VE1_HPV51
ID VE1_HPV51 Reviewed; 634 AA.
AC P26544;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, 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 51.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10595;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1649326; DOI=10.1128/jvi.65.8.4216-4225.1991;
RA Lungu O., Crum C.P., Silverstein S.J.;
RT "Biologic properties and nucleotide sequence analysis of human
RT papillomavirus type 51.";
RL J. Virol. 65:4216-4225(1991).
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 -!- SIMILARITY: Belongs to the papillomaviridae E1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04000}.
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DR EMBL; M62877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A40415; W1WL51.
DR SMR; P26544; -.
DR PRIDE; P26544; -.
DR Proteomes; UP000009125; 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; Nucleotide-binding; Phosphoprotein.
FT CHAIN 1..634
FT /note="Replication protein E1"
FT /id="PRO_0000133146"
FT DOMAIN 437..587
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 92..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..338
FT /note="DNA-binding region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOTIF 85..87
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT COMPBIAS 95..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 463..470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 95
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
SQ SEQUENCE 634 AA; 71685 MW; C429CCBFA515CEE1 CRC64;
MDCEGTEDEG AGCNGWFFVE AIVEKKTGDN VSDDEDENAD DTGSDLINFI DSETSICSQA
EQETARALFQ AQELQANKEA VHQLKRKFLV SPRSSPLGDI TNQNNTHSHS QANESQVKRR
LLDSYPDSGY GNTQVETVEA TLQVDGQHGG SQNSVCSSGG GSVMDVETTE SCANVELNSI
CEVLKSSNAK ATLMAKFKEL YGISYNELVR VFKSDKTCCI DWVCALFGVS PMVAENLKTL
IKPFCMYYHI QCLSCDWGTI VLMLIRFSCA KNRTTIAKCL STLVNIPQSQ MFIEPPKLRS
TPVALYFYRT GISNISNTYG ETPEWITRQT QLQHSFEDST FELSQMVQWA FDHEVLDDSE
IAFHYAQLAD IDSNAAAFLK SNCQAKYVKD CGTMARHYKR AQRKSLSMSA WIRYRCDRAK
DGGNWREIAK FLRYQGVNFM SFIQMFKQFL KGTPKHNCIV IYGPPNTGKS LFAMSLMKFM
QGSIISYVNS GSHFWLQPLE DAKIALLDDA TYGCWTYIDQ YLRNFLDGNP CSIDRKHRSL
IQLVCPPLLI TSNINPQEDA NLMYLHTRVT VLKFLNTFPF DNNGNAVYTL NDENWKNFFS
TTWSRLDLEE EEDKENGDPM PPFKCVPGEN TRLL
