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Database: UniProt
Entry: A0A0Q4C311_9SPHN
LinkDB: A0A0Q4C311_9SPHN
Original site: A0A0Q4C311_9SPHN 
ID   A0A0Q4C311_9SPHN        Unreviewed;       245 AA.
AC   A0A0Q4C311;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Protein-disulfide isomerase {ECO:0000313|EMBL:KQM22158.1};
GN   ORFNames=ASE49_02325 {ECO:0000313|EMBL:KQM22158.1};
OS   Novosphingobium sp. Leaf2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM22158.1, ECO:0000313|Proteomes:UP000050893};
RN   [1] {ECO:0000313|EMBL:KQM22158.1, ECO:0000313|Proteomes:UP000050893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf2 {ECO:0000313|EMBL:KQM22158.1,
RC   ECO:0000313|Proteomes:UP000050893};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM22158.1, ECO:0000313|Proteomes:UP000050893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf2 {ECO:0000313|EMBL:KQM22158.1,
RC   ECO:0000313|Proteomes:UP000050893};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000256|ARBA:ARBA00005791}.
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:KQM22158.1}.
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DR   EMBL; LMJY01000001; KQM22158.1; -; Genomic_DNA.
DR   RefSeq; WP_056768364.1; NZ_LMJY01000001.1.
DR   AlphaFoldDB; A0A0Q4C311; -.
DR   STRING; 1735670.ASE49_02325; -.
DR   OrthoDB; 8478320at2; -.
DR   Proteomes; UP000050893; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.40.110; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:KQM22158.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050893};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..245
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006213204"
FT   DOMAIN          48..234
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13462"
SQ   SEQUENCE   245 AA;  26696 MW;  CCC83CC0B3F3D756 CRC64;
     MRIHARMKTA LRITALAACA VASIAAAPKH APAARGVNWI GVTAVTANGG HRLGNPDAPL
     KLVEYVSYTC PHCAHFTKES EPVLRMTLIP KGQISVTVVN LLRNPIDMTV AMLTNCGDPK
     RFFVRNNAFF ASQDQWLGTA VKFSAEQQKR WYQGEPPQRM RAMAADLGLY DKMATWGITR
     AQADACLGDK AILAKLKAQQ TEVQSLGLTS TPSFTLNGEV LDGHDWESVS KAITDKMAEQ
     REGST
//
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