ID   A0A182VDE1_ANOME        Unreviewed;       653 AA.
AC   A0A182VDE1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
OS   Anopheles merus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM013072-PA, ECO:0000313|Proteomes:UP000075903};
RN   [1] {ECO:0000313|Proteomes:UP000075903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles merus MAF (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEM013072-PA}
RP   IDENTIFICATION.
RC   STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM013072-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A182VDE1; -.
DR   STRING; 30066.A0A182VDE1; -.
DR   EnsemblMetazoa; AMEM013072-RA; AMEM013072-PA; AMEM013072.
DR   VEuPathDB; VectorBase:AMEM013072; -.
DR   VEuPathDB; VectorBase:AMEM21_008965; -.
DR   Proteomes; UP000075903; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
DR   CDD; cd02997; PDI_a_PDIR; 3.
DR   CDD; cd03067; PDI_b_PDIR_N; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 5.
DR   InterPro; IPR046374; PDI_a_PDIR.
DR   InterPro; IPR041865; PDI_b_PDIR_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR45672:SF2; PROTEIN DISULFIDE-ISOMERASE A5; 1.
DR   PANTHER; PTHR45672; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1.
DR   Pfam; PF00085; Thioredoxin; 4.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 4.
PE   4: Predicted;
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          144..273
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          274..394
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          395..520
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          523..647
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          393..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..408
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   653 AA;  73636 MW;  C780A2329331645A CRC64;
     LEKHRWQLLC LVRWESGMKM KLSVVLFIIA ALGIASAYAK TQKSPVIDNI TDMKELKKLF
     RTKTNVLILF VAGMKENNAL LASFRDAAHA VKGQGTMVLF DCNNSEVKKI CKKLKATPAP
     FALKHFKDGD FHKDYDRQLT TTSMVNFMRD PTGDLPWEED PIGADVVHVP DAVTLGKFLK
     KEVKPTLVMF YAPWCGFCKT LKPEFSAAAT ELKGRYVLAA IDVNRPENSI IRKQYNITGF
     PTLLYYENGR MKYTFEGENN KAGIVAFMKN PAAPTPTKPK EADWASESSS EIVHLTAGSF
     EPALKDEKSV LVMFYAPWCG HCKKMKPEYE KAAEIMKAKN IPGVLAALDA TKEASVGQQY
     GVKGYPTVKY FSNGEFKFDV NVREADKIVK FMENPTEPPP PPAPETPWED EPSEVVHLNE
     ETFKPFLKKK KHVLVMFYAP WCGHCKRAKP EFARAAEHFK EDPKTELAAV DCTRHSAVCS
     SYEVRGYPTI KYFSYLKTVR DYNGGRTETD FIAYLKDPSA TPLKTDKVAE PFGDFPGSDK
     ILILTDANFE EVSKREPNLL VMFYAPWCGH CKHMKPDFAK VAQLLATEKV SAKVAALDCT
     VHMKTAEKFQ IRGYPTLKLF ANGQFRRNYE GKRTAQDMLQ FLRTDGAVAK DEL
//