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Q00216 (TIGA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 92. 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:
Protein disulfide-isomerase tigA

EC=5.3.4.1
Gene names
Name:tigA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Catalyzes the rearrangement of -S-S- bonds in proteins.

Subcellular location

Endoplasmic reticulum lumen Potential.

Induction

By stress, and tunicamycin. Ref.1

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 359340Protein disulfide-isomerase tigA
PRO_0000034245

Regions

Domain20 – 129110Thioredoxin 1
Domain131 – 250120Thioredoxin 2
Motif356 – 3594Prevents secretion from ER Potential

Sites

Active site491Nucleophile By similarity
Active site521Nucleophile By similarity
Active site1691Nucleophile By similarity
Active site1721Nucleophile By similarity
Site501Contributes to redox potential value By similarity
Site511Contributes to redox potential value By similarity
Site1151Lowers pKa of C-terminal Cys of first active site By similarity
Site1701Contributes to redox potential value By similarity
Site1711Contributes to redox potential value By similarity
Site2361Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Disulfide bond49 ↔ 52Redox-active By similarity
Disulfide bond169 ↔ 172Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q00216 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 346B64197BA37608

FASTA35938,592
        10         20         30         40         50         60 
MVRLSNLVSC LGLASAVTAA VVDLVPKNFD DVVLKSGKPA LVEFFAPWCG HCKNLAPVYE 

        70         80         90        100        110        120 
ELGQAFAHAS DKVTVGKVDA DEHRDLGRKF GVQGFPTLKW FDGKSDEPED YKGGRDLESL 

       130        140        150        160        170        180 
SSFISEKTGV KPRGPKKEPS KVEMLNDATF KGAVGGDNDV LVAFTAPWCG HCKNLAPTWE 

       190        200        210        220        230        240 
ALANDFVLEP NVVIAKVDAD AENGKATARE QGVSGYPTIK FFPKGSTESV PYEGARSEQA 

       250        260        270        280        290        300 
FIDFLNEKTG THRTVGGGLD TKAGTIASLD ELIASTSAAD LAAAVKKAAT ELKDKYAQYY 

       310        320        330        340        350 
VKVADKLSQN AEYAAKELAR LEKILAKGGS APEKVDDLIS RSNILRKFVG EEKEAKDEL 

« Hide

References

[1]"Isolation and characterisation of a novel stress-inducible PDI-family gene from Aspergillus niger."
Jeenes D.J., Pfaller R., Archer D.B.
Gene 193:151-156(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98748 Genomic DNA. Translation: CAA67299.1.

3D structure databases

ProteinModelPortalQ00216.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0526.

Family and domain databases

Gene3D1.20.1150.12. 1 hit.
3.40.30.10. 2 hits.
InterProIPR005788. Disulphide_isomerase.
IPR011679. ER_p29_C.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF07749. ERp29. 1 hit.
PF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMSSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 2 hits.
TIGRFAMsTIGR01126. pdi_dom. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTIGA_ASPNG
AccessionPrimary (citable) accession number: Q00216
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families