ID A0A2P1HBM0_HPV16 Unreviewed; 649 AA. AC A0A2P1HBM0; DT 23-MAY-2018, integrated into UniProtKB/TrEMBL. DT 23-MAY-2018, sequence version 1. DT 26-FEB-2020, entry version 11. 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, ECO:0000256|SAAS:SAAS01053039}; 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., Cullen M., RA Boland J., Wentzensen N., Nelson C., Raine-Bennett T., Zigui C., Bass S., RA Song L., Yang Q., Steinberg M., Burdett L., Dean M., Roberson D., RA Mitchell J., Lorey T., Franceschi S., Castle P., Walker J., Zuna R., RA Kreimer A., Beachler D., Hildesheim A., Gonzalez P., Porras C., Burk R., RA 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 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, 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 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, ECO:0000256|SAAS:SAAS01053038}. CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|HAMAP-Rule:MF_04000, CC 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 of CC 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: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 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, ECO:0000256|PIRNR:PIRNR003383, KW 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, ECO:0000256|PIRNR:PIRNR003383, KW 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 FT /note="SF3 helicase" FT /evidence="ECO:0000259|PROSITE:PS51206" FT REGION 186..352 FT /note="DNA-binding region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000" FT MOTIF 87..89 FT /note="Nuclear localization signal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000" FT MOTIF 106..115 FT /note="Nuclear export signal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000" FT MOD_RES 93 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000" FT MOD_RES 107 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04000" FT CROSSLNK 558 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="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 //