ID A0A2T3B6P1_AMORE Unreviewed; 677 AA.
AC A0A2T3B6P1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=M430DRAFT_98957 {ECO:0000313|EMBL:PSS22403.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS22403.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS22403.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS22403.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(2018).
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DR EMBL; KZ679009; PSS22403.1; -; Genomic_DNA.
DR RefSeq; XP_024722558.1; XM_024870156.1.
DR AlphaFoldDB; A0A2T3B6P1; -.
DR STRING; 857342.A0A2T3B6P1; -.
DR GeneID; 36578237; -.
DR InParanoid; A0A2T3B6P1; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000241818; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000241818};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 620..669
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 390..417
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..70
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 75825 MW; 2D90636D8FBDBF58 CRC64;
MSTRRVPLSS NPNAVNSPYR ALTATAAASK PKRSHATVQR EDSYGGQPPA KKQMLESQLR
TPPRQQPTQP SAEGRLFTRK SNATQPTAFE RKCVAASQKP SQPAAVTKVD KVSDEGLESI
RQWQKHIKRI FPKFVFYFES VSEEARLKCT RQVIALGARE EKFFSNAVTH VVTTRAIPPE
HDPNSVPPSN TNDSELQNGQ PQTINPSLLD RTSEVANAQS DLLAAKGKFT FEVPLNRRLA
PQGHDGEIKR QRGRNADVLY RARELGMKIW ALEKLQRMMN TMFDTDTGYQ ATHGHNTRSN
SVGIAAIPRT SREADLSQLL RNERLNGPSD RDPTVATKEL NIFKGPFIYI HDIDEKQRPI
MVREYAKVAH KEDGDWPQFR SVANGKCPFV EEVDYSRREA EKERERLRLQ RQQEKERSMV
PRTRAAAAIE AAAMQPPKIA GTKRALAEVD DGSNRTVTVL SKQSNPFDTA RNPFSAEPSS
RGTQNAFVSR AAAGRLFGGE PVASGLQQSN VTSAIRSQMI SSTAAQPGAK AGTSKEVHGL
QRKVLEKNSG GPASYGGLAS SHRMTDISTA AREELAARPD KRKERLDLIE EDPSEREENA
RKAENTRKAR AVQQRKLEKR DPKPGYCENC QDKFEDFDEH ILSRKHRKFA EKPENWRELD
ALLNQLARPL REAQEGY
//
