DNB2_ADECR
ID DNB2_ADECR Reviewed; 454 AA.
AC Q96687;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04054};
DE Short=DBP {ECO:0000255|HAMAP-Rule:MF_04054};
DE AltName: Full=Early 2A protein {ECO:0000255|HAMAP-Rule:MF_04054};
DE AltName: Full=Early E2A DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04054};
GN Name=DBP {ECO:0000255|HAMAP-Rule:MF_04054};
OS Canine adenovirus serotype 1 (strain RI261) (CAdV-1) (Canine adenovirus 1
OS (strain RI261)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX NCBI_TaxID=69151;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9129661; DOI=10.1099/0022-1317-78-4-873;
RA Morrison M.D., Onions D.E., Nicolson L.;
RT "Complete DNA sequence of canine adenovirus type 1.";
RL J. Gen. Virol. 78:873-878(1997).
CC -!- FUNCTION: Plays a role in the elongation phase of viral strand
CC displacement replication by unwinding the template in an ATP-
CC independent fashion, employing its capacity to form multimers. Also
CC enhances the rate of initiation. Released from template upon second
CC strand synthesis. Assembles in complex with viral pTP, viral pol, host
CC NFIA and host POU2F1/OCT1 on viral origin of replication. Covers the
CC whole ssDNA genome during synthesis. The complementary strand synthesis
CC induces its relese from DNA template. May inhibit cellular
CC transcription mediated by the interaction between host SRCAP and CBP.
CC {ECO:0000255|HAMAP-Rule:MF_04054}.
CC -!- SUBUNIT: Homomultimerizes on viral ssDNA bound to pTP. Forms a
CC initiation complex with viral polymerase, pTP and hosts NFIA and
CC POU2F1/OCT1. Interacts with host SRCAP. {ECO:0000255|HAMAP-
CC Rule:MF_04054}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04054}.
CC Note=Accumulates in infected cells. {ECO:0000255|HAMAP-Rule:MF_04054}.
CC -!- DOMAIN: The C-terminal arm bridges DBP molecules together, thereby
CC creating a chain. {ECO:0000255|HAMAP-Rule:MF_04054}.
CC -!- SIMILARITY: Belongs to the adenoviridae E2A DNA-binding protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04054}.
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DR EMBL; Y07760; CAA69038.1; -; Genomic_DNA.
DR RefSeq; AP_000061.1; AC_000003.1.
DR RefSeq; NP_044200.1; NC_001734.1.
DR SMR; Q96687; -.
DR GeneID; 1488933; -.
DR KEGG; vg:1488933; -.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0039687; P:viral DNA strand displacement replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.269.10; -; 1.
DR Gene3D; 3.90.148.10; -; 1.
DR HAMAP; MF_04054; ADV_DNB2; 1.
DR InterPro; IPR036367; Ad_DBP_C_sf.
DR InterPro; IPR036368; ADBP_zn-bd_sf.
DR InterPro; IPR003176; Adenovirus_DNA-bd_a.
DR InterPro; IPR036362; Adenovirus_DNA-bd_N_sf.
DR InterPro; IPR005376; Adenovirus_DNA-bd_zn-bd.
DR InterPro; IPR037540; ADV_DNB2.
DR Pfam; PF02236; Viral_DNA_bi; 1.
DR Pfam; PF03728; Viral_DNA_Zn_bi; 2.
DR SUPFAM; SSF47724; SSF47724; 1.
DR SUPFAM; SSF57917; SSF57917; 2.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; Early protein; Host nucleus;
KW Host-virus interaction; Metal-binding; Phosphoprotein;
KW Viral DNA replication; Zinc.
FT CHAIN 1..454
FT /note="DNA-binding protein"
FT /id="PRO_0000221685"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..260
FT /note="Flexible loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT REGION 440..454
FT /note="C-terminal arm, DBP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT MOD_RES 129
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
SQ SEQUENCE 454 AA; 50294 MW; 50D95E4995BDF38C CRC64;
MSHKKVVAIS ESSSDEEVPV APPTAPPKKR QRKAVEEPRG HQAMVEIARQ ATAALKARGD
PGSIIVQTFC DQTVDVDKEG NVIFTPAKQK SICNKSGSPL ASVASKIFKA SEHKWQSAME
FALKVLNAYQ VDHSKLTLLP DEGTLECFKK AVQAYITTSK MHVTYTFTNQ KTFLHVAGRL
LLDFVIKAAE LAPGVNPSGC VVWQHGCQSS LMCLHGSPMI QKEQLVEMDV NSENAQRALK
ENPEKTKIVS NRWGRNVVQF KNEDAFCCSM DVNMSGGNFS GASCGMFYTD GPKAIMAFQQ
IMAFLKACYP SMPNAESHLL MPLKCECNWN SSLPLLGRQT CKITPFSLAS ANHIDKSEVD
DQKMLATLNN PAMLVFQCCN PVYRNSKAAP QKNCDFKISS VDLVSCLQIA KQIWLSTVGE
KPPVKFPEFH WSDEHRYQTT ILPQGQHDDD LVLF
