ID A0A1I7VNN8_LOALO Unreviewed; 248 AA.
AC A0A1I7VNN8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Thioredoxin domain-containing protein {ECO:0000313|WBParaSite:EN70_4580};
OS Loa loa (Eye worm) (Filaria loa).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Loa.
OX NCBI_TaxID=7209 {ECO:0000313|Proteomes:UP000095285, ECO:0000313|WBParaSite:EN70_4580};
RN [1] {ECO:0000313|Proteomes:UP000095285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Nutman T.B., Fink D.L., Russ C., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Henn M.R.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Loa loa.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:EN70_4580}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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DR AlphaFoldDB; A0A1I7VNN8; -.
DR STRING; 7209.A0A1I7VNN8; -.
DR WBParaSite; EN70_4580; EN70_4580; EN70_4580.
DR eggNOG; KOG0910; Eukaryota.
DR Proteomes; UP000095285; Unassembled WGS sequence.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000095285};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 70..183
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 182..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..248
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 248 AA; 28410 MW; 21F1A748DF29982B CRC64;
MLRSNEMLTG SRTHPQLYRM HKLFLSRCVA SSNIQCISSF PTRLIKIPLQ RLRINNGLIP
KNSVLFRRFC NDESSAVIFN VEDEEDFTEK VMNSSVPVLV DFYADWCGPC KMLGPRIEAK
VVSREGNIKL AKVNVDYAAD VAMDYDVRSV PTVVAMKSGQ VVARFQGVKT DDELDYFIDT
QRKRKKHEEK KESKHQVIPV IWSGKSNTSR NPTSNPQDRK QMKKNEDDDD DDDDDGDDDD
DNDDDVRL
//