ID A0A1I5Z2H8_9RHOB Unreviewed; 244 AA.
AC A0A1I5Z2H8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Protein-disulfide isomerase {ECO:0000313|EMBL:SFQ50661.1};
GN ORFNames=SAMN05421853_107183 {ECO:0000313|EMBL:SFQ50661.1};
OS Roseivivax halotolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=93684 {ECO:0000313|EMBL:SFQ50661.1, ECO:0000313|Proteomes:UP000243106};
RN [1] {ECO:0000313|Proteomes:UP000243106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10271 {ECO:0000313|Proteomes:UP000243106};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000256|ARBA:ARBA00005791}.
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DR EMBL; FOXV01000007; SFQ50661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5Z2H8; -.
DR STRING; 93684.SAMN05421853_107183; -.
DR Proteomes; UP000243106; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR13887:SF55; DISULFIDE BOND FORMATION PROTEIN D; 1.
DR PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:SFQ50661.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243106}.
FT DOMAIN 70..238
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13462"
SQ SEQUENCE 244 AA; 26609 MW; AC81F19C4106780C CRC64;
MTMTRMISAT ALAAVLGAGG FWAIERLGAP DTAEFELPGA AQAQDNADAG ESADAEGTET
EAAQADGGVQ EMTLGAEDAA VEVIEYASYT CPHCATFHQN VFDRIKENYV DTGDVKFTYR
EVYFDKYGMW ASLVARCGGN QERFFGITDM IYEQQSEWVR AGSDAAVADE LRRIGRVAGL
DGDQLESCLT DGDKLRTLVE WYRTNATEDG IQSTPSFVID GELHSNMNYD DFAALLDEKI
AEAE
//