VE1_BPV1
ID VE1_BPV1 Reviewed; 605 AA.
AC P03116; Q9WMH1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 132.
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 Bovine papillomavirus type 1.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC Deltapapillomavirus.
OX NCBI_TaxID=337052;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6289124; DOI=10.1038/299529a0;
RA Chen E.Y., Howley P.M., Levinson A.D., Seeburg P.H.;
RT "The primary structure and genetic organization of the bovine
RT papillomavirus type 1 genome.";
RL Nature 299:529-534(1982).
RN [2]
RP FUNCTION.
RX PubMed=1846806; DOI=10.1002/j.1460-2075.1991.tb07967.x;
RA Ustav M., Stenlung A.;
RT "Transient replication of BPV-1 requires two viral polypeptides encoded by
RT the E1 and E2 open reading frames.";
RL EMBO J. 10:449-457(1991).
RN [3]
RP CHARACTERIZATION.
RX PubMed=8389467; DOI=10.1073/pnas.90.11.5086;
RA Yang L., Mohr I., Fouts E., Lim D.A., Nohaile M., Botchan M.;
RT "The E1 protein of bovine papilloma virus 1 is an ATP-dependent DNA
RT helicase.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5086-5090(1993).
RN [4]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-102, NUCLEAR LOCALIZATION
RP SIGNAL, AND MUTAGENESIS OF 84-LYS--ARG-85.
RX PubMed=8382303; DOI=10.1128/jvi.67.3.1414-1423.1993;
RA Lentz M.R., Pak D., Mohr I., Botchan M.R.;
RT "The E1 replication protein of bovine papillomavirus type 1 contains an
RT extended nuclear localization signal that includes a p34cdc2
RT phosphorylation site.";
RL J. Virol. 67:1414-1423(1993).
RN [5]
RP PHOSPHORYLATION AT SER-109, AND MUTAGENESIS OF SER-109.
RX PubMed=9024804; DOI=10.1006/viro.1996.8375;
RA Zanardi T.A., Stanley C.M., Saville B.M., Spacek S.M., Lentz M.R.;
RT "Modulation of bovine papillomavirus DNA replication by phosphorylation of
RT the viral E1 protein.";
RL Virology 228:1-10(1997).
RN [6]
RP DNA-BINDING, AND INTERACTION WITH PROTEIN E2.
RX PubMed=9525573; DOI=10.1128/jvi.72.4.2567-2576.1998;
RA Chen G., Stenlund A.;
RT "Characterization of the DNA-binding domain of the bovine papillomavirus
RT replication initiator E1.";
RL J. Virol. 72:2567-2576(1998).
RN [7]
RP SUMOYLATION, FUNCTION, AND MUTAGENESIS OF LYS-514.
RX PubMed=11005821; DOI=10.1074/jbc.m007777200;
RA Rangasamy D., Woytek K., Khan S.A., Wilson V.G.;
RT "SUMO-1 modification of bovine papillomavirus E1 protein is required for
RT intranuclear accumulation.";
RL J. Biol. Chem. 275:37999-38004(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH HOST RPA1.
RX PubMed=14747526; DOI=10.1128/jvi.78.4.1605-1615.2004;
RA Loo Y.M., Melendy T.;
RT "Recruitment of replication protein A by the papillomavirus E1 protein and
RT modulation by single-stranded DNA.";
RL J. Virol. 78:1605-1615(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH HOST TOP1.
RX PubMed=16415033; DOI=10.1128/jvi.80.3.1584-1587.2006;
RA Clower R.V., Fisk J.C., Melendy T.;
RT "Papillomavirus E1 protein binds to and stimulates human topoisomerase I.";
RL J. Virol. 80:1584-1587(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 159-303.
RX PubMed=10949036; DOI=10.1016/s1097-2765(05)00016-x;
RA Enemark E.J., Chen G., Vaughn D.E., Stenlund A., Joshua-Tor L.;
RT "Crystal structure of the DNA binding domain of the replication initiation
RT protein E1 from papillomavirus.";
RL Mol. Cell 6:149-158(2000).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 159-309.
RX PubMed=11889054; DOI=10.1093/emboj/21.6.1487;
RA Enemark E.J., Stenlund A., Joshua-Tor L.;
RT "Crystal structures of two intermediates in the assembly of the
RT papillomavirus replication initiation complex.";
RL EMBO J. 21:1487-1496(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 305-577.
