VE1_BPV3
ID VE1_BPV3 Reviewed; 613 AA.
AC Q8BDD7;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Replication protein E1 {ECO:0000255|HAMAP-Rule:MF_04000};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_04000};
DE AltName: Full=ATP-dependent helicase E1 {ECO:0000255|HAMAP-Rule:MF_04000};
GN Name=E1 {ECO:0000255|HAMAP-Rule:MF_04000};
OS Bovine papillomavirus type 3.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Xipapillomavirus.
OX NCBI_TaxID=10561;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12208979; DOI=10.1128/jvi.76.19.10020-10023.2002;
RA Terai M., DeSalle R., Burk R.D.;
RT "Lack of canonical E6 and E7 open reading frames in bird papillomaviruses:
RT Fringilla coelebs papillomavirus and Psittacus erithacus timneh
RT papillomavirus.";
RL J. Virol. 76:10020-10023(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Delius H., de Villiers E.M.;
RT "Sequencing of the complete genomes of BPV 3, BPV 5 and BPV 6.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent DNA helicase required for initiation of viral
CC DNA replication. It forms a complex with the viral E2 protein. The E1-
CC E2 complex binds to the replication origin which contains binding sites
CC for both proteins. During the initial step, a dimer of E1 interacts
CC with a dimer of protein E2 leading to a complex that binds the viral
CC origin of replication with high specificity. Then, a second dimer of E1
CC displaces the E2 dimer in an ATP-dependent manner to form the E1
CC tetramer. Following this, two E1 monomers are added to each half of the
CC site, which results in the formation of two E1 trimers on the viral
CC ori. Subsequently, two hexamers will be created. The double hexamer
CC acts as a bi-directional helicase machinery and unwinds the viral DNA
CC and then recruits the host DNA polymerase to start replication.
CC {ECO:0000255|HAMAP-Rule:MF_04000}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04000};
CC -!- SUBUNIT: Can form hexamers. Interacts with E2 protein; this interaction
CC increases E1 DNA binding specificity. Interacts with host DNA
CC polymerase subunit POLA2. Interacts with host single stranded DNA-
CC binding protein RPA1. Interacts with host TOP1; this interaction
CC stimulates the enzymatic activity of TOP1. {ECO:0000255|HAMAP-
CC Rule:MF_04000}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000}.
CC -!- PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04000}.
CC -!- SIMILARITY: Belongs to the papillomaviridae E1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04000}.
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DR EMBL; AF486184; AAN09957.1; -; Genomic_DNA.
DR EMBL; AJ620207; CAF05679.1; -; Genomic_DNA.
DR RefSeq; NP_694447.1; NC_004197.1.
DR SMR; Q8BDD7; -.
DR PRIDE; Q8BDD7; -.
DR GeneID; 955386; -.
DR KEGG; vg:955386; -.
DR Proteomes; UP000006369; Genome.
DR Proteomes; UP000185274; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.510; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04000; PPV_E1; 1.
DR InterPro; IPR001177; DNA_helicase_E1_C_Papillomavir.
DR InterPro; IPR014000; DNA_helicase_E1_N_Papillomavir.
DR InterPro; IPR014015; Helicase_SF3_DNA-vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016393; Rep_E1_papillomaV.
DR InterPro; IPR037102; Znf_lg_T-Ag_D1_dom_sf.
DR Pfam; PF00519; PPV_E1_C; 1.
DR Pfam; PF00524; PPV_E1_N; 1.
DR PIRSF; PIRSF003383; Rep_E1_papillomaV; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51206; SF3_HELICASE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Early protein; Helicase;
KW Host nucleus; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..613
FT /note="Replication protein E1"
FT /id="PRO_0000133092"
FT DOMAIN 413..566
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..317
FT /note="DNA-binding region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 588..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 71..73
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT BINDING 442..449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 77
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 92
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
SQ SEQUENCE 613 AA; 69428 MW; 3C40E0D76A6A2A41 CRC64;
MDPNLKGITG QSFLDDQAEC SESDNSEQGC EESLSDLSDL IDNAECEQGN SAELFAQQEA
FAFQEHIRTT KRKLKLSFRN PLQCITSQSN RSPGRAAPKR RVLDDSGYNE DILAEVAQVD
ENGGSEGYGS LASQSLSGQS QKNGKNRVNN GNKENIDCTR LLAASSHRAV QLAIFKEKFG
ISLNSLTRIF KNDKTCCSNW VGVVFGAREE LLAASQTILQ RVCDSIMLLT HTCKLGFMGL
YLLEFKNAKS RDTVRHLFQQ ILQVENNDML LEPPKIKSLP AATFWWKLRH SSAAFLFGNL
PDWIARQTSI THQIQEDQPF DLSAMVQWAY DHNFVDEAQI AYYYARLASE DSNAAAFLRC
NNQVKHVKEC AQMTRYYKTA EMREMSMSKW IKKCLNEIEG TGDWKQIINF IKYQNINFLS
FLACFRDLLH SVPKRNCLVI VGPPNTGKSM FVMSLMRTLK GRVLSFVNSK SHFWLQPLNA
AKIAILDDAT RPTWSYIDTY LRNGLDGTPV SLDMKHRAPM QICFPPLIIT TNVDVAKDPT
FVYLHSRLMS FEFANAFPLD ENGKPALILN ELSWKSFFER LWNQLDLTEP EDEDDGDPPS
PFRCSARAAA RDL
