ID   BUR1_DEBHA              Reviewed;         608 AA.
AC   Q6BV06;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Serine/threonine-protein kinase BUR1;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
GN   Name=BUR1; OrderedLocusNames=DEHA2C06358g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968;
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; CR382135; CAG86021.1; -; Genomic_DNA.
DR   RefSeq; XP_457963.1; XM_457963.1.
DR   AlphaFoldDB; Q6BV06; -.
DR   SMR; Q6BV06; -.
DR   STRING; 284592.Q6BV06; -.
DR   GeneID; 2900800; -.
DR   KEGG; dha:DEHA2C06358g; -.
DR   VEuPathDB; FungiDB:DEHA2C06358g; -.
DR   eggNOG; KOG0600; Eukaryota.
DR   HOGENOM; CLU_000288_181_21_1; -.
DR   InParanoid; Q6BV06; -.
DR   OrthoDB; 10753at2759; -.
DR   Proteomes; UP000000599; Chromosome C.
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   CDD; cd07866; STKc_BUR1; 1.
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..608
FT                   /note="Serine/threonine-protein kinase BUR1"
FT                   /id="PRO_0000085681"
FT   DOMAIN          39..346
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          383..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..561
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         45..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   608 AA;  69467 MW;  B27C11E4AAB8D95C CRC64;
     MECPEPSESV IPNDQSTKSC SIKLQPMNRF RDMSKLRNYE IIQKLGQGTF GVVQKARNIK
     TKELVALKQL INHSAKEGFP ITAMREITIL KKLNHKNILK IIDMIYEEPK ISNPQDILHQ
     RGCFYTVSPY MCSDLVGLLE NPNINLEVSH IKCFMEQLLH GIQYIHEQMF LHRDIKAANI
     LIDRNGTLKI ADFGLARVYH GSPPKFMSGP GGGERAYTGL VVTRWYRPPE LLLGERRYTT
     AVDMWGIGCV FGELFTRKPI LVGKTDSHQA QLIFDLVGPP NSISWSEATS LPNKHDLNIG
     LTCQRSLESK FAPLMNPDGI NLLSGLLTLD PYKRFNALDA LNHNYFKNEP LPMKPQELPK
     FEECHEIDKE RFKLLREKKN NIHEANKIPK AHFPKGPGEY NNSNNYPRNR NGSFPLALPK
     QPKFYNQHQQ EAHVPQQMHT DTYIPKKRDD KPGANAPQKE SSEPITSYQS LRDRSPRREG
     HISRKPSTTN SNNISSNSSA SNVGGTLSNP THQKNRPNAK ASAGIFMTNS RKQRPKPNPQ
     SSSRNVSDQF KKRKLLPDEQ NESDLTDFDE DVKDSKQLDS FLDWDTFTRS PENRKLQHEK
     KQFETKYS
//