RX PubMed=16855583; DOI=10.1038/nature04943;
RA Enemark E.J., Joshua-Tor L.;
RT "Mechanism of DNA translocation in a replicative hexameric helicase.";
RL Nature 442:270-275(2006).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 301-605.
RX PubMed=17881379; DOI=10.1093/nar/gkm705;
RA Sanders C.M., Kovalevskiy O.V., Sizov D., Lebedev A.A., Isupov M.N.,
RA Antson A.A.;
RT "Papillomavirus E1 helicase assembly maintains an asymmetric state in the
RT absence of DNA and nucleotide cofactors.";
RL Nucleic Acids Res. 35:6451-6457(2007).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (19.00 ANGSTROMS) OF 301-605.
RX PubMed=26240379; DOI=10.1093/nar/gkv778;
RA Chaban Y., Stead J.A., Ryzhenkova K., Whelan F., Lamber E.P., Antson A.,
RA Sanders C.M., Orlova E.V.;
RT "Structural basis for DNA strand separation by a hexameric replicative
RT helicase.";
RL Nucleic Acids Res. 43:8551-8563(2015).
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:11005821,
CC ECO:0000269|PubMed:14747526, ECO:0000269|PubMed:16415033,
CC ECO:0000269|PubMed:1846806}.
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.
CC {ECO:0000250|UniProtKB:P03114, ECO:0000255|HAMAP-Rule:MF_04000,
CC ECO:0000269|PubMed:14747526, ECO:0000269|PubMed:16415033,
CC ECO:0000269|PubMed:9525573}.
CC -!- INTERACTION:
CC P03116; P63279: UBE2I; Xeno; NbExp=2; IntAct=EBI-7015985, EBI-80168;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000,
CC ECO:0000269|PubMed:8382303}.
CC -!- PTM: Phosphorylated. Probably phosphorylated by host PKA and PKC at
CC Ser-109. Phosphorylated by host CDK1 at Thr-102. {ECO:0000255|HAMAP-
CC Rule:MF_04000, ECO:0000269|PubMed:8382303, ECO:0000269|PubMed:9024804}.
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; X02346; CAB46511.1; -; Genomic_DNA.
DR PIR; A03663; W1WLEB.
DR RefSeq; NP_056739.1; NC_001522.1.
DR PDB; 1F08; X-ray; 1.90 A; A/B=159-303.
DR PDB; 1KSX; X-ray; 3.20 A; A/B/E/F/I/J/M/N=159-303.
DR PDB; 1KSY; X-ray; 3.05 A; A/B/C=159-309.
DR PDB; 2GXA; X-ray; 3.15 A; A/B/C/D/E/F/G/H/I/J/K/L=305-577.
DR PDB; 2V9P; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=301-605.
DR PDB; 5A9K; EM; 19.00 A; A/B/C/D/E/F=301-605.
DR PDB; 7APD; EM; 3.90 A; A/B/C/D/E/F=308-605.
DR PDBsum; 1F08; -.
DR PDBsum; 1KSX; -.
DR PDBsum; 1KSY; -.
DR PDBsum; 2GXA; -.
DR PDBsum; 2V9P; -.
DR PDBsum; 5A9K; -.
DR PDBsum; 7APD; -.
DR SMR; P03116; -.
DR DIP; DIP-40903N; -.
DR ELM; P03116; -.
DR IntAct; P03116; 5.
DR MINT; P03116; -.
DR iPTMnet; P03116; -.
DR GeneID; 1489019; -.
DR KEGG; vg:1489019; -.
DR EvolutionaryTrace; P03116; -.
DR Proteomes; UP000006567; 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 3D-structure; ATP-binding; DNA replication; DNA-binding; Early protein;
KW Helicase; Host nucleus; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..605
FT /note="Replication protein E1"
FT /id="PRO_0000133090"
FT DOMAIN 407..557
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 90..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..308
FT /note="DNA-binding region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT REGION 582..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 84..86
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000,
FT ECO:0000269|PubMed:8382303"
FT MOTIF 105..108
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:8382303"
FT COMPBIAS 591..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 433..440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 90
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 94
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000"
FT MOD_RES 102
FT /note="Phosphothreonine; by host CDK1"
FT /evidence="ECO:0000269|PubMed:8382303"
FT MOD_RES 109
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:9024804"
FT CROSSLNK 514
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04000,
FT ECO:0000269|PubMed:11005821"
FT MUTAGEN 84..85
FT /note="KR->GG: About 95% loss of nuclear localization."
