VE1_COPV6
ID VE1_COPV6 Reviewed; 597 AA.
AC Q89536;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Canine oral papillomavirus (strain Y62) (COPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Lambdapapillomavirus.
OX NCBI_TaxID=766192;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8091677; DOI=10.1006/viro.1994.1552;
RA Delius H., van Ranst M.A., Jenson A.B., zur Hausen H., Sundberg J.P.;
RT "Canine oral papillomavirus genomic sequence: a unique 1.5-kb intervening
RT sequence between the E2 and L2 open reading frames.";
RL Virology 204:447-452(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Isegawa N., Ohta M., Shirasawa H., Tokita H., Simizu B., Yamaura A.;
RT "Nucleotide sequence of a canine oral papillomavirus containing a long
RT noncoding region.";
RL Int. J. Oncol. 7:155-159(1995).
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; D55633; BAA09500.1; -; Genomic_DNA.
DR EMBL; L22695; AAA61746.1; -; Genomic_DNA.
DR RefSeq; NP_056815.1; NC_001619.1.
DR SMR; Q89536; -.
DR GeneID; 1497240; -.
DR KEGG; vg:1497240; -.
DR Proteomes; UP000008788; Genome.
DR Proteomes; UP000097271; 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..597
FT /note="Replication protein E1"
FT /id="PRO_0000133165"
FT DOMAIN 400..550
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 119..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..300
FT /note="DNA-binding region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 574..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 75..77
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOTIF 90..99
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT BINDING 426..433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 81
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 91
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 104
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT CROSSLNK 507
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
SQ SEQUENCE 597 AA; 67983 MW; 0D11CEFD913D6932 CRC64;
MAARKGTDSE TEDGGWVLIE ADCSEVDSAD ETSENASNVS DLVDNASIAE TQGLSLQLFQ
QQELTECEEQ LQQLKRKFVQ SPQSRDLCSL SPQLASISLT PRTSKKVKKQ LFATDSGIQS
SNEADDSLEG QRQVEPLPGR EENGADALFK VRDKRAFLYS KFKSSFGISF TDLTRVYNSD
KTCSSDWVVC LYHVSDDRRE AGKTLLQDHC EYFFLHSMGF CTLLLLCLFV PKCRNTLFKL
CRSLFHISNV QMLADPPKTR SPAVALYWYK KGFASGTFTH GELPSWIAQQ TLITHHLAAE
KTFDLSEMVQ WAYDNDLKDE SEIAYKYAAL AETDENALAF LKSNNQPKHV KDCATMCRYY
KKAEMKRLSM SQWIDERCKA TDDGPGDWKE VVKFLRHQGI EFILFLADFK RFLRGRPKKN
CLVFWGPPNT GKSMFCMSLL SFLHGVVISY VNSKSHFWLQ PLTEGKMGLL DDATRPCWLY
IDTYLRNALD GNTFSVDCKH KAPLQLKCPP LLITTNVNVC GDEKFKYLRS RCSFFHFPQE
FPLDDNGNPG FQLNDQSWAS FFKRFWKHLD LSDPEDGEDG ETQRGLRLTA RGTTESV
