ID W4K5G0_HETIT Unreviewed; 633 AA.
AC W4K5G0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 18-JUN-2025, entry version 43.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=HETIRDRAFT_476839 {ECO:0000313|EMBL:ETW81047.1};
OS Heterobasidion irregulare (strain TC 32-1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Bondarzewiaceae; Heterobasidion;
OC Heterobasidion annosum species complex.
OX NCBI_TaxID=747525 {ECO:0000313|EMBL:ETW81047.1, ECO:0000313|Proteomes:UP000030671};
RN [1] {ECO:0000313|EMBL:ETW81047.1, ECO:0000313|Proteomes:UP000030671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC 32-1 {ECO:0000313|EMBL:ETW81047.1,
RC ECO:0000313|Proteomes:UP000030671};
RX PubMed=22463738; DOI=10.1111/j.1469-8137.2012.04128.x;
RA Olson A., Aerts A., Asiegbu F., Belbahri L., Bouzid O., Broberg A.,
RA Canback B., Coutinho P.M., Cullen D., Dalman K., Deflorio G.,
RA van Diepen L.T., Dunand C., Duplessis S., Durling M., Gonthier P.,
RA Grimwood J., Fossdal C.G., Hansson D., Henrissat B., Hietala A.,
RA Himmelstrand K., Hoffmeister D., Hogberg N., James T.Y., Karlsson M.,
RA Kohler A., Kues U., Lee Y.H., Lin Y.C., Lind M., Lindquist E., Lombard V.,
RA Lucas S., Lunden K., Morin E., Murat C., Park J., Raffaello T., Rouze P.,
RA Salamov A., Schmutz J., Solheim H., Stahlberg J., Velez H., de Vries R.P.,
RA Wiebenga A., Woodward S., Yakovlev I., Garbelotto M., Martin F.,
RA Grigoriev I.V., Stenlid J.;
RT "Insight into trade-off between wood decay and parasitism from the genome
RT of a fungal forest pathogen.";
RL New Phytol. 194:1001-1013(2012).
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DR EMBL; KI925459; ETW81047.1; -; Genomic_DNA.
DR RefSeq; XP_009547727.1; XM_009549432.1.
DR AlphaFoldDB; W4K5G0; -.
DR FunCoup; W4K5G0; 87.
DR STRING; 747525.W4K5G0; -.
DR GeneID; 20677716; -.
DR KEGG; hir:HETIRDRAFT_476839; -.
DR eggNOG; KOG4139; Eukaryota.
DR HOGENOM; CLU_017715_1_0_1; -.
DR InParanoid; W4K5G0; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000030671; 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 FunFam; 6.10.250.3410:FF:000001; Protein DBF4 homolog A; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
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 PROSITE; PS51265; ZF_DBF4; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030671};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 508..557
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..37
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..355
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..633
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 71635 MW; CF86BC4D7D79766E CRC64;
MTTLLRRPAL TPRTLPQLPT VVSPLQARSK ASTSTSSKRP RSPDPMFDNQ SNSVKRLRAT
PPQTASRDDD PKNKDRRRAE REAQNEEFKT KYTRAFPTFV FYVDWDADAE GQAVKERLCA
RVLHMGAQID DFFSNAITHF ITNKPIPSDD LGANKENMSR SRLRTSRTPS LLKSPIRLKG
RVTDDVPYDN LVRKAISFGM KVWSITKLES VLDRCQAPGA PAAAAASSAA LSNQRSLSRA
LRLEQLNGTT ERDPQQKQYK FRYFSKNSYF VLVEDLKQEL ATIHSMEYRI TKKPDGSEQV
SWPVLHCHPK ARGPFIEYDE REARRAAKLE KQDKEREEER RRRKAKLRER ERRRRAHEEA
QAQMQAKRSG DLRRTVSMVN LYRRVQEEDA ANGLIDLDAE LCDTMDSANA SGYLQSGTYM
AASGNSVSIT STTGTTSTAG HQLRSVQLPA GLRERLQQQV VTSRRVTLGP AAQNRKIGDM
GPPVGIPERK PLRKSKSTNT MKLPEREEGS KPGYCECCRT KFLSFSEHIK SVKHRNFAAN
DNNFLQLDDV LARVRRQTCQ ETEAAKDREA AMRGDVGDHE YSPSRSESEE VEVDRNVRTV
SSSEGDLLPP PQVQENEEYD SEADAEGEDD DEL
//
