ID A0A2P1HBM0_HPV16 Unreviewed; 649 AA. AC A0A2P1HBM0; DT 23-MAY-2018, integrated into UniProtKB/TrEMBL. DT 23-MAY-2018, sequence version 1. DT 03-JUL-2019, entry version 7. DE RecName: Full=Replication protein E1 {ECO:0000256|HAMAP-Rule:MF_04000, ECO:0000256|PIRNR:PIRNR003383, ECO:0000256|SAAS:SAAS01053043}; 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:AVN68973.1}; OS Human papillomavirus type 16. OC Viruses; Papillomaviridae; Firstpapillomavirinae; Alphapapillomavirus. OX NCBI_TaxID=333760 {ECO:0000313|EMBL:AVN68973.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:AVN68973.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCI_0573 {ECO:0000313|EMBL:AVN68973.1}; RA Mirabello L., Yeager M., Yu K., Clifford G., Xiao Y., Zhu B., RA Cullen M., Boland J., Wentzensen N., Nelson C., Raine-Bennett T., RA Zigui C., Bass S., Song L., Yang Q., Steinberg M., Burdett L., RA Dean M., Roberson D., Mitchell J., Lorey T., Franceschi S., Castle P., RA Walker J., Zuna R., Kreimer A., Beachler D., Hildesheim A., RA Gonzalez P., Porras C., Burk R., Schiffman M.; RT "HPV16 E7 Genetic Conservation Is Critical to Carcinogenesis."; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ATP-dependent DNA helicase required for initiation of CC viral DNA replication. It forms a complex with the viral E2 CC protein. The E1-E2 complex binds to the replication origin which CC contains binding sites for both proteins. During the initial step, CC a dimer of E1 interacts with a dimer of protein E2 leading to a CC complex that binds the viral origin of replication with high CC specificity. Then, a second dimer of E1 displaces the E2 dimer in CC an ATP-dependent manner to form the E1 tetramer. Following this, CC two E1 monomers are added to each half of the site, which results CC in the formation of two E1 trimers on the viral ori. Subsequently, CC two hexamers will be created. The double hexamer acts as a bi- CC directional helicase machinery and unwinds the viral DNA and then CC recruits the host DNA polymerase to start replication. CC {ECO:0000256|HAMAP-Rule:MF_04000, ECO:0000256|SAAS:SAAS01053033}. 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, ECO:0000256|SAAS:SAAS01120154}; CC -!- SUBUNIT: Can form hexamers. Interacts with E2 protein; this CC interaction increases E1 DNA binding specificity. Interacts with CC host DNA polymerase subunit POLA2. Interacts with host single CC stranded DNA-binding protein RPA1. Interacts with host TOP1; this CC interaction stimulates the enzymatic activity of TOP1. CC {ECO:0000256|HAMAP-Rule:MF_04000, ECO:0000256|SAAS:SAAS01053038}. CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|HAMAP- CC Rule:MF_04000, ECO:0000256|SAAS:SAAS01053029}. 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 ECO:0000256|SAAS:SAAS01053032}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04000}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MG847689; AVN68973.1; -; Genomic_DNA. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule. 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 Pfam; PF00519; PPV_E1_C; 1. DR Pfam; PF00524; PPV_E1_N; 1. DR PIRSF; PIRSF003383; Rep_E1_papillomaV; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS51206; SF3_HELICASE_1; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04000, KW ECO:0000256|PIRNR:PIRNR003383, ECO:0000256|SAAS:SAAS01105244}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_04000, KW ECO:0000256|PIRNR:PIRNR003383, ECO:0000256|SAAS:SAAS01105238}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_04000, KW ECO:0000256|PIRNR:PIRNR003383, ECO:0000256|SAAS:SAAS01053031}; KW Early protein {ECO:0000256|HAMAP-Rule:MF_04000, KW ECO:0000256|PIRNR:PIRNR003383}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_04000, KW ECO:0000256|PIRNR:PIRNR003383, ECO:0000256|SAAS:SAAS01053036}; KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04000, KW ECO:0000256|SAAS:SAAS01053030}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04000, KW ECO:0000256|PIRNR:PIRNR003383, ECO:0000256|SAAS:SAAS00150732}; KW Isopeptide bond {ECO:0000256|HAMAP-Rule:MF_04000}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04000, KW ECO:0000256|PIRNR:PIRNR003383, ECO:0000256|SAAS:SAAS01105243}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04000}; KW Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_04000}. FT DOMAIN 451 601 SF3 helicase. {ECO:0000259|PROSITE: FT PS51206}. FT REGION 186 352 DNA-binding region. {ECO:0000256|HAMAP- FT Rule:MF_04000}. FT MOTIF 87 89 Nuclear localization signal. FT {ECO:0000256|HAMAP-Rule:MF_04000}. FT MOTIF 106 115 Nuclear export signal. FT {ECO:0000256|HAMAP-Rule:MF_04000}. FT MOD_RES 93 93 Phosphoserine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04000}. FT MOD_RES 107 107 Phosphoserine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04000}. FT CROSSLNK 558 558 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT {ECO:0000256|HAMAP-Rule:MF_04000}. SQ SEQUENCE 649 AA; 72879 MW; 5831FC870B3973FE CRC64; MADPAGTNGE EGTGCNGWFY VEAVVEKKTG DAISDDENEN DSDTGEDLVD FIVNDNDYLT QAETETAHAL FTAQEAKQHR DAVQVLKRKY LGSPLSDISG CVDNNISPRL KAICIEKQSR AAKRRLFESE DSGYGNTEVE TQQMLQVEGR HETETPCSQY SGGSGGGCSQ YSSGSGGEGV SERHTICQTP LTNILNVLKT SNAKAAMLAK FKELYGVSFS ELVRPFKSNK STCCDWCIAA FGLTPSIADS IKTLLQQYCL YLHIQSLACS WGMVVLLLVR YKCGKNRETI EKLLSKLLCV SPMCMMIEPP KLRSTAAALY WYKTGISNIS EVYGDTPEWI QRQTVLQHSF NDCTFELSQM VQWAYDNDIV DDSEIAYKYA QLADTNSNAS AFLKSNSQAK IVKDCATMCR HYKRAXKXQM SMSQWIKYRC DRVDDGGDWK QIVMFLRYQG VEFMSFLTAL KRFLQGIPKK NCILLYGAXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXAXIGM LDDATVPCWN YIDDNLRNAL DGNLVSMDVK HRPLVQLKCP PLLITSNINA GTDSRWPYLH NRLVVFTFPN EFPFDENGNP VYELNDKNWK SFFSRTWSRL SLHEDEDKEN DGDSLPTFKC VSGQNTNTL //