSTVSINTPPPYLTLACNEKLPTVLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGMLTAAAIEVLHEKLLQLGENRPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGEERKVNGLQDIFQIAKDLAKITKCSNILVKGGHIPWNDEKEKYITDVLFLGAEQKFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSVYGGIEYVQNAVAIGCDVTKETVKDNGPINHVYAVEIPLEKMLSDECFTASDVIPKKPLKSAADKIPGGNFYEYLINHPKVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEKELVIVGGVRTEMGQHEKRLKEVFGVKDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKVTAPEGSVYHEWCETYASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTAALEYE
|
Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and also probably that of HMP to HMP-P.
|
Q08224
|
Q06J52
|
YCF4_BIGNA
|
Photosystem I assembly protein Ycf4
|
Bigelowiella
|
MENVFIYRYTVLGSKKISNLIFAIFIFLGSIFFLKASIFSFLDLKTNSLNGNIVFFPQGLVMGFYSLLGLLFTFYSLLTFFLKIGFGYNEFNKKENVIRIFRWGFPGKNRRIEACYSINDIKSIKISSNTGPKNISISLKGDIDIPFIREGFSDSFSNIEEQAIDIASFLGIPLVYNQ
|
Seems to be required for the assembly of the photosystem I complex.
|
Q06J52
|
P46815
|
WAG31_MYCLE
|
Antigen 84
|
Mycobacterium
|
MPLTPADVHNVAFSKPPIGKRGYNEDEVDAFLDLVENELTQLIEENSDLRQRIEELDHELAAGGGTGAGPVIAVQPTQALSTFEPELVSAKQAPVAAVAETAEELAMKATRVLSLAQDTADQLTSTAKVESDKMLADARVNADQILGEARLTAEATVAEAQQRADAMLADAQTRSEVQSRQAQEKADALQAEAERKHSEIMGAISQQRTVLEGRLEQLRTFEREYRTRLKTYLESQLEELGQRGSAAPVDSNADAGGFDQFNRGNN
|
Important for maintaining cell shape and cell wall integrity by localizing peptidoglycan synthesis to the cell poles.
|
P46815
|
Q72IH5
|
TRMN_THET2
|
tRNA:m2G6 methyltransferase
|
Thermus
|
MWLEATTHPGLEDLLLEELSALYPGEGAEVDARKGRVRIPRAWVGEEALGLRLAHHLVLFRARLLLSREDPLGALERAALALPWPELEGAGSFRVEARREGEHPFTSPEVERRVGEALHRAYGVPVDLKRPAVRVRVDVRGEEAFLGVQLTERPLSRRFPKAALRGSLTPVLAQALLRLADARPGMRVLDPFTGSGTIALEAASTLGPTSPVYAGDLDEKRLGLAREAALASGLSWIRFLRADARHLPRFFPEVDRILANPPHGLRLGRKEGLFHLYWDFLRGALALLPPGGRVALLTLRPALLKRALPPGFALRHARVVEQGGVYPRVFVLEKL
|
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the methylation of the guanosine nucleotide at position 6 (m2G6) in tRNA(Phe).
|
Q72IH5
|
Q56WD9
|
THIK2_ARATH
|
Peroxisome defective protein 1
|
Arabidopsis
|
MEKAIERQRVLLEHLRPSSSSSHNYEASLSASACLAGDSAAYQRTSLYGDDVVIVAAHRTPLCKSKRGNFKDTYPDDLLAPVLRALIEKTNLNPSEVGDIVVGTVLAPGSQRASECRMAAFYAGFPETVAVRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGLESMTTNPMAWEGSVNPAVKKFAQAQNCLLPMGVTSENVAQRFGVSRQEQDQAAVDSHRKAAAATAAGKFKDEIIPVKTKLVDPKTGDEKPITVSVDDGIRPTTTLASLGKLKPVFKKDGTTTAGNSSQVSDGAGAVLLMKRSVAMQKGLPVLGVFRTFAAVGVDPAIMGIGPAVAIPAAVKAAGLELDDIDLFEINEAFASQFVYCRNKLGLDPEKINVNGGAMAIGHPLGATGARCVATLLHEMKRRGKDCRFGVVSMCIGTGMGAAAVFERGDGVDELRNARKVEAQGLLSKDAR
|
Involved in long chain fatty-acid beta-oxidation prior to gluconeogenesis during germination and subsequent seedling growth. Confers sensitivity to 2,4-dichlorophenoxybutiric acid (2,4-DB). Required for local and systemic induction of jasmonic acid (JA) biosynthesis after wounding. Seems to be involved in JA biosynthesis during senescence.
|
Q56WD9
|
Q17DT0
|
UBA5_AEDAE
|
Ubiquitin-like modifier-activating enzyme 5
|
Stegomyia
|
MATMEELKLQIETLQSELCKLKATSAGGAREKIEKMSSEVVDSNPYSRLMALQRMGIVSEYERIRQKSVAVVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAAKTLNFINPDVKILTNNYNITTVESFDKFLNAIKTGGIEEGTPVDLVLSCVDNFEARMAINTACNELSLNWFESGVSENAVSGHIQFIRPGDTACFACAPPLVVAENIDEKTLKREGVCAASLPTTMGIVAGMLVQNTLKYLLNFGTVSDYLGYNALIDFFPKMSLKPNPTCDDRFCIDRQKDYAARPKEERVEEVPEEETPLHEENLYGIELVAEDDTQGSQPSTGTTHSISTGLKLAYEPPASTKHSETTSTTAVSDDVSLDELMAQMKSM
|
E1-like enzyme which activates UFM1.
|
Q17DT0
|
Q3ABS0
|
TRPD_CARHZ
|
Anthranilate phosphoribosyltransferase
|
Carboxydothermus
|
MVREVLERLMRGENLNFSEALATMNELMEGKYTEAQVAAFLVALKMKGETEEEISAFALALREKARRVITQTEGLVDTCGTGGDGRQTFNISTAAAFVVAGAGIPVAKHGNRSVSSRSGSADVLEALGVNIDLDAKGTARCVDEIGIGFLFAPNLHPAMRHVAKTRREIGVRTVFNILGPLANPANIVGQVLGVFTPELQETLAKVLNNLGVERAFVVHGHGGLDEVSLTGPTRVFELNRGKIDSYLFDPLSYGFSYCSLRDLQGGDAFENARLLQEILDGKPGPLRDVVLLNAAFGIMAGGVNDFREALVMARESIDKGLAAEKLEKLRRLSHEIKEAG
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q3ABS0
|
Q98G87
|
UBIG_RHILO
|
3-demethylubiquinone 3-O-methyltransferase
|
Mesorhizobium
|
MPEPRRSTIDAGEVERFSALAAEWWNPNGKFRPLHKFNPVRLSYIRDQIAARFGRDPRAARPFEGLRILDIGCGGGLLCEPMARLGAEVVGADASETNIEVAKLHAAEGNVIVDYRATTAEDLADAGETFDVILNMEVVEHVADIDLFVAKCGQMVRPGGIMFVATINRTLKALGLAIIGAEYVLRWLPRGTHQFGKLVRPEELEKALGGASLTIIDRTGVTYNPLADRWARSKDMDVNYMVLAEKGSV
|
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
|
Q98G87
|
C0ZN46
|
Y390_RHOE4
|
Nucleoid-associated protein RER_03900
|
Rhodococcus erythropolis group
|
MQPGGAPDMSALLAQAQQMQQQLMAAQQEMAQAEVTGQAGGGLVVATVKGTGEVVGLQIDPKVVDPEDVETLQDLVIGAIEDASRKAQEVAAEKLGPLAGGLGGGLPGLPGF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
C0ZN46
|
A7FWJ3
|
YQGF_CLOB1
|
Putative pre-16S rRNA nuclease
|
Clostridium
|
MRILGLDIGDRTIGIAISDPLGFTAQGITTIRRKSEAYDLEEIKKICDKYEVDTIVSGLPKNMNGTLGPQSEKVLEFCDLIKEHLNIEIKMWDERLTTVAATRAMLEADLSRSKRKKIVDKVAATYILQGYLDSLSK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
A7FWJ3
|
O28544
|
TRUA_ARCFU
|
tRNA-uridine isomerase I
|
Archaeoglobus
|
MMKFAFKIAYFGDNFHGSQFQPDQRTVEGEVINALRRLGVENPRLRSAGRTDAGVHAYGQVISFYSEDKIFPRMLNAELPEDITAWAWAKVSEDFDPRRAKSRVYTYVMYGSDYDISAMRKAVKELIGVHDFSNFTKKFGEGESCVREIISADIRADREFIIFEIEGNAFTWNMVRCIVTAIMEIGKQHRSIEWFRDLLNPEKHKERVEPAPPYGLILKDVKYDDVEFEIDDYAFKTLQSRIEDRIIYHGTIFKLFSLFRQSGIS
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
O28544
|
Q65N07
|
TSAD_BACLD
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Bacillus
|
MNHKKDLYVLGIETSCDETAAAIVKNGTDIISNVVASQIESHKRFGGVVPEIASRHHVEQITIVLEEAFAQADMTFDDIDAIAVTEGPGLVGALLIGVNAAKALSFARGIPLVGVHHIAGHIYANRLVQDIQFPAIALVVSGGHTELVYMKEHGSFEVIGETLDDAAGEAYDKVARTMGLPYPGGPHIDKLAQKGEANVPLPRAWLEEGSYHFSFSGLKSAVINTLHNASQKGETIAPEDLSASFQESVIDVLVTKTERAAEAYGVKQVLLAGGVAANKGLRAALEKTFSSRPEIELLIPPLSLCTDNAAMIAAAGTVAFEKGIRGKYDMNGQPGLDLTSY
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
Q65N07
|
Q9M8Z7
|
U80A2_ARATH
|
UDP-glucose:sterol glucosyltransferase 80A2
|
Arabidopsis
|
MPEISPAELAKVSSSSSSSSSSSSGRASVKIEEIEGGAAASGVVIVSEELETNPKTVVASIADETVAESSGTGNKSFSRVWTMPLEGSSSSDKAESSSTNQPRLDKSKTERQQKVTHILAEDAAKIFDDKISAGKKLKLLNRIATVKHDGTVEFEVPADAIPQPIVVDRGESKNGVCADESIDGVDLQYIPPMQIVMLIVGTRGDVQPFVAIAKRLQDYGHRVRLATHANFKEFVLTAGLEFYPLGGDPKVLAGYMVKNKGFLPSGPSEIPIQRNQMKDIIYSLLPACKEPDPDSGISFKADAIIANPPAYGHTHVAEALKIPIHVFFTMPWTPTSEFPHPLSRVKQPAGYRLSYQIVDSLIWLGIRDMVNDLRKKKLKLRPVTYLSGTQGSGSNIPHGYMWSPHLVPKPKDWGPQIDVVGFCYLDLASNYEPPAELVEWLEAGDKPIYIGFGSLPVQEPEKMTEIIVEALQRTKQRGIINKGWGGLGNLKEPKDFVYLLDNVPHDWLFPRCKAVVHHGGAGTTAAGLKASCPTTIVPFFGDQPFWGERVHARGVGPSPIPVDEFSLHKLEDAINFMLDDKVKSSAETLAKAMKDEDGVAGAVKAFFKHLPSAKQNISDPIPEPSGFLSFRKCFGCS
|
Involved in the biosynthesis of sterol glucosides. Catalyzes the synthesis of steryl glycosides (SGs) and acyl steryl glycosides (ASGs) which are the most abundant sterol derivatives in higher plants. Can act on several sterols like sitosterol, campesterol and stigmasterol. Both UGT80A2 and UGT80B1 are required for the normal production of SGs and ASGs in seeds.
