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Q00216

- TIGA_ASPNG

UniProt

Q00216 - TIGA_ASPNG

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Protein

Protein disulfide-isomerase tigA

Gene

tigA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491NucleophileBy similarity
Sitei50 – 501Contributes to redox potential valueBy similarity
Sitei51 – 511Contributes to redox potential valueBy similarity
Active sitei52 – 521NucleophileBy similarity
Sitei115 – 1151Lowers pKa of C-terminal Cys of first active siteBy similarity
Active sitei169 – 1691NucleophileBy similarity
Sitei170 – 1701Contributes to redox potential valueBy similarity
Sitei171 – 1711Contributes to redox potential valueBy similarity
Active sitei172 – 1721NucleophileBy similarity
Sitei236 – 2361Lowers pKa of C-terminal Cys of second active siteBy similarity

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. response to stress Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Stress response

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase tigA (EC:5.3.4.1)
Gene namesi
Name:tigA
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 359340Protein disulfide-isomerase tigAPRO_0000034245Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 52Redox-activePROSITE-ProRule annotation
Disulfide bondi169 ↔ 172Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By stress, and tunicamycin.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ00216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 129110Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini131 – 250120Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi356 – 3594Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 2 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiCOG0526.

Family and domain databases

Gene3Di1.20.1150.12. 1 hit.
3.40.30.10. 2 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR011679. ER_p29_C.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF07749. ERp29. 1 hit.
PF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 2 hits.
TIGRFAMsiTIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00216-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVRLSNLVSC LGLASAVTAA VVDLVPKNFD DVVLKSGKPA LVEFFAPWCG
60 70 80 90 100
HCKNLAPVYE ELGQAFAHAS DKVTVGKVDA DEHRDLGRKF GVQGFPTLKW
110 120 130 140 150
FDGKSDEPED YKGGRDLESL SSFISEKTGV KPRGPKKEPS KVEMLNDATF
160 170 180 190 200
KGAVGGDNDV LVAFTAPWCG HCKNLAPTWE ALANDFVLEP NVVIAKVDAD
210 220 230 240 250
AENGKATARE QGVSGYPTIK FFPKGSTESV PYEGARSEQA FIDFLNEKTG
260 270 280 290 300
THRTVGGGLD TKAGTIASLD ELIASTSAAD LAAAVKKAAT ELKDKYAQYY
310 320 330 340 350
VKVADKLSQN AEYAAKELAR LEKILAKGGS APEKVDDLIS RSNILRKFVG

EEKEAKDEL
Length:359
Mass (Da):38,592
Last modified:November 1, 1996 - v1
Checksum:i346B64197BA37608
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98748 Genomic DNA. Translation: CAA67299.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98748 Genomic DNA. Translation: CAA67299.1 .

3D structure databases

ProteinModelPortali Q00216.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0526.

Family and domain databases

Gene3Di 1.20.1150.12. 1 hit.
3.40.30.10. 2 hits.
InterProi IPR005788. Disulphide_isomerase.
IPR011679. ER_p29_C.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF07749. ERp29. 1 hit.
PF00085. Thioredoxin. 2 hits.
[Graphical view ]
SUPFAMi SSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 2 hits.
TIGRFAMsi TIGR01126. pdi_dom. 2 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiTIGA_ASPNG
AccessioniPrimary (citable) accession number: Q00216
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3