ID   DBF4A_XENTR             Reviewed;         663 AA.
AC   Q28FY7;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Protein DBF4 homolog A;
GN   Name=dbf4; Synonyms=dbf4a; ORFNames=TGas125n02.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory subunit for cdc7 which activates its kinase
CC       activity thereby playing a central role in DNA replication and cell
CC       proliferation. Not required during the initiation of DNA replication in
CC       egg and during early embryonic development but is required later
CC       throughout development. The complex cdc7-dbf4a phosphorylates mcm2
CC       subunit (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with cdc7. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
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DR   EMBL; CR761670; CAJ83752.1; -; mRNA.
DR   RefSeq; NP_001037970.1; NM_001044505.1.
DR   AlphaFoldDB; Q28FY7; -.
DR   STRING; 8364.ENSXETP00000005307; -.
DR   PaxDb; Q28FY7; -.
DR   Ensembl; ENSXETT00000005307; ENSXETP00000005307; ENSXETG00000002490.
DR   GeneID; 733748; -.
DR   KEGG; xtr:733748; -.
DR   CTD; 10926; -.
DR   Xenbase; XB-GENE-972991; dbf4.
DR   eggNOG; KOG4139; Eukaryota.
DR   HOGENOM; CLU_030726_2_0_1; -.
DR   InParanoid; Q28FY7; -.
DR   OrthoDB; 615385at2759; -.
DR   PhylomeDB; Q28FY7; -.
DR   Reactome; R-XTR-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-XTR-68962; Activation of the pre-replicative complex.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000002490; Expressed in ovary and 12 other tissues.
DR   ExpressionAtlas; Q28FY7; baseline.
DR   GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IBA:GO_Central.
DR   GO; GO:1901987; P:regulation of cell cycle phase transition; IBA:GO_Central.
DR   Gene3D; 6.10.250.3410; -; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR006572; Znf_DBF.
DR   InterPro; IPR038545; Znf_DBF_sf.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF07535; zf-DBF; 1.
DR   SMART; SM00586; ZnF_DBF; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS51265; ZF_DBF4; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..663
FT                   /note="Protein DBF4 homolog A"
FT                   /id="PRO_0000234063"
FT   DOMAIN          18..111
FT                   /note="BRCT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   DOMAIN          136..161
FT                   /note="BRCT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   ZN_FING         269..317
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   REGION          84..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   BINDING         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   BINDING         289
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
SQ   SEQUENCE   663 AA;  73838 MW;  635DC7D3453A59BB CRC64;
     MKSTVATVKN PTGKVQADIC KPFSGKVFYL DLTSKLISEK LEKDIKELGG TVEGFLSKEI
     SYLITSKKEA KCVKTLKYVC SVPSPEPAQN TGESSTSPGN RRLPQEGNSS KKNEKSLVSR
     GKSLVKKAIK EQEILPKNSI LSNALNWGVK ILHVEEAKRY IEKKKSSLQQ VKKSQPVVKS
     ESKHPARRKV KPQKLKSPYI KVEDCSCQYR PLYLVLPQFR SFQNTTSNYL VEVDKKADVG
     QKLAETKQSI NKTGHVQDGA NNANIKLKEQ KKHGYCECCL KKYDSLESHI LSPQHKNYSE
     SAYYQVVDDL ISTFEFDFVD WSKYKNGRKS VGILMLTEKY KAEGQERNEA SKANTFSERV
     SATTPLQENT LKDPYATSCS VPPTPVCNTD PMFSLPSPVG SAELCNKKYT TDNFEQLVAT
     SVPALCLKDN LPGSLGEREM SVVYNETKQN ETIDHTMERP KIGWDASNIP SNILLYVPQK
     VDAVAQYANV SLKGNIHCSK LTACQAALTY GKMDPAVCDN ITFPKTVNHL HNKEGHRTMD
     QIYPTVQSDE LQSLLPDYSP SGNLHRKLKT SAQTNLADDE LLCRLSHKVS VPQQNDVLNV
     PSETLLAMFE SSEDKTEFFG FAGSCVCDPC SMDDGDNRDQ AHKNLLLSLF SHTTTSGSSF
     LGF