VE1_HPV54
ID VE1_HPV54 Reviewed; 633 AA.
AC Q81020;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 type 54.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=1671798;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Delius H.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
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; U37488; AAA79189.1; -; Genomic_DNA.
DR RefSeq; NP_043290.1; NC_001676.1.
DR SMR; Q81020; -.
DR PRIDE; Q81020; -.
DR GeneID; 1497434; -.
DR KEGG; vg:1497434; -.
DR Proteomes; UP000007665; 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; 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 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Early protein; Helicase;
KW Host nucleus; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Ubl conjugation.
FT CHAIN 1..633
FT /note="Replication protein E1"
FT /id="PRO_0000133149"
FT DOMAIN 434..584
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..335
FT /note="DNA-binding region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 608..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 84..86
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOTIF 107..116
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT COMPBIAS 154..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 460..467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 90
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 94
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 108
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT CROSSLNK 541
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
SQ SEQUENCE 633 AA; 71836 MW; D5214297199A6172 CRC64;
MADNQGTEEE GTGCNGWFFV EAIVERKTGD IISDDEPEDV EDSGLDMVDF IDNSVSQVEG
QENPQALLHA QQLQADVEAV QQLKRKYIGS PYVSPVANSE PCVEKDLSPR LGAISLGRRS
AKAKRRLFDK AQPPPNGHTD VEAAVEVNTE GTDETETDQV QTVSGETTTD SLGRQQITEL
IHNTNIRVAL FGMFKDLYGL SFMDLARPFK SDKTVCTDWV IAAFGIYHGI TDGFKTLLEP
HCLYGHIQWL TCRWGMVLLL LTRFKCGKNR LTVSKCLGML LNIPETQMLI DPPKLRTPAA
ALYWYRQGLS NASEIFGTPP EWLARQTVIE YSLADSQFDL SKMVQWAYDH NYIDDSIIAL
EYAKLADIDE NAAAFLGSNC QAKYVKDCGT MCRHYIRAQK MQMTMSQWIK HRCDLVEEEG
EWKEIVRFLR YQHVDFISFM IALKQFLQGI PKHNCILLYG PPDTGKSNFA MSLISFLGGV
VLSYVNSSSH FWLEPLADAK IAMLDDATTQ CWNYMDIYMR NALDGNPMCF DRKHRAMVQT
KCPPLIVTSN INASTDDRWR YLHSRVKCFC FPNRFPFDSN GNPVYDLSNK NWKSFFKRSW
SRLALNDNDN EEEENGDPSN TFRCVPGKAS RPI
