GenomeNet

Database: UniProt
Entry: A0A0S3QR86_THET7
LinkDB: A0A0S3QR86_THET7
Original site: A0A0S3QR86_THET7 
ID   A0A0S3QR86_THET7        Unreviewed;       262 AA.
AC   A0A0S3QR86;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Thiol:disulfide interchange protein DsbC {ECO:0000313|EMBL:BAT70848.1};
DE            EC=5.3.4.1 {ECO:0000313|EMBL:BAT70848.1};
GN   ORFNames=TST_0038 {ECO:0000313|EMBL:BAT70848.1};
OS   Thermosulfidibacter takaii (strain DSM 17441 / JCM 13301 / NBRC 103674 /
OS   ABI70S6).
OC   Bacteria; Aquificota; Aquificae; Aquificales.
OX   NCBI_TaxID=1298851 {ECO:0000313|EMBL:BAT70848.1, ECO:0000313|Proteomes:UP000063234};
RN   [1] {ECO:0000313|Proteomes:UP000063234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17441 / JCM 13301 / NBRC 103674 / ABI70S6
RC   {ECO:0000313|Proteomes:UP000063234};
RX   PubMed=29420286; DOI=10.1126/science.aao3407;
RA   Nunoura T., Chikaraishi Y., Izaki R., Suwa T., Sato T., Harada T., Mori K.,
RA   Kato Y., Miyazaki M., Shimamura S., Yanagawa K., Shuto A., Ohkouchi N.,
RA   Fujita N., Takaki Y., Atomi H., Takai K.;
RT   "A primordial and reversible TCA cycle in a facultatively
RT   chemolithoautotrophic thermophile.";
RL   Science 359:559-563(2018).
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; AP013035; BAT70848.1; -; Genomic_DNA.
DR   RefSeq; WP_068548532.1; NZ_AP013035.1.
DR   AlphaFoldDB; A0A0S3QR86; -.
DR   STRING; 1298851.TST_0038; -.
DR   KEGG; ttk:TST_0038; -.
DR   OrthoDB; 12976at2; -.
DR   Proteomes; UP000063234; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.10.450.70; Disulphide bond isomerase, DsbC/G, N-terminal; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N.
DR   InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR35272:SF3; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC; 1.
DR   PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   SUPFAM; SSF54423; DsbC/DsbG N-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:BAT70848.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063234};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..262
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006616342"
FT   DOMAIN          75..258
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   262 AA;  29697 MW;  091ABC6879392F37 CRC64;
     MRYLVGFLAF LLLTVNSFGK VPEAVTAKVK KIVGKEAKIV GVEPLPIKGL YGVFLQGTRG
     MGVIVVTEDG NYLILGKILK VQDINKPEDV IAEIAKKKRY LKPPKPKKVD MSKIDIKNSP
     RIGKEEAPEI VLYFDPTCPF CKKELATLRE MEKKGEVAFY PKYFIVHGKT AKEKAIEAEC
     IREAYGKEAY YDYLLEGKKP KKEAKCDKEA IKKRIERDIK EAKELGITGT PTWIYNKEMY
     VGYRPESEVK RIIDKGKGSK VE
//
DBGET integrated database retrieval system