(data stored in SCRATCH zone)

SWISSPROT: C6WF93_ACTMD

ID   C6WF93_ACTMD            Unreviewed;       226 AA.
AC   C6WF93;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 52.
DE   SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:ACU34225.1};
GN   OrderedLocusNames=Amir_0256 {ECO:0000313|EMBL:ACU34225.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34225.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34225.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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DR   EMBL; CP001630; ACU34225.1; -; Genomic_DNA.
DR   RefSeq; WP_012782888.1; NC_013093.1.
DR   ProteinModelPortal; C6WF93; -.
DR   STRING; 446462.Amir_0256; -.
DR   EnsemblBacteria; ACU34225; ACU34225; Amir_0256.
DR   KEGG; ami:Amir_0256; -.
DR   eggNOG; ENOG41081FP; Bacteria.
DR   eggNOG; COG0526; LUCA.
DR   HOGENOM; HOG000052451; -.
DR   OMA; LWAYWCA; -.
DR   OrthoDB; POG091H08GJ; -.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
DR   PRODOM; C6WF93.
DR   SWISS-2DPAGE; C6WF93.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     29       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        30    226       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002972802.
FT   DOMAIN       85    226       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
SQ   SEQUENCE   226 AA;  23213 MW;  65B5C8B009BF2954 CRC64;
     MSAAARWSVV VLVLAVAGVV ALWPRGEDPA SPVIPQPQRD TSQRADLGVA RNKAALRPCD
     QFSGNSASPA SANAASPSPA SPSAGPTSTS AGPEALRGAT AVCLGDGERV DAATALSGRV
     LVNFWASWCA PCREELRVLD DYSQRPGAIP VLGVQVKSGE ADGLDLLSRI GVHLPSLVDD
     SEALLRAFKV PPTLPASFLV GADGSITPVT DPLVFTSVDQ VREVVG
//

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