GenomeNet

Database: UniProt
Entry: A0A3B7MKN2_9BACT
LinkDB: A0A3B7MKN2_9BACT
Original site: A0A3B7MKN2_9BACT 
ID   A0A3B7MKN2_9BACT        Unreviewed;       367 AA.
AC   A0A3B7MKN2;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=AhpC/TSA family protein {ECO:0000313|EMBL:AXY73853.1};
GN   ORFNames=D3H65_07605 {ECO:0000313|EMBL:AXY73853.1};
OS   Paraflavitalea soli.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Paraflavitalea.
OX   NCBI_TaxID=2315862 {ECO:0000313|EMBL:AXY73853.1, ECO:0000313|Proteomes:UP000263900};
RN   [1] {ECO:0000313|EMBL:AXY73853.1, ECO:0000313|Proteomes:UP000263900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5GH32-13 {ECO:0000313|EMBL:AXY73853.1,
RC   ECO:0000313|Proteomes:UP000263900};
RA   Weon H.-Y., Heo J., Kwon S.-W.;
RT   "Genome sequencing of strain 6GH32-13.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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; CP032157; AXY73853.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B7MKN2; -.
DR   KEGG; pseg:D3H65_07605; -.
DR   OrthoDB; 750178at2; -.
DR   Proteomes; UP000263900; Chromosome.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR025380; DUF4369.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   Pfam; PF14289; DUF4369; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000263900};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..367
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017831583"
FT   DOMAIN          229..367
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   367 AA;  40764 MW;  AE1A1D38D58E80C7 CRC64;
     MTTKKKPVLA LLLAAAVGAL SWQKAATPDG FTLTGNVPDF KDSIVFLTYG TFDNTKIDSA
     IVSNGKFAFK GEVAEPLQGM LFSRNYRLRL DLFVDKGNVT VDGPIEDMKV TGSPVVNEYE
     VFNRAIMANR KWVNKIYTEA YEAKQAGDTT RAKGLEADGS KWYAYEYEIR KNYIKQHPAS
     PISVRELLMY VNNKTLAECT PMYTALDSTV MASAQGLELT KRMQLLNKIT TGKPALAFAQ
     ANVEGKTITL KSYKGKYVLL EFWASWCGPC RAENPNLRKQ VELFGSKGFN VLGVSLDKTK
     APWVQAIEKD GLTWPQVSDL KGWNNEIALL YGVKAVPANF LIDPTGTIIA QDLRGEALNQ
     KLKEIFK
//
DBGET integrated database retrieval system