ID A0A0Q9EWD2_9GAMM Unreviewed; 209 AA.
AC A0A0Q9EWD2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:KRD68046.1};
GN ORFNames=ASE45_13900 {ECO:0000313|EMBL:KRD68046.1};
OS Lysobacter sp. Root96.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1736612 {ECO:0000313|EMBL:KRD68046.1, ECO:0000313|Proteomes:UP000050805};
RN [1] {ECO:0000313|EMBL:KRD68046.1, ECO:0000313|Proteomes:UP000050805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root96 {ECO:0000313|EMBL:KRD68046.1,
RC ECO:0000313|Proteomes:UP000050805};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD68046.1, ECO:0000313|Proteomes:UP000050805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root96 {ECO:0000313|EMBL:KRD68046.1,
RC ECO:0000313|Proteomes:UP000050805};
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 -!- 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:KRD68046.1}.
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DR EMBL; LMJN01000003; KRD68046.1; -; Genomic_DNA.
DR RefSeq; WP_055900916.1; NZ_LMJN01000003.1.
DR AlphaFoldDB; A0A0Q9EWD2; -.
DR STRING; 1736612.ASE45_13900; -.
DR OrthoDB; 9796554at2; -.
DR Proteomes; UP000050805; Unassembled WGS sequence.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
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; 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 SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000050805};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..209
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006371402"
FT DOMAIN 59..197
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 27..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 209 AA; 22005 MW; 1BC8BC3FC88A5424 CRC64;
MTLRRLAPIL ALSLLTVALA GCNKPAPTPE PKVEAPAPKP PVEAPAPAPA EPAAAEAAAA
KPGAVPELKL PTLDNGEFDL AAHRGKWVVV NFWATWCAPC LKEMPELSAM DAMREHIEVI
GLAYEEIDAA DMRAFLKKRP VVYPIAIVDT YDPPKAFDTP RGLPTTYLVG PDGKIVDKFM
GPVTATMIEG AIAKAGGPAA PAEAKPSRS
//
