DNB2_ADE07
ID DNB2_ADE07 Reviewed; 517 AA.
AC P04497;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Human adenovirus B serotype 7 (HAdV-7) (Human adenovirus 7).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX NCBI_TaxID=10519;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6325415; DOI=10.1016/s0021-9258(17)42946-2;
RA Quinn C.O., Kitchingman G.R.;
RT "Sequence of the DNA-binding protein gene of a human subgroup B adenovirus
RT (type 7). Comparisons with subgroup C (type 5) and subgroup A (type 12).";
RL J. Biol. Chem. 259:5003-5009(1984).
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; K02530; AAA42508.1; -; Genomic_DNA.
DR PIR; A03834; ERADA7.
DR SMR; P04497; -.
DR PRIDE; P04497; -.
DR GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB.
DR GO; GO:0019028; C:viral capsid; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
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:0039693; P:viral DNA genome replication; ISS:UniProtKB.
DR GO; GO:0039687; P:viral DNA strand displacement replication; ISS:UniProtKB.
DR Gene3D; 1.10.269.10; -; 1.
DR Gene3D; 3.90.148.10; -; 2.
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..517
FT /note="DNA-binding protein"
FT /id="PRO_0000221680"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..316
FT /note="Flexible loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT REGION 501..517
FT /note="C-terminal arm, DBP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT COMPBIAS 29..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 453
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 180
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
SQ SEQUENCE 517 AA; 58306 MW; A2CC8B1C4A1F191F CRC64;
MASRGGNQSS DRQREHTPER GMGSASHPPP RPDRSPSQSP PPLPPKRNTY RRVGSNSSIE
SQVVLVSETS RSSLSPERSN SPPPIPPKKK PRKTKHVPLQ DISQDSEEER EQVQLVRVGF
SYPPVRIIEK DGKRSVEKID NNDPISKGAT SIAVRNPLSL PLVSAWEKGM EVMAVLMERY
RLDNDLRTSF KLMPEQHEQY KRICHQYVNE EHRGIPLTFS SMKTLTAMMG RFMQGLVHSY
SEIAHNNWEC TGCALWAHGC TDYEGKVKCL HGTIMIQKDH IIEMDVASEN GQRAMKENPD
RAKITQNRWG RNVVQLANND ARCCVNDANC ATNQFSSKSC GMFYTEGIKA QEAFKQYEAF
MKAVYPGITP DQARMMLIPI HCDCNHKPGC APVMGRQTCK MTPFGMANAE DLDVATISDP
TVLASVRHPA LMVFQCCNPV YRNSRVQNAG PNCDFKISAP DLLGALQLTR KLWQDTFPEI
PVPKLVIPEF KWQNRLQFRN VSLPAGHYDS RQNPFDF
