DBF4A_CRIGR
ID DBF4A_CRIGR Reviewed; 676 AA.
AC Q99MU0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein DBF4 homolog A;
DE AltName: Full=ChDBF4;
GN Name=DBF4; Synonyms=DBF4A;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=11250080; DOI=10.1016/s0378-1119(01)00332-8;
RA Guo B., Lee H.;
RT "Cloning and characterization of Chinese hamster homologue of yeast DBF4
RT (ChDBF4).";
RL Gene 264:249-256(2001).
CC -!- FUNCTION: Regulatory subunit for CDC7 which activates its kinase
CC activity thereby playing a central role in DNA replication and cell
CC proliferation. Required for progression of S phase. The complex CDC7-
CC DBF4A selectively phosphorylates MCM2 subunit at 'Ser-40' and 'Ser-53'
CC and then is involved in regulating the initiation of DNA replication
CC during cell cycle (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with CDC7. Note that CDC7 forms distinct
CC complex either with DBF4A or DBF4B. Such complexes are stable upon
CC replication stress. Interacts with MEN1, MCM2, ORC2, ORC4 and ORC6 (By
CC similarity). Interacts (via IBM motifs) with PSIP1 (via IBD domain);
CC phosphorylation increases its affinity for PSIP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBU7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11250080}.
CC -!- INDUCTION: Up-regulated when cells reaches the G(1)/S boundary. Down-
CC regulated by gamma-irradiation. {ECO:0000269|PubMed:11250080}.
CC -!- PTM: Phosphorylation increases its interaction with PSIP1.
CC {ECO:0000250|UniProtKB:Q9UBU7}.
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DR EMBL; AF292400; AAK21856.1; -; mRNA.
DR RefSeq; NP_001233700.1; NM_001246771.1.
DR AlphaFoldDB; Q99MU0; -.
DR SMR; Q99MU0; -.
DR STRING; 10029.NP_001233700.1; -.
DR PRIDE; Q99MU0; -.
DR GeneID; 100689339; -.
DR KEGG; cge:100689339; -.
DR CTD; 10926; -.
DR eggNOG; KOG4139; Eukaryota.
DR OrthoDB; 615385at2759; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 6.10.250.3410; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR006572; Znf_DBF.
DR InterPro; IPR038545; Znf_DBF_sf.
DR Pfam; PF07535; zf-DBF; 1.
DR SMART; SM00586; ZnF_DBF; 1.
DR PROSITE; PS51265; ZF_DBF4; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; DNA replication; Metal-binding; Nucleus; Phosphoprotein;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..676
FT /note="Protein DBF4 homolog A"
FT /id="PRO_0000234060"
FT DOMAIN 40..128
FT /note="BRCT 1"
FT DOMAIN 154..179
FT /note="BRCT 2"
FT ZN_FING 289..337
FT /note="DBF4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 616..640
FT /note="Integrase domain-binding motif 1 (IBM1)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU7"
FT MOTIF 657..676
FT /note="Integrase domain-binding motif 2 (IBM2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU7"
FT COMPBIAS 26..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU7"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU7"
FT MOD_RES 345
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU7"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU7"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU7"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU7"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU7"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU7"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU7"
SQ SEQUENCE 676 AA; 75850 MW; EC7EEBDD80D40B8C CRC64;
MNSGAMRIHS KGHFQGGIQV KNEKNRPSLK SLKTDNRPEK SKCKPLWEKV FYLDLPSVTI
SEKLQKDIKD LGGRVEEFLS KDISYLVSNK KEAKYAQTLG QVSPVPSPES AYTAETTSPH
PSHDGSSFKS PDRVCLSRGK LLAEKAVKDH DFIPANSILS NALTWGVKIL HIDDIRYYIE
QKKKELCSLK KSSTSVRDSG KKAGTTIQKA RTGRLKKPFL KVEDVNRSYR PFYLQLTSVP
SINYATHKPC SPFDIEKPSS VQKQAQPKPR PNTDGDKCGG TPVQLQLKEK RKKGYCECCL
QKYEDLETHL LSEKHKNFAQ SNQYQVVDDI VSKLVFDFVE YERDTPKKKR IKYSVGSFSS
VSANVLKNTE PKEKLQLEPI FQKDMVESNG QLPEEIFQCE DIQCEDIQKP EQRLVLASEP
MSYSSTGLKG RDEKAASMLN ASEPDIKQKF TQLPPCKNEQ EGILDVSEHK LIINRNDLEQ
RVGDSVGVPR SCVQVSHLSP ENSLPQPKLT ADTTHFSAKD LQEKDLHFVF GHDSDLVTLN
TSKEQLTVKA GTPSCGPQQP NECDTENTDN LPCGKIQRKV RLLLGQKKKN VDPSAELDKK
RTEFLPMCED RTCGSPVQSL LDLFQTSGEK SDFLGFTSYT ENSGLCDVLD VWEDENSSSL
LSTFFSSPSA STFIGF
