位置:首页 > 蛋白库 > BUR1_ASHGO
BUR1_ASHGO
ID   BUR1_ASHGO              Reviewed;         753 AA.
AC   Q75D46;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Serine/threonine-protein kinase BUR1;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
GN   Name=BUR1; OrderedLocusNames=ABR177C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Serine/threonine-protein kinase involved in transcription
CC       regulation. Phosphorylates the UBC2/RAD6 ubiquitin-conjugating enzyme
CC       (E2), leading to monoubiquitination of histone H2B and the silencing of
CC       telomeric-associated genes. Also required for histone H3 methylation.
CC       Necessary for the recovery from pheromone-induced growth arrest in the
CC       cell cycle G1 phase (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.22;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC         [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC         COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC         ChEBI:CHEBI:456216; EC=2.7.11.23;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016815; AAS50949.1; -; Genomic_DNA.
DR   RefSeq; NP_983125.1; NM_208478.1.
DR   AlphaFoldDB; Q75D46; -.
DR   SMR; Q75D46; -.
DR   STRING; 33169.AAS50949; -.
DR   EnsemblFungi; AAS50949; AAS50949; AGOS_ABR177C.
DR   GeneID; 4619235; -.
DR   KEGG; ago:AGOS_ABR177C; -.
DR   eggNOG; KOG0600; Eukaryota.
DR   HOGENOM; CLU_000288_167_1_1; -.
DR   InParanoid; Q75D46; -.
DR   OMA; LEARIYG; -.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR   GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR   GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IEA:EnsemblFungi.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..753
FT                   /note="Serine/threonine-protein kinase BUR1"
FT                   /id="PRO_0000085677"
FT   DOMAIN          56..372
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          404..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..506
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..635
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..693
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..745
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         62..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   753 AA;  84823 MW;  8F60C0B2E803FFF0 CRC64;
     MSQEGSAKRA DFKYKIGKIK HTPPVLKDVR SGLEFIELEK RDDEKVYGVT KFLGNYKEEK
     KLGQGTFGEV YRGVHLATQR QVAMKKILVK TENDLFPITA QREITILKRL NHRNVVQLIE
     MVYDYPPAQN GAAYGQDSSQ ASASADTMKS FYMILPYMVA DLSGILHNPR VTLEMADIKN
     MMLQILEGIN YIHCKKFMHR DIKTANILLD HKGILKIADF GLARNYYGAP PNLKYPGGAG
     TDAKYTSVVV TRWYRAPELV LGDKNYTTAV DIWGIGCVFA EFFEKRPILQ GKTDIDQGHV
     IFKLMGTPSD SDWQLARYLP GAELTRTSYE PTYKERFGKY LTEKGLDLLS TLLSLDPYKR
     LTAMAAMQHP FFSEDPLPKL QLTLPCEESH ETDIARYGQE MQKTVSNLPP AAPSGHAVEQ
     SQTQQQSSRH HQSQPYQSLP PQKSSQPHPQ QIPEAAPVQQ PSQQPPQEPS AHQQQYSSRG
     PQQHRTTPAP TSLPPKPKPA PPGARYNREA PPQNKPVKPL TRHLGAQYQH NNYGNYYNHW
     QGGERYYETY NDGYPHADRY SDDTHYNGYG YRSRGYQRYD MRREGESRYN QRPYAPQQGA
     AYRPNRRDTY KLVDRTGQPY PPERVPNPEL HPSPAPRPKR TLTNTTQLSS HSSAATGSTA
     ASGSAVSNSS EPVRRSSTAS LDNSESGNIL QQKPPPPVAN PLEARIYGRD EVQSNHPGGR
     LYPRSTPDSK NSEGAAPSEA STDPTKRNIV DYY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024