ID G2NCT4_STREK Unreviewed; 608 AA.
AC G2NCT4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:AEN11095.1};
GN ORFNames=SACTE_3229 {ECO:0000313|EMBL:AEN11095.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN11095.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN11095.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN11095.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
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DR EMBL; CP002993; AEN11095.1; -; Genomic_DNA.
DR AlphaFoldDB; G2NCT4; -.
DR STRING; 862751.SACTE_3229; -.
DR KEGG; ssx:SACTE_3229; -.
DR PATRIC; fig|862751.12.peg.3361; -.
DR eggNOG; COG0526; Bacteria.
DR eggNOG; COG4257; Bacteria.
DR HOGENOM; CLU_013730_1_0_11; -.
DR Proteomes; UP000001397; Chromosome.
DR CDD; cd14951; NHL-2_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR045302; NHL2_NHL_rpt_dom.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR46388; NHL REPEAT-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR46388:SF2; NHL REPEAT-CONTAINING PROTEIN 2; 1.
DR Pfam; PF01436; NHL; 2.
DR Pfam; PF13905; Thioredoxin_8; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51125; NHL; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 8..154
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REPEAT 402..432
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
SQ SEQUENCE 608 AA; 65155 MW; 6AD58AA1B62FC807 CRC64;
MLTGGMTARA RVRAPELIGK GGWLNTGDRS YTLADLRGRI VILDFWTFCC VNCLHVLDEL
RELEEKHRDT VVIIGVHSPK FVHEAEHQAV VDAVERYEVH HPVLDDPELA TWKQYAVRAW
PTLVVVDPEG YVVAQHAGEG HAHAIEKLVE ELEAEHAAKG TLRRGDGPYV APEPVATHLR
FPGKALALAD GGFLVSDTTR HRLVELDADG ETVRGHFGTG ERGLTDGGPG EARFSEPQGL
ALLPDGRIAV ADTVNHAIRA LDLTTGATTT LAGTGRQWWQ GSATSGPAAE VDLSSPWDVA
WFGDRLWIAM AGVHQLWTYD PEDGTVRVAA GTTNEGLVDG PGPEAWFAQP SGLAATDDRL
WVADSETSAL RYVDLDGAVH TAVGTGLFDF GHRDGAADQA LFQHPLGVTA LPDGSVAVSD
TYNHALRRFD PESGRVTTLA TDLREPSDAV LVDGDLVVVE SARHRLTRLR LPEEAVRVAD
RAHRTQRAAT GIAPGTLRLD VVFQAPAGQK LDTRYGPSTR LLVSSTPPEL LAEGSGPGTD
LSRDLVLADG VTEGVLHVSA MAASCDDDPA NEYPACHVHQ QDWGVPVQVT ADGVARLPLV
LAGLDEEG
//
