ID   VE1_HPV27               Reviewed;         643 AA.
AC   P36723;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 92.
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 27.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Alphapapillomavirus.
OX   NCBI_TaxID=333752;
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).
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; X74473; CAA52538.1; -; Genomic_DNA.
DR   PIR; S36499; S36499.
DR   SMR; P36723; -.
DR   Proteomes; UP000009114; 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..643
FT                   /note="Replication protein E1"
FT                   /id="PRO_0000133125"
FT   DOMAIN          445..595
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   REGION          30..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..346
FT                   /note="DNA-binding region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   MOTIF           84..86
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   MOTIF           102..111
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   COMPBIAS        148..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         471..478
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         103
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   CROSSLNK        552
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
SQ   SEQUENCE   643 AA;  72372 MW;  442E5D8134A78546 CRC64;
     MEDSEGTDGT EEDGCRAGGW FHVEAIITHG QRQVSSDEDE DCTETGEDVD FIDNRVPGDG
     QEIPLQLYTQ QIAQDDEATV QALKRKFVAS PLSACSCIEN DLSPRLDAIS LNRKSEKAKR
     RLFETEPPDS GYGNTQMVVG TPEEVTGDEN SEGGRPVEDK EEERQGGDGE ADLTVQTPQS
     GTDAAGSVLT LLRSSNLKAT LLSKFKELFG VGYYELVRQF KSSKTACADW VVCAFGVYYA
     VAEGIKQLIQ PHTQYAHIQV LTCSWGMVVF MLLRYNCAKN RDTVSKNMSM LLNIPEKHML
     IEPPKLRSTP AALYWYKTAM GNGSEVYGET PEWIVRQTLV GHSMEDEQFR LSVMVQFAYD
     HDIVEESVLA FEYAQLADVD ANAAAFLNSN CQAKYVKDAV TMCRHYKRAE RAQMSMSQWI
     TFRGNKVLEE GDWKPIVKFL RHQGVEFVSF LAAFKLFLKG VPKKNCIVFY GPADTGKSYF
     CMSLLQFLGG AVISYANSSS HFWLQPLSDS KIGLLDDATP QCWSYIDTYL RNLLDGNPVS
     IDRKHKTLLQ LKCPPLMITT NINPLEEDRW KYLRSRLTLF TFNNPFPFAS PGEPLYPINN
     ANWKCFFQRS WSRLDLNSPE EQDDNGNTSE PFRCVPGDVA RTL