ID A0A094L2C7_9GAMM Unreviewed; 248 AA.
AC A0A094L2C7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Protein-disulfide isomerase {ECO:0000313|EMBL:KFZ28778.1};
GN ORFNames=IDAT_06110 {ECO:0000313|EMBL:KFZ28778.1};
OS Pseudidiomarina atlantica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=1517416 {ECO:0000313|EMBL:KFZ28778.1, ECO:0000313|Proteomes:UP000053718};
RN [1] {ECO:0000313|EMBL:KFZ28778.1, ECO:0000313|Proteomes:UP000053718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A10513 {ECO:0000313|EMBL:KFZ28778.1,
RC ECO:0000313|Proteomes:UP000053718};
RA Du J., Lai Q., Shao Z.;
RT "Draft genome sequence of Idiomarina sp. MCCC 1A10513.";
RL Submitted (JUN-2014) 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:KFZ28778.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPIN01000006; KFZ28778.1; -; Genomic_DNA.
DR RefSeq; WP_051986611.1; NZ_JPIN01000006.1.
DR AlphaFoldDB; A0A094L2C7; -.
DR STRING; 1517416.IDAT_06110; -.
DR eggNOG; COG1651; Bacteria.
DR OrthoDB; 9780340at2; -.
DR Proteomes; UP000053718; Unassembled WGS sequence.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd03023; DsbA_Com1_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR PANTHER; PTHR35272:SF5; THIOREDOXIN-LIKE_FOLD DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:KFZ28778.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..248
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001907454"
FT DOMAIN 53..247
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 248 AA; 27547 MW; 81A640CAB9041141 CRC64;
MTFTKVSYLT AALALGIASL FAQPVVAQQL TAEQEQNLAN IEKLLRRNPD IIPSVAQSLE
QFVEQQSAQR KAFNNYHDWL YKNPSHPTLG AADAAHQIVV FTDYNCPYCK KLEPGLEALV
KKHPDVQVIN VYVPLRQQQV QGLATNSSHF ALDIWRSQRS AFTRAHALMM RKSGMHDAQS
LRQIAEATDT EQLLQPDPAS ARVIDSNMKA FQALGLRGTP SILIGQQIIP GYVVEAQLLQ
AVEQTFGL
//
