ID BUR1_EREGS Reviewed; 753 AA.
AC Q75D46;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 123.
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 Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS Y-1056) (Yeast) (Ashbya 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}.
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DR EMBL; AE016815; AAS50949.1; -; Genomic_DNA.
DR RefSeq; NP_983125.1; NM_208478.1.
DR AlphaFoldDB; Q75D46; -.
DR SMR; Q75D46; -.
DR STRING; 284811.Q75D46; -.
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 OrthoDB; 10753at2759; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR PANTHER; PTHR24056:SF584; SERINE_THREONINE-PROTEIN KINASE BUR1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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
//
