ID F8S574_HPV52 Unreviewed; 647 AA.
AC F8S574;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 08-NOV-2023, entry version 54.
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:AEI61592.1};
OS Human papillomavirus 52.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus; Alphapapillomavirus 9.
OX NCBI_TaxID=10618 {ECO:0000313|EMBL:AEI61592.1, ECO:0000313|Proteomes:UP000138961};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|Proteomes:UP000121450, ECO:0000313|Proteomes:UP000130986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Qv02124 {ECO:0000313|EMBL:AEI61584.1}, Qv02575
RC {ECO:0000313|EMBL:AEI61576.1}, Qv12377 {ECO:0000313|EMBL:AEI61568.1},
RC and Qv18359 {ECO:0000313|EMBL:AEI61592.1};
RX PubMed=21673791; DOI=10.1371/journal.pone.0020183;
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 Human Papillomavirus 16 (HPV16)-
RT Related Variant Genomes: HPV31, HPV33, HPV35, HPV52, HPV58 and HPV67.";
RL PLoS ONE 6:E20183-E20183(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; HQ537747; AEI61568.1; -; Genomic_DNA.
DR EMBL; HQ537748; AEI61576.1; -; Genomic_DNA.
DR EMBL; HQ537749; AEI61584.1; -; Genomic_DNA.
DR EMBL; HQ537750; AEI61592.1; -; Genomic_DNA.
DR Proteomes; UP000121450; Genome.
DR Proteomes; UP000130986; Genome.
DR Proteomes; UP000138961; Genome.
DR Proteomes; UP000163147; 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:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
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 447..597
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51206"
FT REGION 146..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..348
FT /note="DNA-binding region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT MOTIF 86..88
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT BINDING 473..480
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 106
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000"
SQ SEQUENCE 647 AA; 72968 MW; A0658A91A40D648F CRC64;
MEDPEGTEGE REGCTGWFEV EAIIEKQTGD NISEDEDENA YDSGTDLIDF IDDSNINNEQ
AEHEAARALF NAQEGEDDVH AVSAVKRKFT SSPESAGQDG VEKHGSSRAK HICVNTECVS
PKRKPCQVED SGYGNSEVEA QQMADQVDGQ NGDWQSNSSQ SSGVGASNSD VSCTSIEDNE
ENGNGTLKSI QNIMCENSIK TTVLFKFKET YGVSFMELVR PFKSNRSSCT DWCIIGMGVT
PSVAEGLKVL IQPYSIYAHL QCLTCDRGVL ILLLIRFKCG KNRLTVSKLM SQLLNIPETH
MVIEPPKLRS ATCALYWYRT GLSNISEVYG TTPEWIEQQT VLQHSFDNSI FDFGEMVQWA
YDHDITDDSD IAYKYAQLAD VNSNAAAFLK SNSQAKIVKD CATMCRHYKR AERKHMNIGQ
WIQYRCDRID DGGDWRPIVR FLRYQEIEFT AFLDAFKKFL KGIPKKNCLV LYGPANTGKS
YFGMSLIRFL SGCVISYVNS KSHFWLQPLT DAKVGMIDDV TPICWSYIDD YMRNALDGND
ISVDVKHRAL VQIKCPPLIL TTNTNAGTDP RWPYLHSRLV VFHFKNPFPF DENGNPIYEI
NNENWKSFFS RTWCKLDLIQ EEDKENDGVD TGTFKCSAGK NTRSIRS
//
