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Protein

Glutaredoxin-1

Gene

grx1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase. Thioltransferase catalyzes cellular thiol-disulfide transhydrogenation reactions. It transfers reducing equivalents to cytosolic protein and nonprotein disulfides (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-1
Gene namesi
Name:grx1
ORF Names:SPAC4F10.20
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC4F10.20.
PomBaseiSPAC4F10.20. grx1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 101101Glutaredoxin-1PRO_0000141610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 28Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiO36032.

Interactioni

Protein-protein interaction databases

BioGridi279973. 2 interactions.
MINTiMINT-4673029.

Structurei

3D structure databases

ProteinModelPortaliO36032.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 10197GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glutaredoxin family.Curated
Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000095204.
InParanoidiO36032.
KOiK03676.
OMAiIAMHENG.
OrthoDBiEOG75F4SQ.
PhylomeDBiO36032.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O36032-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSVESFVDS AVADNDVVVF AKSYCPYCHA TEKVIADKKI KAQVYQIDLM
60 70 80 90 100
NNGDEIQSYL LKKTGQRTVP NIFIHQKHVG GNSDFQALFK KGELDSLFNT

A
Length:101
Mass (Da):11,261
Last modified:January 1, 1998 - v1
Checksum:i30557E19BF33E9BB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521N → D in AAF19628 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015167 mRNA. Translation: BAA28750.1.
AF121275 mRNA. Translation: AAD25391.1.
AF192764 Genomic DNA. Translation: AAF19628.1.
CU329670 Genomic DNA. Translation: CAB11722.1.
PIRiT38824.
RefSeqiNP_594763.1. NM_001020190.2.

Genome annotation databases

EnsemblFungiiSPAC4F10.20.1; SPAC4F10.20.1:pep; SPAC4F10.20.
GeneIDi2543556.
KEGGispo:SPAC4F10.20.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015167 mRNA. Translation: BAA28750.1.
AF121275 mRNA. Translation: AAD25391.1.
AF192764 Genomic DNA. Translation: AAF19628.1.
CU329670 Genomic DNA. Translation: CAB11722.1.
PIRiT38824.
RefSeqiNP_594763.1. NM_001020190.2.

3D structure databases

ProteinModelPortaliO36032.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279973. 2 interactions.
MINTiMINT-4673029.

Proteomic databases

MaxQBiO36032.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC4F10.20.1; SPAC4F10.20.1:pep; SPAC4F10.20.
GeneIDi2543556.
KEGGispo:SPAC4F10.20.

Organism-specific databases

EuPathDBiFungiDB:SPAC4F10.20.
PomBaseiSPAC4F10.20. grx1.

Phylogenomic databases

HOGENOMiHOG000095204.
InParanoidiO36032.
KOiK03676.
OMAiIAMHENG.
OrthoDBiEOG75F4SQ.
PhylomeDBiO36032.

Miscellaneous databases

NextBioi20804565.
PROiO36032.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "S.pombe glutaredoxin."
    Kawamukai M.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Characterization of cDNA encoding thioltransferase (glutaredoxin) from Schizosaccharomyces pombe."
    Kim H.-G., Cho Y.-W., Park E.-H., Lim C.-J.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Isolation and expression of the genomic DNA encoding thioltransferase (Glutaredoxin) from Schizosaccharomyces pombe."
    Cho Y.-W., Kim H.-G., Lim C.-J.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiGLRX1_SCHPO
AccessioniPrimary (citable) accession number: O36032
Secondary accession number(s): Q9US58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: November 11, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.