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Database: UniProt
Entry: VE1_HPV04
LinkDB: VE1_HPV04
Original site: VE1_HPV04 
ID   VE1_HPV04               Reviewed;         599 AA.
AC   Q07846;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   08-NOV-2023, entry version 97.
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 4.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Gammapapillomavirus; Gammapapillomavirus 1.
OX   NCBI_TaxID=10617;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8389082; DOI=10.1006/viro.1993.1320;
RA   Egawa K., Delius H., Matsukura T., Kawashima M., de Villiers E.M.;
RT   "Two novel types of human papillomavirus, HPV 63 and HPV 65: comparisons of
RT   their clinical and histological features and DNA sequences to other HPV
RT   types.";
RL   Virology 194:789-799(1993).
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   -!- 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; X70827; CAA50159.1; -; Genomic_DNA.
DR   RefSeq; NP_040891.1; NC_001457.1.
DR   SMR; Q07846; -.
DR   GeneID; 1489453; -.
DR   KEGG; vg:1489453; -.
DR   OrthoDB; 4795at10239; -.
DR   Proteomes; UP000009253; 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; 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; DNA replication; DNA-binding; Early protein; Helicase;
KW   Host nucleus; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..599
FT                   /note="Replication protein E1"
FT                   /id="PRO_0000133100"
FT   DOMAIN          402..552
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   REGION          124..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..303
FT                   /note="DNA-binding region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   REGION          575..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           78..80
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   MOTIF           92..101
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   COMPBIAS        580..599
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         428..435
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT   MOD_RES         84
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   CROSSLNK        509
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
SQ   SEQUENCE   599 AA;  68670 MW;  00FCF5F26B40AD91 CRC64;
     MADKGTDNFD LEGNNWYIVH EAECTDSIDT LDDLCDESND DSNISNLIDD DVVDQGNSLA
     LYNAQINEDC DNALAHLKRK YNKSPEQAVA ELSPQLQAVK ITPERHSKRR LFQDSGIFED
     EAENSLTQVE SESQAGPSSQ DGGGDINLLL LQSSNRRATM LAKFKEWYGV SYNEITRIYK
     SDKSCSDNWV IVIFRAAVEV LESSKIVLKQ HCTYIQVKIF GFSALYLVQF KSAKSRETVQ
     KLMCSILNIQ EYQMLCDPPK LRSVPTALYF YKHAMLTESS VFGQTPDWIA KQTLVSHQAA
     TTAETFELSR MVQWAYDNNY VDECDIAYHY AMYAEEDANA AAYLKSNNQV KHVRDCSTMV
     RMYKRYEMRD MSMSEWIYKC CDECSEEGDW KPISQFLKYQ GVNILSFLIV LKSFLKGIPK
     KNCIVIHGPP DTGKSLFCYS FIKFLKGKVV SYVNRSSHFW LQPLMDCKVG FMDDATYVCW
     TYIDQNLRNA LDGNPMCIDA KHRAPQQLKL PPMLITSNID IKQEQSLMYL HSRIQCFNFP
     NKMPILDDGS PMYTFTDGTW KSFFQKLGRQ LELTDPEEEN NGVPSRTFRC TSRSNSDSY
//
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