ID   VE1_HPV17               Reviewed;         609 AA.
AC   Q02512;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   03-AUG-2022, entry version 94.
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   Human papillomavirus 17.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Betapapillomavirus.
OX   NCBI_TaxID=10607;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8205838; DOI=10.1007/978-3-642-78487-3_2;
RA   Delius H., Hofmann B.;
RT   "Primer-directed sequencing of human papillomavirus types.";
RL   Curr. Top. Microbiol. Immunol. 186:13-31(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 336-387.
RX   PubMed=1326639; DOI=10.1128/jvi.66.10.5714-5725.1992;
RA   Chan S.-Y., Bernard H.U., Ong C.K., Chan S.P., Birgit H., Delius H.;
RT   "Phylogenetic analysis of 48 papillomavirus types and 28 subtypes and
RT   variants: a showcase for the molecular evolution of DNA viruses.";
RL   J. Virol. 66:5714-5725(1992).
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; X74469; CAA52514.1; -; Genomic_DNA.
DR   EMBL; M96319; AAA47008.1; -; Genomic_DNA.
DR   PIR; S36481; S36481.
DR   SMR; Q02512; -.
DR   Proteomes; UP000006932; 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..609
FT                   /note="Replication protein E1"
FT                   /id="PRO_0000133115"
FT   DOMAIN          411..561
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   REGION          149..312
FT                   /note="DNA-binding region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   REGION          584..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           81..83
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   MOTIF           93..102
FT                   /note="Nuclear export signal"
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         87
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        518
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
SQ   SEQUENCE   609 AA;  70478 MW;  C5684AB46C383E1E CRC64;
     MTDDNKGTKF DPKEGCSQWC ILEAECSDNS LDGDLEKLFE EGTDTEISDL IDDEDIIQGN
     SRELLCQQES EESEQQIQLL KRKYLSSQEV LQLSPRLQSI TISPQHKSKR RLFERDSGLE
     LSFNEAEDLT QQTLEVQEVS ATGSVPAEQG VKGLGIVKDL LKCSNVKAML LAKFKEAFGV
     GYMDLTRQYK SSKTCCRDWV VTLYAVQDEL IESSKQLLLQ HCAYIWLQHM SPMCLYLLCF
     NVGKSRETVS RLLMNILQVA EVQMLAEPPK LRSMLSALFW YKGSMNPNVY AHGEYPEWIL
     TQTMINHQTA QATQFDLSTM IQFAYDNEYL QEDEIAYHYA KLADTDANAR AFLQHNSQAR
     FVKECAIMVR HYKRGEMKEM SISTWVHRKL LVVEGDGHWS DIVKFIRYQD INFIRFLDIF
     KSFLHNKPKK NCILIHGPPD TGKSMFTMSL IKVLKGKVLS FANCRSNFWL QPLADTKLAL
     IDDVTFVCWD YIDQYLRNGL DGNVVCLDLK HRAPCQIKFP PLLLTSNIDV MKEDKYRYLH
     SRIQSFAFPN KFPFDNNNMP QFRLTDQSWK SFFERLWHQL DLSDQEEEGD DGQSQRTFQC
     TAREPNGHL