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Q00216

- TIGA_ASPNG

UniProt

Q00216 - TIGA_ASPNG

Protein

Protein disulfide-isomerase tigA

Gene

tigA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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 lumen Source: UniProtKB-SubCell

    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

    MVRLSNLVSC LGLASAVTAA VVDLVPKNFD DVVLKSGKPA LVEFFAPWCG    50
    HCKNLAPVYE ELGQAFAHAS DKVTVGKVDA DEHRDLGRKF GVQGFPTLKW 100
    FDGKSDEPED YKGGRDLESL SSFISEKTGV KPRGPKKEPS KVEMLNDATF 150
    KGAVGGDNDV LVAFTAPWCG HCKNLAPTWE ALANDFVLEP NVVIAKVDAD 200
    AENGKATARE QGVSGYPTIK FFPKGSTESV PYEGARSEQA FIDFLNEKTG 250
    THRTVGGGLD TKAGTIASLD ELIASTSAAD LAAAVKKAAT ELKDKYAQYY 300
    VKVADKLSQN AEYAAKELAR LEKILAKGGS APEKVDDLIS RSNILRKFVG 350
    EEKEAKDEL 359
    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 1, 2014
    This is version 94 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