DBF2_CANAL
ID DBF2_CANAL Reviewed; 710 AA.
AC Q59KM8; A0A1D8PHQ1;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cell cycle protein kinase DBF2;
DE EC=2.7.11.1;
DE AltName: Full=Dumbbell forming protein 2;
GN Name=DBF2; OrderedLocusNames=CAALFM_C206670CA;
GN ORFNames=CaO19.1223, CaO19.8809;
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 [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 [2]
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 [3]
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).
RN [4]
RP INDUCTION.
RX PubMed=19477921; DOI=10.1091/mbc.e09-03-0210;
RA Cote P., Hogues H., Whiteway M.;
RT "Transcriptional analysis of the Candida albicans cell cycle.";
RL Mol. Biol. Cell 20:3363-3373(2009).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=19460099; DOI=10.1111/j.1365-2958.2009.06729.x;
RA Gonzalez-Novo A., Labrador L., Pablo-Hernando M.E., Correa-Bordes J.,
RA Sanchez M., Jimenez J., Vazquez de Aldana C.R.;
RT "Dbf2 is essential for cytokinesis and correct mitotic spindle formation in
RT Candida albicans.";
RL Mol. Microbiol. 72:1364-1378(2009).
CC -!- FUNCTION: Ser/Thr-protein kinase involved in the mitotic exit network
CC (MEN) and required after the metaphase to anaphase cell cycle
CC transition. Required for proper nuclear segregation, mitotic spindle
CC organization, actomyosin ring contraction, primary septum assembly, and
CC normal hyphal morphogenesis. {ECO:0000269|PubMed:19460099}.
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=2.7.11.1;
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=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:19460099}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:19460099}. Nucleus
CC {ECO:0000269|PubMed:19460099}. Bud neck {ECO:0000269|PubMed:19460099}.
CC Note=In small unbudded G1 cells, localizes to the spindle pole body
CC (SPB). At the G1/S transition, remains associated with the SPB but also
CC starts to accumulate in a linear structure in the nuclei of the cells.
CC During mitosis, a very faint signal along the mother-bud axis is
CC observed, suggesting association with the mitotic spindle during this
CC part of the cell cycle. Finally, localizes to the bud neck at the end
CC of mitosis and cytokinesis.
CC -!- INDUCTION: Cell cycle-regulated with a peak during M/G1.
CC {ECO:0000269|PubMed:19477921}.
CC -!- DISRUPTION PHENOTYPE: Leads to inviable cells.
CC {ECO:0000269|PubMed:19460099}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; CP017624; AOW27668.1; -; Genomic_DNA.
DR RefSeq; XP_710294.2; XM_705202.2.
DR AlphaFoldDB; Q59KM8; -.
DR SMR; Q59KM8; -.
DR BioGRID; 1231186; 1.
DR STRING; 237561.Q59KM8; -.
DR PRIDE; Q59KM8; -.
DR GeneID; 3648101; -.
DR KEGG; cal:CAALFM_C206670CA; -.
DR CGD; CAL0000197161; DBF2.
DR VEuPathDB; FungiDB:C2_06670C_A; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000288_67_4_1; -.
DR InParanoid; Q59KM8; -.
DR OrthoDB; 759391at2759; -.
DR PRO; PR:Q59KM8; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IEA:EnsemblFungi.
DR GO; GO:0044732; C:mitotic spindle pole body; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0034973; C:Sid2-Mob1 complex; IEA:EnsemblFungi.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005816; C:spindle pole body; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0061163; P:endoplasmic reticulum polarization; IEA:EnsemblFungi.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:2000250; P:negative regulation of actin cytoskeleton reorganization; IEA:EnsemblFungi.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:EnsemblFungi.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:1903473; P:positive regulation of mitotic actomyosin contractile ring contraction; IEA:EnsemblFungi.
DR GO; GO:1902846; P:positive regulation of mitotic spindle elongation; IEA:EnsemblFungi.
DR GO; GO:1902854; P:positive regulation of nuclear migration during mitotic telophase; IEA:EnsemblFungi.
DR GO; GO:1905758; P:positive regulation of primary cell septum biogenesis; IEA:EnsemblFungi.
DR GO; GO:0031028; P:septation initiation signaling; IEA:EnsemblFungi.
DR InterPro; IPR000961; AGC-kinase_C.
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; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..710
FT /note="Cell cycle protein kinase DBF2"
FT /id="PRO_0000425151"
FT DOMAIN 240..557
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 559..658
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 246..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 696..703
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 710 AA; 82356 MW; B7FAE0C61BCBD306 CRC64;
MTNFFNRSPK HQSHHYQPHQ QDVTDISYSM ENVSISSNAM MDIDTSYRSS KPTYNNPQQQ
QQQQQQQQAQ NNLFNKENIT PLNSPTKSIL HNSPQQAKSS TSPQHLYNKL VNANYNGNSP
QPGIQQQQNN RALQNNINQL QPPLNKRYKL TEAEFYAKAN SARTKRLTSI AQLYFLDYYC
DMFDYVINRR ERTAIVEKNL LTDPMYKNDI TKQQFEWKNY IGRERALLRK RRLKPKHKDF
EMITQIGQGG YGQVFLSRKR DTREICALKI LNKKLLIKLD ETRHVLTERD ILTNTRSDWL
VKLLYAFQDQ EKVFLAMEFV PGGDFRTLLN NTGYLIPPHA RFYISEMFAA VNSLHELGFT
HRDLKPENFL IDSKGHIKLT DFGLAAGTVC NDRIESMKIK LQNLQNLNDF NDDSNNDNHH
YQVPSSLIYE RQKIFKQSQQ QQQQQNSNNT TANSIVGSPD YMALEVLEGK NYNYTIDYWS
LGCMLFEALC GYPPFSGSKQ DETYYNLKHW KTALRRPQTK DGRYVFSDRT WNLIIKLIAS
PNNRLQNFKQ VQQQSYFSDI KDWGNLRQKT PPFTPQLDNE EDAGYFDDFE DDEMMMKYKD
VFARQEQNEQ LLEKSNTTTT TTTTTTTKNG KRFSPGSKFN DNFIGFTFKH KSNPNNKFTN
GSGNTGRYGN GNGNNNNNGE INLLNMVENG NGIGNGNSRS SRLNPLATLY
