UniProtKB - P03116 (VE1_BPV1)

BLAST

>sp|P03116|VE1_BPV1 Replication protein E1 OS=Bovine papillomavirus type 1 OX=337052 GN=E1 PE=1 SV=1
MANDKGSNWDSGLGCSYLLTEAECESDKENEEPGAGVELSVESDRYDSQDEDFVDNASVF
QGNHLEVFQALEKKAGEEQILNLKRKVLGSSQNSSGSEASETPVKRRKSGAKRRLFAENE
ANRVLTPLQVQGEGEGRQELNEEQAISHLHLQLVKSKNATVFKLGLFKSLFLCSFHDITR
LFKNDKTTNQQWVLAVFGLAEVFFEASFELLKKQCSFLQMQKRSHEGGTCAVYLICFNTA
KSRETVRNLMANTLNVREECLMLQPAKIRGLSAALFWFKSSLSPATLKHGALPEWIRAQT
TLNESLQTEKFDFGTMVQWAYDHKYAEESKIAYEYALAAGSDSNARAFLATNSQAKHVKD
CATMVRHYLRAETQALSMPAYIKARCKLATGEGSWKSILTFFNYQNIELITFINALKLWL
KGIPKKNCLAFIGPPNTGKSMLCNSLIHFLGGSVLSFANHKSHFWLASLADTRAALVDDA
THACWRYFDTYLRNALDGYPVSIDRKHKAAVQIKAPPLLVTSNIDVQAEDRYLYLHSRVQ
TFRFEQPCTDESGEQPFNITDADWKSFFVRLWGRLDLIDEEEDSEEDGDSMRTFTCSARN
TNAVD

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History
Entry version 115 (10 Oct 2018)
Sequence version 1 (21 Jul 1986)
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Protein

Replication protein E1

Gene

E1

Organism

Bovine papillomavirus type 1

Status

Reviewed-Annotation score: -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 key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	433 – 440	ATPUniRule annotation		8

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-UniRule
ATP-dependent DNA helicase activity Source: UniProtKB-UniRule
DNA binding Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

DNA replication Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Helicase, Hydrolase
Biological process	DNA replication
Ligand	ATP-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
Organismⁱ	Bovine papillomavirus type 1
Taxonomic identifierⁱ	337052 [NCBI]
Taxonomic lineageⁱ	Viruses › dsDNA viruses, no RNA stage › Papillomaviridae › Firstpapillomavirinae › Deltapapillomavirus
Virus hostⁱ	Bos taurus (Bovine) [TaxID: 9913]
Proteomesⁱ	UP000006567 Componentⁱ: Genome

Subcellular locationⁱ

Host nucleus
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_04000
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.

GO - Cellular componentⁱ

host cell nucleus Source: UniProtKB-SubCell

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Host nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	84 – 85	KR → GG: About 95% loss of nuclear localization. 1 Publication	2
Mutagenesisⁱ	109	S → A: About 50% increase in replication of viral DNA. 1 Publication	1
Mutagenesisⁱ	514	K → R: Complete loss of sumoylation. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000133090	1 – 605	Replication protein E1Add BLAST		605

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	90	Phosphoserine; by hostUniRule annotation	1
Modified residueⁱ	94	Phosphoserine; by hostUniRule annotation	1
Modified residueⁱ	102	Phosphothreonine; by host CDK11 Publication	1
Modified residueⁱ	109	Phosphoserine; by host1 Publication	1
Cross-linkⁱ	514	Glycyl 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

Proteomic databases

PRIDEⁱ	P03116

PRIDEⁱ

P03116

PTM databases

iPTMnetⁱ	P03116

iPTMnetⁱ

P03116

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

With	Entry	#Exp.	IntAct	Notes
UBE2I	P63279	2	EBI-7015985,EBI-80168	From Homo sapiens.

With

Entry

#Exp.

IntAct

Notes

UBE2I

P63279

EBI-7015985,EBI-80168

From Homo sapiens.

Protein-protein interaction databases

Database of interacting proteins More...DIPⁱ	DIP-40903N
ELMⁱ	P03116
IntActⁱ	P03116, 5 interactors
Molecular INTeraction database More...MINTⁱ	P03116

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	161 – 171	Combined sources	11
Helixⁱ	175 – 177	Combined sources	3
Beta strandⁱ	189 – 198	Combined sources	10
Helixⁱ	201 – 212	Combined sources	12
Beta strandⁱ	215 – 225	Combined sources	11
Beta strandⁱ	228 – 241	Combined sources	14
Helixⁱ	243 – 254	Combined sources	12
Helixⁱ	258 – 260	Combined sources	3
Beta strandⁱ	261 – 264	Combined sources	4
Helixⁱ	271 – 280	Combined sources	10
Beta strandⁱ	283 – 285	Combined sources	3
Beta strandⁱ	287 – 290	Combined sources	4
Helixⁱ	294 – 299	Combined sources	6
Helixⁱ	313 – 322	Combined sources	10
Helixⁱ	328 – 337	Combined sources	10
Turnⁱ	338 – 341	Combined sources	4
Helixⁱ	343 – 348	Combined sources	6
Helixⁱ	354 – 375	Combined sources	22
Helixⁱ	378 – 388	Combined sources	11
Helixⁱ	396 – 404	Combined sources	9
Helixⁱ	409 – 421	Combined sources	13
Beta strandⁱ	427 – 432	Combined sources	6
Beta strandⁱ	434 – 438	Combined sources	5
Helixⁱ	439 – 450	Combined sources	12
Beta strandⁱ	453 – 455	Combined sources	3
Helixⁱ	457 – 459	Combined sources	3
Helixⁱ	463 – 469	Combined sources	7
Beta strandⁱ	475 – 480	Combined sources	6
Helixⁱ	482 – 490	Combined sources	9
Helixⁱ	494 – 497	Combined sources	4
Beta strandⁱ	501 – 503	Combined sources	3
Beta strandⁱ	506 – 508	Combined sources	3
Beta strandⁱ	511 – 513	Combined sources	3
Beta strandⁱ	518 – 524	Combined sources	7
Turnⁱ	526 – 528	Combined sources	3
Helixⁱ	530 – 535	Combined sources	6
Turnⁱ	536 – 538	Combined sources	3
Beta strandⁱ	539 – 543	Combined sources	5
Beta strandⁱ	552 – 554	Combined sources	3
Helixⁱ	561 – 570	Combined sources	10
Turnⁱ	572 – 576	Combined sources	5

