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Database: UniProt
Entry: A0A1G6UIY1_9RHOB
LinkDB: A0A1G6UIY1_9RHOB
Original site: A0A1G6UIY1_9RHOB 
ID   A0A1G6UIY1_9RHOB        Unreviewed;       236 AA.
AC   A0A1G6UIY1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Protein-disulfide isomerase {ECO:0000313|EMBL:SDD40676.1};
GN   ORFNames=SAMN05421538_101548 {ECO:0000313|EMBL:SDD40676.1};
OS   Paracoccus isoporae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=591205 {ECO:0000313|EMBL:SDD40676.1, ECO:0000313|Proteomes:UP000199344};
RN   [1] {ECO:0000313|EMBL:SDD40676.1, ECO:0000313|Proteomes:UP000199344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22220 {ECO:0000313|EMBL:SDD40676.1,
RC   ECO:0000313|Proteomes:UP000199344};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be required for disulfide bond formation in some
CC       proteins. {ECO:0000256|ARBA:ARBA00003565}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000256|ARBA:ARBA00005791}.
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DR   EMBL; FNAH01000001; SDD40676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6UIY1; -.
DR   STRING; 591205.SAMN05421538_101548; -.
DR   OrthoDB; 8478320at2; -.
DR   Proteomes; UP000199344; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   CDD; cd02972; DsbA_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR13887:SF14; CLPXP ADAPTER PROTEIN SPXH; 1.
DR   PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:SDD40676.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199344};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..236
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011643392"
FT   DOMAIN          14..162
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          29..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   236 AA;  25569 MW;  75F5D2475DC08B7F CRC64;
     MTFELRHLLT ASLFSAALSM PAFAQDSATQ ADDAETAAES SDAAESETAA QAEPQILDDV
     VLGDESAPLT IYEYASFTCP HCAAFHEDGF PQLKSEYIDT GKVRFIQRDV YFDQVGLWAG
     ILARCDEDKF YPVADMLMGG QDEWMGAKNG EELVANLRKI GAKAGMTAEQ IDACWADGDR
     VADLVATFQH NAAEDEINAT PTFMIGGEQV SNQPWTDLKA VIDEKLAEAE DAAPAE
//
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