ID   VE1_FPVL                Reviewed;         152 AA.
AC   P06455;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Replication protein E1;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase E1;
DE   Flags: Fragment;
GN   Name=E1;
OS   Avian papillomavirus fpv-l.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Etapapillomavirus; unclassified Etapapillomavirus.
OX   NCBI_TaxID=10577;
OH   NCBI_TaxID=8782; Aves.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6088809; DOI=10.1128/jvi.51.3.872-875.1984;
RA   Moreno-Lopez J., Ahola H., Stenlund A., Osterhaus A., Pettersson U.;
RT   "Genome of an avian papillomavirus.";
RL   J. Virol. 51:872-875(1984).
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   -!- 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   -!- SUBCELLULAR LOCATION: Host nucleus.
CC   -!- SIMILARITY: Belongs to the papillomaviridae E1 protein family.
CC       {ECO:0000305}.
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DR   EMBL; K02019; AAA46922.1; -; Genomic_DNA.
DR   SMR; P06455; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR001177; DNA_helicase_E1_C_Papillomavir.
DR   InterPro; IPR014015; Helicase_SF3_DNA-vir.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00519; PPV_E1_C; 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.
FT   CHAIN           <1..>152
FT                   /note="Replication protein E1"
FT                   /id="PRO_0000133096"
FT   DOMAIN          23..>152
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   BINDING         49..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   NON_TER         1
FT   NON_TER         152
SQ   SEQUENCE   152 AA;  17021 MW;  AD6A797EAA37E19C CRC64;
     YDVESTDEDG WKKILVFLTF QHINFKEFIS ILCMWLKGRP KKSCITIAGV PDSGKSMFAY
     SLIKFLNGSV LSFANSKSHF WLQPLTECKA ALIDDVTLPC WDYVDTFLRN ALDGNAICID
     CKHRAPVQTK CPPLLLTSNY DPRLHGVDSG GG