DNB2_ADE41
ID DNB2_ADE41 Reviewed; 474 AA.
AC P11807;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 F serotype 41 (HAdV-41) (Human adenovirus 41).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus F.
OX NCBI_TaxID=10524;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3279700; DOI=10.1016/0042-6822(88)90227-9;
RA Vos H.L., der Lee F.M., Reemst A.M.C.B., van Loon A.E., Sussenbach J.S.;
RT "The genes encoding the DNA binding protein and the 23K protease of
RT adenovirus types 40 and 41.";
RL Virology 163:1-10(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RC STRAIN=Tak;
RX PubMed=2349115; DOI=10.1093/nar/18.10.3069;
RA Slemenda S.B., Pieniazek N.J., Velarde J. Jr., Pieniazek D., Luftig R.B.;
RT "Nucleotide sequence of the region coding for 100K and 33K proteins of
RT human enteric adenovirus type 41 (Tak).";
RL Nucleic Acids Res. 18:3069-3069(1990).
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; M21163; AAA42463.1; -; Genomic_DNA.
DR EMBL; X52532; CAA36759.1; -; Genomic_DNA.
DR PIR; D28645; ERAD41.
DR SMR; P11807; -.
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; -; 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..474
FT /note="DNA-binding protein"
FT /id="PRO_0000221683"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..278
FT /note="Flexible loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT REGION 460..474
FT /note="C-terminal arm, DBP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 413
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 142
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
SQ SEQUENCE 474 AA; 53658 MW; 4350AE593088B19E CRC64;
MAGRQREHPT VTPYLQETSP ERPPPLPPKK KLRKNLQVPE QVHAPALSPE VVPDSEEDEE
VLYHGFSYPG VEVVQKGNGK RQIRRLEKTV IPRDLTPPEE EENNQSGSSK AVTMLITNPQ
VDPLVSAWEK GMELMNVLME KYHVENDEKT AFKFLPEQNA VYRKICQTWL NEERRGLSLT
FTTQKTFTEL MGRFLAAYVE TYAGVKHHNW DTTGCAVWAH GCTREEGVLR CFHGREMIQK
EQVVEVDVGS ENGQRALKEQ PSKTKVVQNR WGRSVVQIKN DDARCCAEDV SCGNNMFSSK
SCGLFFSEGL KAQIAFKQMQ AFLQAEYPQM QRGQQRILVP LRCECLNKKD LVPQLGRQMC
KVTPFALSGA EDLKTSEVTD KSALASILHP CVLVFQCANP VYRNSRGSAG PNCDFKISAP
DVISALQLVR QFWKENVEDP LPKLIIPEFK WSTRLQYRNV ALPTGHGDAE VEPF
