ID   VE1_BPV4                Reviewed;         608 AA.
AC   P08344; P08351;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 102.
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   Bos taurus papillomavirus 4 (Bovine papillomavirus 4).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Xipapillomavirus.
OX   NCBI_TaxID=10562;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3039043; DOI=10.1099/0022-1317-68-8-2117;
RA   Patel K.R., Smith K.T., Campo M.S.;
RT   "The nucleotide sequence and genome organization of bovine papillomavirus
RT   type 4.";
RL   J. Gen. Virol. 68:2117-2128(1987).
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; X05817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; C27129; W7WLB4.
DR   PIR; D27129; W1WLB4.
DR   SMR; P08344; -.
DR   Proteomes; UP000007613; 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.
FT   CHAIN           1..608
FT                   /note="Replication protein E1"
FT                   /id="PRO_0000133093"
FT   DOMAIN          411..561
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   REGION          145..312
FT                   /note="DNA-binding region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   BINDING         437..444
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   MOD_RES         74
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
SQ   SEQUENCE   608 AA;  69210 MW;  7DB0D324AF39B19A CRC64;
     MDPKGTTVLD FIEEQAECSQ SDSEQGSEEN CSDISDLIDN AEYEQGNSAE LFAQQQAFDF
     HKDICTTKRN LKRSLRNAFQ CITSQSNTPA SRSAPKRRLL DDSGYNEDIS TEVVQVDENG
     GSEGYGSLTS QHLSGVCLNQ GDNGGVDKEN VDCTALLRAG SRRAAYLGVF KEKFTISFTA
     LTRIFKNDKT CCRNWVGTVY RAREELLEAS KTILQKCCDF ILLLTHTCKY GFLALFLLEF
     KTAKSRETVQ RLFEHILQVE KEDMLLEPPK LKSLPAATFW WKIQHSNNSF KWGTLPDWIA
     RQTMISHQIA DDEPFSLSVM VQWAYDHNYT EESTIAYHYA KLASEDSNAA AFLKCNNQVK
     HVKECAQMTR YYKTAEMTEM SMGQWIKKCI GEIEGVGDWK QICKFLKFQN VNFLSFMSAL
     KDLLHRVPKR NCMVICGPPN TGKSMFVMSF MKALQGKVLS FVNSKSHFWL QPLRGAKVAV
     LDDATRATWT YFDTYLRNGL DGTPVSLDMK HRAPLQICFP PLVITTNVNV MQDPAYFYLH
     SRIVCFEFPN TFPLDEAGNP LLLIDELSWK SFFERLWTQL DLTDAEEDED GEPRSPFRCC
     PRSVATSL