(data stored in SCRATCH zone)

SWISSPROT: E6S818_INTC7

ID   E6S818_INTC7            Unreviewed;       124 AA.
AC   E6S818;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 43.
DE   RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN   OrderedLocusNames=Intca_0373 {ECO:0000313|EMBL:ADU46922.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 /
OS   NBRC 12989 / 7 KIP).
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU46922.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU46922.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S.,
RA   Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7
RT   KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|PIRNR:PIRNR000077}.
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DR   EMBL; CP002343; ADU46922.1; -; Genomic_DNA.
DR   RefSeq; WP_013491243.1; NC_014830.1.
DR   STRING; 710696.Intca_0373; -.
DR   EnsemblBacteria; ADU46922; ADU46922; Intca_0373.
DR   KEGG; ica:Intca_0373; -.
DR   eggNOG; ENOG41080RH; Bacteria.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000292977; -.
DR   KO; K03671; -.
DR   OrthoDB; 1630944at2; -.
DR   BioCyc; ICAL710696:GH9U-382-MONOMER; -.
DR   Proteomes; UP000008914; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6S818.
DR   SWISS-2DPAGE; E6S818.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008914};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000077-4};
KW   Redox-active center {ECO:0000256|PIRSR:PIRSR000077-4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008914}.
FT   DOMAIN        1    105       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID     30     33       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000077-4}.
SQ   SEQUENCE   124 AA;  13426 MW;  4EBA9870663E7666 CRC64;
     MSTRNLTYAD FESVVSAEGI VLVDFWASWC GPCRMFAPVY EAASETHADI TFGKVDTEAE
     QQLAAAARIT SIPTLMAFRD GILVFSQPGA LPAAALEQVV QAVRDLDMED VRRQVEAQSA
     KADA
//

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