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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi433 – 440ATPUniRule annotation8

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)DescriptionActionsGraphical viewLength
Mutagenesisi84 – 85KR → GG: About 95% loss of nuclear localization. 1 Publication2
Mutagenesisi109S → A: About 50% increase in replication of viral DNA. 1 Publication1
Mutagenesisi514K → R: Complete loss of sumoylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001330901 – 605Replication protein E1Add BLAST605

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei90Phosphoserine; by hostUniRule annotation1
Modified residuei94Phosphoserine; by hostUniRule annotation1
Modified residuei102Phosphothreonine; by host CDK11 Publication1
Modified residuei109Phosphoserine; by host1 Publication1
Cross-linki514Glycyl 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 interactors.
MINTiMINT-91530.

Structurei

Secondary structure

1605
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi161 – 171Combined sources11
Helixi175 – 177Combined sources3
Beta strandi189 – 198Combined sources10
Helixi201 – 212Combined sources12
Beta strandi215 – 225Combined sources11
Beta strandi228 – 241Combined sources14
Helixi243 – 254Combined sources12
Helixi258 – 260Combined sources3
Beta strandi261 – 264Combined sources4
Helixi271 – 280Combined sources10
Beta strandi283 – 285Combined sources3
Beta strandi287 – 290Combined sources4
Helixi294 – 299Combined sources6
Helixi313 – 322Combined sources10
Helixi328 – 337Combined sources10
Turni338 – 341Combined sources4
Helixi343 – 348Combined sources6
Helixi354 – 375Combined sources22
Helixi378 – 388Combined sources11
Helixi396 – 404Combined sources9
Helixi409 – 421Combined sources13
Beta strandi427 – 432Combined sources6
Beta strandi434 – 438Combined sources5
Helixi439 – 450Combined sources12
Beta strandi453 – 455Combined sources3
Helixi457 – 459Combined sources3
Helixi463 – 469Combined sources7
Beta strandi475 – 480Combined sources6
Helixi482 – 490Combined sources9
Helixi494 – 497Combined sources4
Beta strandi501 – 503Combined sources3
Beta strandi506 – 508Combined sources3
Beta strandi511 – 513Combined sources3
Beta strandi518 – 524Combined sources7
Turni526 – 528Combined sources3
Helixi530 – 535Combined sources6
Turni536 – 538Combined sources3
Beta strandi539 – 543Combined sources5
Beta strandi552 – 554Combined sources3
Helixi561 – 570Combined sources10
Turni572 – 576Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03116.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini407 – 557SF3 helicaseUniRule annotationAdd BLAST151

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni142 – 308DNA-binding regionUniRule annotationAdd BLAST167

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi84 – 86Nuclear localization signalUniRule annotation1 Publication3
Motifi105 – 108Nuclear localization signal1 Publication4

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. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-40903N.
IntActiP03116. 5 interactors.
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. 1 hit.
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...

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: November 30, 2016
This is version 101 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, Reference 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.