P68460 (GLRX2_VACCW) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 55.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glutaredoxin-2 | ||||
| Gene names |
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| Organism | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) [Reference proteome] | ||||
| Taxonomic identifier | 10254 [NCBI] | ||||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Poxviridae › Chordopoxvirinae › Orthopoxvirus › Vaccinia virus | ||||
| Virus host | Bos taurus (Bovine) [TaxID: 9913] |
Protein attributes
| Sequence length | 124 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. Ref.3 Ref.4 Ref.5 Ref.6 |
| Subunit structure | 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. Ref.6 |
| Subcellular location | |
| Sequence similarities | Belongs to the glutaredoxin family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Cellular component | Host cytoplasm |
| Domain | Redox-active center |
| PTM | Disulfide bond |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 124 | 124 | Glutaredoxin-2 | PRO_0000141629 | ||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Disulfide bond | 13 ↔ 16 | Redox-active Ref.5 | ||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||
| Mutagenesis | 13 | 1 | C → S: Complete loss of substrate oxidation. Ref.5 | |||||||||||||||||||||||||||
| Mutagenesis | 16 | 1 | C → S: Partial loss of substrate oxidation. Ref.5 | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Beta strand | 3 – 9 | 7 | ||||||||||||||||||||||||||||
| Helix | 14 – 24 | 11 | ||||||||||||||||||||||||||||
| Turn | 25 – 29 | 5 | ||||||||||||||||||||||||||||
| Beta strand | 30 – 36 | 7 | ||||||||||||||||||||||||||||
| Helix | 46 – 48 | 3 | ||||||||||||||||||||||||||||
| Helix | 58 – 65 | 8 | ||||||||||||||||||||||||||||
| Helix | 66 – 69 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 71 – 77 | 7 | ||||||||||||||||||||||||||||
| Turn | 78 – 81 | 4 | ||||||||||||||||||||||||||||
| Beta strand | 82 – 85 | 4 | ||||||||||||||||||||||||||||
| Helix | 89 – 91 | 3 | ||||||||||||||||||||||||||||
| Helix | 99 – 101 | 3 | ||||||||||||||||||||||||||||
| Helix | 104 – 113 | 10 | ||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | J03399 Genomic DNA. Translation: AAB59814.1. AY243312 Genomic DNA. Translation: AAO89360.1. | ||||||||||||
| RefSeq | YP_232963.1. NC_006998.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P68460. | ||||||||||||
| SMR | P68460. Positions 1-121. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 3707537. | ||||||||||||
Phylogenomic databases | |||||||||||||
| ProtClustDB | PHA3075. | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 3.40.30.10. 1 hit. | ||||||||||||
| InterPro | IPR008554. Glutaredoxin-like. IPR012336. Thioredoxin-like_fold. [Graphical view] | ||||||||||||
| Pfam | PF05768. DUF836. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P68460. | ||||||||||||
Entry information
| Entry name | GLRX2_VACCW | ||||||||
| Accession | Primary (citable) accession number: P68460 Secondary accession number(s): P21025, Q76ZU1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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