|
Q9M8Z7
|
Q6NV31
|
WDR82_DANRE
|
Protein word of mouth
|
Danio
|
MKLTDSVLRSFRVAKVFRENSDKINCFDFSSNGETVISSSDDDSIVLYDCQEGKPKRTLYSKKYGVDLIRYTHAANTVVYSSNKIDDTIRYLSLHDNKYIRYFPGHNKRVVALSMSPVDDTFISGSLDKTIRLWDLRSPNCQGLMHLQGKPVCSFDPEGLIFAAGVNSEMVKLYDLRSFDKGPFATFKLQYERTCEWTGLKFSNDGKLILVSTNGGTLRVLDAFKGAVLHSFGGYNNSKGVILEASFTPDSQFIMIGSEDGKIHVWNAESGMKVALLDGKHTGPVTCLQFNPKFMTFASACSNMAFWLPTIDD
|
Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes. Facilitates histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A). Part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs).
|
Q6NV31
|
O07528
|
YHCZ_BACSU
|
Uncharacterized transcriptional regulatory protein YhcZ
|
Bacillus
|
MKIVIADDHHVVRKGLRFFFATQDDIEVVGEAATGLEALRVIEETKPDLVLMDLSMPEMDGIQAIKKAIQQFPDTNIIVLTSYSDQEHVIPALQAGAKAYQLKDTEPEELVKTRQVHGGEYKLSTAIMPHVLTHMKNQHDPEKEKYYQLTRREKDVLTEIANGKSNKEIAAALFISEKTVKTHVSNLLAKLEVADRTQAALFAVKYNLNGEISK
|
Member of the two-component regulatory system YhcY/YhcZ.
|
O07528
|
Q65FN2
|
TGL_BACLD
|
Transglutaminase
|
Bacillus
|
MISVSGYRLRPEDIEKLNVSQTQRDIANRMLAMPSGYRYGSISELLFELRFREHTVKSARELINSGAKFATFSKTYGNEEFWRVTPEGALELKYRAPASKAIRNIFESGPSYAFECATAIVIIFYMALLKTIGDQTFDRNYQRIILYDWHYERLPIYTDKGNDYLPGDCLYFKNPEFDPSRPQWRGENAILLENNLYAAHGLGILSGETIIEKLNGLRKPHAQTSAYLLSQVTRVDIPALIQMIR
|
Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links.
|
Q65FN2
|
Q5FUS6
|
UPPP_GLUOX
|
Undecaprenyl pyrophosphate phosphatase
|
Gluconobacter
|
MTLLQALILAIVQGITEPFPVSSLGHAVLLPALLHWDLDEHAPMFLPFLTMLHVGTLVALAGVFWRDWMAILGGMFGRYGSYRQMEAIRIFGLLVIATIPAVLVGWLLEHRLRAVFGTPLAVAGFLILNGFLLMVTEWLRRQKGHRDHKPIATLAPKDAVIIGIWQCLALLPGLSRSGATMNGGLLRGLDHETAARFSLLMAQPIVLAATVREAWQMRHMTISHDIMVQCVAGAVVAGLTALICSLVMLRFFRNHDGWALTPFGVYCVLAGLFAGAVILL
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
Q5FUS6
|
B2A2M1
|
TMCAL_NATTJ
|
tRNA(Met) cytidine acetate ligase
|
Natranaerobius
|
MQGLGIIAEYNPFHNGHLYHITNSLEQIRPDFVMAVMSGNWVQRGEPAIIDKWTRAEMALNQGVDLVVELPFLWATQSAREFAQGAVALLKDSGVISYQSFGSETGDLTLLQRAAKLSLEESEHFRQTLHNYLDQGFNFSEALAKALNLNELASNDILGIEYLKSHDLLSSDISCITVQRQGSPYHKSEISGKFSSATAIRQAAKNGDLSLIKHTVPDQTWNLLSQNKTDWIFFKMLEQHILYKFRITNKETIEQLMEWEQGLENRIYNASLDSCTLEEFISKLKTKRYTRTRLNRLMLHALMEIDKSLLNHFNTTGPPYLRVLGMNQRGRQALKTISDRASLPILTRPARDLRSLSHYCRQCFHWEVKASAFYNLLKQKDGREEYIRPPIVHPD
|
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
|
B2A2M1
|
B4PPU6
|
TOTZ_DROYA
|
Protein Turandot Z
|
Sophophora
|
MYFAIRLSFVLAVLFCLTGNGNARMLGADFNRLQQLQRRSHQSNDANTQLKIAYEVIGIYDKYKGQKGSDLLREAQLNSEVNDFKRKNVVVDGVPAQGGGIKDAVKKIADEVPDDVKKNAKDIAVKIAKSVTKSIFKYFLN
|
A humoral factor that may play a role in stress tolerance.
|
B4PPU6
|
B1LF56
|
TSAD_ECOSM
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Escherichia
|
MRVLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQEALKESGLTAKDIDAVAYTAGPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEDNPPAFPFVALLVSGGHTQLISVTGIGQYELLGESIDDAAGEAFDKTAKLLGLDYPGGPLLSKMAAQGTAGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRDNGTDDQTRADIARAFEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMKKRRGEVFYARPEFCTDNGAMIAYAGMVRFKAGATADLGVSVRPRWPLAELPAA
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
B1LF56
|
B0BM40
|
TPIS_XENTR
|
Triose-phosphate isomerase
|
Silurana
|
MSSRKFFVGGNWKMNGDKKSLTELINTLNSGKISADTEVVCGAPTIYLDFARQKLDAKFAVSAQNCYKVAKGAFTGEISPAMIKDCGATWVILGHSERRHVFGESDELIGQKVAHALSENVGVIGCIGEKLDQREAGITEKVVFEQTKAIADNVKDWSKVVLAYEPVWAIGTGKTATPEQAQEVHKKLREWLKTNVSEDVAKSVRIIYGGSVTGGTCKELGAQPDIDGFLVGGASLKPEFIDIINAKQ
|
It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids.
|
B0BM40
|
Q7NRL4
|
THIG_CHRVO
|
Thiazole synthase
|
Chromobacterium
|
MDDKLVIAGREYGSRLLVGTGKYKDFEQTAAALDVSGTEIVTAAIRRVNLGQNANEPNLLDFLPKNRYNLLPNTAGCYSAEDAIRTLRLARELLDDHRFVKLEVLGDPNNLYPNVRETLKAAEVLVAEGFDVLVYTSDDPIVARELEQIGCCAIMPLASLIGSGMGILNPWNLQLIIEQSKVPVIVDAGVGTASDAAIAMELGCDGVLMNTAIAAARDPVRMAHAMKLAVEAGRAAYLAGRMPKRFYSAVPSSPSEGVISSVKS
|
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
|
Q7NRL4
|
Q8R9U5
|
Y1491_CALS4
|
DegV domain-containing protein TTE1491
|
Caldanaerobacter
|
MEKIAIVTDSLSDIPEDLIKTYGIFVVPLTINIDGKSYKDGVDIKKEEFYKLLREGKMPTTTQASPVEFMEVFEDLLKSFDYVIAIILTSKFSGTYQSAVIARDMVDKNRIEVIDSRHFTLGNGMLVLKAARMAVEGASKEEIVSTVYETIPRIRGIMVFDSLDYLYRGGRLSRTQSIIGGILNVKPILTNEDGELKVIDKVRGQKKAIRWIIDYMKNTGIDFAEREVGLIHTDKEEFLNEIEAALRSELEITRFIRSQAGCGIGTHAGPDAAGVFFEEK
|
May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism.
|
Q8R9U5
|
P39888
|
TCMG_STRGA
|
Tetracenomycin polyketide synthesis hydroxylase TcmG
|
Streptomyces
|
MPVSDRPKGCILSTEEVPVLIVGGGLTGLSAALFLSQHGVSCRLVEKHRGTTVLTRASGISSRTMELLRGVGLERTVIERGPKLVEGARWRELGQPADQIPWVVIRANGLHDLENAVTVEEPSLDVGHLSPTRPYWCGQDRLEPILRDEAVRRGARIDFNTRMEAFTADESGVTATIVDQATGEQSTVRARYLIAADGVRSPVRETLGITRTGHGTIGNAMSVLFKADLRDTVKGRRFVICYLPNPDEPGVLQLPEVPAVLQLFDEDRWIFGFFFDPRETSPEQFTDERCAQIIRTATGLPGLPVEVQMARPWEMSHNSARSYRSGRVFLAGDAAHVHPPAGAFGANGGIQDAHNLAWKLAAVLKGTAGDALLDTYEQERLPIGAAVADQAWIRHTWRLNDSEELRRALRESTLVATGYRYTSDAVLGAAYPEPIPAAHDLTGRPGYRVPHVWLGRGGERVSTVDLGGDAFVVLAGPDGGEWQAAADKVAQDLGVPVHCHPVGGDGQLTDPDGAFLGTTGLTRNGALLIRPDGFVAWRAEYLPEDAAGELRSALERILARTSGTPGGTALEG
|
Hydroxylates tetracenomycin A2 at positions C-4, C-4A, and C12A to give tetracenomycin C (TCM C). Hydroxylates as well 9-carboxymethyl-TCM B3 to yield 8-demethyl-TMC C, a side reaction.
