ID A0A0D0CHF7_9AGAR Unreviewed; 597 AA.
AC A0A0D0CHF7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=GYMLUDRAFT_48733 {ECO:0000313|EMBL:KIK54363.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK54363.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK54363.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK54363.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN834816; KIK54363.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0CHF7; -.
DR HOGENOM; CLU_021868_1_1_1; -.
DR OrthoDB; 52245at2759; -.
DR Proteomes; UP000053593; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd02961; PDI_a_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45672; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1.
DR PANTHER; PTHR45672:SF3; THIOREDOXIN DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053593};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..597
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002208389"
FT TRANSMEM 554..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..138
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 143..266
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 134..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 65779 MW; 9A005C3D0B113A69 CRC64;
MTTLKLWQHL RNLPLILSLS LLCSALPVHS TELTPDNFSD SISDGVWFIE HFSPYCGHCR
AFAPTWEELV QKNSEGGEDP TGIKLAQVNC AVHGDLCNAN GVKGYPQMNI YKDGEFVETF
KGARELPRLT EFLKRHAPVT PTEEPEDEET ELETPGTNPN PTGSVIVLDD SNFDNVLSEG
PAFVKFYAPW CGHCKKLAPT WKNLAKSMQY KLTVAEVDCE AHKALCKTNG IEGFPTLHYF
AEGSKTEYSG SRKLERLREF AEKASEGGVK PTQADDLEKD VFEESLVYAL LYPSSDRKLV
SVLKPLFAPL LGSPAVYTVS DPPSSLTSRL SLPPSSWAIV SFKDHDFATP SAIYTSQTPS
SQLRHQSASL DEIKSWLSLH RLPTTSELTQ DSFQSIMNSP ARPLVVLAAV SSGTKDKVQA
RMEELGQKWR ARTGGSGMLT KGSKERPVVF AWMDVERWKD WMSSMYGIKS KGSASTELED
IDVVIADHKA LLYYKTDASG SPIKLSTSSS VFSTLEGIAQ DSIEAQNSEN FIERVARYLN
SKLQTLESYI INHPMHIVFL VIVGFVLVIM AARKALADDP IDGPGGGSAK NGKGRLD
//