Show more details

3D structure databases

ProteinModelPortalⁱ	P03116
SMRⁱ	P03116
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P03116

EvolutionaryTraceⁱ

P03116

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	407 – 557	SF3 helicaseUniRule annotationAdd BLAST		151

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	142 – 308	DNA-binding regionUniRule annotationAdd BLAST		167

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	84 – 86	Nuclear localization signalUniRule annotation1 Publication		3
Motifⁱ	105 – 108	Nuclear localization signal1 Publication		4

Sequence similaritiesⁱ

Belongs to the papillomaviridae E1 protein family.UniRule annotation

Phylogenomic databases

Database of Orthologous Groups More...OrthoDBⁱ	VOG090000HF

OrthoDBⁱ

VOG090000HF

Family and domain databases

HAMAPⁱ	MF_04000 PPV_E1, 1 hit
InterProⁱ	View protein in InterPro IPR001177 DNA_helicase_E1_C_Papillomavir IPR014000 DNA_helicase_E1_N_Papillomavir IPR014015 Helicase_SF3_DNA-vir IPR027417 P-loop_NTPase IPR016393 Rep_E1_papillomaV
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00519 PPV_E1_C, 1 hit PF00524 PPV_E1_N, 1 hit
PIRSFⁱ	PIRSF003383 Rep_E1_papillomaV, 1 hit
SUPFAMⁱ	SSF52540 SSF52540, 1 hit
PROSITEⁱ	View protein in PROSITE PS51206 SF3_HELICASE_1, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P03116-1 [UniParc]FASTA Add 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

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X02346 Genomic DNA Translation: CAB46511.1
PIRⁱ	A03663 W1WLEB
NCBI Reference Sequences More...RefSeqⁱ	NP_056739.1, NC_001522.1

Genome annotation databases

GeneIDⁱ	1489019
KEGGⁱ	vg:1489019

Protein	Similar proteins		Species	Score	Length	Source
P03116	Replication protein E1		BPV2		604	UniRef90_P03116
Replication protein E1		Bos grunniens papillomavirus type 1		606
Replication protein E1		Bovine papillomavirus type 13		606
Replication protein E1		Bos taurus papillomavirus 13		606
Replication protein E1		BPV1		605
+13

Protein	Similar proteins		Species	Score	Length	Source
P03116	Replication protein E1		BPV2		604	UniRef50_P03116
Replication protein E1		BPV5		626
Replication protein E1		PAPVE		611
Replication protein E1		Bovine papillomavirus type 13		606
Replication protein E1		Bos taurus papillomavirus 13		606
+28

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X02346 Genomic DNA Translation: CAB46511.1
PIRⁱ	A03663 W1WLEB
RefSeqⁱ	NP_056739.1, NC_001522.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1F08	X-ray	1.90	A/B	159-303	[»]
	1KSX	X-ray	3.20	A/B/E/F/I/J/M/N	159-303	[»]
	1KSY	X-ray	3.05	A/B/C	159-309	[»]
	2GXA	X-ray	3.15	A/B/C/D/E/F/G/H/I/J/K/L	305-577	[»]
	2V9P	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L	301-605	[»]
	5A9K	electron microscopy	19.00	A/B/C/D/E/F	301-605	[»]
ProteinModelPortalⁱ	P03116
SMRⁱ	P03116
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

DIPⁱ	DIP-40903N
ELMⁱ	P03116
IntActⁱ	P03116, 5 interactors
MINTⁱ	P03116

PTM databases

iPTMnetⁱ	P03116

iPTMnetⁱ

P03116

Proteomic databases

PRIDEⁱ	P03116

PRIDEⁱ

P03116

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	1489019
KEGGⁱ	vg:1489019

Phylogenomic databases

OrthoDBⁱ	VOG090000HF

OrthoDBⁱ

VOG090000HF

Miscellaneous databases

EvolutionaryTraceⁱ	P03116

EvolutionaryTraceⁱ

P03116

Family and domain databases

HAMAPⁱ	MF_04000 PPV_E1, 1 hit
InterProⁱ	View protein in InterPro IPR001177 DNA_helicase_E1_C_Papillomavir IPR014000 DNA_helicase_E1_N_Papillomavir IPR014015 Helicase_SF3_DNA-vir IPR027417 P-loop_NTPase IPR016393 Rep_E1_papillomaV
Pfamⁱ	View protein in Pfam PF00519 PPV_E1_C, 1 hit PF00524 PPV_E1_N, 1 hit
PIRSFⁱ	PIRSF003383 Rep_E1_papillomaV, 1 hit
SUPFAMⁱ	SSF52540 SSF52540, 1 hit
PROSITEⁱ	View protein in PROSITE PS51206 SF3_HELICASE_1, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	VE1_BPV1
Accessionⁱ	P03116Primary (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:	October 10, 2018
	This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Viral Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P03116 (VE1_BPV1)

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Replication protein E1

E1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Keywords - Developmental stagei

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Keywords - Developmental stageⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