(data stored in SCRATCH zone)

SWISSPROT: C7QJ27_CATAD

ID   C7QJ27_CATAD            Unreviewed;       192 AA.
AC   C7QJ27;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 46.
DE   SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:ACU69169.1};
GN   OrderedLocusNames=Caci_0214 {ECO:0000313|EMBL:ACU69169.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69169.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69169.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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DR   EMBL; CP001700; ACU69169.1; -; Genomic_DNA.
DR   RefSeq; WP_012784464.1; NC_013131.1.
DR   ProteinModelPortal; C7QJ27; -.
DR   STRING; 479433.Caci_0214; -.
DR   EnsemblBacteria; ACU69169; ACU69169; Caci_0214.
DR   KEGG; cai:Caci_0214; -.
DR   eggNOG; ENOG4108V81; Bacteria.
DR   eggNOG; COG1225; LUCA.
DR   HOGENOM; HOG000022344; -.
DR   OMA; GCTPQAC; -.
DR   OrthoDB; POG091H09GI; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
DR   PRODOM; C7QJ27.
DR   SWISS-2DPAGE; C7QJ27.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   DOMAIN       22    188       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
SQ   SEQUENCE   192 AA;  20907 MW;  8173FE297AB371B2 CRC64;
     MHDIYTLPAD LPIPQDDGAA DHLPGARVPE LTLTSTAGEA IALAALGEGR TVLYIYPLSG
     RPGEEAPEGW SAIPGARGCT TEACDFRDHH KELLEAGAAR VFGLSSQDSA YQQELVERLR
     LPFAMLSDTG LRLAAELDLP TFEAGGRLLY KRITLVIRDG VIEHAFYPIF PPDRHAGEVL
     GWLTKNPVRR IP
//

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