ID A0A182DXG3_ONCOC Unreviewed; 607 AA.
AC A0A182DXG3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Thioredoxin domain-containing protein {ECO:0000313|WBParaSite:nOo.2.0.1.t00340-RA};
GN ORFNames=NOO_LOCUS340 {ECO:0000313|EMBL:VDK61940.1};
OS Onchocerca ochengi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t00340-RA};
RN [1] {ECO:0000313|Proteomes:UP000077448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
RN [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t00340-RA}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDK61940.1, ECO:0000313|Proteomes:UP000271087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GET4 family.
CC {ECO:0000256|ARBA:ARBA00005351}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000256|ARBA:ARBA00025719}.
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DR EMBL; UYRW01000032; VDK61940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182DXG3; -.
DR STRING; 42157.A0A182DXG3; -.
DR WBParaSite; nOo.2.0.1.t00340-RA; nOo.2.0.1.t00340-RA; nOo.2.0.1.g00340.
DR Proteomes; UP000077448; Unassembled WGS sequence.
DR Proteomes; UP000271087; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR GO; GO:0045048; P:protein insertion into ER membrane; IEA:InterPro.
DR CDD; cd03016; PRX_1cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR007317; GET4.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR12875:SF0; GOLGI TO ER TRAFFIC PROTEIN 4 HOMOLOG; 1.
DR PANTHER; PTHR12875; UNCHARACTERIZED; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF04190; GET4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000271087}.
FT DOMAIN 380..551
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 607 AA; 69473 MW; 128970E5FD6E5260 CRC64;
MSRIEEKLEL CFKNGNYYEA HQIYRTLYNR MSNQGKWQEL QNMLYSGILR LLAEKEAASA
IDLAELFVDT LEKSKTPVSS VVLDRFEKLL SLLPAQLEKD LEANSEREDR RLQYILSGIK
WTKAVGDRKR FRRRGHPELH FRIAKSLWRE GNYVNARNHF MYSDNPETFA AFLTEYQLKY
GYTAEKDLFI AQTVMQMLCD RKPKSALKLL QSYCDIHPDI RSGFPYPFPL LNFLHFAIIC
IANKEVTYFT VLVEQYESEI SRDPEYKQFL DRIGQIYFGL PRPQIARGGF LGNMIKGLLK
TSENESGTTE EFETDSEEAL HIPLSNETEC LVGTSKSKLA SGIFPMDAAQ SDVEKRFITT
VSSCEYVFVI VFKSKMSKGI LLGDKFPDFQ AETNEGFISS FYDWIGKDSW AILFSHPRDF
TPVCTTELAR LVQLAPEFKK RNVKLIGLSC DSADSHSKWA DDILALYKMK CVDCDSEKKL
PYPIIADEDR SLATELGMMD PDERDEKGNT LTARCVFIIG SDKTLKLSIL YPATTGRNFD
EILRVVDSLQ LTAVKLVATP VDWKDGDDCV VLPTIDDNEA KKLFGEKIHT IDLPSGKHYL
RMVPHPK
//
