AC   MF_04000;
DC   Protein; auto
TR   HAMAP; MF_04000; -; 1; level=0
XX
Names: PPV_E1
XX
ID   VE1
DE   RecName: Full=Replication protein E1;
DE            EC=5.6.2.4;
DE   AltName: Full=ATP-dependent helicase E1;
DE   AltName: Full=DNA 3'-5' helicase E1;
GN   Name=E1;
XX
CC   -!- FUNCTION: ATP-dependent DNA 3'-5' helicase required for initiation of
CC       viral DNA replication. It forms a complex with the viral E2 protein.
CC       The E1-E2 complex binds to the replication origin which contains
CC       binding sites for both proteins. During the initial step, a dimer of E1
CC       interacts with a dimer of protein E2 leading to a complex that binds
CC       the viral origin of replication with high specificity. Then, a second
CC       dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form
CC       the E1 tetramer. Following this, two E1 monomers are added to each half
CC       of the site, which results in the formation of two E1 trimers on the
CC       viral ori. Subsequently, two hexamers will be created. The double
CC       hexamer acts as a bi-directional helicase machinery and unwinds the
CC       viral DNA and then recruits the host DNA polymerase to start
CC       replication.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
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.
CC   -!- SUBCELLULAR LOCATION: Host nucleus.
CC   -!- PTM: Phosphorylated.
case <FTTag:Ubl>
CC   -!- PTM: Sumoylated.
end case
CC   -!- SIMILARITY: Belongs to the papillomaviridae E1 protein family.
XX
DR   PROSITE; PS51206; SF3_HELICASE_1; 1; trigger=yes
DR   Pfam; PF00519; PPV_E1_C; 1; trigger=no
DR   Pfam; PF20450; PPV_E1_DBD; 1; trigger=no
DR   Pfam; PF00524; PPV_E1_N; 1; trigger=no
DR   PIRSF; PIRSF003383; Rep_E1_papillomaV; 1; trigger=no
XX
KW   ATP-binding
KW   DNA replication
KW   DNA-binding
KW   Early protein
KW   Helicase
KW   Host nucleus
KW   Hydrolase
KW   Isomerase
KW   Nucleotide-binding
KW   Phosphoprotein
case <FTTag:Ubl>
KW   Ubl conjugation
KW   Isopeptide bond
end case
XX
GO   GO:0042025; C:host cell nucleus
GO   GO:0005524; F:ATP binding
GO   GO:0043138; F:3'-5' DNA helicase activity
GO   GO:0003677; F:DNA binding
GO   GO:0006260; P:DNA replication
XX
FT   From: VE1_BPV1 (P03116)
FT   BINDING         433..440
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-x-x-x-x-G-K-S
FT   MOTIF           84..86
FT                   /note="Nuclear localization signal"
FT   Condition: K-R-K
FT   REGION          142..308
FT                   /note="DNA-binding region"
FT   MOD_RES         102
FT                   /note="Phosphothreonine; by host"
FT   Condition: T
FT   MOD_RES         109
FT                   /note="Phosphoserine; by host"
FT   Condition: S
FT   CROSSLNK        514
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT   Tag: Ubl; Condition: K
FT   From: VE1_HPV11 (P04014)
FT   MOTIF           106..115
FT                   /note="Nuclear export signal"
FT   Optional; Condition: [LIV]-x-x-x-[LIV]-x-x-[LIV]-x-[LIV]
FT   MOD_RES         89
FT                   /note="Phosphoserine; by host"
FT   Optional; Condition: S
FT   MOD_RES         93
FT                   /note="Phosphoserine; by host"
FT   Optional; Condition: S
FT   MOD_RES         107
FT                   /note="Phosphoserine; by host"
FT   Optional; Condition: S
XX
Size: 580-700;
Related: None;
Template: P03116; P04014;
Scope:
 Viruses; Papillomaviridae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Version: 12
# Last updated date: 2025-03-24
# Created date: 2015-10-29
//