BUR1_CANGA
ID BUR1_CANGA Reviewed; 667 AA.
AC Q6FQ83;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serine/threonine-protein kinase BUR1;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
GN Name=BUR1; OrderedLocusNames=CAGL0I08349g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380955; CAG60548.1; -; Genomic_DNA.
DR RefSeq; XP_447611.1; XM_447611.1.
DR AlphaFoldDB; Q6FQ83; -.
DR SMR; Q6FQ83; -.
DR STRING; 5478.XP_447611.1; -.
DR EnsemblFungi; CAG60548; CAG60548; CAGL0I08349g.
DR GeneID; 2889404; -.
DR KEGG; cgr:CAGL0I08349g; -.
DR CGD; CAL0132354; CAGL0I08349g.
DR VEuPathDB; FungiDB:CAGL0I08349g; -.
DR eggNOG; KOG0600; Eukaryota.
DR HOGENOM; CLU_000288_167_0_1; -.
DR InParanoid; Q6FQ83; -.
DR OMA; DINAPER; -.
DR Proteomes; UP000002428; Chromosome I.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
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..667
FT /note="Serine/threonine-protein kinase BUR1"
FT /id="PRO_0000085680"
FT DOMAIN 60..378
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 408..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 66..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 667 AA; 75961 MW; 2D5D6197E6CAC4F6 CRC64;
MSQENSNVPA LKRTESKYKI GRVKSLPTVQ IDEKTGDSYI ELAPRSEGKI YGCTTFQGNY
KEEEKLGQGT FGEVYKGLHL QTQRKVAMKR IIVNQENDLF PITAQREITI LKRLNHKNII
KLLEMVYDFP PESNNKDYAQ FNQNNSANPP AVPKKFFYMI LPYMVADLSG ILHNPRIELK
MADIKNMMKQ ILEGVNFIHC SKFMHRDIKT ANLLIDHNGV LKLADFGLAR QYYGSPPNIK
FPGSAGSGAK YTSVVVTRWY RAPELVLGDK YYTTAVDIWG VGCVFAEFFE KKPILQGKTD
IDQGHVIFKL MGTPDERTWE LAKYLPGAEL TKTEYKSTID ERFGKHLTPT GLSFLKGLLA
LDPYKRLTAM SAMKHPFFQE EPLAADRLTL PCEESHEADI KRYKEELHEA MSQKGPSAPP
GHIKEATPSP AKFEKKSGIK REQPYQSNQK NDQYPIKRQK FNQNPSVPHP QPKANRYGGS
SLPSGPKYGR YEGNNHSGSL RNRITPSNMG THSNPRAENM GSKPYQSEGR YSSNEDRKNG
YNRGYSSSVN SRYNNRAAFN ETEDQSITTT TLNRYRHKGY HDNNQSQTRL QGHSSLPGKP
TSKYNSTQTN IPYRRTEIPN PNEYNASKLG SQDTKKNDYP KHSETQKQQN NEEKKIHSEQ
KDIADLY
