ID   A0A2P1HBM0_HPV16        Unreviewed;       649 AA.
AC   A0A2P1HBM0;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   14-DEC-2022, entry version 20.
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:AVN68973.1};
OS   Human papillomavirus type 16.
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   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}.
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|HAMAP-Rule:MF_04000}.
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; 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: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; 1.10.10.510; -; 1.
DR   Gene3D; 3.40.1310.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
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; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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          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
//