ID   A0A2P1HBM0_HPV16        Unreviewed;       649 AA.
AC   A0A2P1HBM0;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   16-JAN-2019, entry version 5.
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; dsDNA viruses, no RNA stage; Papillomaviridae;
OC   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}.
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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: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:SAAS00697081};
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
//