ID A0A261DBF6_9RICK Unreviewed; 107 AA.
AC A0A261DBF6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN ORFNames=RiCNE_06040 {ECO:0000313|EMBL:OZG31978.1};
OS Rickettsia endosymbiont of Culicoides newsteadi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia.
OX NCBI_TaxID=1961830 {ECO:0000313|EMBL:OZG31978.1, ECO:0000313|Proteomes:UP000216097};
RN [1] {ECO:0000313|EMBL:OZG31978.1, ECO:0000313|Proteomes:UP000216097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RiCNE {ECO:0000313|EMBL:OZG31978.1,
RC ECO:0000313|Proteomes:UP000216097};
RX PubMed=28805302;
RA Pilgrim J., Ander M., Garros C., Baylis M., Hurst G.D.D., Siozios S.;
RT "Torix group Rickettsia are widespread in Culicoides biting midges
RT (Diptera: Ceratopogonidae), reach high frequency and carry unique genomic
RT features.";
RL Environ. Microbiol. 19:4238-4255(2017).
CC -!- FUNCTION: Component of the thioredoxin-thioredoxin reductase system.
CC Participates in various redox reactions through the reversible
CC oxidation of its active center dithiol to a disulfide and catalyzes
CC dithiol-disulfide exchange reactions. {ECO:0000256|ARBA:ARBA00025303}.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
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:OZG31978.1}.
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DR EMBL; MWZE01000026; OZG31978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261DBF6; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000216097; 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 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; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; 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 ECO:0000256|PIRSR:PIRSR000077-4};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000077-4};
KW Reference proteome {ECO:0000313|Proteomes:UP000216097};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..106
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 30
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 33
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 24
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 31
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 32
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 30..33
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 107 AA; 12013 MW; 62197DF14799264F CRC64;
MTSNITDDSF DKEVLQSTDP VLVDFWAEWC GPCKMLTPIL EELSKELVGK VKIVKMDIEQ
NPNIPSSLGI RAIPTMILFK DGKQLATKTG LFPKNAIEEW IDSSIKM
//