|
P39888
|
Q675B8
|
TR117_RAT
|
Taste receptor type 2 member 39
|
Rattus
|
MQHNLKTIFVISHSTLTIILFTELVTGIIGNGFMALVHCMDWLRRKKISLVNQILTALAISRIFQLCLLFISLVISFSYPDLTTTSLIKVTCNLWIIVNHFNIWLATCLGIFYFLKISNFSNSLFLYLKWRVEKVVLVTLLVSLVLLTLNSLLINLEINICINEYQRNITYSFNSYYHANCHRQMLSLHIIFLSVPFVLSLSTFLLLIFSLGTHHKKMQQHVQGRRDASTMAHFKALQTVIAFLLLYSIFILSVLVQIWKYELLKKNLFILFCQVAYVAFPSFHSYILILGDMKMRQACLSVLWWQKFRKNYVEPLDL
|
Putative taste receptor which may play a role in the perception of bitterness.
|
Q675B8
|
Q39I64
|
UVRC_BURL3
|
Excinuclease ABC subunit C
|
Burkholderia cepacia complex
|
MTSPEASDTPFEPKKILAQLPHMPGVYRYYDTAGAVLYVGKARDLKKRVSSYFTKTQLSPRIAMMVTRIARIETTVTRSEAEALLLENNLIKALAPRYNILFRDDKSYPYLKLTAHRFPRMAYYRGSVDKQNQYFGPFPSAWAVRESIQILQRVFQLRTCEDSVFNNRTRPCLLHQIGRCTAPCVGAISDEDYAIDVSNAARFLLGRQSEVMKELEQKMHAFAAELKFEQAAAVRNQMSSLATVLHQQAIEVGSDSDVDILAVVAQGGRVCVNLAMVRGGRHLGDKAYFPTHVESALTLAEGGIGDESELAEAVDAPADAMPDLPAEEPGRARSDAAASVEAEVLDAFIAQHYLGNRVPPVLVVSHAPASRDLLELLSEQAGHKVSLVRQPQGQRRAWLSMAEQNAQIALMRLLSEQGSQQARTRALAETLSYECDDLTTLRIECFDISHTMGEATQASCVVYHHHKMQSGEYRRYNITGITPGDDYAAMRQVLTRRYEKMVEQAAQAAAADDAAGIDGESTRQAEASSLLPNIVLIDGGKGQVEIARQVFTELGLDTSMLVGVAKGEGRKVGLETLVFADGRTPLELGKESAALMVVAQIRDEAHRFAITGMRAKRAKARQTSRLEELEGVGAKRRQRLLARFGGLRGVVAASVEELASVEGISHALAEQIYKQLH
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
Q39I64
|
Q8ZVR0
|
TBP_PYRAE
|
TATA-box factor
|
Pyrobaculum
|
MSSKGPSYRIENIVATVNLGVELDLEQLAERLTMAEYNPDQFPGLILRLTKPRISALIFRTGKMVCTGAKNEEDLKNAVRALVKLLKDHGADVPFDPEVQIQNIVASGNLHAEVDLEQAVLMLENAMYEPEQFPGLIYRMSSPRVVILIFGSGKIVCTGAKSEKDVATAVQKLYNQLKELGVLYVEEGGEELEEFEEEL
|
General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation.
|
Q8ZVR0
|
A8LSF9
|
TRPB_DINSH
|
Tryptophan synthase beta chain
|
Dinoroseobacter
|
MPDDLINSFMTGPDENGRFGDFGGRFVSETLMPLILELERQYEFAKTDQAFWDEMHHLWTHYVGRPSPLYFAERLTERLGGAKVYLKRDELNHTGAHKINNVLGQIILARRMGKTRIIAETGAGQHGVATATVCAKFGLKCVVYMGAHDVERQAPNVFRMKLLGAEVVPVTSGRGTLKDAMNDALRDWVTNVRETFYCIGTVAGPHPYPAMVRDFQAIIGQEAREQMMEAEGRLPDTLIAAIGGGSNAMGLFYPFLDDKEVAIIGVEAGGKGVNEKMEHCASLTGGRPGVLHGNRTYLLQDDDGQILEGFSISAGLDYPGIGPEHAWLHDIGRAKYVSITDAEALDAFQLCCETEGIIPALEPSHALAHVAKIAPDLPRDHIICMNMCGRGDKDIFTVAKALGQDMSGAV
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
A8LSF9
|
P18695
|
TBG_EMENI
|
Gamma-tubulin
|
Aspergillus subgen. Nidulantes
|
MPREIITIQAGQCGNNVGSQFWQQLCLEHGISQDGNLEEFATEGGDRKDVFFYQSDDTRYIPRAILLDLEPRVLNGIQSGPYKNIYNPENFFIGQQGIGAGNNWGAGYAAGEVVQEEVFDMIDREADGSDSLEGFMFLHSIAGGTGSGLGSFLLERMNDRFPKKLIQTYSVFPDTQAADVVVNPYNSLLAMRRLTQNADSVVVLDNAALSRIVADRLHVQEPSFQQTNRLVSTVMSASTTTLRYPGYMHNDLVGIIASLIPTPRSHFLLTSYTPFTGDNIDQAKTVRKTTVLDVMRRLLQPKNRMVSINPSKSSCYISILNIIQGEADPTDVHKSLLRIRERRLASFIPWGPASIQVALTKKSPYIQNTHRVSGLMLANHTSVATLFKRIVQQYDRLRKRNAFLEQYKKEAPFQDGLDEFDEARAVVMDLVGEYEAAERENYLDPDAGKDEVGV
|
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle pole or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly. Interacts physically with beta-tubulin and is involved in microtubule function.
|
P18695
|
Q2SL19
|
UPPP_HAHCH
|
Undecaprenyl pyrophosphate phosphatase
|
Hahella
|
MTWLEIVVLALIQGLTEFLPISSSAHLILPSEVWGWQDQGLAFDVAVHVGTLLAVMVYFRADIFNLLNGWIKQITGGGASQESRLAWAVILGTIPACVAGLLLDSWIEENLRSALVIALTTIGFGVLLGMADRKEGTRDIDQFTLKDALIIGVSQALALIPGTSRSGITMTSALFLGLNRDTAARFSFLLSIPLIAAAGLFKGLELADTGTSSQWSEIAGATLISAVSAYACIHLFLKFLQKIGFMPFVIYRMLLGAGLLVWLYVA
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
Q2SL19
|
P32925
|
TBB2_GEOCN
|
Beta-2-tubulin
|
Geotrichum
|
MREIVSIQCGQAGMNQVSTAFWSTITDEHGLDADGHLRPDASSLESDRLDVFFNEASNKKYVPRAVAVDLEPATLDAIRSGPLGHIYRPDNLISGESGAGNNWAKGFYTEGAELMDSVMDIIRREAEQSESLQGFQLAHSLGGGTGSGLGTLLLTKIREEYPDRMLSTYSVLPSPKVSDTVTEPYNAVLSFHQLIDNADATYCLDNEALYDICEKTLKINRPSHQDLNSLIALVMSGVTTGLRYPGQLNGDLRKLAVNLVPFPRLHFFTTGFAPLFAKNSRAFHNLTVPELTQQLFNPANVMAACNPYHGRYLTISTIFRGQVAMKEVEDAIHTARTKYSPYFVEWIPNNVQTSVCNVPPKGLTTSATFIANSTAVQELFERTANQFSVMFKRKGFLHWYTGEGMEPVEFSEAQSDLEDLILEYQQYQNAGVDEDEELMDHEEYADEGVEDFN
|
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
P32925
|
A8H968
|
UBIB_SHEPA
|
Ubiquinone biosynthesis protein UbiB
|
Shewanella
|
MTVKSIRRAYHVIRTALHYGLDDLLPPKLTPWYFKLLRYCFFWLRNQHKDKVGGERLKLAMQELGPVYIKFGQMLSTRRDLLSDEWAEELAMLQDRVPPFDSAIARESIEKELNAPIERYFNDFDDTPLASASISQVHTATLKSNGAAVVLKVLRPDVEKKVHADLLLMSQAADFLERLLGANNRLRPAEVVEDYRTTIEGELNLKLEALNAIKLRNNFIDSNALYIPYMYEELCFTRLIVMERIDGIPVSDKVALEAQGTNLKLLAERGVELFFTQVFRDNFFHADMHPGNVFVSREHPNDPFYIGLDCGIMGTLTDEDKRYLAENFLAFFNRDYRRIAQLYIESGWVSADTDVGAFEQAVKVVCEPMFNKPLDEISFGHVLLELFRTARRFDMVVQPQLVLLEKTLLYIEGLGRQLYPQLDLWQTAKPFLEQWMAEQVGPKAMAAKVKQQLPYWAEHLPELPELIYDNLKIGRDLSKNQNKLLDRYLKHQQKAHKSNYLLITSAILVICGTILLNQDATLWPSYGSIGIGITLWVLGWRSRPKNRKI
|
Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis.
|
A8H968
|
Q02NV3
|
TAL_PSEAB
|
Transaldolase
|
Pseudomonas
|
MTSKLEQLKQYTTVVADTGDFDAIARLKPVDATTNPSLLLKAAALPRYAEHLRQATAGSGGDAGLACDRFAVAVGKDILGVIPGRISTEVDARLSFDSEATLARAHRLIELYDEQGIDRERVLIKIASTWEGIRAAEILEREGIQTNLTLLFSFAQAVACADAGVFLISPFVGRIYDWYKKSENRDYAGAEDPGVQSVSRIYRYYKANGYKTVVMGASFRNLGQIEQLAGCDRLTISPDLLQQLADAQGELPRLLLPGEGEPRQVLDESAFRWQMNEDAMATEKLAEGIRLFARDQEKLEYQLATRH
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
Q02NV3
|
Q8BGZ8
|
ZPLD1_MOUSE
|
Zona pellucida-like domain-containing protein 1, secreted form
|
Mus
|
MERVWLLFLLAIRVSPGSAQFNSYNCDANLHSRFPAERDISVYCGVQAITMKINFCTVLFSGYSETDLALNGRHGDSHCRGFINNNTFPAVVIFIINLSTLEGCGNNLVVSTIPGVGASGNATTVQIGNISGYIDTPDPPAVISYLPGLLYKFSCSYPLEYLVNNTQLASSSAAISVRENNGTFVSTLNLLLYNDSTYREQLIIPSIGLPLKTKVFAAVQATNLDGRWNVLMDYCYTTPSGNPNDDTRYDLFLSCDKDPQTTVIENGRSQRGRFSFEVFRFVKHKNQKMSTVFLHCLTKLCRADDCPLLMPICGNRKRRDAQSWTTWAPQSTSGNAVLSAGPIITRSDETPTNNSQLGSLSVPPFQLNAVTSSLISGMVILGVLCFSLLLCSLALLHRKGSTSLVLNGVRNPVFE
|
Glycoprotein which is a component of the gelatinous extracellular matrix in the cupulae of the vestibular organ.
