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Database: UniProt
Entry: A0A1M3ENJ7_9CELL
LinkDB: A0A1M3ENJ7_9CELL
Original site: A0A1M3ENJ7_9CELL 
ID   A0A1M3ENJ7_9CELL        Unreviewed;       203 AA.
AC   A0A1M3ENJ7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Redoxin {ECO:0000313|EMBL:OJV60460.1};
GN   ORFNames=BGO38_01750 {ECO:0000313|EMBL:OJV60460.1};
OS   Cellulomonas sp. 73-145.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1895739 {ECO:0000313|EMBL:OJV60460.1, ECO:0000313|Proteomes:UP000184491};
RN   [1] {ECO:0000313|EMBL:OJV60460.1, ECO:0000313|Proteomes:UP000184491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-145 {ECO:0000313|EMBL:OJV60460.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJV60460.1}.
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DR   EMBL; MKTI01000003; OJV60460.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3ENJ7; -.
DR   STRING; 1895739.BGO38_01750; -.
DR   Proteomes; UP000184491; Unassembled WGS sequence.
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; IPR036249; Thioredoxin-like_sf.
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   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
FT   DOMAIN          34..178
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   203 AA;  20004 MW;  34E54007B7996BC3 CRC64;
     MGTAACGGAA RPAGHPSDVV DQGYRSGDGS TTTWPVGQRK GPVTLSGTDY SGATQDVSAW
     RGDVVLLNTW YAACPPCRAE APTLVALANE DAAKGLKVLG INGTDAAGAA DAFVRQFAVP
     YPTIQDTGGS AIAALQGVVP VNAVPTTVLL DRQGKVAARI LGLADPSTLR TLVDSLLAEP
     GGSAATSGAT SGPSASTTAG AAG
//
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