ID O56936_9PAPI Unreviewed; 609 AA.
AC O56936;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JUN-1998, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Replication protein E1 {ECO:0000256|HAMAP-Rule:MF_04000, ECO:0000256|PIRNR:PIRNR003383};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_04000, ECO:0000256|PIRNR:PIRNR003383};
DE AltName: Full=ATP-dependent helicase E1 {ECO:0000256|HAMAP-Rule:MF_04000};
GN Name=E1 {ECO:0000256|HAMAP-Rule:MF_04000,
GN ECO:0000313|EMBL:CAA75451.1};
OS human papillomavirus 75.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Betapapillomavirus; Betapapillomavirus 3.
OX NCBI_TaxID=69984 {ECO:0000313|EMBL:CAA75451.1};
RN [1] {ECO:0000313|EMBL:CAA75451.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9454709; DOI=10.1006/viro.1997.8943;
RA Delius H., Saegling B., Bergmann K., Shamanin V., de Villiers E.M.;
RT "The genomes of three of four novel HPV types, defined by differences of
RT their L1 genes, show high conservation of the E7 gene and the URR.";
RL Virology 240:359-365(1998).
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:0000256|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:0000256|HAMAP-Rule:MF_04000,
CC ECO:0000256|PIRNR:PIRNR003383};
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:0000256|HAMAP-
CC Rule:MF_04000}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147,
CC ECO:0000256|HAMAP-Rule:MF_04000}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- PTM: Phosphorylated. {ECO:0000256|HAMAP-Rule:MF_04000}.
CC -!- SIMILARITY: Belongs to the papillomaviridae E1 protein family.
CC {ECO:0000256|HAMAP-Rule:MF_04000, ECO:0000256|PIRNR:PIRNR003383}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04000}.
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DR EMBL; Y15173; CAA75451.1; -; Genomic_DNA.
DR Proteomes; UP000246682; Genome.
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; 3.40.1310.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.10.510; Zinc finger, large T-antigen D1 domain; 1.
DR HAMAP; MF_04000; PPV_E1; 1.
DR InterPro; IPR014015; Helicase_SF3_DNA-vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001177; PPV_DNA_helicase_E1_C.
DR InterPro; IPR014000; PPV_DNA_helicase_E1_N.
DR InterPro; IPR046832; PPV_E1_DBD.
DR InterPro; IPR046935; PPV_E1_DBD_sf.
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; PF20450; PPV_E1_DBD; 1.
DR Pfam; PF00524; PPV_E1_N; 1.
DR PIRSF; PIRSF003383; Rep_E1_papillomaV; 1.
DR SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51206; SF3_HELICASE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_04000};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_04000};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_04000};
KW Early protein {ECO:0000256|ARBA:ARBA00022518, ECO:0000256|HAMAP-
KW Rule:MF_04000};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_04000};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|HAMAP-
KW Rule:MF_04000};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_04000};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_04000};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_04000}.
FT DOMAIN 411..561
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51206"
FT MOTIF 78..80
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOTIF 90..99
FT /note="Nuclear export signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT BINDING 437..444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOD_RES 83
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOD_RES 91
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
SQ SEQUENCE 609 AA; 70277 MW; 0F70E6741E732C92 CRC64;
MADDKGTDPK EGCSEWFLDN EADCSDLEND LEQLFDENPQ SNISELIDDD EDVEQGNSRD
LFRLQEFEES AEQVQMLKRK YFSPKAVQQL SPRLQSLSIS PQQKSKRRLF EQDSGLELSG
CEQTLSNEVE DITTELEVPA VQPAEQGGQG LGNLHYKELM RCSNSRARLL SKVKEYFGVG
FYELARQYKS NKTCCRDWVI GAYGVREELL EGAKQLLLNH CSYVWINMNG IMSLFLLCFN
NAKSRETVGR LLMSMLDVQL LQLICEPPKL RSVVSALYWY KGSMDSSVYA HGTYPDWIVN
QTMLTHQAAA EAVQFDLSQM IQWAYDTDLT DEADIAYGYA KMAESDSNAR AWLAHNSQAK
FVRECAQMVR HYRRGEMRDM SISEWIHYRI EQVEGEGHWS EIVKFIRFQE INFILFLDAF
KQFLHGKPKK SCLLIYGPPD CGKSMFAMSL IRVLKGRVIS FVNAKSQFWL SPLAECKIGL
LDDATDPCWQ YIDAYLRNGI DGNIVSVDCK HKTPLQIRFP PLLITSNYNI KDNDKYRYLY
SRIVIFEFKH KFPFKEDGSP EFLLTDQSWK SFFKRLWSQL ELSDPEDEAD NGGTQRSFQC
TTRQIDGHL
//