FT /evidence="ECO:0000269|PubMed:8382303"
FT MUTAGEN 109
FT /note="S->A: About 50% increase in replication of viral
FT DNA."
FT /evidence="ECO:0000269|PubMed:9024804"
FT MUTAGEN 514
FT /note="K->R: Complete loss of sumoylation."
FT /evidence="ECO:0000269|PubMed:11005821"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:1F08"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1F08"
FT STRAND 189..198
FT /evidence="ECO:0007829|PDB:1F08"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:1F08"
FT STRAND 215..225
FT /evidence="ECO:0007829|PDB:1F08"
FT STRAND 228..241
FT /evidence="ECO:0007829|PDB:1F08"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:1F08"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1F08"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:1F08"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:1F08"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:1F08"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1F08"
FT HELIX 294..299
FT /evidence="ECO:0007829|PDB:1F08"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:2V9P"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:2V9P"
FT TURN 338..341
FT /evidence="ECO:0007829|PDB:2V9P"
FT HELIX 343..348
FT /evidence="ECO:0007829|PDB:2V9P"
FT HELIX 354..375
FT /evidence="ECO:0007829|PDB:2V9P"
FT HELIX 378..388
FT /evidence="ECO:0007829|PDB:2V9P"
FT HELIX 396..404
FT /evidence="ECO:0007829|PDB:2V9P"
FT HELIX 409..421
FT /evidence="ECO:0007829|PDB:2V9P"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:2V9P"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:2V9P"
FT HELIX 439..450
FT /evidence="ECO:0007829|PDB:2V9P"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:2V9P"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:2V9P"
FT HELIX 463..469
FT /evidence="ECO:0007829|PDB:2V9P"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:2V9P"
FT HELIX 482..490
FT /evidence="ECO:0007829|PDB:2V9P"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:2V9P"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:2GXA"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:2GXA"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:2GXA"
FT STRAND 518..524
FT /evidence="ECO:0007829|PDB:2V9P"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:2GXA"
FT HELIX 530..535
FT /evidence="ECO:0007829|PDB:2V9P"
FT TURN 536..538
FT /evidence="ECO:0007829|PDB:2V9P"
FT STRAND 539..543
FT /evidence="ECO:0007829|PDB:2V9P"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:2GXA"
FT HELIX 561..570
FT /evidence="ECO:0007829|PDB:2V9P"
FT TURN 572..576
FT /evidence="ECO:0007829|PDB:2V9P"
SQ SEQUENCE 605 AA; 68190 MW; C8400B7B8F606E0B CRC64;
MANDKGSNWD SGLGCSYLLT EAECESDKEN EEPGAGVELS VESDRYDSQD EDFVDNASVF
QGNHLEVFQA LEKKAGEEQI LNLKRKVLGS SQNSSGSEAS ETPVKRRKSG AKRRLFAENE
ANRVLTPLQV QGEGEGRQEL NEEQAISHLH LQLVKSKNAT VFKLGLFKSL FLCSFHDITR
LFKNDKTTNQ QWVLAVFGLA EVFFEASFEL LKKQCSFLQM QKRSHEGGTC AVYLICFNTA
KSRETVRNLM ANTLNVREEC LMLQPAKIRG LSAALFWFKS SLSPATLKHG ALPEWIRAQT
TLNESLQTEK FDFGTMVQWA YDHKYAEESK IAYEYALAAG SDSNARAFLA TNSQAKHVKD
CATMVRHYLR AETQALSMPA YIKARCKLAT GEGSWKSILT FFNYQNIELI TFINALKLWL
KGIPKKNCLA FIGPPNTGKS MLCNSLIHFL GGSVLSFANH KSHFWLASLA DTRAALVDDA
THACWRYFDT YLRNALDGYP VSIDRKHKAA VQIKAPPLLV TSNIDVQAED RYLYLHSRVQ
TFRFEQPCTD ESGEQPFNIT DADWKSFFVR LWGRLDLIDE EEDSEEDGDS MRTFTCSARN
TNAVD
