ID T2A5L0_HPV68 Unreviewed; 640 AA.
AC T2A5L0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Replication protein E1 {ECO:0000256|HAMAP-Rule:MF_04000, ECO:0000256|PIRNR:PIRNR003383};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_04000, ECO:0000256|PIRNR:PIRNR003383};
DE AltName: Full=ATP-dependent helicase E1 {ECO:0000256|HAMAP-Rule:MF_04000};
GN Name=E1 {ECO:0000256|HAMAP-Rule:MF_04000,
GN ECO:0000313|EMBL:AGU90713.1};
OS Human papillomavirus 68.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus; Alphapapillomavirus 7.
OX NCBI_TaxID=45240 {ECO:0000313|EMBL:AGU90713.1, ECO:0000313|Proteomes:UP000136219};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AGU90713.1, ECO:0000313|Proteomes:UP000136219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Qv01017 {ECO:0000313|EMBL:AGU90713.1};
RX PubMed=23977318;
RA Chen Z., Schiffman M., Herrero R., Desalle R., Anastos K., Segondy M.,
RA Sahasrabuddhe V.V., Gravitt P.E., Hsing A.W., Burk R.D.;
RT "Evolution and Taxonomic Classification of Alphapapillomavirus 7 Complete
RT Genomes: HPV18, HPV39, HPV45, HPV59, HPV68 and HPV70.";
RL PLoS ONE 8:E72565-E72565(2013).
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:0000256|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:0000256|HAMAP-Rule:MF_04000,
CC ECO:0000256|PIRNR:PIRNR003383};
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:0000256|HAMAP-
CC Rule:MF_04000}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147,
CC ECO:0000256|HAMAP-Rule:MF_04000}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- PTM: Phosphorylated. {ECO:0000256|HAMAP-Rule:MF_04000}.
CC -!- PTM: Sumoylated. {ECO:0000256|HAMAP-Rule:MF_04000}.
CC -!- SIMILARITY: Belongs to the papillomaviridae E1 protein family.
CC {ECO:0000256|HAMAP-Rule:MF_04000, ECO:0000256|PIRNR:PIRNR003383}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04000}.
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DR EMBL; KC470269; AGU90713.1; -; Genomic_DNA.
DR Proteomes; UP000136219; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_04000}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_04000};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_04000};
KW Early protein {ECO:0000256|ARBA:ARBA00022518, ECO:0000256|HAMAP-
KW Rule:MF_04000};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_04000};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562, ECO:0000256|HAMAP-
KW Rule:MF_04000};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_04000};
KW Isopeptide bond {ECO:0000256|HAMAP-Rule:MF_04000};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_04000};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_04000}; Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_04000}.
FT DOMAIN 441..591
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51206"
FT REGION 141..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..342
FT /note="DNA-binding region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT COILED 58..92
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 86..88
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT BINDING 467..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOD_RES 92
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOD_RES 96
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOD_RES 101
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
SQ SEQUENCE 640 AA; 72319 MW; 298A88D1B7B0F66A CRC64;
MANCEGTNGD GTGCNGWFFV EAIVDKQTGD TVSEDEDENA TDTGSDMVDF IDDSTHICIQ
AERETAQVLL NMQEAQRDAQ RVRALKRKYT DSIESSPLAK SPLQELSLNV SSTQARQPAY
TVPDSGYGNM EVETNSEVTV APNINGEDGE NEGENGDSIR EDCSSVDSAI DSENQDPKSP
TTQLKVLLQC NNKQAAMLTE FKKVYGLSFN DLVRTFKSDK TTCTDWVAAI FGVNPTIAEG
FKTLIKQYAL YTHIQCLDTK TGILILMLIR YKCGKNRITV GKGLSTLLHV PDSCMLLQPP
KLRSPVAALY WYRTGISNIS EVCGDTPEWI KRLTIIQHGI DDSVFDLSDM VQWAFDNELT
DDSDIAFQYA MLADCNSNAA AFLKSNCQAK YVKDCATMCR HYKRAQKRQM TMPQWIKFRC
SKCDEGGDWR PIVQFLRYQG LEFITFLCAL KDFLKGTPKR NCIVIHGPPN TGKSYFCMSL
IQFLQGTIIS YVNSASHFWL EPLADAKIAM LDDATGTCWS YFDNYMRNAL DGNPISLDRK
HRHLIQIKCP PMLITSNTNP VEDNRWPYLH SRLTVFKFPN AFPFDQNRNP VYTINDKNWK
CFFEKTWCRL DLQQDEDEGD NDGNTFPTFK CVTGENIRTL
//
