ID W3WY13_PESFW Unreviewed; 666 AA.
AC W3WY13;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 18-JUN-2025, entry version 50.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=PFICI_09833 {ECO:0000313|EMBL:ETS77771.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Amphisphaeriales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS77771.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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DR EMBL; KI912115; ETS77771.1; -; Genomic_DNA.
DR RefSeq; XP_007836605.1; XM_007838414.1.
DR AlphaFoldDB; W3WY13; -.
DR FunCoup; W3WY13; 133.
DR STRING; 1229662.W3WY13; -.
DR GeneID; 19274846; -.
DR KEGG; pfy:PFICI_09833; -.
DR eggNOG; KOG4139; Eukaryota.
DR HOGENOM; CLU_017715_0_0_1; -.
DR InParanoid; W3WY13; -.
DR OMA; GMKIWAI; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000030651; 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; 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:UP000030651};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 598..647
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..577
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 74829 MW; 3E04464AF81C8532 CRC64;
MPHARRVPLS MNPSAANSPI RASGLSKPKR SSASIQREEA YGQPPPAKKQ ILDSGIPRPL
KSPQQQRVAK TQLSLQSRRH ASTYESKLAR ERSGQHHHHA ESASTGKYTE KDLDEIRRWQ
SHHRQKFPKM VFYFDSIPED TRAKLVKQIT SLGAREERFF SSEITHVVTS RPIPPEQRGG
RRADDVDAET HAEQQQPQTI NPSLLDRTAD QSVRRKLFTD ALGDAKSKSQ LSSRSGLAQM
PETRPKRSTD VLSRAREMSK KIWSLDKLNR MLSMLLETDL NVSAAIAYGS RSASVSASHT
HSKATDERSL LQLLQNERVN GPSDRDPTVT TKEMHYFRGP YLYIYDFEEK QKPIMAREYQ
RVQEKSDGDW PQFRTAPLGR CPFIEDYDHH REVVRPKKRE VAKPAIESKL VLQPPEDSQR
HAKPVTGKRS LSEMESAHNR GSSITANLFN PSKSLAGKKF DFGPNPFGSR AATDKLFGGE
PLASGVQPSN ITSAIRSQMI SSTAATPGAI GVVSKEVHGL QRKVLQRNSS HEMTSRRTAS
AGASLKEDTE SKRSTLSRTS SKKLDQIDEQ SAVDENEAGQ SAKASVPAEK RVVKPKKKEP
KPGYCENCQD KFADFDEHIL SRKHRKFADN DDNWGELDDL LDQLAREPKH KSYPTWAPAL
PEFPVY
//
