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Protein

Replication protein E1

Gene

E1

Organism
Bovine papillomavirus type 1
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication.UniRule annotation4 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi433 – 4408ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Replication protein E1UniRule annotation (EC:3.6.4.12UniRule annotation)
Alternative name(s):
ATP-dependent helicase E1UniRule annotation
Gene namesi
Name:E1UniRule annotation
OrganismiBovine papillomavirus type 1
Taxonomic identifieri10559 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePapillomaviridaeDeltapapillomavirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
Proteomesi
  • UP000006567 Componenti: Genome

Subcellular locationi

  • Host nucleus UniRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi84 – 852KR → GG: About 95% loss of nuclear localization. 1 Publication
Mutagenesisi109 – 1091S → A: About 50% increase in replication of viral DNA. 1 Publication
Mutagenesisi514 – 5141K → R: Complete loss of sumoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 605605Replication protein E1PRO_0000133090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei90 – 901Phosphoserine; by hostUniRule annotation
Modified residuei94 – 941Phosphoserine; by hostUniRule annotation
Modified residuei102 – 1021Phosphothreonine; by host CDK11 Publication
Modified residuei109 – 1091Phosphoserine; by host1 Publication
Cross-linki514 – 514Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)UniRule annotation1 Publication

Post-translational modificationi

Phosphorylated. Probably phosphorylated by host PKA and PKC at Ser-109. Phosphorylated by host CDK1 at Thr-102.UniRule annotation2 Publications
Sumoylated.UniRule annotation

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

PTM databases

iPTMnetiP03116.

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Can form hexamers. Interacts with E2 protein; this interaction increases E1 DNA binding specificity. Interacts with host DNA polymerase subunit POLA2. Interacts with host single stranded DNA-binding protein RPA1. Interacts with host TOP1; this interaction stimulates the enzymatic activity of TOP1.UniRule annotationBy similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UBE2IP632792EBI-7015985,EBI-80168From a different organism.

Protein-protein interaction databases

DIPiDIP-40903N.
IntActiP03116. 5 interactions.
MINTiMINT-91530.

Structurei

Secondary structure

1
605
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi161 – 17111Combined sources
Helixi175 – 1773Combined sources
Beta strandi189 – 19810Combined sources
Helixi201 – 21212Combined sources
Beta strandi215 – 22511Combined sources
Beta strandi228 – 24114Combined sources
Helixi243 – 25412Combined sources
Helixi258 – 2603Combined sources
Beta strandi261 – 2644Combined sources
Helixi271 – 28010Combined sources
Beta strandi283 – 2853Combined sources
Beta strandi287 – 2904Combined sources
Helixi294 – 2996Combined sources
Helixi313 – 32210Combined sources
Helixi328 – 33710Combined sources
Turni338 – 3414Combined sources
Helixi343 – 3486Combined sources
Helixi354 – 37522Combined sources
Helixi378 – 38811Combined sources
Helixi396 – 4049Combined sources
Helixi409 – 42113Combined sources
Beta strandi427 – 4326Combined sources
Beta strandi434 – 4385Combined sources
Helixi439 – 45012Combined sources
Beta strandi453 – 4553Combined sources
Helixi457 – 4593Combined sources
Helixi463 – 4697Combined sources
Beta strandi475 – 4806Combined sources
Helixi482 – 4909Combined sources
Helixi494 – 4974Combined sources
Beta strandi501 – 5033Combined sources
Beta strandi506 – 5083Combined sources
Beta strandi511 – 5133Combined sources
Beta strandi518 – 5247Combined sources
Turni526 – 5283Combined sources
Helixi530 – 5356Combined sources
Turni536 – 5383Combined sources
Beta strandi539 – 5435Combined sources
Beta strandi552 – 5543Combined sources
Helixi561 – 57010Combined sources
Turni572 – 5765Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F08X-ray1.90A/B159-303[»]
1KSXX-ray3.20A/B/E/F/I/J/M/N159-303[»]
1KSYX-ray3.05A/B/C159-309[»]
2GXAX-ray3.15A/B/C/D/E/F/G/H/I/J/K/L305-577[»]
2V9PX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L301-605[»]
5A9Kelectron microscopy19.00A/B/C/D/E/F301-605[»]
ProteinModelPortaliP03116.
SMRiP03116. Positions 159-303, 305-577.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03116.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini407 – 557151SF3 helicaseUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni142 – 308167DNA-binding regionUniRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi84 – 863Nuclear localization signalUniRule annotation1 Publication
Motifi105 – 1084Nuclear localization signal1 Publication

