ID A0A178EQ20_TRIRU Unreviewed; 666 AA.
AC A0A178EQ20;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 08-OCT-2025, entry version 31.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=A7C99_6467 {ECO:0000313|EMBL:OAL61896.1};
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL61896.1, ECO:0000313|Proteomes:UP000243015};
RN [1] {ECO:0000313|EMBL:OAL61896.1, ECO:0000313|Proteomes:UP000243015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA Zhan P., Tao Y., Liu W.;
RT "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:OAL61896.1}.
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DR EMBL; LHPM01000019; OAL61896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EQ20; -.
DR VEuPathDB; FungiDB:TERG_03005; -.
DR Proteomes; UP000243015; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 612..661
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..404
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 73995 MW; A6F52E92C74571F7 CRC64;
MTTRRAPLAN VPNATNSPHR AVSTATTATM KRTRPPGLPW DSAAAPPPLK KQVLDTADNV
DARFSQRSLN QHQPQAGESK IFTRRTNTQP TAFEKKLAAV RDKPKQQQNA LKVSRNIKYC
PESVESVRQW QRHYRKVFPS YVFYFESIPE EVRKKYVRQI MSLGATEEKF FSRVVTHVVT
SRSIPPEVES EKHTEAAQSA SAENNMSGSV QTVNPSMLEK GIDAQLGKTR SRTGFSMIEP
ENKKGMGGGS GDLLHRARQM NMKIWTLDKL QRVIFTMNDK ELAHILQPTR NGTAPAKNKT
EDDLSLALQH EKLHAPIDSD SLTLNKGLVP FKGPYLYIWD YNRETRPVVI REYPKVNRKQ
DGAWPQFRSV ELGKCPFVET AGGRKTEKDR QKQQQAKANN TQTTLVTKTM APPARGPSKT
TNQQQQQQQP NMTAANQDDT ESALEDSAGR PIEPMENTAA TTTPTNVGPR PVSKGSISAS
SLPFKFGGEI AASGIQPSNI TSAIRSQMIS STAATQGARA STSKEVHELK RKVLEKSSGM
VSTAISSCHR ADAAAAPQSQ SVRVPIARAA KLKAQANDHG TIQLTERNRG ASDVAPKKQS
GLRKQPAGSK KRDPKPGYCE NCREKFEDYE DHIATRKHRK FASNSINFFE IDAFILGLNQ
NYHRYR
//
