ID A0A3D8RM59_9HELO Unreviewed; 682 AA.
AC A0A3D8RM59;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=BP6252_06314 {ECO:0000313|EMBL:RDW75172.1};
OS Coleophoma cylindrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Coleophoma.
OX NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW75172.1, ECO:0000313|Proteomes:UP000256645};
RN [1] {ECO:0000313|EMBL:RDW75172.1, ECO:0000313|Proteomes:UP000256645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP6252 {ECO:0000313|EMBL:RDW75172.1,
RC ECO:0000313|Proteomes:UP000256645};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDW75172.1}.
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DR EMBL; PDLM01000006; RDW75172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8RM59; -.
DR STRING; 1849047.A0A3D8RM59; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000256645; Unassembled WGS sequence.
DR GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IEA:TreeGrafter.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IEA:TreeGrafter.
DR GO; GO:1901987; P:regulation of cell cycle phase transition; IEA:TreeGrafter.
DR CDD; cd00027; BRCT; 1.
DR FunFam; 6.10.250.3410:FF:000001; Protein DBF4 homolog A; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
DR Gene3D; 6.10.250.3410; DBF zinc finger; 1.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR055116; DBF4_BRCT.
DR InterPro; IPR013939; Regulatory_Dfp1/Him1.
DR InterPro; IPR051590; Replication_Regulatory_Kinase.
DR InterPro; IPR006572; Znf_DBF.
DR InterPro; IPR038545; Znf_DBF_sf.
DR PANTHER; PTHR15375; ACTIVATOR OF S-PHASE KINASE-RELATED; 1.
DR PANTHER; PTHR15375:SF26; PROTEIN CHIFFON; 1.
DR Pfam; PF22437; DBF4_BRCT; 1.
DR Pfam; PF08630; Dfp1_Him1_M; 1.
DR Pfam; PF07535; zf-DBF; 1.
DR SMART; SM00586; ZnF_DBF; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR PROSITE; PS51265; ZF_DBF4; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000256645};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 624..673
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 29..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..601
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..621
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 76359 MW; 3D436C233CFA54C1 CRC64;
MSTQRRVPLS SNPNAVNSPF RAVAAAAASK QKRSYATVQR EDSYGQQPPA KKQMLDTHHI
LRTPPRQQST QTTEGRVFTR KSNAPQTAFE KKLTAVGQKP QQTVTRAEKT QEEQLQQIRV
WQRHHRKVFP QYVFYFESIP EESRLRYTKQ VVALGAREAK FFSNEVTHVV TSRAIPPEGR
VLDATSSTID DSHSQGSQPQ TINPTLLDRS SESTSQPDPF GAKGKFTFDV PMSRRLVSQQ
HGGDTRRPQG RNADVLHRAR ELGMKIWSLD KLHRMMSTMF DTDTQLAHGH NTRSNTVHGL
AAVPKASREA DLQQLLRNEK LNGPSDRDPT VVTKEMSLFK GPFLYIHDID EKQKPIMVRE
YAKVAHKEDG DWPQFRSVAN GKCPFVEEVD YGRREAEKES IRQQRHESRE KTKAPRTRAA
TAVEAAMQPP KLVDTKRVLN ETEDASNRTV RVSSKQTNPF DGPRAYPPQV ESVSSSKGPQ
NAFVSRAGTG RLFGGEPLAS GLQASNLTSA IRSQMISSTA AQPGAKAGTS KEVHGLQRKV
LEKNSGGPGS YGQMSSHRMT DLGATAAAAA AANEQANRPS RRRANDQLGL IEEDQDPSEV
EEQARKAEAA RKAKAVQKRR TEKRDPKPGY CENCQDKFED FDEHVVSRKH RKFAEKLENW
TELDSLLNQL VRPLKPYSGS DY
//
