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Protein

Glutaredoxin-2

Gene

VACWR081

Organism
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Glutaredoxin necessary for virion morphogenesis and virus replication. Functions as a thiol-disulfide transfer protein between membrane-associated A2.5 and substrates L1 or F9. The complete pathway for formation of disulfide bonds in intracellular virion membrane proteins sequentially involves oxidation of E10, A2.5 and G4. Exhibit thioltransferase and dehydroascorbate reductase activities in vitro.4 Publications

GO - Biological processi

  1. oxidation-reduction process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-2
Gene namesi
Ordered Locus Names:VACWR081
ORF Names:G4L
OrganismiVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Taxonomic identifieri10254 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
ProteomesiUP000000344: Genome

Subcellular locationi

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131C → S: Complete loss of substrate oxidation. 1 Publication
Mutagenesisi16 – 161C → S: Partial loss of substrate oxidation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 124124Glutaredoxin-2PRO_0000141629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi13 ↔ 16Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer (Probable). Interacts with A2.5; this interaction involves formation of a transient disulfide-bonded intermediate, allowing disulfide bond transfer. Interacts with L1; this interaction involves formation of a transient disulfide-bonded intermediate, allowing disulfide bond transfer.1 PublicationCurated

Structurei

Secondary structure

1
124
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Helixi14 – 2411Combined sources
Turni25 – 295Combined sources
Beta strandi30 – 367Combined sources
Helixi46 – 483Combined sources
Helixi58 – 658Combined sources
Helixi66 – 694Combined sources
Beta strandi71 – 777Combined sources
Turni78 – 814Combined sources
Beta strandi82 – 854Combined sources
Helixi89 – 913Combined sources
Helixi99 – 1013Combined sources
Helixi104 – 11310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G2QX-ray2.50A/B/C1-124[»]
ProteinModelPortaliP68460.
SMRiP68460. Positions 1-121.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68460.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutaredoxin family.Curated

Keywords - Domaini

Redox-active center

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR008554. Glutaredoxin-like.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF05768. DUF836. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.

Sequencei

Sequence statusi: Complete.

P68460-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKNVLIIFGK PYCSICENVS DAVEELKSEY DILHVDILSF FLKDGDSSML
60 70 80 90 100
GDVKRGTLIG NFAAHLSNYI VSIFKYNPQT KQMAFVDINK SLDFTKTDKS
110 120
LVNLEILKSE IEKATYGVWP PVTE
Length:124
Mass (Da):13,987
Last modified:November 23, 2004 - v1
Checksum:iDFBE2D7B3A1A9CA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03399 Genomic DNA. Translation: AAB59814.1.
AY243312 Genomic DNA. Translation: AAO89360.1.
RefSeqiYP_232963.1. NC_006998.1.

Genome annotation databases

GeneIDi3707537.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03399 Genomic DNA. Translation: AAB59814.1.
AY243312 Genomic DNA. Translation: AAO89360.1.
RefSeqiYP_232963.1. NC_006998.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G2QX-ray2.50A/B/C1-124[»]
ProteinModelPortaliP68460.
SMRiP68460. Positions 1-121.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3707537.

Miscellaneous databases

EvolutionaryTraceiP68460.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR008554. Glutaredoxin-like.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF05768. DUF836. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic and molecular biological characterization of a vaccinia virus gene which renders the virus dependent on isatin-beta-thiosemicarbazone (IBT)."
    Meis R.J., Condit R.C.
    Virology 182:442-454(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb."
    Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Vaccinia virus G4L gene encodes a second glutaredoxin."
    Gvakharia B.O., Koonin E.K., Mathews C.K.
    Virology 226:408-411(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "A glutaredoxin, encoded by the G4L gene of vaccinia virus, is essential for virion morphogenesis."
    White C.L., Weisberg A.S., Moss B.
    J. Virol. 74:9175-9183(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Vaccinia virus G4L glutaredoxin is an essential intermediate of a cytoplasmic disulfide bond pathway required for virion assembly."
    White C.L., Senkevich T.G., Moss B.
    J. Virol. 76:467-472(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISULFIDE BOND, MUTAGENESIS OF CYS-13 AND CYS-16.
  6. "Complete pathway for protein disulfide bond formation encoded by poxviruses."
    Senkevich T.G., White C.L., Koonin E.V., Moss B.
    Proc. Natl. Acad. Sci. U.S.A. 99:6667-6672(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH A2.5, INTERACTION WITH L1.
  7. "The structure of G4, the poxvirus disulfide oxidoreductase essential for virus maturation and infectivity."
    Su H.P., Lin D.Y., Garboczi D.N.
    J. Virol. 80:7706-7713(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Entry informationi

Entry nameiGLRX2_VACCW
AccessioniPrimary (citable) accession number: P68460
Secondary accession number(s): P21025, Q76ZU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: January 7, 2015
This is version 61 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

External Data

Dasty 3

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 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.