Sequence similaritiesi

Belongs to the papillomaviridae E1 protein family.UniRule annotation
Contains 1 SF3 helicase domain.UniRule annotation

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_04000. PPV_E1.
InterProiIPR001177. DNA_helicase_E1_C_Papillomavir.
IPR014000. DNA_helicase_E1_N_Papillomavir.
IPR014015. Helicase_SF3_DNA-vir.
IPR027417. P-loop_NTPase.
IPR016393. Rep_E1_papillomaV.
[Graphical view]
PfamiPF00519. PPV_E1_C. 1 hit.
PF00524. PPV_E1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003383. Rep_E1_papillomaV. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51206. SF3_HELICASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANDKGSNWD SGLGCSYLLT EAECESDKEN EEPGAGVELS VESDRYDSQD
60 70 80 90 100
EDFVDNASVF QGNHLEVFQA LEKKAGEEQI LNLKRKVLGS SQNSSGSEAS
110 120 130 140 150
ETPVKRRKSG AKRRLFAENE ANRVLTPLQV QGEGEGRQEL NEEQAISHLH
160 170 180 190 200
LQLVKSKNAT VFKLGLFKSL FLCSFHDITR LFKNDKTTNQ QWVLAVFGLA
210 220 230 240 250
EVFFEASFEL LKKQCSFLQM QKRSHEGGTC AVYLICFNTA KSRETVRNLM
260 270 280 290 300
ANTLNVREEC LMLQPAKIRG LSAALFWFKS SLSPATLKHG ALPEWIRAQT
310 320 330 340 350
TLNESLQTEK FDFGTMVQWA YDHKYAEESK IAYEYALAAG SDSNARAFLA
360 370 380 390 400
TNSQAKHVKD CATMVRHYLR AETQALSMPA YIKARCKLAT GEGSWKSILT
410 420 430 440 450
FFNYQNIELI TFINALKLWL KGIPKKNCLA FIGPPNTGKS MLCNSLIHFL
460 470 480 490 500
GGSVLSFANH KSHFWLASLA DTRAALVDDA THACWRYFDT YLRNALDGYP
510 520 530 540 550
VSIDRKHKAA VQIKAPPLLV TSNIDVQAED RYLYLHSRVQ TFRFEQPCTD
560 570 580 590 600
ESGEQPFNIT DADWKSFFVR LWGRLDLIDE EEDSEEDGDS MRTFTCSARN

TNAVD
Length:605
Mass (Da):68,190
Last modified:July 21, 1986 - v1
Checksum:iC8400B7B8F606E0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02346 Genomic DNA. Translation: CAB46511.1.
PIRiA03663. W1WLEB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02346 Genomic DNA. Translation: CAB46511.1.
PIRiA03663. W1WLEB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F08X-ray1.90A/B159-303[»]
1KSXX-ray3.20A/B/E/F/I/J/M/N159-303[»]
1KSYX-ray3.05A/B/C159-309[»]
2GXAX-ray3.15A/B/C/D/E/F/G/H/I/J/K/L305-577[»]
2V9PX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L301-605[»]
5A9Kelectron microscopy19.00A/B/C/D/E/F301-605[»]
ProteinModelPortaliP03116.
SMRiP03116. Positions 159-303, 305-577.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-40903N.
IntActiP03116. 5 interactions.
MINTiMINT-91530.

