ID W6KNM6_MAGSQ Unreviewed; 305 AA.
AC W6KNM6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative thioredoxin {ECO:0000313|EMBL:CCQ75297.1};
GN ORFNames=MGMAQ_3472 {ECO:0000313|EMBL:CCQ75297.1};
OS Magnetospira sp. (strain QH-2) (Marine magnetic spirillum (strain QH-2)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Magnetospira.
OX NCBI_TaxID=1288970 {ECO:0000313|EMBL:CCQ75297.1, ECO:0000313|Proteomes:UP000032733};
RN [1] {ECO:0000313|EMBL:CCQ75297.1, ECO:0000313|Proteomes:UP000032733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QH-2 {ECO:0000313|EMBL:CCQ75297.1,
RC ECO:0000313|Proteomes:UP000032733};
RX PubMed=23841906; DOI=10.1111/1462-2920.12180;
RA Ji B., Zhang S.D., Arnoux P., Rouy Z., Alberto F., Philippe N., Murat D.,
RA Zhang W.J., Rioux J.B., Ginet N., Sabaty M., Mangenot S., Pradel N.,
RA Tian J., Yang J., Zhang L., Zhang W., Pan H., Henrissat B., Coutinho P.M.,
RA Li Y., Xiao T., Medigue C., Barbe V., Pignol D., Talla E., Wu L.F.;
RT "Comparative genomic analysis provides insights into the evolution and
RT niche adaptation of marine Magnetospira sp. QH-2 strain.";
RL Environ. Microbiol. 16:525-544(2014).
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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DR EMBL; FO538765; CCQ75297.1; -; Genomic_DNA.
DR RefSeq; WP_046022435.1; NZ_FO538765.1.
DR AlphaFoldDB; W6KNM6; -.
DR STRING; 1288970.MGMAQ_3472; -.
DR KEGG; magq:MGMAQ_3472; -.
DR HOGENOM; CLU_046120_1_1_5; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000032733; Chromosome.
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:UP000032733};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 13..129
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 305 AA; 32277 MW; C65589A4161F6570 CRC64;
MDILLDNDGT PVSAGGTPAG DLIKDSDLNG FTTDVLEASR SVPVIVDFWA PWCEPCKTLG
PALEKIVKQM AGAVRMVKIN VDENQNLAAQ MRVQSVPTVY AFKDGQPVDA FQGAVPESQL
RAFVDKLTDG AQSPLEAALE QAKALLDGGD PQNAASLYNQ VLQAEPEQVA ALAGLARCLI
ASGDTDAAAS FLDGLSDKLK MMSEIQAARS ALDLAGTGGG DVAALQAKLD SNPDDNDARF
DLANSLYAAG DAEAAIEQLL DLVKRDRGWN EEAGRKQLVK LFETLGHTHP TTVAARKRLS
TLLFS
//
