DBF4B_XENLA
ID DBF4B_XENLA Reviewed; 784 AA.
AC Q283Q6; Q7SZM4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Protein DBF4 homolog B;
DE AltName: Full=Dbf4-related factor 1;
DE AltName: Full=XDrf1;
GN Name=dbf4b; Synonyms=drf1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, DEVELOPMENTAL STAGE,
RP AND INTERACTION WITH CDC7.
RX PubMed=16507577; DOI=10.1074/jbc.m510278200;
RA Silva T., Bradley R.H., Gao Y., Coue M.;
RT "Xenopus CDC7/DRF1 complex is required for the initiation of DNA
RT replication.";
RL J. Biol. Chem. 281:11569-11576(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-784, FUNCTION, AND INTERACTION WITH CDC7.
RX PubMed=12897072; DOI=10.1074/jbc.m307144200;
RA Yanow S.K., Gold D.A., Yoo H.Y., Dunphy W.G.;
RT "Xenopus Drf1, a regulator of Cdc7, displays checkpoint-dependent
RT accumulation on chromatin during an S-phase arrest.";
RL J. Biol. Chem. 278:41083-41092(2003).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, DEVELOPMENTAL STAGE, AND
RP INTERACTION WITH CDC7.
RX PubMed=16204181; DOI=10.1101/gad.1339805;
RA Takahashi T.S., Walter J.C.;
RT "Cdc7-Drf1 is a developmentally regulated protein kinase required for the
RT initiation of vertebrate DNA replication.";
RL Genes Dev. 19:2295-2300(2005).
CC -!- FUNCTION: Regulatory subunit for cdc7 which activates its kinase
CC activity thereby playing a central role in DNA replication and cell
CC proliferation. Specifically required during the initiation of DNA
CC replication in egg and during early embryonic development. The complex
CC cdc7-dbf4b phosphorylates mcm2 and mcm4 subunits and is required for
CC cdc45 loading. {ECO:0000269|PubMed:12897072,
CC ECO:0000269|PubMed:16204181, ECO:0000269|PubMed:16507577}.
CC -!- SUBUNIT: Forms a complex with cdc7.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16204181}.
CC Note=Binding of complex to chromatin is dependent on pre-replication
CC complex assembly but is not regulated by ATR checkpoint pathways.
CC -!- DEVELOPMENTAL STAGE: Present early in development. During oogenesis and
CC maturation, low levels are detected in growing oocyte stages V-VI.
CC Expression increases significantly during oocyte maturation. After
CC fertilization, the level decreases slowly until the mid-blastula
CC transition (MBT, stage 8.5). A sharper decrease occurs after MBT. Not
CC detected in embryos past stage 10 of development (at protein level).
CC {ECO:0000269|PubMed:16204181, ECO:0000269|PubMed:16507577}.
CC -!- PTM: Phosphorylated. Stably phosphorylated throughout the cell cycle.
CC {ECO:0000269|PubMed:16204181, ECO:0000269|PubMed:16507577}.
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DR EMBL; DQ205095; ABB16337.1; -; mRNA.
DR EMBL; AY328889; AAQ19270.1; -; mRNA.
DR RefSeq; NP_001082740.1; NM_001089271.1.
DR AlphaFoldDB; Q283Q6; -.
DR BioGRID; 100026; 4.
DR PRIDE; Q283Q6; -.
DR GeneID; 398696; -.
DR KEGG; xla:398696; -.
DR CTD; 398696; -.
DR Xenbase; XB-GENE-5829790; dbf4b.L.
DR OrthoDB; 615385at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 398696; Expressed in egg cell and 9 other tissues.
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 Gene3D; 6.10.250.3410; -; 1.
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 1: Evidence at protein level;
KW Cell cycle; Developmental protein; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..784
FT /note="Protein DBF4 homolog B"
FT /id="PRO_0000317554"
FT DOMAIN 27..117
FT /note="BRCT"
FT ZN_FING 244..293
FT /note="DBF4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT REGION 222..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT CONFLICT 149
FT /note="R -> S (in Ref. 2; AAQ19270)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="K -> M (in Ref. 2; AAQ19270)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="E -> G (in Ref. 2; AAQ19270)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="Q -> E (in Ref. 2; AAQ19270)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="R -> S (in Ref. 2; AAQ19270)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="C -> V (in Ref. 2; AAQ19270)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="K -> R (in Ref. 2; AAQ19270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 784 AA; 85981 MW; D220B1A38CD74561 CRC64;
MASVISVLHG QVMQQDDEPP LAKRRRCREI TFAGKSFYLD VPANRQTQLL TKAIGRLGGI
IESFLSRDVD YVVTGSKKAV ASVSSVATRR GEKSQIQAAE RKEPIHCSRG KQLLKKVVHS
QECNSVLTNA RSWGVTVLYV EDVVSYIERL ERPPSRGIQN KTAEGRAADS TRPSLKIARL
RSPFIKIEDQ SRKFRPLQCT FTSFPELSFV CSDKSPFETV QTVKKKDPGD QEEEEGQRSQ
KPQARKRKGY CECCEETFDT LSEHLVGEHH FRFVSNPLSY KMIDDLAAQL TCDLMELPFG
SPTSPEAERS SQNEDWDLDL APGEAEPAGN EGHELGILKA TRLDKDGHAD CEDQGAPAYL
RDGGAEEPDQ RCGEIPLANI EVDVYNVCSF DQPVVTCTME LPDVSAEGKI HSNLLGSTVG
DERVLQRTNG TCEPHIDLAL GNGRELKHAE LQKDPLTKDS QPELLSTAHE QLPTSAPCML
LEGASVVHFP SHGGTVGSQG DVTSHSAANK PHTENCPVDS TGDRHAQPAG SDALAMSCVI
PTLDNGGRHV DATMQSHWEV PLGCTTDTLL SYSTTVTVGE LGPEAHNPTP EQQPLLISTC
SSITTVCCTD TEFKSCTVSV HSTSHSPPNQ NVKSNQTPSL LEMDLANPNC HRAKRKHWDS
LLSPPGKKPT SPSHCQSLTL PMWLLCQFPN YGQQVQLPVW ADLCKWDGTA AAEEGTVDCS
SSSTLPKLHQ DSFSSESDWD AHLPSFFQNN PQQSLQCGDL RTAQVTLNES WYGKQLCNIL
THDP