PTM databases

iPTMnetiP03116.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03116.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_04000. PPV_E1.
InterProiIPR001177. DNA_helicase_E1_C_Papillomavir.
IPR014000. DNA_helicase_E1_N_Papillomavir.
IPR014015. Helicase_SF3_DNA-vir.
IPR027417. P-loop_NTPase.
IPR016393. Rep_E1_papillomaV.
[Graphical view]
PfamiPF00519. PPV_E1_C. 1 hit.
PF00524. PPV_E1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003383. Rep_E1_papillomaV. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51206. SF3_HELICASE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The primary structure and genetic organization of the bovine papillomavirus type 1 genome."
    Chen E.Y., Howley P.M., Levinson A.D., Seeburg P.H.
    Nature 299:529-534(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Transient replication of BPV-1 requires two viral polypeptides encoded by the E1 and E2 open reading frames."
    Ustav M., Stenlung A.
    EMBO J. 10:449-457(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "The E1 protein of bovine papilloma virus 1 is an ATP-dependent DNA helicase."
    Yang L., Mohr I., Fouts E., Lim D.A., Nohaile M., Botchan M.
    Proc. Natl. Acad. Sci. U.S.A. 90:5086-5090(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "The E1 replication protein of bovine papillomavirus type 1 contains an extended nuclear localization signal that includes a p34cdc2 phosphorylation site."
    Lentz M.R., Pak D., Mohr I., Botchan M.R.
    J. Virol. 67:1414-1423(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-102, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 84-LYS--ARG-85.
  5. "Modulation of bovine papillomavirus DNA replication by phosphorylation of the viral E1 protein."
    Zanardi T.A., Stanley C.M., Saville B.M., Spacek S.M., Lentz M.R.
    Virology 228:1-10(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-109, MUTAGENESIS OF SER-109.
  6. "Characterization of the DNA-binding domain of the bovine papillomavirus replication initiator E1."
    Chen G., Stenlund A.
    J. Virol. 72:2567-2576(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, INTERACTION WITH PROTEIN E2.
  7. "SUMO-1 modification of bovine papillomavirus E1 protein is required for intranuclear accumulation."
    Rangasamy D., Woytek K., Khan S.A., Wilson V.G.
    J. Biol. Chem. 275:37999-38004(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION, FUNCTION, MUTAGENESIS OF LYS-514.
  8. "Recruitment of replication protein A by the papillomavirus E1 protein and modulation by single-stranded DNA."
    Loo Y.M., Melendy T.
    J. Virol. 78:1605-1615(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST RPA1.
  9. "Papillomavirus E1 protein binds to and stimulates human topoisomerase I."
    Clower R.V., Fisk J.C., Melendy T.
    J. Virol. 80:1584-1587(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST TOP1.
  10. "Crystal structure of the DNA binding domain of the replication initiation protein E1 from papillomavirus."
    Enemark E.J., Chen G., Vaughn D.E., Stenlund A., Joshua-Tor L.
    Mol. Cell 6:149-158(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 159-303.
  11. "Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex."
    Enemark E.J., Stenlund A., Joshua-Tor L.
    EMBO J. 21:1487-1496(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 159-309.
  12. "Mechanism of DNA translocation in a replicative hexameric helicase."
    Enemark E.J., Joshua-Tor L.
    Nature 442:270-275(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 305-577.
  13. "Papillomavirus E1 helicase assembly maintains an asymmetric state in the absence of DNA and nucleotide cofactors."
    Sanders C.M., Kovalevskiy O.V., Sizov D., Lebedev A.A., Isupov M.N., Antson A.A.
    Nucleic Acids Res. 35:6451-6457(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 301-605.
  14. "Structural basis for DNA strand separation by a hexameric replicative helicase."
    Chaban Y., Stead J.A., Ryzhenkova K., Whelan F., Lamber E.P., Antson A., Sanders C.M., Orlova E.V.
    Nucleic Acids Res. 43:8551-8563(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (19.00 ANGSTROMS) OF 301-605.

Entry informationi

Entry nameiVE1_BPV1
AccessioniPrimary (citable) accession number: P03116
Secondary accession number(s): Q9WMH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 8, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.