|
Q8BGZ8
|
A1R1C9
|
URED_PAEAT
|
Urease accessory protein UreD
|
Paenarthrobacter
|
MGPDSTLALGEGAVRGRLELGVCLRGGRSVASRQFHEGALRVLRPHYLDESGQVGYVMVNPGGAYLGADLFLIDVTVENNAALLLTTQSATKVYRTPGSFAEQRMSVRLGEGSRLELMPDQLIAYREASYRQNSRISLHPTSSLIMAEVITPGWSPDGASFKYQEVRLRNEIWIDDENGAKLLALDNLLIRPPLGDVTGMGFMEGFSHLGSLVVVDPRVNQGLADELDLIARDFDAYTGMSLTATIAGSTGLVLRSLSNSTEELNNLLGACAGVLRERWYGQAPLNLRKY
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
A1R1C9
|
Q6D9I8
|
UBIA_PECAS
|
4-HB polyprenyltransferase
|
Pectobacterium
|
MERSVTAGKWLAYCRLMRIDKPIGSLLLLWPTLWALWLAGGGAPAPWTLFVFVAGVFLMRAAGCVINDYADRHFDGHVKRTASRPLPSGEVSEQSAKILFVVLVLLAFGLVLTLNKMTIWLSVAGLVLAWVYPFMKRVSHLPQFVLGAAFGWSIPMAYAAVSESLPATCWMMFLAYICWTVAYDTQYAMVDRDDDLKIGVKSTAILFGRFDNIIIGLLQFSMLALLLALGNITGLGIPYTISLLVAAGMFIYQQILTAGRERDACFKAFHNNKYAGMAIFIGVLFGL
|
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
|
Q6D9I8
|
B0THR7
|
TRUB_HELMI
|
tRNA-uridine isomerase
|
Heliomicrobium
|
MEPLELEGFLNLLKPPGMTSHDVVAKARRLLKEKRIGHLGTLDPDAAGVLPIAIGQATRLIELVAGVDKAYRTQLRLGAVTDSQDASGRIVKTGAVPALSRDDWEETLRPFRGQILQTPPMVSAVSVGGKRLYEYARQGIEVERSARPVSISRIEIVHYDPATPEEIVIDVECSAGTYIRTLCHDIGQRLGCGGHMGWLIRTRSGLFSLRDSLTLESLAEGPPKEQIVTPFEALAHLPALEIGENRLAALSRGLAQYLQGDGWSEGQWIRMHRRQKLLAVGQAIRKDEQWLCQPRKVFTRLETRSK
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
B0THR7
|
Q587N7
|
TRIM5_CHLAE
|
TRIM5alpha
|
Chlorocebus
|
MASGILLNVKEEVTCPICLELLTEPLSLPCGHSFCQACITANHKESMLYKEEERSCPVCRISYQPENIQPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCQEDSKVICWLCERSQEHRGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADIREEKASWKIQIDYDKTNVSADFEQLREILDWEESNELQNLEKEEEDILKSLTKSETEMVQQTQYMRELISDLEHRLQGSMMELLQGVDGIIKRVENMTLKKPKTFHKNQRRVFRAPDLKGMLDMFRELTDVRRYWVDVTLAPNNISHAVIAEDKRQVSYQNPQIMYQAPGSSFGSLTNFNYCTGVLGSQSITSRKLTNFNYCTGVLGSQSITSGKHYWEVDVSKKSAWILGVCAGFQPDATYNIEQNENYQPKYGYWVIGLQEGDKYSVFQDSSSHTPFAPFIVPLSVIICPDRVGVFVDYEACTVSFFNITNHGFLIYKFSQCSFSKPVFPYLNPRKCTVPMTLCSPSS
|
Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2.
|
Q587N7
|
B7LRD2
|
TAM_ESCF3
|
Trans-aconitate 2-methyltransferase
|
Escherichia
|
MSDWTPSLYLHFAAERSRPAVELLARVPLENIEYVADLGCGPGNSTALLHHRWPAARITGIDSSPAMIAEARSALPDCQFVEADIRNWQPKQALDLIFANASLQWLPDHYELFPHLVSLLSPQGVLAVQMPDNWLEPTHVLMREVAWEQNYPDRGREPLAGVHAYYDILSEAGCEVDIWRTTYYHQMPSHQAIIDWVTATGLRPWLQDLTESEQQHFLTRYHQMLEEQYPLQENGQILLAFPRLFIVARRTE
|
Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate.
|
B7LRD2
|
Q1GYF5
|
TRPD_METFK
|
Anthranilate phosphoribosyltransferase
|
Methylobacillus
|
MSMTPKLALQRLIDHTDFTHEEMLDVMQQIMGGAFTTVQIAGFLAGLRVKGETVTEIAAAAQVMRALSSKVEVEDSSYLVDTCGTGGAPTKAFNVSTASAFVAAGAGARIAKHGGRAASSKSGSADVLEALGVNIGLTPEQVARCVNEAGIGFMFAPNHHAAMKYAAPVRRELGVRTMFNLLGPMTNPAGAKRQVMGVFDRDLVSLLAHTLKKLGSEHVMVVHSADGMDEISFSADTYVAELKHGEVNEYTLNPAQFDMPLHEIDSIHVENAQQSSEIILGVLSGARGPARDIVLLNAGAAIYVSGIAGDLQDGIAQAAHSLDSGAALHKLQQLKALSQAA
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q1GYF5
|
Q88MH6
|
UPPS_PSEPK
|
Undecaprenyl pyrophosphate synthase
|
Pseudomonas
|
MEKTKPAAPSSVPRHVAIIMDGNNRWAKKRLLPGVAGHKAGVDAVRAVIEVCAKSGVEVLTLFAFSSENWQRPAEEVGALMELFFSALRREAKRLDENNISLRIIGDRSRFHPELQAAMREAEAVTAGNNRFILQIAANYGGQWDIAQAAQRLAREVQAGHLRPEDITPGLLQTCLATGDLPLPDLCIRTGGEHRISNFLLWQLAYAELYFSDLYWPDFKHEAMRNALADFASRQRRFGKTSEQVEAGARA
|
Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
|
Q88MH6
|
B8E5F0
|
TIG_SHEB2
|
PPIase
|
Shewanella
|
MQVSVEATQGLERRLTISVPAEQIEKLVKDSLQREAKRARIPGFRPGKVPITVINKRYGAAIRQDIMGEVMQRNFIEAIIAEKLNPAGAPTFVPGSTDGEKFEFIATFEIYPEVELKGLDAIEVEQPKAEVTDADVDTMIETLRKQHATFAAVEREAADGDKVKMNFVGSVDGEEFEGGKADDFELQLGSGRMIPGFEAGILGHKAGEEFVIDVNFPEEYHAENLKGKAAKFAITLTEVQAANLPEVNDEFAALFGISEGGLEALKAEIRKNMNRELEQALKANVKEQVINGLLANNDITLPKALIDGEVNVLRQQAMQRFGNQTANMPELPAELFTEQAARRVKIGLLLGEVIKTNELKAEDERVQGLIASMASAYEDPSEVVAYYNSNKELMQNMRNVALEEQAVEALLKSAKVTEKEVAFEEFMNKATGRA
|
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
|
B8E5F0
|
Q8XT38
|
TREA_RALSO
|
Alpha,alpha-trehalose glucohydrolase
|
Ralstonia
|
MLDPRGLARPSRFCPRIIYAGTSHIRRATAAALLAASLCALPACADVGVGAALPLSPDKLYGELFVAVQTAQVYPDQKTFVDTVPKADPAVILQAYRAQKDVPGFSLKAFVDQYFTVPFETVITPPAGQSLRAHINWLWPALTRTTATAPDNSSLIPLPKPYVVPGGRFREVYYWDTYFTMLGLQASGRDDLVDSMLDNFAYQINRFGHIPNGNRTYYLSRSQPPFFALMVELAATKEGEAAYTRYLAPLRKEYAYWMRGAAGTAPGQASGNVVVLPDGTVLNRYWDDEATPRPESYLQDVATAQQAPDRPAAEVWRDLRAAAESGWDFSSRWFGDSATLATIRTTSILPVDLNALMFQLEKTIAKGCAVARDFACTVEFGNHARKRAVAVERYLWHPAGYYADYDWKLGKVRDNLSAAATYPLFVQMAPWGRARQTLRQTQTALLQVGGLSTTTLHTQQQWDAPNGWAPLQWIALQASQHYGQALLAQTIGERFLGSVERLYAAEQKLVEKYIVDGSGTGGGGGEYPLQDGFGWTNGVTLRLLDAYGRGQ
|
Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.
|
Q8XT38
|
Q81J84
|
TILS_BACCR
|
tRNA(Ile)-lysidine synthetase
|
Bacillus cereus group
|
MKDTFVEKVDDFVKQHDVLKNDSTIVVGVSGGPDSLALLYYLLEKRAEKQLEIVVAHVDHMFRGDESYEDLQFVQGLCEELGIICETIRINVSQYQQQYGMNAQVAARECRYAFLERIMKKYDARYVALGHHGDDQVETILMRLVRGSTPKGYAGIAVKRPFHNGYLIRPLLGVTKEEIVDYCNKLNLMPRIDPSNKKEVYTRNRLRKYVLPHLKEENPQMHEKFQKFSVQMQEDEAYLQELAFEKMNKVITKKSDKQISLSIPAFESMSMPLQRRGIQLILNYLYEYKIPSSLSSIHIDKLIEFFKRTQPSGSLDFPGDLKIVRSYEECSFRFKQEIVSPFSQDLLVPGTITLLNGDKFVTEVSEDIPSNMNETVFVAKYNDISYPLRIRSRENGDRMSIQGMNGTKKIKAIFIEAKVPKEKREEWPVVCDASGTIIWVPLLKRSAFAISKEMAKKDKYMIIHYKSKESSGRIMK
|
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
|
Q81J84
|
B5XJH4
|
VATB_STRPZ
|
V-ATPase subunit B
|
Streptococcus
|
MSVLKEYRTVSEVVGPLMIVDQVAGVHYNELVDITLHNGERRKGQVLEVQGDKAMVQLFEGSTGINLAKTKVRFTGHSLELAVSEDMVGRIFDGMGQPIDGGPELIPEKYLDIDGQAINPVARDYPDEFIQTGISAIDHLNTLVRGQKLPVFSGSGLPHNELAAQIARQATVLNSDDNFAVVFAAMGITFEEAEFFMNDLRETGAIDRSVLFINLANDPAIERIATPRIALTTAEYLAYEKGMHVLVIMTDMTNYCEALREVSAARREVPGRRGYPGYLYTNLSTLYERAGRLIGKKGSVTQIPILTMPEDDITHPIPDLTGYITEGQIILSQELYKNGFRPPINVLPSLSRLKDKGSGEGKTRQDHAATMNQLFAAYAQGKQAKELAVVLGESALSETDKLYVAFTNRFEEEYINQGFYTNRSIEESLDLGWELLSILPRTELKRIKDDMLDRYLPKADTTMTKVFVAND
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.
