ID A0A165FL69_XYLHT Unreviewed; 720 AA.
AC A0A165FL69;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 18-JUN-2025, entry version 33.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=L228DRAFT_284177 {ECO:0000313|EMBL:KZF21106.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF21106.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF21106.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF21106.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
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DR EMBL; KV407461; KZF21106.1; -; Genomic_DNA.
DR RefSeq; XP_018186661.1; XM_018336202.1.
DR AlphaFoldDB; A0A165FL69; -.
DR FunCoup; A0A165FL69; 135.
DR STRING; 1328760.A0A165FL69; -.
DR GeneID; 28901339; -.
DR InParanoid; A0A165FL69; -.
DR OMA; DRKHRKF; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000076632; 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:UP000076632};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 667..716
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..52
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..646
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 80292 MW; 377A79D86B612E66 CRC64;
MAAVSVPPSP QALPSTMSSR RVPLANVPNA ANSPYRAVAA AAASKRSRSQ SSVQRELPYG
QAPPAKKLMY ELNPSNSLEA SKQQQLAQSA EGRVFTKRST NSQPTAFERR LVAARDKAVQ
LKTAKNEKIV NENLETIRQW QKHYRKVFPH FTFFFESIPE DIRVKCSKQI KALGAQEEKF
FSKAVTHVVT TRPIPPELDA KTAANLDHTP AVNTAQEDQT RVDQPDQPRT IDPSLLERSS
DATHAQSQAS QLRCKFTFEA PLGRKIPTTL PFQDAHSKKQ QGSSGDVLHR AREMGMKIWA
LEKFQRMMTT LFDTDTGSYP QHTHNTRGNA AATAAGTKLD ALSVLLRNEK LKGPADRDPT
VSTKELIHFR GPFIYIHDME EKNRPIMVRE YPKVAHREDG EWPQFRSVGN GRCPFIHDGS
SKRDREKERA RLREVEAQKR LETAPKTRAV TALEASRQQS AVVETEKRDS NQVEPTDKPT
SKQTPEMPSV KLFEPPKAVP AKRGSLDRVA RESQPTTYSA FGGLNGLSRL HGGEPVASGV
QPSNITSAIR SQMISSTAAA PGAKAGTSKE VQELKRKVLE RNSVPSANSV SSSFRVTDAA
AAAAAAATTR HSRPIPQTRL AKRKPDGIHD ELGDIEEEPT PSEEEEAARR QQGVRKFREP
QRRVERKEPK PGYCENCREK FDDFDEHTFS RRHRRFALSL DNWAELDALL AQLDRPLKGM
//
