BUR1_CANAL
ID BUR1_CANAL Reviewed; 745 AA.
AC Q9Y7W4; A0A1D8PH82; Q59ZJ5; Q59ZJ6; Q59ZR0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Serine/threonine-protein kinase BUR1;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
GN Name=CRK1; Synonyms=BUR1; OrderedLocusNames=CAALFM_C204930CA;
GN ORFNames=CaO19.11006, CaO19.3523/3524;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11073971; DOI=10.1128/mcb.20.23.8696-8708.2000;
RA Chen J., Zhou S., Wang Q., Chen X., Pan T., Liu H.;
RT "Crk1, a novel Cdc2-related protein kinase, is required for hyphal
RT development and virulence in Candida albicans.";
RL Mol. Cell. Biol. 20:8696-8708(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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). Required for pseudohyphal growth
CC and virulence in mice. {ECO:0000250, ECO:0000269|PubMed:11073971}.
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; U92261; AAD25159.1; -; Genomic_DNA.
DR EMBL; CP017624; AOW27512.1; -; Genomic_DNA.
DR RefSeq; XP_714883.2; XM_709790.2.
DR AlphaFoldDB; Q9Y7W4; -.
DR SMR; Q9Y7W4; -.
DR BioGRID; 1226444; 3.
DR IntAct; Q9Y7W4; 2.
DR MINT; Q9Y7W4; -.
DR STRING; 237561.Q9Y7W4; -.
DR PRIDE; Q9Y7W4; -.
DR GeneID; 3643414; -.
DR KEGG; cal:CAALFM_C204930CA; -.
DR CGD; CAL0000191033; CRK1.
DR VEuPathDB; FungiDB:C2_04930C_A; -.
DR eggNOG; KOG0600; Eukaryota.
DR HOGENOM; CLU_000288_181_21_1; -.
DR InParanoid; Q9Y7W4; -.
DR OrthoDB; 925637at2759; -.
DR PHI-base; PHI:172; -.
DR PRO; PR:Q9Y7W4; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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..745
FT /note="Serine/threonine-protein kinase BUR1"
FT /id="PRO_0000085679"
FT DOMAIN 44..349
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 50..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 249..250
FT /note="LW -> QR (in Ref. 1; AAD25159)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="G -> GG (in Ref. 1; AAD25159)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="A -> G (in Ref. 1; AAD25159)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="K -> Q (in Ref. 1; AAD25159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 745 AA; 83339 MW; 8D0006B955C239FB CRC64;
MSVIAGHHVP RSNDQRQYDT PSVPINIAPD SEGHIHEMSR LKDYEVIEKL GQGTFGVVQK
AKSKKDGSLV AIKQLINHSA KEGFPITAMR EITILKQLNH KNILTIQDMI FEEPKMSNRT
DIITMRGSFY TVTPYMSSDL VGLLENPKIK LELGQIKCIM QQLLKGIQYV HNQKFLHRDI
KAANILIGQD GVLKIADFGL ARIYHGNVPR LGMGPGGGEK AYTGLVVTRW YRPPEILLGE
RKYTTAVDLW GIGCVFAELF TGKPILVGKS DSHQAQIVFE LVGSPLTWTD AAKLPNKNEY
SCGLACKRSL EAKFASIMPT EAIDLLSGLL TLDPFKRLNA LDALNHKFFS TDPLPLLPTQ
MPKFEESHEI DKERFKKLKD KEQAVSELKP PTEIRYDNHS ESRYNADHST FGGGVGGKET
SFSSGKSDYI DHYEPRARRD HYEPRIRNDN KDSNDVRGEF ESATRQEQRR RDIQNRLDAG
GMDTYIPKTT TAKLREHSGT ESLSKKYDNY QPINVSRGSK SPSPSKLSSI SQSKADLISK
PSAPKVASRE SSLERKQVSN GIRTTTDVEP PRARARRPTD MFGRPLTSNS TQAQPTRNKS
VERPKDLEKP TNGVTEDRNK KPVLEEKKEV VKPNLAIPKI KKSSSLVSLS SRSSTTPVIS
NPSKVTKRAA SSVTPPVLPK KPKISKTSSE SEVSDLEEDS DFTGENATVF ERFMALEQLQ
KSPVYKRIIN EKMRFEKLSG GHKSM