|
B5XJH4
|
Q9STF9
|
THA8L_ARATH
|
Protein THYLAKOID ASSEMBLY 8-like, chloroplastic
|
Arabidopsis
|
MTAIRVCSRKFPTFASIFFQNITRNPSIHRISFSNLKPKTLLHPIPPKPFTVFVSRFHDGRPRGPLWRGKKLIGKEALFVILGLKRLKEDDEKLDKFIKTHVFRLLKLDMLAVIGELERQEETALAIKMFEVIQKQEWYQPDVFMYKDLIVSLAKSKRMDEAMALWEKMKKENLFPDSQTYTEVIRGFLRDGCPADAMNVYEDMLKSPDPPEELPFRVLLKGLLPHPLLRNKVKKDFEELFPEKHAYDPPEEIFGRC
|
Binds weakly to specific single strand RNA (ssRNA).
|
Q9STF9
|
P22097
|
TRPB1_VIBPA
|
Tryptophan synthase beta chain 1
|
Vibrio
|
MAKLNAYFGEYGGQYVPQILVPALKQLEQAFIDAQEDPEFRSEFMTLLQEYAGRPTALTLTRNLTKGTKTKLYLKREDLLHGGAHKTNQVLGQALLAKRMGKHEIIAETGAGQHGVATALACALLGLKCRVYMGAKDVERQSPNVFRMKLMGAEVIPVHSGSATLKDACNEALRDWSGSYEDAHYLLGTAAGPHPFPTIVREFQRMIGEETKNQILAREGRLPDAVIACVGGGSNAIGMFADFIEEESVRLIGVEPAGKGIDTDQHGAPLKHGKTGIFFGMKAPLMQDENGQVEESYSVSAGLDFPSVGPQHAHLNAIGRAEYDNVTDDEALEAFQELARSEGIIPALESSHALAHALRMARENPEKEQLLVVNLSGRGDKDIFTVHAILEEKGVI
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
P22097
|
D4A615
|
TONSL_RAT
|
Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 2
|
Rattus
|
MTLEQELRQLSKAKARAQRNGQLCEEAVCCHQLGELLASHGRFQEALEEHQQELHLLESVQDTLGCAVAHRKIGERLAEMENYSAALKHQHLYLDLAGSLSNHTELQRAWATIGRTHLDVYDHCQSRDSLLQAQAAFEKSLAIVDEKLEGMLTQRELSEMRTRLYLNLGLTCESLQQTAQCNNYFKKSIFLAEQNHLYEDLFRARYNLGAIHWRGGQHSQAMRCLEGARECARAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLGSQKPNQRVAICQSLKYVLAVVRLQQQLQEAEGNDLQGAMAICEQLGDLFSKADDFPKASEAYQKQLHFAELLNRPDLELAVIHESLATTLGDMKDYHKAVHHYEEELRLRKGNALEEAKTWFNIGLAREEAGDAYELLAPCFQKAFGCAQQAQRYQLQRQILQHLYTVQLKLQPQEARDTEIRLQELSMAKDTEEEEEEEEEEEEEASEALETSEMELSESEDDADGLSQQLEEEEELQGCVGRRKINKWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLETLQQWVKLYFRDLDLETRQKAASMERRLQMASSGQASHSSPALQTIPNNHLFDPETSPPSSPCPKPPSYTPRPPEASPAPAKVFLEETVSAVCRPRKNRHRPASSSSSSEDDDDNTNPCRPSQKRLRHSTQQGEAKTPDPSKSRETAISSACRAAYQAAIRGVGSAQSRRLVPSLPRGSNEVPAPKTALIPEEEFLAEEWLEVDTPLTRSSSSSRPSTSISDYERCPARPRTRAKQSRPASLDGWCTRTKAADASLTAEPTENSSMPRTTGPNKENCAAGQPLLLVQPPPIRVRVQIQDNLFLIPVPHSDVHSVAWLAEQAAQRYFQTCGLLPRLTLRKDGALLAPQDPIPDVLQSNDEVMAEVTSWDLPPLKDRYRRACQSLGQGEHQQVLQAMEHQSSSPSFSACSLALCQAQLTPLLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGQTAFQNVEELDLSMNPLGDGCAQALASLLRTCPVLRTLRLQACGFSPSFFLSHQAALGSAFKDAEHLKTLSLSYNTLGAPALARVLQSLPTCTLLHLELSSVAASKSNSSLIEPVIKYLTKEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANPEVSCAGLEELLSALQERPQGLSFFDLSGCSIQGPLNSDLWDKILSQLQELQLCSKDLTTKDRDTLCQRLPAGACTLNQGSKLFFKCL
|
Component of the MMS22L-TONSL complex, a complex that promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication. It mediates the assembly of RAD51 filaments on single-stranded DNA (ssDNA): the MMS22L-TONSL complex is recruited to DSBs following histone replacement by histone chaperones and eviction of the replication protein A complex (RPA/RP-A) from DSBs. Following recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of RAD51 filaments and subsequent homologous recombination. Within the complex, TONSL acts as histone reader, which recognizes and binds newly synthesized histones following their replacement by histone chaperones. Specifically binds histone H4 lacking methylation at 'Lys-20' (H4K20me0) and histone H3.1.
|
D4A615
|
Q8WUA4
|
TF3C2_HUMAN
|
Transcription factor IIIC subunit beta
|
Homo
|
MDTCGVGYVALGEAGPVGNMTVVDSPGQEVLNQLDVKTSSEMTSAEASVEMSLPTPLPGFEDSPDQRRLPPEQESLSRLEQPDLSSEMSKVSKPRASKPGRKRGGRTRKGPKRPQQPNPPSAPLVPGLLDQSNPLSTPMPKKRGRKSKAELLLLKLSKDLDRPESQSPKRPPEDFETPSGERPRRRAAQVALLYLQELAEELSTALPAPVSCPEGPKVSSPTKPKKIRQPAACPGGEEVDGAPRDEDFFLQVEAEDVEESEGPSESSSEPEPVVPRSTPRGSTSGKQKPHCRGMAPNGLPNHIMAPVWKCLHLTKDFREQKHSYWEFAEWIPLAWKWHLLSELEAAPYLPQEEKSPLFSVQREGLPEDGTLYRINRFSSITAHPERWDVSFFTGGPLWALDWCPVPEGAGASQYVALFSSPDMNETHPLSQLHSGPGLLQLWGLGTLQQESCPGNRAHFVYGIACDNGCIWDLKFCPSGAWELPGTPRKAPLLPRLGLLALACSDGKVLLFSLPHPEALLAQQPPDAVKPAIYKVQCVATLQVGSMQATDPSECGQCLSLAWMPTRPHQHLAAGYYNGMVVFWNLPTNSPLQRIRLSDGSLKLYPFQCFLAHDQAVRTLQWCKANSHFLVSAGSDRKIKFWDLRRPYEPINSIKRFLSTELAWLLPYNGVTVAQDNCYASYGLCGIHYIDAGYLGFKAYFTAPRKGTVWSLSGSDWLGTIAAGDISGELIAAILPDMALNPINVKRPVERRFPIYKADLIPYQDSPEGPDHSSASSGVPNPPKARTYTETVNHHYLLFQDTDLGSFHDLLRREPMLRMQEGEGHSQLCLDRLQLEAIHKVRFSPNLDSYGWLVSGGQSGLVRIHFVRGLASPLGHRMQLESRAHFNAMFQPSSPTRRPGFSPTSHRLLPTP
|
Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. May play a direct role in stabilizing interactions of TFIIIC2 with TFIIIC1.
|
Q8WUA4
|
P0C2P4
|
VSTX2_GRARO
|
Voltage sensor toxin 2
|
Grammostola
|
YCQKWMWTCDEERKCCEGLVCRLWCKKKIEEG
|
Binds the voltage-sensor domain of the potassium channel KvAP (from the archaeon Aeropyrum pernix) and affects channel gating.
|
P0C2P4
|
O31443
|
YBFA_BACSU
|
Putative HTH-type DNA-binding domain-containing acetyltransferase YbfA
|
Bacillus
|
MKTRESSVGLKFRKFNRFYTNVLGFLNEHIYDSPFSLTETRILFEIYNTPNCTAKALQDKLGLDRGYVSRIVKQFEKEDLIYKQRSKDDARHHYIFVTETGKTIYKKLEEKANEQVELMLKVINQKEQHKLAEAMAEIEAILSQSLSARASEISIRDYFLSEDLQLLIEKQRQFYAEAHGWDDTFLAYLQETFDADIEKIWIAESGGKFAGSVGLVKHDEKTVQLRWFLVDADFRGRGLGTQLLEHLVAYCQDMKFDRIFLWTVSTMAEARPLYKKFGFRISEVKQEAPLWGQQLTEERWDLELS
|
Putative DNA-binding acetyltransferase.
|
O31443
|
P86530
|
VSP1_DABRR
|
Snake venom serine protease
|
Daboia
|
VIGGDECNINEHPFLA
|
Snake venom serine protease that may act in the hemostasis system of the prey.
