ID A0A197JP02_9FUNG Unreviewed; 105 AA.
AC A0A197JP02;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN ORFNames=K457DRAFT_115713 {ECO:0000313|EMBL:OAQ26211.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ26211.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ26211.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ26211.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|PIRNR:PIRNR000077}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV442069; OAQ26211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197JP02; -.
DR STRING; 1314771.A0A197JP02; -.
DR OrthoDB; 45858at2759; -.
DR Proteomes; UP000078512; Unassembled WGS sequence.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR46115:SF5; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46115; THIOREDOXIN-LIKE PROTEIN 1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000077-4};
KW Redox-active center {ECO:0000256|PIRSR:PIRSR000077-4};
KW Reference proteome {ECO:0000313|Proteomes:UP000078512}.
FT DOMAIN 1..105
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 30
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 33
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 24
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 31
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 32
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 30..33
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 105 AA; 11497 MW; 9ECCC1B32DD22C6C CRC64;
MVRAIQSTAE FNELIASGKK VIVDYHATWC GPCKVIAPKY EAFAKENEDI EFVKVDVDEL
GEVSAAAGIR AMPTFQTYHK GQKFGELLGA DVKKLQELIA TVHAA
//
