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Replication protein E1 (EC 3.6.4.12) (ATP-dependent helicase E1)

 VE1_HPV18               Reviewed;         657 AA.
P06789; Q84181;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
20-JUN-2018, entry version 119.
RecName: Full=Replication protein E1 {ECO:0000255|HAMAP-Rule:MF_04000};
EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_04000};
AltName: Full=ATP-dependent helicase E1 {ECO:0000255|HAMAP-Rule:MF_04000};
Name=E1 {ECO:0000255|HAMAP-Rule:MF_04000};
Human papillomavirus type 18.
Viruses; dsDNA viruses, no RNA stage; Papillomaviridae;
Firstpapillomavirinae; Alphapapillomavirus.
NCBI_TaxID=333761;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3039146; DOI=10.1016/0022-2836(87)90343-3;
Cole S.T., Danos O.;
"Nucleotide sequence and comparative analysis of the human
papillomavirus type 18 genome. Phylogeny of papillomaviruses and
repeated structure of the E6 and E7 gene products.";
J. Mol. Biol. 193:599-608(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-528.
PubMed=2833614;
Inagaki Y., Tsunokawa Y., Takebe N., Nawa H., Nakanishi S., Terada M.,
Sugimura T.;
"Nucleotide sequences of cDNAs for human papillomavirus type 18
transcripts in HeLa cells.";
J. Virol. 62:1640-1646(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-274.
PubMed=3034571;
Seedorf K., Oltersdorf T., Kraemer G., Roewekamp W.;
"Identification of early proteins of the human papilloma viruses type
16 (HPV 16) and type 18 (HPV 18) in cervical carcinoma cells.";
EMBO J. 6:139-144(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
PubMed=3023067;
Schneider-Gaedicke A., Schwarz E.;
"Different human cervical carcinoma cell lines show similar
transcription patterns of human papillomavirus type 18 early genes.";
EMBO J. 5:2285-2292(1986).
[5]
INTERACTION WITH HUMAN SMARCB1/INI1 PROTEIN, AND MUTAGENESIS OF
225-SER-PHE-226; LEU-305; 395-ASN-ALA-396 AND 418-HIS-TYR-419.
PubMed=10365963; DOI=10.1038/20966;
Lee D., Sohn H., Kalpana G.V., Choe J.;
"Interaction of E1 and hSNF5 proteins stimulates replication of human
papillomavirus DNA.";
Nature 399:487-491(1999).
[6]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 210-354.
PubMed=14593106; DOI=10.1074/jbc.M311681200;
Auster A.S., Joshua-Tor L.;
"The DNA-binding domain of human papillomavirus type 18 E1. Crystal
structure, dimerization, and DNA binding.";
J. Biol. Chem. 279:3733-3742(2004).
-!- FUNCTION: ATP-dependent DNA helicase required for initiation of
viral DNA replication. It forms a complex with the viral E2
protein. The E1-E2 complex binds to the replication origin which
contains binding sites for both proteins. During the initial step,
a dimer of E1 interacts with a dimer of protein E2 leading to a
complex that binds the viral origin of replication with high
specificity. Then, a second dimer of E1 displaces the E2 dimer in
an ATP-dependent manner to form the E1 tetramer. Following this,
two E1 monomers are added to each half of the site, which results
in the formation of two E1 trimers on the viral ori. Subsequently,
two hexamers will be created. The double hexamer acts as a bi-
directional helicase machinery and unwinds the viral DNA and then
recruits the host DNA polymerase to start replication.
{ECO:0000255|HAMAP-Rule:MF_04000}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000255|HAMAP-Rule:MF_04000}.
-!- SUBUNIT: Can form hexamers. Interacts with E2 protein; this
interaction increases E1 DNA binding specificity. Interacts with
host DNA polymerase subunit POLA2. Interacts with host single
stranded DNA-binding protein RPA1. Interacts with host TOP1; this
interaction stimulates the enzymatic activity of TOP1.Interacts
with human SMARCB1/INI1 protein, stimulating viral replication.
{ECO:0000255|HAMAP-Rule:MF_04000, ECO:0000269|PubMed:10365963}.
-!- INTERACTION:
P09914:IFIT1 (xeno); NbExp=8; IntAct=EBI-7015660, EBI-745117;
Q12824-1:SMARCB1 (xeno); NbExp=5; IntAct=EBI-7015660, EBI-7015645;
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-
Rule:MF_04000}.
-!- PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04000}.
-!- PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_04000}.
-!- SIMILARITY: Belongs to the papillomaviridae E1 protein family.
{ECO:0000255|HAMAP-Rule:MF_04000}.
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EMBL; X05015; CAA28666.1; -; Genomic_DNA.
EMBL; M20325; AAA99516.1; -; mRNA.
EMBL; X04773; CAA28468.1; -; Genomic_DNA.
EMBL; A06324; CAA00541.1; -; Unassigned_DNA.
EMBL; M26798; AAA46948.1; -; Genomic_DNA.
PIR; C26165; W1WL18.
RefSeq; NP_040312.1; NC_001357.1.
PDB; 1R9W; X-ray; 1.80 A; A=210-354.
PDB; 1TUE; X-ray; 2.10 A; A/D/F/H/K/M=428-631.
PDBsum; 1R9W; -.
PDBsum; 1TUE; -.
