ID   A0A0N5AJF0_9BILA        Unreviewed;       949 AA.
AC   A0A0N5AJF0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=thioredoxin-disulfide reductase {ECO:0000256|ARBA:ARBA00012610};
DE            EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
OS   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000458901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000458901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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DR   AlphaFoldDB; A0A0N5AJF0; -.
DR   STRING; 451379.A0A0N5AJF0; -.
DR   WBParaSite; SMUV_0000458901-mRNA-1; SMUV_0000458901-mRNA-1; SMUV_0000458901.
DR   Proteomes; UP000046393; Unplaced.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0042302; F:structural constituent of cuticle; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR002486; Col_cuticle_N.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR   NCBIfam; TIGR01438; TGR; 1.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF8; THIOREDOXIN REDUCTASE 1; 1.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SMART; SM01088; Col_cuticle_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          652..704
FT                   /note="Nematode cuticle collagen N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01088"
FT   REGION          758..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          798..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..815
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..845
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        856..874
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        888..902
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   949 AA;  101145 MW;  BFB5BB47B1B0532B CRC64;
     MESGTRATKP AGTVDASAEG CDCCSHSTKS KISEHDLAIA REVFKTAVNV KILVVSLKGS
     KPCTESRLVC FLKFFLVTYL KHFLKTFVLL SKYSGDLKSF EINEHTASEV FRVTGWDSLP
     LIFIKGDCIG GYTQLCALDQ RSILKGWLED HTYDLIVIGG GSGGLAAAKE AASLGKKVAC
     LDFVKPSVQG STWGLGGTCV NVGCIPKKLM HRASILGEHI SDAKKFGWQI PEGDITMDWV
     KLKNAVQEHI GSLNWGYRVQ LREKSVQYFN SYGRFIDTHT IQAEDKKGRI KTLTADRFLI
     ATGLRPKYPD IIGAKECCIS SDDLFSLPYN PGKTLCVGAS YISLESAGFL RAIGNDVTVM
     VRSILLRGFD QDMAERIRQQ MLDMGVKFLS GVPFKYEKLE EPHDNKPGLI RVYNIETLPD
     GSKRESYENY NTVLMAIGRY AVTDNIGLDK LGVELAPSKK IIGRHEQSIS CPYIYAIGDV
     LEGHPELTPV ARTAGKTLMK RLYTGNCELT EYDKIPTTVF TPLEYGCCGL SEEAAVERYG
     EDNINVYHAK FIPLEFTVPQ RIDTKHCYLK LICLKTDKDR VLGFHILTPD AGEITQGFAI
     ALKLNATKTD FDRLIGIHPT VAEVDTEKLL KGRNCSVITP FSDVELICFF RAYAYSAVTF
     SVVSVISICI TLPMAYNYIS NAKAQLYGEI KECKSTVRDI WTDIQELSKV ALKSNRTARS
     AAFTGGLSGY GSAAGNVANL GNRGGCNCGC VPGVPGARGS PGARGRPGKP GAAGVPGLPG
     RPAATPCEPI VPPPCKPCPQ GPPGPPGPPG LIGDPGLPGS PGSDSLPSPQ GPMGPPGPPG
     NEGTPGQMGP PGDPGTSPES TLPIPGPPGP VGEAGPPGQD GAPGLPGEPS LQGPPGPPGP
     QGPIGQQGAS GRPGPKGLPG GPGTDGEKGI CPKYCAVDGG VFFEDGTRR
//