ID   VE1_BPV2                Reviewed;         604 AA.
AC   P11298;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 98.
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 2 (Bovine papillomavirus 2).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Deltapapillomavirus.
OX   NCBI_TaxID=2758382;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Groff D.E., Mitra R., Lancaster W.D.;
RL   Submitted (MAY-1988) 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.
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   -!- PTM: Sumoylated. {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; M20219; AAA66833.1; -; Genomic_DNA.
DR   PIR; C31169; W1WLB2.
DR   SMR; P11298; -.
DR   IntAct; P11298; 1.
DR   MINT; P11298; -.
DR   Proteomes; UP000007612; 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; Isopeptide bond; Nucleotide-binding;
KW   Phosphoprotein; Ubl conjugation.
FT   CHAIN           1..604
FT                   /note="Replication protein E1"
FT                   /id="PRO_0000133091"
FT   DOMAIN          406..556
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   REGION          24..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..307
FT                   /note="DNA-binding region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   REGION          581..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           84..86
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   COMPBIAS        590..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         432..439
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   MOD_RES         90
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   MOD_RES         94
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   CROSSLNK        513
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
SQ   SEQUENCE   604 AA;  68077 MW;  D2D7036ADE88A9DD CRC64;
     MANDKGSNWD SALGCSYLLT EAECESDKEN EEPGAGVELS VESDRYDSQD EDFLDNASVF
     QGNHLEVFQA LEKKAGEEQL LNLKRKVLGS SENSSGSEAS ETPAKRQKAG AKRRLFSENE
     ANRVLTPLQV QGGEWRQGFN EDQAISHRLL QLVKSKNATV FKLGLFKSLF LCSFHDLTRL
     FKNDKTTNQQ WVLAVFGIAE VFFEASLELL KKQCSFVQMQ KRSHEGGTCA VYLLCFNTAK
     SRETVRNLMA NMLNVREECL LMQPPKIRGL SAALFWFKSS LSPATLKHGA LPEWIRAQTT
     LHDSLATEKF DFGTMVQWAY DHKYAEESKI AYEYALAAGS DSNARAFLAT NSQAKHVKDC
     ATMVRHYLRA ETQALSMPAY IKTRCKLATG EGSWKSILTF FNYQNIELIT FINALKLWLN
     GIPKKNCLAF IGPPKTGKSM LCNSLIHFLG GSVLSFANHK SHFWLASLAD ARAALVDDAT
     HACWRYFDTY LRNALDGYPV SIDRKHKAAV QIKAPPLLVT SNIDVQAEER YLYLHSRVQT
     FRFEQPCTDE SGEQPFTITD ADWKSFFVRL WGRLDLVDEE EDSEEDGDSM RTFTCSARNT
     NAVD