ID   VE1_PAPVE               Reviewed;         611 AA.
AC   P11328;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 99.
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   European elk papillomavirus (EEPV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Deltapapillomavirus.
OX   NCBI_TaxID=10565;
OH   NCBI_TaxID=9860; Cervus elaphus (Red deer).
OH   NCBI_TaxID=9870; Rangifer tarandus (Reindeer) (Cervus tarandus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3034730; DOI=10.1016/0378-1119(86)90324-0;
RA   Ahola H., Bergman P., Stroem A.C., Moreno-Lopez J., Petterson U.;
RT   "Organization and expression of the transforming region from the European
RT   elk papillomavirus (EEPV).";
RL   Gene 50:195-205(1986).
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; M15953; AAA66852.1; -; Genomic_DNA.
DR   PIR; C29499; W1WLEP.
DR   RefSeq; NP_041304.1; NC_001524.1.
DR   SMR; P11328; -.
DR   GeneID; 1488989; -.
DR   KEGG; vg:1488989; -.
DR   Proteomes; UP000009060; 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; Reference proteome; Ubl conjugation.
FT   CHAIN           1..611
FT                   /note="Replication protein E1"
FT                   /id="PRO_0000133170"
FT   DOMAIN          412..562
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   REGION          112..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..313
FT                   /note="DNA-binding region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   MOTIF           74..76
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   MOTIF           89..98
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   COMPBIAS        112..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         438..445
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   MOD_RES         80
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   MOD_RES         84
FT                   /note="Phosphoserine; by host"
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   CROSSLNK        519
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
SQ   SEQUENCE   611 AA;  68111 MW;  43612B9CA806CDB0 CRC64;
     MAETAGSSGQ GGGAYICFEA DCSDSDTEVD SPVQCSDSSD EDLVDNANIV PGNHLELFQT
     QEKEAGERQI SLLKRKFCLS PGTSEVEELS PGLAGIRISP PKRNPVVRRR LFDAGGRDAV
     RTPRDHEVNS SPEPRSQVQS GSSSRSWEGH LESINEPASD GNMAAVMHKL FKTLYIAGFG
     EITRVFQSDK TNNNQWVIAA HGASEVLYAA SFEILSKHCS YLQASRKVHE TGSMSLFLAV
     FNVGKSRETV RKLISGVLNT PCSRLLLQPP KIRGLCPALF WFKLGLSPAT QTHGTTPDWI
     KQQTNVAYNT GEASKFDFGT MVQWAYDHRL TEECKIAYQY AKCAGTDLNA KAFLASTNQA
     RLVKDCCTMV KHYLRAEEQS LTISAFIKRR CDNATGKGSW LSIMNLLKFQ GIEPINFVNA
     LKPWLKGTPK HNCIAIVGPP NSGKSLLCNT LMSFLGGKVL TFANHSSHFW LAPLTDCRVA
     LIDDATHACW RYFDTYLRNV LDGYPVCIDR KHKSAVQLKA PPLLLTSNID VHADEKYFYL
     QSRVKTFYFK EPCPASDTGE PLFFITDADW KNFFERLWER LDLSDQEDEV DEDECSQRSF
     TCSARNTDAM H