VE1_HPV16
ID VE1_HPV16 Reviewed; 649 AA.
AC P03114; P03115; Q71BI5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Replication protein E1 {ECO:0000255|HAMAP-Rule:MF_04000};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_04000};
DE AltName: Full=ATP-dependent helicase E1 {ECO:0000255|HAMAP-Rule:MF_04000};
GN Name=E1 {ECO:0000255|HAMAP-Rule:MF_04000};
OS Human papillomavirus type 16.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=333760;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2990099; DOI=10.1016/0042-6822(85)90214-4;
RA Seedorf K., Krammer G., Durst M., Suhai S., Rowekamp W.G.;
RT "Human papillomavirus type 16 DNA sequence.";
RL Virology 145:181-185(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate European German 131;
RA Terai M., Fu L., Ma Z., Burk R.D.;
RT "Cloning and sequencing of non-European human papillomavirus (HPV) variant
RT complete genomes from cervicovaginal cells by an overlapping PCR method.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=1326651; DOI=10.1128/jvi.66.10.5949-5958.1992;
RA Del Vecchio A.M., Romanczuk H., Howley P.M., Baker C.C.;
RT "Transient replication of human papillomavirus DNAs.";
RL J. Virol. 66:5949-5958(1992).
RN [4]
RP FUNCTION, AND INTERACTION WITH PROTEIN E2 AND HOST POLA2.
RX PubMed=9696837; DOI=10.1128/jvi.72.9.7407-7419.1998;
RA Masterson P.J., Stanley M.A., Lewis A.P., Romanos M.A.;
RT "A C-terminal helicase domain of the human papillomavirus E1 protein binds
RT E2 and the DNA polymerase alpha-primase p68 subunit.";
RL J. Virol. 72:7407-7419(1998).
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:0000255|HAMAP-Rule:MF_04000, ECO:0000269|PubMed:1326651,
CC ECO:0000269|PubMed:9696837}.
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:0000255|HAMAP-Rule:MF_04000};
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:0000255|HAMAP-
CC Rule:MF_04000, ECO:0000269|PubMed:9696837}.
CC -!- INTERACTION:
CC P03114; P03120: E2; NbExp=3; IntAct=EBI-7387308, EBI-1779322;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000}.
CC -!- PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04000}.
CC -!- PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_04000}.
CC -!- MISCELLANEOUS: HPV16, in comparison to HPV types 6 and 11, is more
CC often associated with malignant genital cancers in humans.
CC -!- SIMILARITY: Belongs to the papillomaviridae E1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04000}.
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DR EMBL; K02718; AAA46936.1; -; Genomic_DNA.
DR EMBL; AF536179; AAQ10714.1; -; Genomic_DNA.
DR PIR; T10424; W1WLHS.
DR SMR; P03114; -.
DR BioGRID; 4263554; 2.
DR IntAct; P03114; 3.
DR MINT; P03114; -.
DR PRIDE; P03114; -.
DR Proteomes; UP000009251; Genome.
DR Proteomes; UP000106302; 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: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; 3.40.50.300; -; 1.
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 InterPro; IPR037102; Znf_lg_T-Ag_D1_dom_sf.
DR Pfam; PF00519; PPV_E1_C; 1.
DR Pfam; PF00524; PPV_E1_N; 1.
DR PIRSF; PIRSF003383; Rep_E1_papillomaV; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51206; SF3_HELICASE_1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA replication; DNA-binding; Early protein; Helicase;
KW Host nucleus; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..649
FT /note="Replication protein E1"
FT /id="PRO_0000133114"
FT DOMAIN 451..601
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 186..352
FT /note="DNA-binding region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 624..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 87..89
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOTIF 106..115
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT BINDING 477..484
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 93
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 107
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT CROSSLNK 558
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT CONFLICT 92
FT /note="V -> G (in Ref. 2; AAQ10714)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="M -> T (in Ref. 2; AAQ10714)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="S -> T (in Ref. 2; AAQ10714)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="I -> M (in Ref. 2; AAQ10714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 649 AA; 72939 MW; EA8B182711929AB5 CRC64;
MADPAGTNGE EGTGCNGWFY VEAVVEKKTG DAISDDENEN DSDTGEDLVD FIVNDNDYLT
QAETETAHAL FTAQEAKQHR DAVQVLKRKY LVSPLSDISG 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 HYKRAEKKQM
SMSQWIKYRC DRVDDGGDWK QIVMFLRYQG VEFMSFLTAL KRFLQGIPKK NCILLYGAAN
TGKSLFGMSL MKFLQGSVIC FVNSKSHFWL QPLADAKIGM LDDATVPCWN YIDDNLRNAL
DGNLVSMDVK HRPLVQLKCP PLLITSNINA GTDSRWPYLH NRLVVFTFPN EFPFDENGNP
VYELNDKNWK SFFSRTWSRL SLHEDEDKEN DGDSLPTFKC VSGQNTNTL
