VE1_HPV18
ID VE1_HPV18 Reviewed; 657 AA.
AC P06789; Q84181;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 137.
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 18.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=333761;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3039146; DOI=10.1016/0022-2836(87)90343-3;
RA Cole S.T., Danos O.;
RT "Nucleotide sequence and comparative analysis of the human papillomavirus
RT type 18 genome. Phylogeny of papillomaviruses and repeated structure of the
RT E6 and E7 gene products.";
RL J. Mol. Biol. 193:599-608(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-528.
RX PubMed=2833614; DOI=10.1128/jvi.62.5.1640-1646.1988;
RA Inagaki Y., Tsunokawa Y., Takebe N., Nawa H., Nakanishi S., Terada M.,
RA Sugimura T.;
RT "Nucleotide sequences of cDNAs for human papillomavirus type 18 transcripts
RT in HeLa cells.";
RL J. Virol. 62:1640-1646(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-274.
RX PubMed=3034571; DOI=10.1002/j.1460-2075.1987.tb04731.x;
RA Seedorf K., Oltersdorf T., Kraemer G., Roewekamp W.;
RT "Identification of early proteins of the human papilloma viruses type 16
RT (HPV 16) and type 18 (HPV 18) in cervical carcinoma cells.";
RL EMBO J. 6:139-144(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RX PubMed=3023067; DOI=10.1002/j.1460-2075.1986.tb04496.x;
RA Schneider-Gaedicke A., Schwarz E.;
RT "Different human cervical carcinoma cell lines show similar transcription
RT patterns of human papillomavirus type 18 early genes.";
RL EMBO J. 5:2285-2292(1986).
RN [5]
RP INTERACTION WITH HUMAN SMARCB1/INI1 PROTEIN, AND MUTAGENESIS OF
RP 225-SER-PHE-226; LEU-305; 395-ASN-ALA-396 AND 418-HIS-TYR-419.
RX PubMed=10365963; DOI=10.1038/20966;
RA Lee D., Sohn H., Kalpana G.V., Choe J.;
RT "Interaction of E1 and hSNF5 proteins stimulates replication of human
RT papillomavirus DNA.";
RL Nature 399:487-491(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 210-354.
RX PubMed=14593106; DOI=10.1074/jbc.m311681200;
RA Auster A.S., Joshua-Tor L.;
RT "The DNA-binding domain of human papillomavirus type 18 E1. Crystal
RT structure, dimerization, and DNA binding.";
RL J. Biol. Chem. 279:3733-3742(2004).
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.Interacts with human
CC SMARCB1/INI1 protein, stimulating viral replication.
CC {ECO:0000255|HAMAP-Rule:MF_04000, ECO:0000269|PubMed:10365963}.
CC -!- INTERACTION:
CC P06789; P09914: IFIT1; Xeno; NbExp=8; IntAct=EBI-7015660, EBI-745117;
CC P06789; Q12824-1: SMARCB1; Xeno; NbExp=5; IntAct=EBI-7015660, EBI-7015645;
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; X05015; CAA28666.1; -; Genomic_DNA.
DR EMBL; M20325; AAA99516.1; -; mRNA.
DR EMBL; X04773; CAA28468.1; -; Genomic_DNA.
DR EMBL; A06324; CAA00541.1; -; Unassigned_DNA.
DR EMBL; M26798; AAA46948.1; -; Genomic_DNA.
DR PIR; C26165; W1WL18.
DR RefSeq; NP_040312.1; NC_001357.1.
DR PDB; 1R9W; X-ray; 1.80 A; A=210-354.
DR PDB; 1TUE; X-ray; 2.10 A; A/D/F/H/K/M=428-631.
DR PDBsum; 1R9W; -.
DR PDBsum; 1TUE; -.
DR SMR; P06789; -.
DR ELM; P06789; -.
DR IntAct; P06789; 2.
DR MINT; P06789; -.
DR DNASU; 1489084; -.
DR GeneID; 1489084; -.
DR KEGG; vg:1489084; -.
DR EvolutionaryTrace; P06789; -.
DR Proteomes; UP000009109; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:BHF-UCL.
DR GO; GO:0042025; C:host cell nucleus; IDA:BHF-UCL.
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; IDA:BHF-UCL.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0019079; P:viral genome replication; IDA:BHF-UCL.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA replication; DNA-binding; Early protein;
KW Helicase; Host nucleus; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..657
FT /note="Replication protein E1"
FT /id="PRO_0000133116"
FT DOMAIN 458..608
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 147..444
FT /note="SMARCB1/INI1-binding"
FT REGION 155..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..359
FT /note="DNA-binding region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 633..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 86..88
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOTIF 109..118
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT BINDING 484..491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 110
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT CROSSLNK 565
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MUTAGEN 225..226
FT /note="SF->PS: Complete loss of SMARCB1/INI1 binding."
