ID S4TH63_9PAPI Unreviewed; 640 AA.
AC S4TH63;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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:AGB34177.1};
OS Eidolon helvum papillomavirus 1.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Dyoupsilonpapillomavirus; Dyoupsilonpapillomavirus 1.
OX NCBI_TaxID=1163701 {ECO:0000313|EMBL:AGB34177.1, ECO:0000313|Proteomes:UP000242725};
RN [1] {ECO:0000313|EMBL:AGB34177.1, ECO:0000313|Proteomes:UP000242725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Garcia-Perez R., Wibbelt G., Mengual-Chulia B., Bravo I.G.;
RT "Uncovering papillomavirus diversity within hosts of the order Chiroptera:
RT Eidolon helvum papillomavirus type 1.";
RL Submitted (MAY-2012) 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: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 -!- 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; JX123128; AGB34177.1; -; Genomic_DNA.
DR OrthoDB; 4795at10239; -.
DR Proteomes; UP000242725; Genome.
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};
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 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}; Reference proteome {ECO:0000313|Proteomes:UP000242725}.
FT DOMAIN 429..593
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51206"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 83..85
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOTIF 103..112
FT /note="Nuclear export signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469..476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOD_RES 89
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOD_RES 104
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
SQ SEQUENCE 640 AA; 72756 MW; A26DE9681301AB50 CRC64;
MADNNHSPQG TQSDPEEGAS GWFVVHEAEC IDGAEDDEWE NVFEASQGDY DFVDDASVNQ
GNILELFQQQ ELEQTETEIQ KLKRKFVESP QQPGRQETPA ETLSPKLQQL QLGSQRGRAK
KKLFEDSGNF SETPGSGDRA GSPFQGSRSP FQGSRNVPAH PGGAAAPVTD VTGGGSTTRT
DDTIRTILAS SNRYNCFLGL FKQLFGVSFG DLTRPFQSDK TCCEDWIGGV CGVNPMLYES
VKDQLSDICT YYFITRECTD TKSIVLLCVN LKHQKNRECF MKYLTGLLRV EANAIFLQPP
KRRSTPAALY FVNRGRSQMV HTAGPLPQWI SKLTLLEHQM NSEKAFCLSD MIQWALDNEY
CEESEIALHY AMLAEEDENA EAFLKSNSQV KFVKDCAQMV KHYKKAQMDK MTMSEWLDYR
CSKFTETPDG WREIVRFLRM QHIELFRFAG AMQRWLKKVP KKCTIVIYGP PDTGKSTFAM
NLTRFLGGRV VSFVNSQSQF WLAPLTEAKS GCIDDATAAF WDYSDTYLRN GLDGNPCSVD
RKHRTALQMH FPPLIITTNI DVTKEDRWKY LTSRLTIFTF EQKYKIDSTG KPLYDLTEGS
WTSFFNRFWS HLGLSDREDD GDRETRQKIK LFRGGNTETL
//
