VE1_BPV5
ID VE1_BPV5 Reviewed; 626 AA.
AC Q705G8; Q8BDG5;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 Bovine papillomavirus type 5.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Epsilonpapillomavirus.
OX NCBI_TaxID=40537;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12208979; DOI=10.1128/jvi.76.19.10020-10023.2002;
RA Terai M., DeSalle R., Burk R.D.;
RT "Lack of canonical E6 and E7 open reading frames in bird papillomaviruses:
RT Fringilla coelebs papillomavirus and Psittacus erithacus timneh
RT papillomavirus.";
RL J. Virol. 76:10020-10023(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Delius H., de Villiers E.M.;
RT "Sequencing of the complete genomes of BPV 3, BPV 5 and BPV 6.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN09926.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF457465; AAN09926.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ620206; CAF05673.1; -; Genomic_DNA.
DR RefSeq; NP_694432.1; NC_004195.1.
DR SMR; Q705G8; -.
DR GeneID; 955403; -.
DR KEGG; vg:955403; -.
DR Proteomes; UP000008785; Genome.
DR Proteomes; UP000185273; 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..626
FT /note="Replication protein E1"
FT /id="PRO_0000133094"
FT DOMAIN 412..576
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 160..327
FT /note="DNA-binding region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 598..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 82..84
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT COMPBIAS 612..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 452..459
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 106
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT CROSSLNK 533
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
SQ SEQUENCE 626 AA; 70425 MW; 6C7326E5ED6870F0 CRC64;
MADKSGRLLG GCSFVLDEAD CSDLEIDSDD ESDKENVPNG QDMCNSFDAE FIDNAPLAQG
NTLALFQSQV AQAGKQKVNY LKRKLHLESS ELGTVGRAVL QPVNHSTPAA KRRLFECSSS
ENEVSYAASP AAANTQVFRN QNSGSVGGSS GFGSQASVSQ SQQNSNLHLQ ILKSKNSAAC
KLAVFKFVYA ASFCDLTRPF KNDKTTNYQW VAAVFGVSEE LFEASKQLLG RSCTYLHATC
RAHEKGSVAL LLLSFHVAKS RETVTNLLKN LLNLRAEHMM LQPPKLRGVT SAMFWYKMTL
SPNTYTWGQL PRWIEQQILI TENSSEVLKF DFSHMVQWAL DNEMMDESSI AFHYAQMADH
DSNARAWLGL SNQAKIVKDV CTMVHHYQRA IMRSMTMSAY VHKMCERVNV TGSWLVIMQF
LKFHGIEPIR FVNALRPWLQ GVPKKNCLAF IGPPDTGKSL FTNSLMSFLK GKVLNFANSA
SHFWLAPLTE AKVALIDDAT HACLKYCDTY LRNFFDGYSV CIDRKHKNAV QIKAPPMLLT
SNIDIQAEEK YSYLKSRVTC FYFNDKCPLN EDGKPLFQIT DPDWKSFFER LWQRLELSDQ
EEEEEGDENG SRGTFICSTR NSNDFT
