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Protein

Protein disulfide-isomerase tigA

Gene

tigA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei49NucleophileBy similarity1
Sitei50Contributes to redox potential valueBy similarity1
Sitei51Contributes to redox potential valueBy similarity1
Active sitei52NucleophileBy similarity1
Sitei115Lowers pKa of C-terminal Cys of first active siteBy similarity1
Active sitei169NucleophileBy similarity1
Sitei170Contributes to redox potential valueBy similarity1
Sitei171Contributes to redox potential valueBy similarity1
Active sitei172NucleophileBy similarity1
Sitei236Lowers pKa of C-terminal Cys of second active siteBy similarity1

GO - Molecular functioni

  • protein disulfide isomerase activity Source: UniProtKB-EC
  • unfolded protein binding Source: ASPGD

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • protein folding Source: ASPGD
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

  • endoplasmic reticulum lumen Source: UniProtKB-SubCell
  • intracellular Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000003424520 – 359Protein disulfide-isomerase tigAAdd BLAST340

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi49 ↔ 52Redox-activePROSITE-ProRule annotation
Disulfide bondi169 ↔ 172Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ00216.

Expressioni

Inductioni

By stress, and tunicamycin.1 Publication

Interactioni

GO - Molecular functioni

  • unfolded protein binding Source: ASPGD

Protein-protein interaction databases

STRINGi5061.CADANGAP00013579.

Structurei

3D structure databases

ProteinModelPortaliQ00216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 129Thioredoxin 1PROSITE-ProRule annotationAdd BLAST110
Domaini131 – 250Thioredoxin 2PROSITE-ProRule annotationAdd BLAST120

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi356 – 359Prevents secretion from ERPROSITE-ProRule annotation4

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

eggNOGiKOG0191. Eukaryota.
COG0526. LUCA.

Family and domain databases

CDDicd00238. ERp29c. 1 hit.
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:
EMBLi
GenBanki
DDBJi
Links Updated
X98748 Genomic DNA. Translation: CAA67299.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98748 Genomic DNA. Translation: CAA67299.1.

3D structure databases

ProteinModelPortaliQ00216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00013579.

Proteomic databases

PaxDbiQ00216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0191. Eukaryota.
COG0526. LUCA.

Family and domain databases

CDDicd00238. ERp29c. 1 hit.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 102 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

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.