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Database: UniProt
Entry: A0A2S2E0S2_9ALTE
LinkDB: A0A2S2E0S2_9ALTE
Original site: A0A2S2E0S2_9ALTE 
ID   A0A2S2E0S2_9ALTE        Unreviewed;       281 AA.
AC   A0A2S2E0S2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Protein disulfide-isomerase A3 {ECO:0000313|EMBL:AWL10880.1};
GN   ORFNames=HMF8227_00374 {ECO:0000313|EMBL:AWL10880.1};
OS   Saliniradius amylolyticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Saliniradius.
OX   NCBI_TaxID=2183582 {ECO:0000313|EMBL:AWL10880.1, ECO:0000313|Proteomes:UP000245728};
RN   [1] {ECO:0000313|EMBL:AWL10880.1, ECO:0000313|Proteomes:UP000245728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF8227 {ECO:0000313|EMBL:AWL10880.1,
RC   ECO:0000313|Proteomes:UP000245728};
RA   Kang H., Kang J., Cha I., Kim H., Joh K.;
RT   "Salinimonas sp. HMF8227 Genome sequencing and assembly.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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DR   EMBL; CP029347; AWL10880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S2E0S2; -.
DR   KEGG; salh:HMF8227_00374; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000245728; Chromosome.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02956; ybbN; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF14561; TPR_20; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 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   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Isomerase {ECO:0000313|EMBL:AWL10880.1};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245728};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..110
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   281 AA;  31642 MW;  67388B0B545F06AA CRC64;
     MDNIVDLTIE NFQQVLLEQS QSKLVIVDFW ADWCEACKTL MPVMEKLATE YGDKVILAKV
     NADEQQQIAM QFGVRSLPTV ILVKDGQPID GFAGAQSEGE IRAVLDKHLP KAEEEKLEQA
     RAALAEKDNE TAFKLAKEAH DLAPERADIK LVLIEAYINL GHIPQAKQLL ETIKLADQDA
     AYHSLKGRIE LAEQASETPE IKALQEKLQQ NPDDLEVKVQ LAVQLQQANR AEEALEFLLQ
     VLQKDMNFGE ARKLMMDTIN ALPDGDPLAS QYRRKMYSLM Y
//
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