ID A0A1Q9VW35_9MICO Unreviewed; 209 AA.
AC A0A1Q9VW35;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 08-NOV-2023, entry version 17.
DE SubName: Full=Redoxin {ECO:0000313|EMBL:OLT54220.1};
GN ORFNames=BJF88_09715 {ECO:0000313|EMBL:OLT54220.1};
OS Cellulosimicrobium sp. CUA-896.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Cellulosimicrobium.
OX NCBI_TaxID=1517881 {ECO:0000313|EMBL:OLT54220.1, ECO:0000313|Proteomes:UP000185790};
RN [1] {ECO:0000313|EMBL:OLT54220.1, ECO:0000313|Proteomes:UP000185790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CUA-896 {ECO:0000313|EMBL:OLT54220.1,
RC ECO:0000313|Proteomes:UP000185790};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT54220.1}.
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DR EMBL; MKKH01000009; OLT54220.1; -; Genomic_DNA.
DR RefSeq; WP_075827818.1; NZ_MKKH01000009.1.
DR AlphaFoldDB; A0A1Q9VW35; -.
DR OrthoDB; 9796554at2; -.
DR Proteomes; UP000185790; 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; IPR006311; TAT_signal.
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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000185790};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..209
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038894004"
FT DOMAIN 54..202
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 209 AA; 21111 MW; 3B59E4CF05255E04 CRC64;
MSPVARRRAL AASGLALAAG LALSACTAES GATTSGDDVV GQGYVSGDGS VRTWEAGDRG
EAVALTGTDY EGATVDTADW QGDVVVLNTW YAACAPCRAE APDLVALAEE RADDGVQVLG
INTTDEPGAA LAFQRTFDVP YPSIDDRSGE VVAQLSGTVP LQAVPSTVVL DREGRVAARV
IGLVEGSTLD ALVDDVVAED ATGDATAGG
//