|
P86530
|
C1DJ26
|
UBID_AZOVD
|
Polyprenyl p-hydroxybenzoate decarboxylase
|
Azotobacter
|
MKYSDLRDFLRALEARGELKRIQTPVSPILEMTEICDRTLRRSGPALLFEKPIGFDMPVLGNLFGTPQRVAFGMGAEDVSELREIGRLLALLKEPEPPKGLKDAWDKLPLFKKVLSMAPKVLKDAPCQEVILEGEDVDLGRLPVQHCWPGDAAPLITWGLTITRGPNKERQNLGIYRQQVLGRNKVIMRWLSHRGGALDYREWCQKHPDRPYPVAVALGADPATILGAVTPVPDTLSEYAFAGLLRGQRTELVKAVGSDLQVPASAEIVLEGHIHPGEMADEGPYGDHTGYYNEVDRFPVFTIERITRRRDAIYHSTYTGRPPDEPAVLGVALNEVFVPILQKQFPEIVDFYLPPEGCSYRMAVVTIRKQYPGHAKRVMLGVWSFLRQFMYTKFVIVTDDDIDARDWNDVIWAITTRMDPKRDTVLIDNTPIDYLDFASPVSGLGSKMGLDATHKWPGETSREWGRAIRQDPAVKQRVDELWPLLGLD
|
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
|
C1DJ26
|
Q9TM07
|
YCF17_CYACA
|
ORF48
|
Cyanidium
|
MPKYGFHQSTELINGRLAMLAFILSLFIEFITEQKILHFLKFL
|
Possible role in chlorophyll and/or carotenoid binding.
|
Q9TM07
|
Q8L1Z5
|
TPIS_BARHE
|
Triose-phosphate isomerase
|
Bartonella
|
MSPNIRPFIAGNWKMNGTGESLGELRAIAAGISSDLGRLFEALICVPATLLSRAFDILGGENILLGGQNCHFDDYGPYTGDISAFMLKEAGASHVIIGHSERRTVYQESDAIVRAKVQAAWRAGLVALICVGETLEERKSNKVLDVLTRQLEGSLPDGATAENIIIAYEPVWAVGTGNTATSADVAEVHAFIHHKMHSRFGDEGAKIRLLYGGSVKPSNAFELLSTAHVNGALIGGASLKAIDFLTICDVYRKL
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q8L1Z5
|
Q4AAI5
|
TIG_MESHJ
|
PPIase
|
Mesomycoplasma
|
MIKREFLPESAELKIKLTADSKKWAEFYQKAEQKQAAKVSLRGFRKGKVPLEKARAYLNPQAVFELALRMFLPELEKQAATNIIDSDNVIESPIFNIVNMDKNNLEIEFLYPVYPEIKLPDYKNLKTKFAIKKITKEDIELQKQKLLEAKGRFIEVNRPVKIGDVINFNFKGFIDDEPFDGGEGENFDLRIGSNSFIAGFEEQLVGLEIKKEADIYVTFPENYQVHTYANKKARFRVRINKIKENQPAKLTNEFVASLKIQNVETISQLEVYLENLTERENIERAKIDFQRNALTEIGEQVEVPLAKKLINLEIERLNEVFHSTLKQQEIPLKEYLKITKFTEKDIYDQFEVEAKKLLKNSFIFAEIAKLEGLVPTQQEYESHVEKLAKFTGKSVQEISETVSYNEIQINITNQKVIDKLIEFNHEAKDEEIVNKNQNDNEIEQDKEQKDNNEEKIKQENNLENK
|
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
|
Q4AAI5
|
Q5QTZ0
|
TRUB_IDILO
|
tRNA-uridine isomerase
|
Idiomarina
|
MSKARLRKGRALTGVVLLNKPQGMSSNHALQRVKRLYNAQKAGHTGALDPLATGILPVCLGEATKFSQYLLDADKAYRVEATLGVRTTTSDAEGEVVEEKPVAVDTAKVADAIKQFIGEQDQSPSIYSALKHEGRPLYYYARQGIEVPKKTRTITVHSIELLNIQDNKVTLQVSCSKGTYIRTLVDDLGQLLGCGAHVSMLHRNAVADIAEAAMVTLEQLETLAEEGYEGLDALLHPADLLLGQLPEVTVTQAQTRDFLHGQPIPLPEQNGNDAEEWRVATENSLFLGVARVKNAELWPRRVIAREHVDL
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
Q5QTZ0
|
B5FAT7
|
XNI_ALIFM
|
Flap endonuclease Xni
|
Aliivibrio
|
MAIHLVIIDALNLIRRVHSAQPNQDDIQAVITTTTRTINKILKETEPTHIIAVFDHHLQDRGWRAEILPQYKEDRKPMPEALQKGMDDIQEAWWKLGIDSLLSDGDEADDLVATLANKVAVHNEQVTIISTDKGYCQLLSPTLRIRDYFQHRWLDAPFVEKEFGLKPEQLADYWGLAGISSSKITGIPGVGPKAALEILTQFPTIEAANESEDLPKKYRKKFDEHYETAILCRQVAGLRTDIELGFNLQDIRYEKGTRDYQV
|
Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment.
|
B5FAT7
|
Q9V1G9
|
TRPA_PYRAB
|
Tryptophan synthase alpha chain
|
Pyrococcus
|
MFRDGSLIPYLTAGDPSAKATLRFLLAIEEYSGAIELGIPFSDPIADGKTIQQSHFRALKGGFKLEHAFNIVREFRKHSDVPIVLMTYYNPVFRVGLREFIGKAKDSGVDGMLIVDLPVMHASEFLEVAREEGIKTVFLAAPNTPDERLKEIDKASTGFVYLISLYGTTGARDKIPETAFNLLKRAKRICKNKVAVGFGVSKREHVEMLLNAGANGVVVGSALINIIAEHGENAEEKLREKVRELAGL
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
Q9V1G9
|
P30931
|
TF_BOVIN
|
Coagulation factor III
|
Bos
|
MATPNGPRVPCPQAAVARALLFGLVLIQGAGVAGTTDVVVAYNITWKSTNFKTILEWEPKPINHVYTVQISPRLGNWKNKCFYTTNTECDVTDEIVKNVRETYLARVLSYPADTSSSTVEPPFTNSPEFTPYLETNLGQPTIQSFEQVGTKLNVTVQDARTLVRANSAFLSLRDVFGKDLNYTLYYWKASSTGKKKATTNTNGFLIDVDKGENYCFHVQAVILSRRVNQKSPESPIKCTSHEKVLSTELFFIIGTVMLVIIIFIVVLSVSLHKCRKVRAERSGKENTPLNAA
|
Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade.
|
P30931
|
Q76PC3
|
YQ73_SCHPO
|
Uncharacterized mitochondrial carrier C1442.03
|
Schizosaccharomyces
|
MEPGIPPMIDKAPAYSHVLIAGGIGGATADFLMHSLDTVKTRQQAALYTNKYNGMVKCYSTILCEEGVFHGLYSGVCPMLIGSLPATALFFSSYEYTKRHLMSNYNLPETLCFLLAGFVGDLFASVVYVPSEVLKTRLQLQGRYNNPHFQSNYNYPSFRGAVKQIAKQEGMKTFFYGYRATILRDIPFSGFQLLFYEKLRQVAQKECGQKDIGVFRELITGSLAGAGAGFLTTPLDVAKTRLQTMIRTTDKVSDDINSGRYFFAKDENSKSKSAASLVKPKIGIRHVLGGLYKSEGLLGLFRGFGPRIFWTSSQSSLMFVFYEGIIRLFNKNNVLERD
|
Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane.
|
Q76PC3
|
A8F9B7
|
TRUA_BACP2
|
tRNA-uridine isomerase I
|
Bacillus
|
MKVKCTVSYDGTHFKGYQVQPGQRTVQTEIESALAKMHKQDELVPIVASGRTDSGVHAKGQVIHFDTPLSIPMERWPFALNSLLPDDIRVLKAEEVDESFHARFSVVSKEYRYKVSTETHQNVFTRQYACHFPYRLDADKMREAAGYLIGTHDFTSFCAANTEVQDKVREIYTLEWKNVSDGLEMRVRGNGFLYNMVRIIAGTLLEVGSGKFHPDEIKAMLAARNREAAGKTAPSHGLYLWEVFYDN
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
A8F9B7
|
Q9PK80
|
TAL_CHLMU
|
Transaldolase
|
Chlamydia
|
MSSQFDQLKLWSVLVGDSGDPDLIKTLDVQDATTNPSLILKVAQEPKYQSMLTEAISWGIRQNGDDVQTLTFVLDKIQVNLGLEILKYVPGRVSLEIDARLSFNTEAMVQRAIFLSQLFEKMGGDKKRLLIKIPGTWEGIRAAEVLENQGIACNVTLIFSLVQAIAAAKAKVTLVSPFVGRIYDWWIAAYGAEGYSIEADPGVASVANIYSYYKKFDIPTQIMAASFRTKEQVLALAGCDFLTISPKILEELKKEQQPVERKLSVEEAKKLDIQPVELSESVFRFLMNEDAMATEKLAEGIRIFSGDTQILESAVTEFIRQIAAQEA
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
Q9PK80
|
C0QD59
|
TATC_DESAH
|
Sec-independent protein translocase protein TatC
|
Desulforapulum
|
MSREEEKSPFTEHLGELRDRLVRSFIAVGVGFVIAYCFKERLFDILTAPLIAAMGEGQKMIFTGLPEAFFTYLKVSLLTGVILATPVLFYEFWMFVSPGLYRKEKRFVLPVVILSIFFFCVGSSFGYFIVFPYGFQFFLGFSSDTIQAMPSMKEYLGFASKMLLAFGFVFELPLVLTFMARMGLVSVEFLKKNRKYAILIFFTGAALITPPDVVTQIMMAIPLMILYEISIIGARVFGKKKDSDEEEAAENSDVQTDKSTDDTTPGEDQN
|
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.
|
C0QD59
|
A9IZF6
|
TSAD_BART1
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Bartonella
|
MRLLGIETSCDETAAAVIEYNNESSSRILSNIVWSQIDHHAPYGGVVPEIAARAHVEILDHLILQALTEANTKLKDIDGIAATSGPGLIGGLLVGVMSAKALSLATGKPFIAVNHLEGHALTAVLTHNVKFPYLLLLVSGGHTQTILVHGVGNYQRLGTTIDDALGEAFDKTAKLLGLPYPGGPALEKAALLGDKNRIPLPRPLKGEKRLDFSFSGLKTAVRQAATAIAPLTENDVADIAASFQAAVTDTVRDRVHLALQHFTHQYPLSHDQEKHSPALVVAGGVAANQALRSTLQELAHQHGFEFIAPPLSLCTDNAAMIAFAGAQKLAQGETSSLDIAPRSRWPLDEKAIPLIGMGRRGTKA
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
A9IZF6
|
O07527
|
YHCY_BACSU
|
Sensor histidine kinase YhcY
|
Bacillus
|
MSKTRMEKLKTLKTIAETLNQGHDIKATLDEVLKELLSLTNLQSGWIFLIEEDGSYTLAADAYLPPALSRKEKVLMCEGECYCLTKFNNGGLRKAANIMNCKRIESAENLHCFDTEGITHHATVPLEDGDRRFGLLNVAAAGKTMFDEEELHLLESVAFQIGTAIQRMRLSEYQQKNALLMERNRLAQELHDSVNQMLFSVSLTAKAAKTLTKDENLQQMIDFIQNLSQDALAEMKALIWQLRPGGLEKGLAEAIKSYGALIGLKIIFTQKGCPVLTDEQEHMLWRVVQEALNNCKKHAGTDTAYVSLTASLCHAELDIIDHGAGFRYEAHAGLPSLGIKGMKERAEKAGAKFWIESALGTGTKLSIRLPLKSRKGGAV
|
Member of the two-component regulatory system YhcY/YhcZ. Probably activates YhcZ by phosphorylation.
