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Database: UniProt
Entry: A0A3D9HXN8_9PROT
LinkDB: A0A3D9HXN8_9PROT
Original site: A0A3D9HXN8_9PROT 
ID   A0A3D9HXN8_9PROT        Unreviewed;       200 AA.
AC   A0A3D9HXN8;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Thioredoxin-like protein {ECO:0000313|EMBL:RED54272.1};
GN   ORFNames=DFP90_1011075 {ECO:0000313|EMBL:RED54272.1};
OS   Aestuariispira insulae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Kiloniellaceae; Aestuariispira.
OX   NCBI_TaxID=1461337 {ECO:0000313|EMBL:RED54272.1, ECO:0000313|Proteomes:UP000256845};
RN   [1] {ECO:0000313|EMBL:RED54272.1, ECO:0000313|Proteomes:UP000256845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8488 {ECO:0000313|EMBL:RED54272.1,
RC   ECO:0000313|Proteomes:UP000256845};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be required for disulfide bond formation in some
CC       proteins. {ECO:0000256|ARBA:ARBA00003565}.
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:RED54272.1}.
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DR   EMBL; QRDW01000001; RED54272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9HXN8; -.
DR   Proteomes; UP000256845; Unassembled WGS sequence.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR13887:SF14; CLPXP ADAPTER PROTEIN SPXH; 1.
DR   PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256845};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..200
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017591601"
FT   DOMAIN          11..199
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   200 AA;  22209 MW;  C2300C28F41E7CC9 CRC64;
     MRRILSVLFF CLIGAMAQAQ ETETPLAVPG DRVLGDPNAP VTIMEFSSLT CPHCASFHKN
     TLPLLKEKYI DTGKVKLVYK DYPIGGKALR AAMLARCVAP SRYFQFLDVL FKQQESWAWE
     ENPDAYLIKL GKLAGVSESK FAACVDDKAV RDGVLKSYVE GSRVYKVDAT PSFIINGEDK
     ISGAEGIEAF DEILEKYLEE
//
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