VE1_HPV35
ID VE1_HPV35 Reviewed; 637 AA.
AC P27220;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 103.
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 35.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Alphapapillomavirus.
OX NCBI_TaxID=10587;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate 35H;
RX PubMed=8205838; DOI=10.1007/978-3-642-78487-3_2;
RA Delius H., Hofmann B.;
RT "Primer-directed sequencing of human papillomavirus types.";
RL Curr. Top. Microbiol. Immunol. 186:13-31(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1310198; DOI=10.1016/0042-6822(92)90045-q;
RA Marich J.E., Pontsler A.V., Rice S.M., McGraw K.A., Dubensky T.W.;
RT "The phylogenetic relationship and complete nucleotide sequence of human
RT papillomavirus type 35.";
RL Virology 186:770-776(1992).
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}.
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}.
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 -!- SIMILARITY: Belongs to the papillomaviridae E1 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04000}.
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DR EMBL; X74477; CAA52563.1; -; Genomic_DNA.
DR EMBL; M74117; AAA46968.1; -; Genomic_DNA.
DR PIR; A40824; W1WL35.
DR PIR; S36523; S36523.
DR SMR; P27220; -.
DR PRIDE; P27220; -.
DR Proteomes; UP000007711; Genome.
DR Proteomes; UP000113298; 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 3: Inferred from homology;
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..637
FT /note="Replication protein E1"
FT /id="PRO_0000133133"
FT DOMAIN 437..587
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 172..338
FT /note="DNA-binding region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
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 463..470
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 97
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 544
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT CONFLICT 31..34
FT /note="DPVS -> SSV (in Ref. 2; AAA46968)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..143
FT /note="QQ -> HE (in Ref. 2; AAA46968)"
FT /evidence="ECO:0000305"
FT CONFLICT 235..258
FT /note="ESLKTLIKPYCLYIHIQCLSCSWG -> NFKHITYVYIYNVYRVHGA (in
FT Ref. 2; AAA46968)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..281
FT /note="CAKNRTTIEKLLS -> VEKREQQLKTIDA (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 417..418
FT /note="EK -> AQ (in Ref. 2; AAA46968)"
FT /evidence="ECO:0000305"
FT CONFLICT 515..552
FT /note="WAYIDQYLRNALDGNPISLDVKHKALVQLKCPPLLITS -> GIYRPIFKKC
FT TRWKSYISFRCKALSIVHIMPTFTYYI (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="V -> E (in Ref. 2; AAA46968)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="D -> V (in Ref. 2; AAA46968)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 637 AA; 72123 MW; 3C694D4451791003 CRC64;
MADPAGTDEG EGTGCNGWFF VEAVVSRRTG DPVSEDENED DCDRGEDMVD FINDTDILNI
QAETETAQAL FHAQEEQTHK EAVQVLKRKY ASSPLSSVSL CVNNNISPRL KAICIENKNT
AAKRRLFELP DSGYGNSEVE IQQIQQVEGH DTVEQCSMGS GDSITSSSDE RHDETPTRDI
IQILKCSNAN AAMLAKFKEL FGISFTELIR PFKSDKSTCT DWCVAAFGIA PSVAESLKTL
IKPYCLYIHI QCLSCSWGMV ILALLRFKCA KNRTTIEKLL SKLLCISAAS MLIQPPKLRS
TPAALYWFKT AMSNISEVDG ETPEWIQRQT VLQHSFNDAI FDLSEMVQWA YDNDFIDDSD
IAYKYAQLAE TNSNACAFLK SNSQAKIVKD CATMCRHYKR AEKREMTMSQ WIKRRCEKVD
DDGDWRDIVR FLRYQQVDFV AFLSALKNFL HGVPKKNCIL IYGAPNTGKS LFGMSLMHFL
QGAIISYVNS KSHFWLQPLY DAKIAMLDDA TSPCWAYIDQ YLRNALDGNP ISLDVKHKAL
VQLKCPPLLI TSNINAGKDD RWPYLHSRVV VFTFHNEFPF DKNGNPVYGL NDKNWKSFFS
RTWCRLNLHE EEDKENDGDA FPAFKCVSGQ NTRTLRD