|
O07527
|
A6LIC2
|
TYSY_PARD8
|
Thymidylate synthase
|
Parabacteroides
|
MKQYLELLNRVLTEGVRKEDRTGTGTISVFGHQMRFNLEEGFPLLTTKKLHLKSIIYELLWFLNGDTNVKYLQDHGVRIWNEWADADGSLGHIYGYQWRSWPDYKGGSIDQITEAVETIKHNPDSRRIIVSAWNVADLDNMNLPPCHAFFQFYVANGRLSLQLYQRSADIFLGVPFNIASYALLLQMMAQATGLKAGDFVHTLGDAHIYSNHLEQVKLQLTREPRALPRMEINPDVKSIFDFKFEDFNLTGYDPHPHIKGEVAV
|
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.
|
A6LIC2
|
Q9W1R5
|
VIR_DROME
|
Protein virilizer
|
Sophophora
|
MADVDDGSELLFFDTFSHEEVTDINLDLVQFPKPVFITQVRIIPLGARVQADFPGGVRLGATNPSKFDLEFFVNDLGMPAASAFENLGLLRYNQNDCIHLDCSQEKIVTDGLVLRGWYSTITLAIYGIFTNSVTEPIASPTLPCEPVGPEIANLSGEVLLQEDVLKDEWQEPMQAELLTAHKGNVSDYDPEDMEYGMSRDHYHQHAEEQEQREMRRLRRSTHSTDHSPPPPRRSHTHSESNDREYIRCSRDKGSRDWSRSPEYSSHRSRRKRSERSRSVVDEHKWPRTPPASIDSPTRPRSPDTMDYEDEDSRSHYKMQSSHYRHSSESLHRGERDRDDEDRSCTPQEQFEPILSDDEIIGDDEEDDAVDAAAIAEYERELEAAAAAAPPAIDAFEPWQKPLLVFEGDMAAHFCKELETLKLLFKKLVLQTRCENVNAFSEEHGASVDEREQFVYLGEQLNNQLGYLAQHYKRRNFVLQQFFGNDELHLRQAANVLQIALSFQAACMQPQPAFKIRHIKLGARMAELLGSSEELFQHLLKEHKFDIFEAVFRLYHEPYMALSIKLQLLKAVYALLDTRMGIEHFMGAKNNGYQMIVEAIKTAKLTRTKYALQAIIKKLHLWEGLESVQIWCRRLFVDRIIIPGNRDQMEDTVITCQQIEFAFEMLMDALFSSQLSYLQPRRFLPVSKKFEVVTDPTAQRSFGNALQSYLGQNSLAESLLVMLANCKELPATTYLSMLDLMHTLLRSHVGIDYFVDDAFPVTQTIVAILLGLDEVPRNPEEKEEKAEKSDAEDKAMEVENEAVEAGGEKPTPPTADEEGKPVAAPISVPAPAAAPQVRPRPILRPVLPRLARLGIEMSYKVQTRYHLDAIAYAAAAPEYDAVKLATHMHAIYSQTCDPAGRQHTVEVLGLNNNLKIFMDLIKKEQRLQTQRQLSSPGTKYKSPVLSYAVDMVDACVRYCEQLDYLIEHGGVILELAKNHETFEPSVSAVLQEMYVYMKPLEAINVFVYDDIMPLVEVIGRSLDYLTTFPGDLIMAMRILRYLSISKPLAGQKAPPVTEELKHRFVALQLYAADGVQLCIQIMERLCAYFEQPGAHAPALMTIQGVHCCQIMLPTLQILRELLSYAILCRDGTYKDLTAIDHLVKVYYLLYYFPTRCQAGPEVEQCKMEVVQTLLAYTQPNEQDEESLHKSLWTLMIREVLKNVDGPAHFIPGLKLLAELLPLPLPMPQPLCDQLQQQHKQRLITERKLWSAHLHPQSGQIAKLVEALAPSSFPQLSELLQRVCMQLSDLAPNMTLLIAKTITELLCNEYQTSNCIPTTNLERLLRFSTRLCAFAPLKSSMLSILSGKFWELFQSLLALNEFNDVVSNCQEAVHRILDSFLDSGISLISHKSTASPALNLAAALPPKELIPRIIDAVFSNLTSVEVTHGISILAVRNLVILTEHDFTFYHLAQLLKQKITEFQAWMERVILHNETVEYNANIESLILLLRSLTQIEPPPAMSAMPHRTLKLGATELAQLVEFQDIELAKPPVLSRILTVMEKHKAVANEAALSDLKQLILLQASKQEILAGTSTETPPEAEGEANPSASSCSASLTVEPYLPQAEGIVTQYEARPIFTRFCATAENAQLTARYWLDPLPIELIEDMNEPIYERIACDLTDLANVCLNPDLNVAGDSKRVMNLSGSPQSNREMTPTAPCFRTRRVEVEPATGRPEKKMFVSSVRGRGFARPPPSRGDLFRSRPPNTSRPPSLHVDDFLALETCGAQPTGPTGYNKIPSMLRGSRVGRNRGSRISAAAAFRQKKMMRIGSPSSWAESPGSYRSASDSHFSSSDSHYSSPHYSGRPRGRGLRSRPSYLR
|
Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of mRNAs, a modification that plays a role in the efficiency of mRNA splicing and is required for sex determination . Required for sex determination and dosage compensation via Sxl alternative splicing: m6A methylation acts as a key regulator of Sxl pre-mRNA and promotes female-specific alternative splicing of Sxl, which determines female physiognomy . M6A methylation is also required for neuronal functions . Required for proper inclusion of regulated exons in Ubx transcripts, leading to isoforms Ia/b and IIa/b .
|
Q9W1R5
|
B8D9L8
|
TYSY_BUCA5
|
Thymidylate synthase
|
Buchnera
|
MKQYIKLIKKIIRVGNQKKDRTGTGTLSIFGYNMKFDLKKGFPLLTTKKCHIASIIYELLWFLKGDTNIAYLNENKISIWNNWANESGDVGPIYGKQWRNWSTPEGHEIDQIKNVLIQLKKNPDSRRMLVSSWNVGDIDKMRLPPCHVLFQFYVFNNTLSCQLYQRSCDVFLGLPFNIASYSILIHMIAQQCDLKVGDFLWTGGDVHLYNNHIELAKKQILRIPRTLPKLTILKKPQSLFQYCFEDFKIIGYHPYPAIKGKISI
|
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.
|
B8D9L8
|
A8FDD4
|
TRUB_BACP2
|
tRNA-uridine isomerase
|
Bacillus
|
MINGVLLLHKERGMTSHDCVFKVRKILHTKKVGHTGTLDPEVSGVLPICIGRATKIVEYLTDKSKTYDAEITIGFSTTTEDQTGEIVEEKKVQNPISEEEIDAALKQFQGTIEQIPPMFSAVKIGGKKLYEYAREGIEIERPSREISIHRIERTTPALFENGTVSFRFTVLCSKGTYVRTLAVDIGKKLGFPAHMSHLIRTGSGDFTLDECITLDELRDISEEGTVDEHLVPIERALNHLPKWEINDTLASKVENGAVLPMPDEFAHFAEEDRVAVFAPSGRCMAIYMKHPTKQNLMKPAKILSQDKQS
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
A8FDD4
|
Q2YQD6
|
UREG2_BRUA2
|
Urease accessory protein UreG 2
|
Brucella
|
MKKIPRIGVGGPVGSGKTAIIEAVVPILIKLGYRILVITNDIVTTEDAKHVQRTLKGVLIEDRIVGVETGGCPHTAVREDPSMNLAAVEEMEAKFPDTDLVLLESGGDNLTLTFSPALIDFFIYVIDVAAGDKIPRKNGPGISQSDILVINKTDLAPYVGASLQVMDDDSRMMRGKKPFVFTNCKTNEGIDDLVHLIRENVLFDTEVSKESA
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
Q2YQD6
|
B6DCT6
|
TX404_LYCSI
|
Toxin-like structure LSTX-C4
|
Lycosa
|
MKVLVLFSVLFLTLFSYSSTEAIDEFDSDAEEDMLSLMANEQVRAKACTPRLHDCSHDRHSCCRGELFKDVCYCFYPEGEDKTEVCSCQQPKSHKYIEKVVDKAKTVVG
|
Enhances the high-affinity desensitization of human P2RX3 purinoceptors.
|
B6DCT6
|
Q02E04
|
UBIA_PSEAB
|
4-HB polyprenyltransferase
|
Pseudomonas
|
MFVTLIKPLARLHPRAWDFVQLVRLDRPIGIYLLLWPTLWSLWIAADGVPELKNLLIFVLGVILMRAAGCVINDFADRNFDGHVARTKARPLATGKISVREAWITFAVLVALSFGLVLLTNATTVWLSFGAVAVASLYPFMKRYTYYPQVVLGAAYSWGILMAFTAERGELPASAWLLFLANVLWTVAYDSYYAMTDREDDLKIGIKSTAILFGDADRLIIGSLQGLTLLLLALAGSRFELGLYFYLGLAVAAACFVWEAWSTRDRDPQACFRAFLHNHWAGLAIFLGTVADYALR
|
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
|
Q02E04
|
B1WAX6
|
TIGAR_XENTR
|
TP53-induced glycolysis and apoptosis regulator
|
Silurana
|
MARFALTIVRHGETRYNKEKLLQGQGIDEPLSEIGFKQADAVGRFLSNVRFTHVFSSDLIRAKQTACAIMENNKISEDIKIIYDRRLRERKYGDAEGRPLSELKVMAKKAGDQCPSYTPPGGETLEQVRARAKDFFEYLCRLVLEESSAKEQSELGASGMGGVTSADLGPFVNHNKEPAELGESRDVTVHASVLLVSHGAYMRNWIKYLVEDLQFTFPPELKKSRELPVSPNTGISHFIVTVSSATPRKPEIQCVCINLHSHLSDINADTSHYQV
|
Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate. Acts as a negative regulator of glycolysis by lowering intracellular levels of fructose-2,6-bisphosphate in a p53/TP53-dependent manner, resulting in the pentose phosphate pathway (PPP) activation and NADPH production. Contributes to the generation of reduced glutathione to cause a decrease in intracellular reactive oxygen species (ROS) content, correlating with its ability to protect cells from oxidative or metabolic stress-induced cell death. May play a role in mitophagy inhibition.
