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Database: UniProt
Entry: A0A316EH98_9BACT
LinkDB: A0A316EH98_9BACT
Original site: A0A316EH98_9BACT 
ID   A0A316EH98_9BACT        Unreviewed;       376 AA.
AC   A0A316EH98;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:PWK22360.1};
GN   ORFNames=LV89_03425 {ECO:0000313|EMBL:PWK22360.1};
OS   Arcicella aurantiaca.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Arcicella.
OX   NCBI_TaxID=591202 {ECO:0000313|EMBL:PWK22360.1, ECO:0000313|Proteomes:UP000245489};
RN   [1] {ECO:0000313|EMBL:PWK22360.1, ECO:0000313|Proteomes:UP000245489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22214 {ECO:0000313|EMBL:PWK22360.1,
RC   ECO:0000313|Proteomes:UP000245489};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAY-2018) 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:PWK22360.1}.
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DR   EMBL; QGGO01000020; PWK22360.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316EH98; -.
DR   Proteomes; UP000245489; Unassembled WGS sequence.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR   CDD; cd02969; PRX_like1; 1.
DR   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR047262; PRX-like1.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR43640; OS07G0260300 PROTEIN; 1.
DR   PANTHER; PTHR43640:SF1; THIOREDOXIN-DEPENDENT PEROXIREDOXIN; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   4: Predicted;
KW   Cytochrome c-type biogenesis {ECO:0000256|ARBA:ARBA00022748};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245489}.
FT   DOMAIN          34..197
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          219..373
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   376 AA;  42210 MW;  9A411BD1323ED6FC CRC64;
     MNFSKLNVCI RKSLLLLIFL FIGNSIFATD VKTLEIGASA PDFSLRGTDG KTYNLNSFAS
     ANVLAIVFTC NHCPTAQAYE DRIIALANDY KAKGVTLIAV SPNDPKAIAL DELGYSDMSD
     SFEEMKIRVK EKGYTFPYLY DGETQKMSRA YGPIATPHLF IFDKNRKLQY VGRLDGSEKI
     GSANAEDARN AFDALLAGNP VATPVTKTFG CSTKWSEKSE WAVKAPLEWA KEPVDMDLID
     DKGIAELLAN KTDKVRLINV WATWCGPCVT ELPDFVNINR MYRRRDFEFI TISADKPDKK
     NKAQELLKKM QASGKNFIYN SENKYKLIEA IDPKWQGALP YTLLIAPNGK ILYRTQGSIV
     PQEMKRMIVE QVGRVY
//
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