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   27-MAR-2024, entry version 127.
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 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
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; 284593.Q6FQ83; -.
DR   EnsemblFungi; CAGL0I08349g-T; CAGL0I08349g-T-p1; 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; PDERTWE; -.
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: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..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
//