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Database: UniProt
Entry: D9VQP8_9ACTN
LinkDB: D9VQP8_9ACTN
Original site: D9VQP8_9ACTN 
ID   D9VQP8_9ACTN            Unreviewed;       235 AA.
AC   D9VQP8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Protein dithiol-disulfide isomerase {ECO:0000313|EMBL:EFL14461.1};
GN   ORFNames=SSNG_01713 {ECO:0000313|EMBL:EFL14461.1};
OS   Streptomyces sp. C.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL14461.1, ECO:0000313|Proteomes:UP000005763};
RN   [1] {ECO:0000313|EMBL:EFL14461.1, ECO:0000313|Proteomes:UP000005763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C {ECO:0000313|EMBL:EFL14461.1,
RC   ECO:0000313|Proteomes:UP000005763};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain C.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG657750; EFL14461.1; -; Genomic_DNA.
DR   RefSeq; WP_007263408.1; NZ_GG657750.1.
DR   AlphaFoldDB; D9VQP8; -.
DR   STRING; 253839.SSNG_01713; -.
DR   eggNOG; COG2761; Bacteria.
DR   HOGENOM; CLU_069253_0_2_11; -.
DR   Proteomes; UP000005763; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd03024; DsbA_FrnE; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR   PANTHER; PTHR13887:SF41; THIOREDOXIN SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:EFL14461.1}.
FT   DOMAIN          3..205
FT                   /note="DSBA-like thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF01323"
SQ   SEQUENCE   235 AA;  25877 MW;  4CE1155E0FCA6FFD CRC64;
     MRVEIWSDIA CPWCYIGKAR FAKGLAEFAH RDEVEVVFRS FELDPNGPKG VTAPVLEMLA
     RKYGRTLDEA RAMEEHVAAS ARAEGLEYRT DGRDHGNTFD IHRLLHLAAA RGRQEQLLDL
     AFRANFAEER SVFDPEVLLA LAVEAGLDET EAREVLADDS AYADRVRADE REAAELGANA
     VPFFVLDRRY GISGGQPAEV FTRALEQAWA GREAVETAPD AEACEPDGAC AVPQG
//
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