FT /evidence="ECO:0000269|PubMed:10365963"
FT MUTAGEN 305
FT /note="L->K: Complete loss of SMARCB1/INI1 binding."
FT /evidence="ECO:0000269|PubMed:10365963"
FT MUTAGEN 395..396
FT /note="NA->HE: Complete loss of SMARCB1/INI1 binding."
FT /evidence="ECO:0000269|PubMed:10365963"
FT MUTAGEN 418..419
FT /note="HY->EH: Complete loss of SMARCB1/INI1 binding."
FT /evidence="ECO:0000269|PubMed:10365963"
FT CONFLICT 94
FT /note="T -> K (in Ref. 2; AAA99516)"
FT /evidence="ECO:0000305"
FT HELIX 211..222
FT /evidence="ECO:0007829|PDB:1R9W"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1R9W"
FT STRAND 240..250
FT /evidence="ECO:0007829|PDB:1R9W"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:1R9W"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:1R9W"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1R9W"
FT STRAND 266..276
FT /evidence="ECO:0007829|PDB:1R9W"
FT STRAND 279..292
FT /evidence="ECO:0007829|PDB:1R9W"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:1R9W"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:1R9W"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:1R9W"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:1R9W"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:1R9W"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:1R9W"
FT HELIX 429..438
FT /evidence="ECO:0007829|PDB:1TUE"
FT HELIX 447..455
FT /evidence="ECO:0007829|PDB:1TUE"
FT HELIX 460..472
FT /evidence="ECO:0007829|PDB:1TUE"
FT STRAND 478..484
FT /evidence="ECO:0007829|PDB:1TUE"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:1TUE"
FT HELIX 490..501
FT /evidence="ECO:0007829|PDB:1TUE"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:1TUE"
FT HELIX 515..520
FT /evidence="ECO:0007829|PDB:1TUE"
FT STRAND 524..531
FT /evidence="ECO:0007829|PDB:1TUE"
FT HELIX 533..542
FT /evidence="ECO:0007829|PDB:1TUE"
FT HELIX 544..548
FT /evidence="ECO:0007829|PDB:1TUE"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:1TUE"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:1TUE"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:1TUE"
FT STRAND 569..575
FT /evidence="ECO:0007829|PDB:1TUE"
FT STRAND 579..582
FT /evidence="ECO:0007829|PDB:1TUE"
FT HELIX 584..587
FT /evidence="ECO:0007829|PDB:1TUE"
FT STRAND 591..594
FT /evidence="ECO:0007829|PDB:1TUE"
FT HELIX 613..623
FT /evidence="ECO:0007829|PDB:1TUE"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:1TUE"
SQ SEQUENCE 657 AA; 73736 MW; B18E68BCE1DB330A CRC64;
MADPEGTDGE GTGCNGWFYV QAIVDKKTGD VISDDEDENA TDTGSDMVDF IDTQGTFCEQ
AELETAQALF HAQEVHNDAQ VLHVLKRKFA GGSTENSPLG ERLEVDTELS PRLQEISLNS
GQKKAKRRLF TISDSGYGCS EVEATQIQVT TNGEHGGNVC SGGSTEAIDN GGTEGNNSSV
DGTSDNSNIE NVNPQCTIAQ LKDLLKVNNK QGAMLAVFKD TYGLSFTDLV RNFKSDKTTC
TDWVTAIFGV NPTIAEGFKT LIQPFILYAH IQCLDCKWGV LILALLRYKC GKSRLTVAKG
LSTLLHVPET CMLIQPPKLR SSVAALYWYR TGISNISEVM GDTPEWIQRL TIIQHGIDDS
NFDLSEMVQW AFDNELTDES DMAFEYALLA DSNSNAAAFL KSNCQAKYLK DCATMCKHYR
RAQKRQMNMS QWIRFRCSKI DEGGDWRPIV QFLRYQQIEF ITFLGALKSF LKGTPKKNCL
VFCGPANTGK SYFGMSFIHF IQGAVISFVN STSHFWLEPL TDTKVAMLDD ATTTCWTYFD
TYMRNALDGN PISIDRKHKP LIQLKCPPIL LTTNIHPAKD NRWPYLESRI TVFEFPNAFP
FDKNGNPVYE INDKNWKCFF ERTWSRLDLH EEEEDADTEG NPFGTFKLRA GQNHRPL
