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Database: UniProt
Entry: A0A162N267_CORDF
LinkDB: A0A162N267_CORDF
Original site: A0A162N267_CORDF 
ID   A0A162N267_CORDF        Unreviewed;       636 AA.
AC   A0A162N267;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   18-JUN-2025, entry version 34.
DE   SubName: Full=Regulatory subunit Dfp1/Him1, central region {ECO:0000313|EMBL:OAA74289.1};
GN   ORFNames=LEL_07870 {ECO:0000313|EMBL:OAA74289.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA74289.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA74289.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA74289.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:OAA74289.1}.
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DR   EMBL; AZHF01000006; OAA74289.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A162N267; -.
DR   STRING; 1081108.A0A162N267; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000076881; 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; 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:UP000076881};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          576..625
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          27..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..578
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   636 AA;  71512 MW;  7F26DDFE0B99E704 CRC64;
     MASRRVPLSN NPNVANSPLR GASALAAYAK QKRSHATIQR EEPYGQAPPA KKQALDNGSA
     RVIRSPSKLP RSQTMSRGTA AAITRPVVRD RQARPGSTSK PHDAENEKEV WKRHHRAKFP
     KMVFYFESIP DDVRAKLIKR VAYLGARQEP FFSIDVTHVV TTRSIPVEKS NTEEADAIDH
     GQGGHAEEQP QTINPSLLLD RPSDARRKLL FEFRQAPMQS QQQDDLIRRS RGVRNNDVLH
     KARDMGKKIW SLDKFQTMLS VLLESEPQQA SYGSRVASAR SQYGANKGAH EPNLLQLLHN
     ERIHGPSDRD PTAMNRELAL FKGPYIYVWD MDEKQKPIMV REYAKVVNKT DGDWPQFRSV
     GNGRCPFVEE LDLPERDHRK TREREKARVV KREEQVTILQ PPENPLPKPV TGKRSLGEME
     DGHNRLRGAS ATEVFNAAKA ALGKQSEMRP QNAFISRADM GRQFAGEPVA SGLQASNITS
     AIRSQMISST SGINGAKAGT SKEVHGLQRK VLQKATPASH DLSSRRVGEI SMDVASSRST
     TMSRQNSKVV ATGEDDSQRA AETRERKPTS QLKSKKDLKP GYCENCQDKF RDFDEHILSR
     KHRKFAENND NWTDLDALLS QLERPPRFAS MDSEEY
//
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