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O17433 (1CPX_DIRIM) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-Cys peroxiredoxin

EC=1.11.1.15
Alternative name(s):
1-CysPxn
Thioredoxin peroxidase
OrganismDirofilaria immitis (Canine heartworm)
Taxonomic identifier6287 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeDirofilaria

Protein attributes

Sequence length235 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Thiol specific antioxidant.

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Cys-49 is the site of oxidation by H2O2. The oxidized intermediate might be Cys-SOH By similarity.

Sequence similarities

Belongs to the AhpC/TSA family. Rehydrin subfamily.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRedox-active center
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionperoxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

peroxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2352351-Cys peroxiredoxin
PRO_0000135106

Regions

Domain5 – 179175Thioredoxin

Sites

Active site491 By similarity

Sequences

Sequence LengthMass (Da)Tools
O17433 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: BCC198C87D88FD97

FASTA23526,342
        10         20         30         40         50         60 
MTKGILLGDK FPDFRAETNE GFIPSFYDWI GKDSWAILFS HPRDFTPVCT TELARLVQLA 

        70         80         90        100        110        120 
PEFNKRNVKL IGLSCDSAES HRKWVDDIMA VCKMKCNDGD TCCSGNKLPF PIIADENRFL 

       130        140        150        160        170        180 
ATELGMMDPD ERDENGNALT ARCVFIIGPE KTLKLSILYP ATTGRNFDEI LRVVDSLQLT 

       190        200        210        220        230 
AVKLVATPVD WKDGDDCVVL PTIDDTEAKK LFGEKINTIE LPSGKHYLRM VAHPK 

« Hide

References

[1]"1-Cys peroxidoxin from Dirofilaria immitis."
McGonigle S., James E.R.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF027387 mRNA. Translation: AAB83998.1.

3D structure databases

ProteinModelPortalO17433.
SMRO17433. Positions 5-234.
ModBaseSearch...

Protein family/group databases

PeroxiBase4935. Di1CysPrx.

Proteomic databases

PRIDEO17433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name1CPX_DIRIM
AccessionPrimary (citable) accession number: O17433
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: December 14, 2011
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families