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UniProtKB/Swiss-Prot entry Q6FR39


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TRXB_CANGA
Primary accession number Q6FR39
Secondary accession numbers None
Integrated into Swiss-Prot on November 9, 2004
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 31)
Name and origin of the protein
Protein name Thioredoxin reductase
Synonym EC 1.8.1.9
Gene name
Name: TRR1
OrderedLocusNames: CAGL0I01166g
From
Candida glabrata (Yeast) (Torulopsis glabrata) [TaxID: 5478] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CR380955; CAG60242.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq XP_447305.1; -.
3D structure databases
ModBase Q6FR39.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004791; Molecular function: thioredoxin-disulfide reductase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019430; Biological process: removal of superoxide radicals (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000759; Adrndx_reductase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR000103; Pyridine_nuc-diS_OxRdtase_2.
IPR005982; Thioredox_reduct.
Graphical view of domain structure.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01292; TRX_reduct; 1.
PROSITE PS00573; PYRIDINE_REDOX_2; 1.
ProtoNet Q6FR39.
Genome annotation databases
GeneID 2889334; -.
KEGG cgr:CAGL0I01166g; -.
Phylogenomic databases
HOGENOM Q6FR39; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   319  319     Thioredoxin reductase. PRO_0000166762
NP_BIND   33    45  13     FAD (By similarity). 
NP_BIND   288   297  10     FAD (By similarity). 
DISULFID   142   145        Redox-active (By similarity). 
Sequence information
Length: 319 AA [This is the length of the unprocessed precursor] Molecular weight: 34386 Da [This is the MW of the unprocessed precursor] CRC64: 9E9919E212B08345 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNHKKVVIIG SGPAAHTAAI YLARAEIKPT MYEGMLANGI AAGGQLTTTT EIENFPGFPD 

        70         80         90        100        110        120 
GMTGSELMDR MRAQSTKFGT EIITETIAKV DLSSRPFKLW TEFNEDGEPI TTDAIVIATG 

       130        140        150        160        170        180 
ASAKRLHIPG EETYWQQGIS ACAVCDGAVP IFRNKPLAVI GGGDSACEEA QFLTKYGSKV 

       190        200        210        220        230        240 
YLIVRKDHLR ASTIMQRRAE QNDKIEILYN TVTLEAQGDG KLLNNLRIKN VKTNEETDLP 

       250        260        270        280        290        300 
VNGLFYAIGH TPATKIVEGQ VETDETGYIK TIPGSSLTSV PGVFAAGDVQ DSKYRQAITS 

       310 
AGSGCMAGLD AEKYLTELE 

Q6FR39 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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