ID W9X2A4_9EURO Unreviewed; 319 AA.
AC W9X2A4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Thioredoxin {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O5_06054 {ECO:0000313|EMBL:EXJ71061.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ71061.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ71061.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ71061.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ71061.1}.
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DR EMBL; AMGX01000008; EXJ71061.1; -; Genomic_DNA.
DR RefSeq; XP_007744840.1; XM_007746650.1.
DR AlphaFoldDB; W9X2A4; -.
DR STRING; 1182543.W9X2A4; -.
DR GeneID; 19190767; -.
DR eggNOG; KOG0908; Eukaryota.
DR HOGENOM; CLU_072377_0_0_1; -.
DR OrthoDB; 45858at2759; -.
DR Proteomes; UP000019471; 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 Gene3D; 2.60.120.470; PITH domain; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR010400; PITH_dom.
DR InterPro; IPR037047; PITH_dom_sf.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR46115:SF5; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46115; THIOREDOXIN-LIKE PROTEIN 1; 1.
DR Pfam; PF06201; PITH; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51532; PITH; 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 Reference proteome {ECO:0000313|Proteomes:UP000019471}.
FT DOMAIN 1..110
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 130..319
FT /note="PITH"
FT /evidence="ECO:0000259|PROSITE:PS51532"
SQ SEQUENCE 319 AA; 35295 MW; 2DE3852C8811CCEE CRC64;
MSNLLVHIES TDQFSALLSS SKIVVADFYA DWCGPCKQIA PIFEKLAEQL SRPNQITFAK
IDTDKQQDIS RSYGIRALPT FVIFKNAQAV KFIQGADREG LSNAVKDLAN EANKIETGEG
SGNSNGDTWL GADLPRGYGD VTAQVDVVGL ELLNWDSEHG NARTLISGSK PKGQAEAKSD
WVESDTDEQL MLYLPFMSTL KIHSLHLTSL PGNTDDDTSP SRPKLLKIYT NRPRILGFDE
AEDTQVAQEI TLSDKDWDAK TGTAKIELRI VKFQNVYSLV LFVVESEGDN EKVRIDRIRV
IGETGEKRDG KIEKIAADD
//
