ID J4G0R1_9APHY Unreviewed; 584 AA.
AC J4G0R1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=FIBRA_01011 {ECO:0000313|EMBL:CCL99003.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCL99003.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCL99003.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCL99003.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; HE796910; CCL99003.1; -; Genomic_DNA.
DR RefSeq; XP_012178286.1; XM_012322896.1.
DR AlphaFoldDB; J4G0R1; -.
DR STRING; 599839.J4G0R1; -.
DR GeneID; 24093914; -.
DR HOGENOM; CLU_021868_1_1_1; -.
DR InParanoid; J4G0R1; -.
DR OrthoDB; 52245at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd02961; PDI_a_family; 2.
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; PTHR46426; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR PANTHER; PTHR46426:SF1; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..584
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003778024"
FT TRANSMEM 542..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..134
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 146..283
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 133..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 64900 MW; 4FE06AE18516E22E CRC64;
MLARLPYTLL ATALAVAVQA LPVDSTELTV LTPDNFESTI SEGVWFIEHF SPYCGHCRKF
LPTWTQLVEN NAKQADPGIR LAQVNCAING DLCSKNGVDG YPQMNLYRNG QFVESYGDSR
EYELLTAYLS SHAEPTSKPK LPPTPTPEPA PIPHAEEPSQ DGKYDPIPEP ARDLNPRGAV
LALTDKTFGD AIKEGTVFIK FYAPWCGHCK KLAPIWTQLA GKMQHKLTIA EVNCEAHDAL
CRNEGVTGFP MLVYYGPNGG GKTEYTGGRK LEQLKAFSEK VIGPAIQEVK YEDLPSIMSE
SPSLYLLLHP PSDSRTIREV LKASSVLFGS PPIYSSSSSF LYDYFSVQSN SAVILALKDH
DDIPAAVYRI THSADENSAL SSWLLRNRLP SSMELDADNF QEVMNAPHKP LVVLIATPKD
QMGVVSSAVQ KIARQWKDTK GDGAISFVWM DGEKWGKWLK SMYGIKADSL PRIVVANHAR
LVYYDKDQFG EDIQLTSTSI FSAIHGAAGG TIPYKHSENM VERMARYLNA KLTATETYVF
SYPWRTAFFI FLGIAVIILV FKRLFAADSD SREYSHMRKA DRLD
//