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Database: UniProt
Entry: A0A8H7UDC6_MORIS
LinkDB: A0A8H7UDC6_MORIS
Original site: A0A8H7UDC6_MORIS 
ID   A0A8H7UDC6_MORIS        Unreviewed;       540 AA.
AC   A0A8H7UDC6;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 16.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=INT43_001651 {ECO:0000313|EMBL:KAG2178805.1};
OS   Mortierella isabellina (Filamentous fungus) (Umbelopsis isabellina).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Umbelopsidomycetes; Umbelopsidales; Umbelopsidaceae; Umbelopsis.
OX   NCBI_TaxID=91625 {ECO:0000313|EMBL:KAG2178805.1, ECO:0000313|Proteomes:UP000654370};
RN   [1] {ECO:0000313|EMBL:KAG2178805.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WA0000067209 {ECO:0000313|EMBL:KAG2178805.1};
RA   Muszewska A., Okrasinska A., Steczkiewicz K., Drgas O., Orlowska M.,
RA   Perlinska-Lenart U., Aleksandrzak-Piekarczyk T., Szatraj K.,
RA   Zielenkiewicz U., Pilsyk S., Malc E., Mieczkowski P., Kruszewska J.S.,
RA   Biernat P., Pawlowska J.;
RT   "Metabolic potential, ecology and presence of endohyphal bacteria is
RT   reflected in genomic diversity of Mucoromycotina.";
RL   Submitted (DEC-2020) 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:KAG2178805.1}.
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DR   EMBL; JAEPQZ010000007; KAG2178805.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8H7UDC6; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000654370; 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   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 6.10.250.3410; DBF zinc finger; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
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; PF00533; 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; PS50172; BRCT; 1.
DR   PROSITE; PS51265; ZF_DBF4; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000654370};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          82..130
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          441..488
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          253..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..443
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..519
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   540 AA;  61298 MW;  1CC16EE061F45C97 CRC64;
     MESSAKTSNT VFQSRCNRTP LSQLNKVDSV WRESRTYARS AIQALELKKQ QQQQENMQRH
     SRNTAGAATK PVLLADERWA RAYIKAFPSF KFYFDGIEDL TRRRLEEKVK ILGATVEQFF
     SAKCTHIVTG RPVPEESKPL AQKKPENASR DGDIFEIAHK HKIKIWSVDK LQNRILPILF
     DNLKHHELPN DHLQHRPKPQ ELPRMLQQEK VFGPSTSKRG EHHGPNFVRF NGHFIFVEDV
     TGSYRPIVVK EYPPCDDPNK HTPAWPTLRK NKGNKSPFVR EGHSDNRQDD GQVAKKEEKP
     VEVTQQLRPK TELPAARPNL KPAMSLRALN NEQVEKLEVH NSGFAESKAS LGTPSLNASG
     MHQFGTSRVV STSGSAVHGL PQPLPPGENI NRLDRRTITN IKANDSPLAV HNKAKADAQV
     NAQAAIPQAS KRQKGVLGKK RPPPKNFCEN CRQRFYDLKE AKPRHREYAS NAENFADLDK
     IIELTRRRYK PNLPSVKAVS RSEVIDGPLP EDEIPDTQEP EPSSTFVVDD SWEKFADIVW
//
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