ProteinModelPortal; P06789; -.
SMR; P06789; -.
ELM; P06789; -.
IntAct; P06789; 2.
MINT; P06789; -.
GeneID; 1489084; -.
KEGG; vg:1489084; -.
KO; K21810; -.
OrthoDB; VOG090000HF; -.
EvolutionaryTrace; P06789; -.
Proteomes; UP000009109; Genome.
GO; GO:0030430; C:host cell cytoplasm; IDA:BHF-UCL.
GO; GO:0042025; C:host cell nucleus; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; IDA:BHF-UCL.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0019079; P:viral genome replication; IDA:BHF-UCL.
HAMAP; MF_04000; PPV_E1; 1.
InterPro; IPR001177; DNA_helicase_E1_C_Papillomavir.
InterPro; IPR014000; DNA_helicase_E1_N_Papillomavir.
InterPro; IPR014015; Helicase_SF3_DNA-vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR016393; Rep_E1_papillomaV.
Pfam; PF00519; PPV_E1_C; 1.
Pfam; PF00524; PPV_E1_N; 1.
PIRSF; PIRSF003383; Rep_E1_papillomaV; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51206; SF3_HELICASE_1; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; DNA replication;
DNA-binding; Early protein; Helicase; Host nucleus; Hydrolase;
Isopeptide bond; Nucleotide-binding; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 657 Replication protein E1.
/FTId=PRO_0000133116.
DOMAIN 458 608 SF3 helicase. {ECO:0000255|HAMAP-
Rule:MF_04000}.
NP_BIND 484 491 ATP. {ECO:0000255|HAMAP-Rule:MF_04000}.
REGION 147 444 SMARCB1/INI1-binding.
REGION 193 359 DNA-binding region. {ECO:0000255|HAMAP-
Rule:MF_04000}.
MOTIF 86 88 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_04000}.
MOTIF 109 118 Nuclear export signal.
{ECO:0000255|HAMAP-Rule:MF_04000}.
MOD_RES 110 110 Phosphoserine; by host.
{ECO:0000255|HAMAP-Rule:MF_04000}.
CROSSLNK 565 565 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000255|HAMAP-Rule:MF_04000}.
MUTAGEN 225 226 SF->PS: Complete loss of SMARCB1/INI1
binding. {ECO:0000269|PubMed:10365963}.
MUTAGEN 305 305 L->K: Complete loss of SMARCB1/INI1
binding. {ECO:0000269|PubMed:10365963}.
MUTAGEN 395 396 NA->HE: Complete loss of SMARCB1/INI1
binding. {ECO:0000269|PubMed:10365963}.
MUTAGEN 418 419 HY->EH: Complete loss of SMARCB1/INI1
binding. {ECO:0000269|PubMed:10365963}.
CONFLICT 94 94 T -> K (in Ref. 2; AAA99516).
{ECO:0000305}.
HELIX 211 222 {ECO:0000244|PDB:1R9W}.
HELIX 226 228 {ECO:0000244|PDB:1R9W}.
STRAND 240 250 {ECO:0000244|PDB:1R9W}.
HELIX 252 256 {ECO:0000244|PDB:1R9W}.
HELIX 258 262 {ECO:0000244|PDB:1R9W}.
HELIX 263 265 {ECO:0000244|PDB:1R9W}.
STRAND 266 276 {ECO:0000244|PDB:1R9W}.
STRAND 279 292 {ECO:0000244|PDB:1R9W}.
HELIX 294 305 {ECO:0000244|PDB:1R9W}.
HELIX 309 311 {ECO:0000244|PDB:1R9W}.
STRAND 312 315 {ECO:0000244|PDB:1R9W}.
HELIX 322 333 {ECO:0000244|PDB:1R9W}.
STRAND 337 341 {ECO:0000244|PDB:1R9W}.
HELIX 345 350 {ECO:0000244|PDB:1R9W}.
HELIX 429 438 {ECO:0000244|PDB:1TUE}.
HELIX 447 455 {ECO:0000244|PDB:1TUE}.
HELIX 460 472 {ECO:0000244|PDB:1TUE}.
STRAND 478 484 {ECO:0000244|PDB:1TUE}.
HELIX 486 488 {ECO:0000244|PDB:1TUE}.
HELIX 490 501 {ECO:0000244|PDB:1TUE}.
STRAND 511 513 {ECO:0000244|PDB:1TUE}.
HELIX 515 520 {ECO:0000244|PDB:1TUE}.
STRAND 524 531 {ECO:0000244|PDB:1TUE}.
HELIX 533 542 {ECO:0000244|PDB:1TUE}.
HELIX 544 548 {ECO:0000244|PDB:1TUE}.
STRAND 552 554 {ECO:0000244|PDB:1TUE}.
STRAND 557 559 {ECO:0000244|PDB:1TUE}.
STRAND 562 564 {ECO:0000244|PDB:1TUE}.
STRAND 569 575 {ECO:0000244|PDB:1TUE}.
STRAND 579 582 {ECO:0000244|PDB:1TUE}.
HELIX 584 587 {ECO:0000244|PDB:1TUE}.
STRAND 591 594 {ECO:0000244|PDB:1TUE}.
HELIX 613 623 {ECO:0000244|PDB:1TUE}.
HELIX 625 627 {ECO:0000244|PDB:1TUE}.
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


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