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Database: UniProt
Entry: A0A2N5UTW0_9BASI
LinkDB: A0A2N5UTW0_9BASI
Original site: A0A2N5UTW0_9BASI 
ID   A0A2N5UTW0_9BASI        Unreviewed;       702 AA.
AC   A0A2N5UTW0;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=PCANC_18664 {ECO:0000313|EMBL:PLW47599.1}, PCASD_10150
GN   {ECO:0000313|EMBL:PLW41189.1};
OS   Puccinia coronata f. sp. avenae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW41189.1, ECO:0000313|Proteomes:UP000235392};
RN   [1] {ECO:0000313|Proteomes:UP000235388, ECO:0000313|Proteomes:UP000235392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12NC29 {ECO:0000313|EMBL:PLW47599.1}, and 12SD80
RC   {ECO:0000313|EMBL:PLW41189.1};
RA   Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA   Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA   Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT   "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT   Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:PLW41189.1}.
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DR   EMBL; PGCI01000092; PLW41189.1; -; Genomic_DNA.
DR   EMBL; PGCJ01000109; PLW47599.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5UTW0; -.
DR   STRING; 200324.A0A2N5UTW0; -.
DR   OrthoDB; 52245at2759; -.
DR   Proteomes; UP000235388; Unassembled WGS sequence.
DR   Proteomes; UP000235392; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd02961; PDI_a_family; 2.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
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   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:UP000235388};
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..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..702
FT                   /note="Thioredoxin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015083908"
FT   TRANSMEM        637..654
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..129
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          197..330
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          131..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   702 AA;  77696 MW;  1BA5BEE090743C34 CRC64;
     MVVLAALLSL LVRGVMGVQL HAGDQLNENS FDSSIQHGLW FIECYSPFCP HCKHFAPTWI
     ELVDKMKPRQ LDGLNMGQVD CIAQGDLCIR LDVDYYPQMK LYEDGKFIES YNGDKKVEAI
     AAYLEQKTEA YRSTHHQQQQ QQQYTDPAAP ATPAPVQGTP SSADDGKTHS ASSTPPDTTH
     TTTEQPGAHP HQTLEHPSVS PKKPTTTATP TGPASTHNPT GSVVTLDKHN WHAYTNPPSN
     PLPIFIQFQT AWCKECRTLA PVWDQVAHLL AKEANVAVLD CEAPENTDIC RAEHAVQFPS
     FVMYHDGTKV AYSGPKEASS MVEFAHKTIA TPGSLEINVR EFEDTLQKKR VFFLLLHSSR
     TPLWIIKAVE TVGKGFQGSA VILKSDSQTL YDRQELSNMK AYMLVFKESE PRAWAKLELE
     EDAGTGTGTV GAGERQQKLG TAIRHWMSVH SIGIQAELGP HNLHRLFNSG ARKLVVLSCL
     SGIVTSTASN NRTSSVPAVD HSNPKALLLR DEIRLWARQW RLSQIARAVD IPIDWVWVNS
     EVWAEWLYDS YGITLPPPSA EDPTKSSSII IVDPQHHVFY LRQENGRPIA FLPASVFQTL
     LAIEMNKLQG SLQGSLASRI AWRVQRLKHS LRMVTEPQWI LFWMVVVGVA GWWYKRRAGR
     SGGGYGGLSS SMPATASSSS SDPKPAFATV FGLVSNVPLK AD
//
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