ID A0A2T6E3I7_9GAMM Unreviewed; 288 AA.
AC A0A2T6E3I7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:PTY35934.1};
GN ORFNames=BGP77_00990 {ECO:0000313|EMBL:PTY35934.1};
OS Saccharospirillum sp. MSK14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Saccharospirillum.
OX NCBI_TaxID=1897632 {ECO:0000313|EMBL:PTY35934.1, ECO:0000313|Proteomes:UP000244044};
RN [1] {ECO:0000313|EMBL:PTY35934.1, ECO:0000313|Proteomes:UP000244044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSK14-1 {ECO:0000313|EMBL:PTY35934.1,
RC ECO:0000313|Proteomes:UP000244044};
RA Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT "Draft genome of Saccharospirillum sp. MSK14-1.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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:PTY35934.1}.
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DR EMBL; MIES01000033; PTY35934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6E3I7; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000244044; Unassembled WGS sequence.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR CDD; cd02956; ybbN; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR Pfam; PF14559; TPR_19; 1.
DR Pfam; PF14561; TPR_20; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000244044};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..114
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 288 AA; 32438 MW; 84866B6596898EFD CRC64;
MSQQASNVIT VTEQNFQQVM VEESQQRLVV MDFWADWCAP CKALMPILEK LAGEYPNQLL
LAKVNADEQP NIVAQFGVRS LPTVAFIQNG QPVDAFMGAE PESAIRQRLE KYLPKPWDEL
LQQAAEFQAA GNPAQALPLV QEAYRLSGED TEIAFMLASV YIDLKRGSEA ETILDAMTMQ
QQTEPHYKEL RSRLKLLAEA AETPEIQELQ QRLESNPDDL EVAYELSVQY SQAGRSEEAL
ETLIGVLTKD RNFRDGGARK TFLDILNGLP KGDPLAARYQ RKLFTLLY
//
