ID A0A1V8M9W9_9GAMM Unreviewed; 145 AA.
AC A0A1V8M9W9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:OQK18391.1};
GN ORFNames=AU255_11400 {ECO:0000313|EMBL:OQK18391.1};
OS Methyloprofundus sedimenti.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methyloprofundus.
OX NCBI_TaxID=1420851 {ECO:0000313|EMBL:OQK18391.1, ECO:0000313|Proteomes:UP000191980};
RN [1] {ECO:0000313|EMBL:OQK18391.1, ECO:0000313|Proteomes:UP000191980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF1 {ECO:0000313|EMBL:OQK18391.1,
RC ECO:0000313|Proteomes:UP000191980};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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:OQK18391.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LPUF01000001; OQK18391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8M9W9; -.
DR STRING; 1420851.AU255_11400; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000191980; Unassembled WGS sequence.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR049299; Thio2_N.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR Pfam; PF21352; Thio2_N; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-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:UP000191980};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 33..145
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 145 AA; 16054 MW; A24D47E5194CD415 CRC64;
MSNFVHIVCP ACLSVNRIPA IRLSDKPQCG KCHRPLFSAL PVDLTASNFQ QHIKRNDIPV
LVDFWAPWCG PCKSMAPAFK LAAAQLEPKI RLAKLNTETE QAIAAQYGIR SIPTLMLFHK
GKELARQSGA IDTQAIISWA NQYIA
//
