ID A0A261CAY3_9PELO Unreviewed; 664 AA.
AC A0A261CAY3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=thioredoxin-disulfide reductase {ECO:0000256|ARBA:ARBA00012610};
DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
DE Flags: Fragment;
GN ORFNames=FL83_06580 {ECO:0000313|EMBL:OZG19096.1};
OS Caenorhabditis latens.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG19096.1, ECO:0000313|Proteomes:UP000216463};
RN [1] {ECO:0000313|EMBL:OZG19096.1, ECO:0000313|Proteomes:UP000216463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX534 {ECO:0000313|EMBL:OZG19096.1,
RC ECO:0000313|Proteomes:UP000216463};
RA Fierst J.L.;
RT "Caenorhabditis latens genome sequence.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZG19096.1}.
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DR EMBL; NIPN01000023; OZG19096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261CAY3; -.
DR STRING; 1503980.A0A261CAY3; -.
DR Proteomes; UP000216463; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; 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; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000216463}.
FT DOMAIN 173..515
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 535..647
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OZG19096.1"
SQ SEQUENCE 664 AA; 73681 MW; 6D909894CD9B9EA6 CRC64;
MKSLGELFGC FKRQPRQGDA TAPADQSTSG TPSMGAVASG MPPPKRPAPA ESPTLSDERN
VDEPGIPLKE ALKEANNAKI AVFYNKADEE KQILEIEAIL KGLKDPSDVE KPLEIPDVQR
IRVSSASKKA IQYLTLHNSW PLIYIKGNAV GGLKELQALK KDYLKEWLRD HTYDLIVIGG
GSGGLAAAKE AARLGKKVAC LDFVKPSPQG TTWGLGGTCV NVGCIPKKLM HQASLLGHSI
HDAQKFGWKL EGKPEHQWGH LRDSVQDHIA SLNWGYRVQL REKTVTYINS YGEFTGPFEI
SATNKKKKVE KITADRFLIA TGLRPKYPDF PGVKEYTITS DDLFQLPYSP GKTLCVGASY
VSLECAGFLH GLGFDVTVMV RSILLRGFDQ DMAERIRKHM IAYGLKFESG VPTRIEQIEE
KTDEKAGKYR VYWQKKNEES GEMQEVSEEY NTILYAIGRE AVTDDVGLET IGVERAKSKK
VVGRREQSTT IPWVYAIGDV LEGTPELTPV AIQAGRVLMR RIFEGANELT EYDQIPTTVF
TPLEYGCCGL AEEDAVKKYG KENIIIYHNV FNPLEYTISE RMDKDHCYLK LICLRNEEEK
VVGFHILTPN AGEITQGFGI ALKLSAKKAD FDRLIGIHPT VAESFTTLTL EKKDGDEELQ
ASGC
//
