Serine/threonine-protein kinase US3 homolog - Varicella-zoster virus (strain Dumas) (HHV-3)

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P09251 (US03_VZVD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase US3 homolog

Alternative name(s):
Protein kinase ORF66
EC=2.7.11.1

Gene names

Name:

Organism

Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3) [Reference proteome]

Taxonomic identifier

10338 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Varicellovirus ›

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and inhibition of apoptosis. Phosphorylates proteins 24 and 27, two critical regulators of capsid budding from nucleus to endoplasmic reticulum, thereby facilitating virion egress. Modulates and redistributes host components of the nuclear envelope, including LMNA, emerin/EMD and the nuclear matrix protein MATR3. Phosphorylates envelope glycoprotein B (gB), probably to direct it to the cell surface. Promotes virus intracellular spread by restructuring host cell cytoskeleton. Blocks host apoptosis to extend cell survival and allow efficient viral replication. Promotes viral gene expression by phosphorylating host HDAC2 to reduce viral genome silencing By similarity. Downregulates class I major histocompatibility complex (MHC-I) surface expression. Additionally, phosphorylates IE62 and targets it to the cytoplasm. The nuclear exclusion of IE62 enables the packaging of abundant levels of IE62 into virions. Ref.5 Ref.6 Ref.7 Ref.8
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Host cytoplasm By similarity. Host nucleus By similarity.
Post-translational modification	Phosphorylated by ORF47; this phosphorylation regulates subsequent phosphorylation of proteins 24 and 27 by ORF66. Autophosphorylated By similarity. Ref.4
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Host-virus interaction Inhibition of host MHC class I molecule presentation by virus Inhibition of host adaptive immune response by virus Modulation of host cell apoptosis by virus Modulation of host chromatin by virus Viral immunoevasion
Cellular component	Host cytoplasm Host nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	modulation by virus of host apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW modulation by virus of host chromatin organization Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 393

393

Serine/threonine-protein kinase US3 homolog

PRO_0000086183

Regions

Domain

93 – 378

286

Protein kinase

Nucleotide binding

99 – 107

ATP By similarity

Sites

Active site

206

Proton acceptor By similarity

Binding site

122

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P09251 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 2396280DC40AFBF7
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FASTA

393

43,680

        10         20         30         40         50         60 
MNDVDATDTF VGQGKFRGAI STSPSHIMQT CGFIQQMFPV EMSPGIESED DPNYDVNMDI 

        70         80         90        100        110        120 
QSFNIFDGVH ETEAEASVAL CAEARVGINK AGFVILKTFT PGAEGFAFAC MDSKTCEHVV 

       130        140        150        160        170        180 
IKAGQRQGTA TEATVLRALT HPSVVQLKGT FTYNKMTCLI LPRYRTDLYC YLAAKRNLPI 

       190        200        210        220        230        240 
CDILAIQRSV LRALQYLHNN SIIHRDIKSE NIFINHPGDV CVGDFGAACF PVDINANRYY 

       250        260        270        280        290        300 
GWAGTIATNS PELLARDPYG PAVDIWSAGI VLFEMATGQN SLFERDGLDG NCDSERQIKL 

       310        320        330        340        350        360 
IIRRSGTHPN EFPINPTSNL RRQYIGLAKR SSRKPGSRPL WTNLYELPID LEYLICKMLS 

       370        380        390 
FDARHRPSAE VLLNHSVFQT LPDPYPNPME VGD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete DNA sequence of varicella-zoster virus." Davison A.J., Scott J.E. J. Gen. Virol. 67:1759-1816(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"DNA sequence of the US component of the varicella-zoster virus genome." Davison A.J. EMBO J. 2:2203-2209(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The herpesvirus protein kinase: a new departure in protein phosphorylation?" Leader D.P., Purves F.C. Trends Biochem. Sci. 13:244-246(1988) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[4]	"Nuclear accumulation of IE62, the varicella-zoster virus (VZV) major transcriptional regulatory protein, is inhibited by phosphorylation mediated by the VZV open reading frame 66 protein kinase." Kinchington P.R., Fite K., Turse S.E. J. Virol. 74:2265-2277(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION OF IE62.
[5]	"Virion association of IE62, the varicella-zoster virus (VZV) major transcriptional regulatory protein, requires expression of the VZV open reading frame 66 protein kinase." Kinchington P.R., Fite K., Seman A., Turse S.E. J. Virol. 75:9106-9113(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Phosphorylation of the varicella-zoster virus (VZV) major transcriptional regulatory protein IE62 by the VZV open reading frame 66 protein kinase." Eisfeld A.J., Turse S.E., Jackson S.A., Lerner E.C., Kinchington P.R. J. Virol. 80:1710-1723(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Downregulation of class I major histocompatibility complex surface expression by varicella-zoster virus involves open reading frame 66 protein kinase-dependent and -independent mechanisms." Eisfeld A.J., Yee M.B., Erazo A., Abendroth A., Kinchington P.R. J. Virol. 81:9034-9049(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"The alphaherpesvirus US3/ORF66 protein kinases direct phosphorylation of the nuclear matrix protein matrin 3." Erazo A., Yee M.B., Banfield B.W., Kinchington P.R. J. Virol. 85:568-581(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MATR3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X04370 Genomic DNA. Translation: CAA27949.1. X00208 Genomic DNA. Translation: CAA25031.1.
PIR	TVBE66. E27345.
RefSeq	NP_040188.1. NC_001348.1.
3D structure databases
ProteinModelPortal	P09251.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1487703.
Phylogenomic databases
ProtClustDB	PHA3212.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

US03_VZVD

Accession

Primary (citable) accession number: P09251

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents