ID A0A9P8TCB7_9ASCO Unreviewed; 460 AA.
AC A0A9P8TCB7;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=WICMUC_003739 {ECO:0000313|EMBL:KAH3673280.1};
OS Wickerhamomyces mucosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Phaffomycetales; Wickerhamomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1378264 {ECO:0000313|EMBL:KAH3673280.1, ECO:0000313|Proteomes:UP000769528};
RN [1] {ECO:0000313|EMBL:KAH3673280.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS6341 {ECO:0000313|EMBL:KAH3673280.1};
RX PubMed=33906412;
RA Schikora-Tamarit M.A., Marcet-Houben M., Nosek J., Gabaldon T.;
RT "Shared evolutionary footprints suggest mitochondrial oxidative damage
RT underlies multiple complex I losses in fungi.";
RL Open Biol. 11:0-0(2021).
RN [2] {ECO:0000313|EMBL:KAH3673280.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS6341 {ECO:0000313|EMBL:KAH3673280.1};
RA Schikora-Tamarit M.A.;
RL Submitted (JAN-2021) 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:KAH3673280.1}.
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DR EMBL; JAEUBF010001028; KAH3673280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P8TCB7; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000769528; 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:UP000769528};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 406..455
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..299
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 460 AA; 53510 MW; C18B12D9A83F8A14 CRC64;
MENIRQPLRD VNTNSPSVKR QRLSNKASIH TFYNKGEQHN HIQEHQEQQE SQQQIQQQYA
VDKLPFSEWQ RKWRKIMLNS TIYFDGSDSH ANTRDLGKIK EKSKAITLFT RVGAHIQAFF
DSNVTIVITS KPHDELSKNI LAYQQHLKIW DYTKALRFLG NLGETSSSDP NDSLSQLLQN
EKVFGANDRD PNAKRDDFYY FKHPYFFVHD LRNVIKPIAI REWKPKEKNE KPWPHLHKSS
YGHSLFQADP ADAHIQKKVD RRRLRYEQQR PYRERLREVY DKDKVSESSS PSSCELSSPQ
EDTIYDVSNI TKAMPPPPPK FTLSRQASTL NNKYIEAQKR DCFEIEASGY NGSTNVSQRS
TEFQTKNGLA PAVSSVASKQ VSSLTKRIIE KRQKLQTTND SNSNVKPKVS GYCENCRIGF
EDFDEHIVSG RHRSFAEDDG QFRDIDDLIK RLKQDIQNKR
//
