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Database: UniProt
Entry: A0A9P8CS66_9HYPO
LinkDB: A0A9P8CS66_9HYPO
Original site: A0A9P8CS66_9HYPO 
ID   A0A9P8CS66_9HYPO        Unreviewed;       649 AA.
AC   A0A9P8CS66;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   28-JAN-2026, entry version 12.
DE   SubName: Full=Dfp1/Him1, central region-domain-containing protein {ECO:0000313|EMBL:KAG9256905.1};
GN   ORFNames=F5Z01DRAFT_492357 {ECO:0000313|EMBL:KAG9256905.1};
OS   Emericellopsis atlantica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Bionectriaceae; Emericellopsis.
OX   NCBI_TaxID=2614577 {ECO:0000313|EMBL:KAG9256905.1, ECO:0000313|Proteomes:UP000887229};
RN   [1] {ECO:0000313|EMBL:KAG9256905.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TS7 {ECO:0000313|EMBL:KAG9256905.1};
RX   PubMed=34372938;
RA   Hagestad O.C., Hou L., Andersen J.H., Hansen E.H., Altermark B., Li C.,
RA   Kuhnert E., Cox R.J., Crous P.W., Spatafora J.W., Lail K., Amirebrahimi M.,
RA   Lipzen A., Pangilinan J., Andreopoulos W., Hayes R.D., Ng V.,
RA   Grigoriev I.V., Jackson S.A., Sutton T.D.S., Dobson A.D.W., Rama T.;
RT   "Genomic characterization of three marine fungi, including Emericellopsis
RT   atlantica sp. nov. with signatures of a generalist lifestyle and marine
RT   biomass degradation.";
RL   IMA Fungus 12:21-21(2021).
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:KAG9256905.1}.
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DR   EMBL; MU251247; KAG9256905.1; -; Genomic_DNA.
DR   RefSeq; XP_046120829.1; XM_046260199.1.
DR   AlphaFoldDB; A0A9P8CS66; -.
DR   GeneID; 70291102; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000887229; 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   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   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:UP000887229};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          588..637
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          16..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..188
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..404
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..421
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..579
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  72224 MW;  7EEF7D20A44B6578 CRC64;
     MATISVSPTP AIAAMASRRG PLTNNPNVAN SPLRVAPAGF AKPKRPYAVL QREEPYGQAP
     PSKKQAVEQR VARSPSKLPR AQALPQRGST TATTSRPVTK ERTQKPAASA KVSLQDEREK
     DAWKKHYRAK FPKMVFYFES IPEDIRAKLT KRITYLGARQ EPFFSIDVTH VITTRAIPTE
     QPETQPEPEV APQDEPALAE QPQTINPSLL DRSSARRKLL LEFRSAPSRS HASADPTKPH
     KPTRNSDVLH KAKDMGKKIW SLEKFWAMVS LLCEAEKPKF DYRGSGTYSN PVPRAAGESA
     HASLNQMLRN ERINGPSDRD VSALSKDLTY FKGPHIYVFD MEERHKPIMV REYAKVSNKM
     DGDWPQFRSV GSGRCPFVEE DPEEKERQKR REQRQLQQEK DDARAAAAKQ AEASKAQAQA
     ALPKPVIGKR TLGEMEDGHN KVRAPATSTI NPAKAALSKQ GSQNAFVSRN EGGRLVHGEP
     VASGVQPSNI TSAIRSQMIS SQAGITGIKA GTSKELHGLQ RQVLQKTGAV SQETSSRRPV
     DNSVEGRSSR SVPSLSRKTS HNGSIPEAHK ATDSRDKRSQ SQAMKSKKDM KPGYCENCQE
     KFRDFDEHIL SRKHRRFAEN PSNWVELDDL LAELTRQPKE FMSSPGYDL
//
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