ID A0A0L6V9L4_9BASI Unreviewed; 668 AA.
AC A0A0L6V9L4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 02-APR-2025, entry version 31.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=VP01_2158g5 {ECO:0000313|EMBL:KNZ57443.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ57443.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ57443.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ57443.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) 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:KNZ57443.1}.
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DR EMBL; LAVV01007012; KNZ57443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6V9L4; -.
DR STRING; 27349.A0A0L6V9L4; -.
DR VEuPathDB; FungiDB:VP01_2158g5; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000037035; 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 InterPro; IPR001357; BRCT_dom.
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 PANTHER; PTHR15375; ACTIVATOR OF S-PHASE KINASE-RELATED; 1.
DR PANTHER; PTHR15375:SF26; PROTEIN CHIFFON; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF22437; DBF4_BRCT; 1.
DR Pfam; PF08630; Dfp1_Him1_M; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR PROSITE; PS51265; ZF_DBF4; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00600};
KW Reference proteome {ECO:0000313|Proteomes:UP000037035};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00600};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00600}.
FT DOMAIN 643..668
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..481
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 75674 MW; 17A0A450510EDE5F CRC64;
MPSLNPNGKR PQIEQHRNPL DPLINNLTKR LKTSLNQQQT NDFLNNKHSI TNSSFINPIT
TNTNLSNQRS TIKKSLSSLI LPLPNQSSNT PLDLLNPSNN HSPTLRPIRL PRTTHPHHHT
LANNIQKDPR ANSKEKQPPT TTKGKDDLKR EMAQWQEKYR VAIKSFVFYL DRLDPSTSAD
LKTKIRAWGA RVDQFFSKDV THIITDIPVP TNIPQPSPSP RKRNSAYSLP SPTRSNKENG
QQILTGILKN SKRLSVACSP EKEDSTDATP YIHPLIRKAL ELKIKIWKTE KLLNVLYRLG
DQRSPVKQQL SIKPSLPSLL LKEAQQGHTN EFDPVALRSD YYYFGPKAMF IMVEDTTQEH
KPIIVKEYSR PKTRESASWP IMWGGTEGKS AFSRHTAKQT YLHVRNRIRQ MFEMRAREMA
RQAKLSTAHE PSQSPERAPS RKQLVDRTPP PAKQQQNLRR ANITTYQPED ATEPGPEEEE
CREIDHVNKI APEHYRGHGR VFLAASGNSV TMTSNVASAT STRSSVIRPG QIGRQLVDKR
LAALGKRPTF EINQPNLTGV GSSSLKREIG AESSKDRLQT LRQELNVSHN KLKRSQSLDS
SLIAKKKAAD DSKAKSRRNG LGVRAKLGNG FELIDLKKLA RNEEPKAGYC ENCRLKYTDF
RKLIAKER
//
