ID F4P6P0_BATDJ Unreviewed; 609 AA.
AC F4P6P0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=BATDEDRAFT_26166 {ECO:0000313|EMBL:EGF79017.1};
OS Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF79017.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF79017.1, ECO:0000313|Proteomes:UP000007241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA Stajich J., Eisen M., Grigoriev I.V.;
RT "The draft genome of Batrachochytrium dendrobatidis.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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; GL882887; EGF79017.1; -; Genomic_DNA.
DR RefSeq; XP_006680331.1; XM_006680268.1.
DR AlphaFoldDB; F4P6P0; -.
DR STRING; 684364.F4P6P0; -.
DR GeneID; 18238977; -.
DR HOGENOM; CLU_021868_1_1_1; -.
DR InParanoid; F4P6P0; -.
DR OMA; IFVYFYD; -.
DR OrthoDB; 52245at2759; -.
DR Proteomes; UP000007241; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
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; 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:UP000007241};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..609
FT /note="Thioredoxin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003312836"
FT TRANSMEM 574..593
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..150
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 172..306
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 609 AA; 68452 MW; 995D952223525718 CRC64;
MPFNRLSLPC LLLALIASLF IHAAQAGGKI PKAVTEAYLR AEKEILHLEQ SSFQTKIQKG
NWMIFYGATW CGHCQKFTPT WLELQKKVET DFKDSNFHVG KVECTLNADL CEQIAGFPTV
YYYQDGKRVG DEVVDQELPD LLKFVKSHAW DKSGQPGLAN LKDAELNAGK PNIALDQSPM
EVLHAYAEQE IHPGADVNPT GLVTHMTRGT FASLTAERSW FVMFHAPWCG HCKTLAPIWD
QVAEELKGQV DIGKVNCDEE KDLMKRFNIK GFPTLVLINE PNAPIVYKGS RRLEDIKKFV
LDSITRPSFL PVTAKEIPDI ISKEEVAFYF AYDANVTDYI PFRMFQSVAK TVKPFAKLYV
SPEVQAFKIL HAEEGKPVLI AVRDGGLDSS VYPGEFAGDG STRTMLREWI MQERFPLVTK
LDTATQADIL ESNRFVALAL VNPDTPDGKG ALDHFKNSAK HWKNIAAAEK RNRVKFAWID
AKMYADYVFS VYSVKPMDLP VFIIANPAME QYYNEFADGK KYDSFAHVVV HDSINEVLDG
KGKAKTNQGT FSRSAKWVNR QFVRTVSIFV TNNIIVTVLI MGGCIMSLTY YAMNRKGGYQ
SVSSISKQE
//
