VE1_HPV11
ID VE1_HPV11 Reviewed; 649 AA.
AC P04014;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 03-AUG-2022, entry version 113.
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 11.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10580;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3008427; DOI=10.1016/0042-6822(86)90110-8;
RA Dartmann K., Schwarz E., Gissmann L., zur Hausen H.;
RT "The nucleotide sequence and genome organization of human papilloma virus
RT type 11.";
RL Virology 151:124-130(1986).
RN [2]
RP NUCLEAR EXPORT SIGNAL, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-89;
RP SER-93 AND SER-107.
RX PubMed=15564503; DOI=10.1128/jvi.78.24.13954-13965.2004;
RA Deng W., Lin B.Y., Jin G., Wheeler C.G., Ma T., Harper J.W., Broker T.R.,
RA Chow L.T.;
RT "Cyclin/CDK regulates the nucleocytoplasmic localization of the human
RT papillomavirus E1 DNA helicase.";
RL J. Virol. 78:13954-13965(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. {ECO:0000255|HAMAP-
CC Rule:MF_04000}.
CC -!- INTERACTION:
CC P04014; P07305: H1-0; Xeno; NbExp=2; IntAct=EBI-7014446, EBI-725224;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000,
CC ECO:0000269|PubMed:15564503}.
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; M14119; AAA46929.1; -; Genomic_DNA.
DR PIR; A03659; W1WL11.
DR SMR; P04014; -.
DR IntAct; P04014; 5.
DR MINT; P04014; -.
DR BindingDB; P04014; -.
DR ChEMBL; CHEMBL4953; -.
DR PRIDE; P04014; -.
DR BRENDA; 3.6.4.12; 10313.
DR Proteomes; UP000008222; 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; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0030911; F:TPR domain binding; IPI:BHF-UCL.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB.
DR GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
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 ATP-binding; DNA replication; DNA-binding; Early protein; Helicase;
KW Host nucleus; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..649
FT /note="Replication protein E1"
FT /id="PRO_0000133109"
FT DOMAIN 452..602
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 146..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..353
FT /note="DNA-binding region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOTIF 83..85
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOTIF 106..115
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000,
FT ECO:0000269|PubMed:15564503"
FT BINDING 478..485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 89
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 93
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 107
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT CROSSLNK 559
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MUTAGEN 89
FT /note="S->A: About 60% loss of nuclear localization."
FT /evidence="ECO:0000269|PubMed:15564503"
FT MUTAGEN 93
FT /note="S->A: About 60% loss of nuclear localization."
FT /evidence="ECO:0000269|PubMed:15564503"
FT MUTAGEN 107
FT /note="S->A: More than 80% loss of nuclear localization."
FT /evidence="ECO:0000269|PubMed:15564503"
SQ SEQUENCE 649 AA; 73530 MW; 6665BE1E55B265A8 CRC64;
MADDSGTENE GSGCTGWFMV EAIVEHTTGT QISEDEEEEV EDSGYDMVDF IDDRHITQNS
VEAQALFNRQ EADAHYATVQ DLKRKYLGSP YVSPISNVAN AVESEISPRL DAIKLTTQPK
KVKRRLFETR ELTDSGYGYS EVEAATQVEK HGDPENGGDG QERDTGRDIE GEGVEHREAE
AVDDSTREHA DTSGILELLK CKDIRSTLHG KFKDCFGLSF VDLIRPFKSD RTTCADWVVA
GFGIHHSIAD AFQKLIEPLS LYAHIQWLTN AWGMVLLVLI RFKVNKSRCT VARTLGTLLN
IPENHMLIEP PKIQSGVRAL YWFRTGISNA STVIGEAPEW ITRQTVIEHS LADSQFKLTE
MVQWAYDNDI CEESEIAFEY AQRGDFDSNA RAFLNSNMQA KYVKDCAIMC RHYKHAEMKK
MSIKQWIKYR GTKVDSVGNW KPIVQFLRHQ NIEFIPFLSK LKLWLHGTPK KNCIAIVGPP
DTGKSCFCMS LIKFLGGTVI SYVNSCSHFW LQPLTDAKVA LLDDATQPCW TYMDTYMRNL
LDGNPMSIDR KHRALTLIKC PPLLVTSNID ISKEEKYKYL HSRVTTFTFP NPFPFDRNGN
AVYELSDANW KCFFERLSSS LDIEDSEDEE DGSNSQAFRC VPGSVVRTL
