ID A0A0P6WZU3_9SPHN Unreviewed; 223 AA.
AC A0A0P6WZU3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Thioredoxin-like fold domain-containing protein {ECO:0000259|Pfam:PF13462};
GN ORFNames=SZ64_08310 {ECO:0000313|EMBL:KPL68120.1};
OS Erythrobacter sp. SG61-1L.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL68120.1, ECO:0000313|Proteomes:UP000049978};
RN [1] {ECO:0000313|EMBL:KPL68120.1, ECO:0000313|Proteomes:UP000049978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG61-1L {ECO:0000313|EMBL:KPL68120.1,
RC ECO:0000313|Proteomes:UP000049978};
RA Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA Pandey G.;
RT "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL Appl. Environ. Microbiol. 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000256|ARBA:ARBA00005791}.
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:KPL68120.1}.
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DR EMBL; JXQC01000003; KPL68120.1; -; Genomic_DNA.
DR RefSeq; WP_054530385.1; NZ_JXQC01000003.1.
DR AlphaFoldDB; A0A0P6WZU3; -.
DR STRING; 1603897.SZ64_08310; -.
DR PATRIC; fig|1603897.4.peg.1573; -.
DR OrthoDB; 8478320at2; -.
DR Proteomes; UP000049978; Unassembled WGS sequence.
DR Gene3D; 1.10.40.110; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR35891; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR PANTHER; PTHR35891:SF2; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000049978};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..223
FT /note="Thioredoxin-like fold domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006132748"
FT DOMAIN 31..219
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13462"
SQ SEQUENCE 223 AA; 24365 MW; 6CB9C80FA48D3790 CRC64;
MKGLIRAGAV VGFALMSVGA APNWLVTVSK TDGGHLLGNP NAKVKLTTFE SYTCPHCADF
EKEAGAELRI SFVQSGKVSL EVRHALRDPV DLTAAMLTEC VAPGKFFATH QAIFRNFDQI
ARTLTTSTKA QQDRWYGQDK AAARRAIASD FGFYPIVASQ GLTRAQADQC LNNNALAKRL
AEQDRADEEK YNITGTPSFA INGVRLIATY QWSLLKPQLD ARL
//