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}. 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; 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 //