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=3.6.4.12; DE AltName: Full=ATP-dependent helicase E1; GN Name=E1; XX 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 -!- 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 -!- 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 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; 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 Nucleotide-binding KW Phosphoprotein case KW Ubl conjugation KW Isopeptide bond end case XX GO GO:0042025; C:host cell nucleus GO GO:0005524; F:ATP binding GO GO:0003678; F: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 # Revision 1.8 2022/11/19 //