ID C7U317_9PAPI Unreviewed; 662 AA.
AC C7U317;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 08-NOV-2023, entry version 67.
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:CBD35696.1};
OS Human papillomavirus 125.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus; Alphapapillomavirus 2.
OX NCBI_TaxID=673323 {ECO:0000313|EMBL:CBD35696.1, ECO:0000313|Proteomes:UP000153148};
RN [1] {ECO:0000313|EMBL:CBD35696.1, ECO:0000313|Proteomes:UP000153148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIBX9 {ECO:0000313|EMBL:CBD35696.1};
RX PubMed=21811601; DOI=10.1371/journal.pone.0022414;
RA Kovanda A., Kocjan B.J., Potonik M., Poljak M.;
RT "Characterization of Novel Cutaneous Human Papillomavirus Genotypes HPV-150
RT and HPV-151.";
RL PLoS ONE 6:e22529-e22529(2011).
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; FN547152; CBD35696.1; -; Genomic_DNA.
DR Proteomes; UP000153148; 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};
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 464..614
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51206"
FT REGION 32..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..365
FT /note="DNA-binding region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT REGION 638..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 88..90
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOTIF 110..119
FT /note="Nuclear export signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT COMPBIAS 39..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 490..497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOD_RES 94
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOD_RES 98
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOD_RES 111
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOD_RES 124
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT CROSSLNK 571
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
SQ SEQUENCE 662 AA; 74350 MW; 8F6B4CD5C21EAB4B CRC64;
MADTSGTEGD ECSEAERAGG WFFVEAIVDR RTGDKVSSDE DEDGDEEDGE DLVDFIDDRP
VGDGQEVAQE LLLQQAAADD DVAVNTVKRK FAPSPYFSPV CEHPSIENEL SPRLDAIKLG
RQTSKAKRRL FVPVNSGDGQ TQVDTESGPQ QVQDICKTSQ KDGRQNANEG SEKNVGGNGS
QEEERAGGDG EESQTQNVQT DKASCGVLAL LKASNLKATL LGKFKEQFGL GYNELVRHFK
SSKTVCMDWV VCVFGVYCSL AESIKTLIQP QCEYAHIQVL SCQWGMTVFM LLRYKRAKNR
ETVAKGLSTL LNVPESHMLI EPPKLRSAPA ALYWYKTSMS NCSEVYGETP EWIVRLTMVG
HALEEAQFSL SEMVQYAYDH DITDESTLAY DYALQADTDP NAAAFLASNC QAKYVKDACT
MCRHYKRGEQ ARMSMSEWIT FRGDKVQGDG DWKPIVQFLK YQNVEFIPFL CALKTFLQGI
PKKSCLVFYG PSDTGKSYFC MSLLRYMGGV VISYANSSSH FWLQPLADAK IGLLDDATSQ
CWYYIDTYLR NALDGSQICI DRKHRALLQL KCPPLLITTN INPLEDEKLK YLRSRVQVFT
FKNTFPLTAQ GEPLYTLNDQ NWKSFFRRLW ARLKLTDPDD EEEHGNPSEP FRCVPGQNSR
TV
//
