VE1_HPV49
ID VE1_HPV49 Reviewed; 609 AA.
AC P36729;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 type 49.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Betapapillomavirus.
OX NCBI_TaxID=10616;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8205838; DOI=10.1007/978-3-642-78487-3_2;
RA Delius H., Hofmann B.;
RT "Primer-directed sequencing of human papillomavirus types.";
RL Curr. Top. Microbiol. Immunol. 186:13-31(1994).
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; X74480; CAA52581.1; -; Genomic_DNA.
DR PIR; S36569; S36569.
DR RefSeq; NP_041834.1; NC_001591.1.
DR SMR; P36729; -.
DR GeneID; 1489442; -.
DR KEGG; vg:1489442; -.
DR Proteomes; UP000009124; 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..609
FT /note="Replication protein E1"
FT /id="PRO_0000133145"
FT DOMAIN 411..561
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 37..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..312
FT /note="DNA-binding region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOTIF 78..80
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437..444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 83
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"
SQ SEQUENCE 609 AA; 70146 MW; B99D32651B2A8DC7 CRC64;
MADDKGTDPK EGCSEWFIDN EADCSDLEND LEQLFDESPK SNISNLLNDE EDVEQGNSRD
LLRQQEFEES AEQVQKLKRK YFSPKAVQQL SPRLQSMSIS PRQKSKRRLF EEDSGLELSG
LEQSLTNEIE DTPAELEVPA ATPAEQGGQG EGNLHYKELM RCNNSRAKLL SKVKEYFGVG
FYELARQYKS DKTCCKDWVI AAYGVREELV ESAKQLLLNH CSYVWINING IMTLYLLCFN
HAKSRETVGR LLMSILDVQL LQLICEPPKL RSVVSALYWY KGSMDSSVYA HGAYPDWIVN
QTMISHQAAA DAMQFDLSEM IQWAYDSDLT DEADIAYLYA KMANSDSNAR AWLAHNNQAR
YLRECAQMVR HYRRGEMRDM SMSEWIHHRI QQVEGEGHWS EIVKFIRFQE INFIIFLDAF
KQFIHGKPKK SCLLIHGPPD CGKSMFAMSL LKVLKGKVIS FVNAKSQFWL SPLSECKIGL
LDDATDPCWQ YIDTYLRNGL DGNVVSVDCK HKTPMQIRFP PLLITSNYNI KANDKYKFLY
SRIAIFEFKH KFPFKEDGTP VFQLTDQSWK SFFERLWTQL ELSDPEDEAD NGGTQRSFQC
TTRDVNGHL