|
B1WAX6
|
Q8A0X7
|
TRMB_BACTN
|
tRNA(m7G46)-methyltransferase
|
Bacteroides
|
MGKNKLEKFADMASYPHVFEYPYSAVDNVPFDMKGKWHQEFFGNDHPIVLELGCGRGEYTVGLGRMFPDKNFIAVDIKGSRMWTGATESLQAGMKNVAFLRTNIEIIERFFAAGEVSEIWLTFSDPQMKKATKRLTSTYFMERYRKFLKPDGIIHLKTDSNFMFTYTKYMIEANQLPVEFITEDLYHSDLVDDILSIKTYYEQQWLDRGLNIKYIKFRLPQEGVLQEPDVEIELDPYRSYNRSKRSGLQTSK
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
Q8A0X7
|
Q6P502
|
TCPG_RAT
|
CCT-gamma
|
Rattus
|
MMGHRPVLVLSQNTKRESGRKVQSGNINAAKTIADIIRTCLGPKSMMKMLLDPMGGIVMTNDGNAILREIQVQHPAAKSMIEISRTQDEEVGDGTTSVIILAGEMLSVAEHFLEQQMHPTVVISAYRMALDDMVSTLKKISTPVDVNNRDMMLNIINSSITTKVISRWSSLACNIALDAVKTVQFEENGRKEIDIKKYARVEKIPGGIIEDSCVLRGVMINKDVTHPRMRRYIKNPRIVLLDSSLEYKKGESQTDIEITREEDFTRILQMEEEYIQQLCEDIIQLKPDVVITEKGISDLAQHYLMRANVTAIRRVRKTDNNRIARACGARIVSRPEELREDDVGTGAGLLEIKKIGDEYFTFITDCKDPKACTILLRGASKEILSEVERNLQDAMQVCRNVLLDPQLVPGGGASEMAVAHALTEKSKAMTGVEQWPYRAVAQALEVIPRTLIQNCGASTIRLLTSLRAKHTQENCETWGVNGETGTLVDMKELGIWEPLAVKLQTYKTAVETAVLLLRIDDIVSGHKKKGDDQNRQTGAPDAGQE
|
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
|
Q6P502
|
Q9Z2B2
|
UCP5_MOUSE
|
Solute carrier family 25 member 14
|
Mus
|
MGIFPGIILIFLRVKFATAAVIVSGHQKSSTLSHEMSGLNWKPFVYGGLASIVAEFGTFPVDLTKTRLQVQGQSIDVRFKEIKYRGMFHALFRIYKEEGILALYSGIAPALLRQASYGTIKIGIYQSLKRLFVERLEDETLLINMICGVVSGVISSTIANPTDVLKIRMQAQGSLFQGSMIGSFIDIYQQEGTRGLWRGVVPTAQRAAIVVGVELPVYDITKKHLIVSGMLGDTILTHFVSSFTCGLAGALASNPVDVVRTRMMNQRAIVGHVDLYKGTLDGILKMWKHEGFFALYKGFWPNWLRLGPWNIIFFITYEQLKRLQI
|
Participates in the mitochondrial proton leak measured in brain mitochondria.
|
Q9Z2B2
|
A4QTV1
|
VPS27_MAGO7
|
Vacuolar protein sorting-associated protein 27
|
Pyricularia
|
MMSWWSSGANTALDEQIEKATSSSLEDIALNLEISDVIRSKTVPPKDAMRSLKKRIGHKNPNTQLSALELTDTCVKNGGQHFLVEIASREFIDNLVSLLKATGPAAVNADVRARILGLIQSWAAVTQGRVELSYIGEVYKTLQHEGFQFPPKVAVATSMIDSSAPPEWTDSDVCMRCRTPFTFTNRKHHCRNCGSCFDQQCSSKSIPLPHLGIMQPVRVDDGCYAKVTDKSRGSGGAGAGAGYDRKSPSLYSSFPHKNRSSSAMQPRSARVDDGFDEDLKKALAMSLEEVKSHSRNYAPASNGVANSGQSKVNGDSSATKTVEEEDDDLKAAIAASLADMEEQKKKHSAVLHEQTHSTEAASASTFVPPKNDYELTPVEAENINLFATLVDRLQTQPPGTILREPQIQELYDSIGTLRPKLARTYGETMSKHDTLLDLHAKLATVVRYYDRMLEERLSKAYGQRNFAGYNMHVPRQTSSPYPSLQGPSAPANVPGESFYTGQPQHDYAEPSRQPSYPPQASGAQQQFHQYAPPHQASQPSEGWQPSHTPAPAAQYAGQPPQQSTESTHSHSSAHNHQNLAAPSAPDQSLPTPTTDPAASYYFNQQQVSALQTPVSVPAEPVQSPYPNLQQQPPAQYQHSPAPQGQAQQQKPPQQPQQPYWQHSASQNTALPTNHQPWPQVPNRQSASYVQEPLPSAPQHAPQKPVVEEALIEL
|
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
|
A4QTV1
|
A8XXC7
|
WDFY2_CAEBR
|
WD repeat and FYVE domain-containing protein 2
|
Caenorhabditis
|
MAAIINQRVDQGESSMGGAKPTLLHKIAGHVARINDVILLSKDEGVWTASDDRSVRLYLKRDNDQFWPSIHHFMPVAPTCLFYSEETYKLLVGLINGNVYEFNVADDFNSMTESRKWTCHAGPISGLGFALSSELIFSCSRDKSIVWHCSENSNKVGSYLLENSCTAMVIDLPFVFVGDHGGHVTVLRIIDNQPNLVSKLSAHTNSITSLTWDGNKKVLYSGSSDHLIIMWDIGGGKGEAYELNGHNGKVTTLCAAPAAKRLFSADEHGKLMCWDMDVRRVETPEWKTSDCCQKCNQPFFWNLQAMWQRKVVGLRQHHCRTCGSAVCGSCCDNWTTYPPMGYETKVRICNDCAGRMKENPGNFDLTPLAIPHEIRTGITAMHLQETLGLLVTSGQNRVVMIWDVRSVCSAPSGSGGH
|
Plays a role in coelomocyte endocytosis.
|
A8XXC7
|
P0C352
|
U6A_CONSP
|
Conotoxin sr7a
|
Lindaconus
|
CLQFGSTCFLGDDDICCSGECFYSGGTFGICS
|
Elicits hyperactivity when injected intracranially into mice and produces paralysis when injected into the pedal muscle of freshwater snails, Pomacea paludosa, but it has no apparent effect after intramuscular injection into the limpet Patella opea or the freshwater fish Lebistes reticulatus.
|
P0C352
|
Q25456
|
TPM_METEN
|
Allergen Met e I
|
Metapenaeus
|
MKLEKDNAMDRADTLEQQNKEANNRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANNQLVEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELSGY
|
Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
|
Q25456
|
Q2T4M4
|
THAA_BURTA
|
Transcriptional repressor ThaA
|
pseudomallei group
|
MSAGREQFVRRMRASRSAGDAFDVVLQRGTELGFQFCAYRLTAPIPITRRRTFVWSNYPNACAASPVLDADRSGRGADTDAQACGVTADATQVFESMADGLWAETSDQGVRYGWALSVRDRWGAVGTLKFARGTREIVQEELDDIEPEMIWLAHLAHDTIGSLMRDETIPGEIARVSLVERQILLWTAEGKTVSEISSILQMSVRNINFHIQNVVGKLGATNKTHAAVKATLVGLIPV
|
Represses thailandamide production.
|
Q2T4M4
|
O58523
|
TYW2_PYRHO
|
tRNA wyosine derivatives biosynthesis protein Taw2
|
Pyrococcus
|
MRTQGIKPRIREILSKELPEELVKLLPKRWVRIGDVLLLPLRPELEPYKHRIAEVYAEVLGVKTVLRKGHIHGETRKPDYELLYGSDTVTVHVENGIKYKLDVAKIMFSPANVKERVRMAKVAKPDELVVDMFAGIGHLSLPIAVYGKAKVIAIEKDPYTFKFLVENIHLNKVEDRMSAYNMDNRDFPGENIADRILMGYVVRTHEFIPKALSIAKDGAIIHYHNTVPEKLMPREPFETFKRITKEYGYDVEKLNELKIKRYAPGVWHVVLDLRVFKS
|
S-adenosyl-L-methionine-dependent transferase that acts as a component of the wyosine derivatives biosynthesis pathway. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to 4-demethylwyosine (imG-14), forming 7-aminocarboxypropyl-demethylwyosine (wybutosine-86) at position 37 of tRNA(Phe).
|
O58523
|
P06526
|
TDT_BOVIN
|
Terminal deoxynucleotidyltransferase
|
Bos
|
MDPLCTASSGPRKKRPRQVGASMASPPHDIKFQNLVLFILEKKMGTTRRNFLMELARRKGFRVENELSDSVTHIVAENNSGSEVLEWLQVQNIRASSQLELLDVSWLIESMGAGKPVEITGKHQLVVRTDYSATPNPGFQKTPPLAVKKISQYACQRKTTLNNYNHIFTDAFEILAENSEFKENEVSYVTFMRAASVLKSLPFTIISMKDTEGIPCLGDKVKCIIEEIIEDGESSEVKAVLNDERYQSFKLFTSVFGVGLKTSEKWFRMGFRSLSKIMSDKTLKFTKMQKAGFLYYEDLVSCVTRAEAEAVGVLVKEAVWAFLPDAFVTMTGGFRRGKKIGHDVDFLITSPGSAEDEEQLLPKVINLWEKKGLLLYYDLVESTFEKFKLPSRQVDTLDHFQKCFLILKLHHQRVDSSKSNQQEGKTWKAIRVDLVMCPYENRAFALLGWTGSRQFERDIRRYATHERKMMLDNHALYDKTKRVFLKAESEEEIFAHLGLDYIEPWERNA
|
Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator . One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells.
|
P06526
|
Subsets and Splits
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