ID A0A0V0VBD9_9BILA Unreviewed; 1211 AA.
AC A0A0V0VBD9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=T09_13514 {ECO:0000313|EMBL:KRX60859.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX60859.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX60859.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX60859.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRX60859.1}.
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DR EMBL; JYDN01000054; KRX60859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VBD9; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PF00069; Pkinase; 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 SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 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:UP000054681}.
FT DOMAIN 151..417
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 83..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX60859.1"
SQ SEQUENCE 1211 AA; 132690 MW; C5FA11792384E790 CRC64;
LDSRMPPVDN VKKPQNLGSL LELIFNSKTI TVVSGRRLKL NKINDYLLSI GSKPCQIADI
SSIQVKLRCS YLCITDRTVM DQQTNTKREE PQQQQQSQSQ PHPPPPPPQQ QQQQPQQQNK
QATSGRESDS DDEDSNSPLE ESPCGRWQKR RERVQRRNVP GIDATYLAMD NELGVEVAWN
EVHFNDRRQL MLQQRSICAM FDRLVELDHP YLVKVHSYWL DEDRARVVLI TDYMSSGSVA
QFLRRTAQGG VSTKPPSSGG RSWRKWCLPV LLALDYLHSF EPPVVHGHLT NSAIFIQQNG
VIKVAFVMPE GAAVELHGLR SAATSREGAR QHHQHMYYVA PECRAPGSRG TVQADIYAFG
VCALEMAAMG LLGDGDQLTR ALQSLENPSQ RQLVEQCFST VPSQRPTAHQ LIFHPALFEV
PSLLLLAAHE VLRGPDTFSE FDPAAAAGAR GGRHASSVGG VGSSGGKLPG RRQSGVLAEL
VGVDGTRHVM VCREDVNTHD LEKLLEDVRN GIYPLAGLQH RSSVDGSYVA GDDDRCPVST
GDSVDASAAS AAVAAAAGGG GVGAGDSDGG GGGDAAVVGV GSSSTYDVVS GRGLGVVGDH
RGSSLSPSRL RPFGGDPLTN GLQHGVSASL MEPKHEARKK PSRAGEFEET RELVELSAEV
RPAEQSGAYV LAMMLKFEDR MNRELTGQFT DDESPEALSD ELVEYGFVRP RDHHRLVDLI
GQAMALCRQS QSTVDEINKD RVLRYLFDIS CRNLLPLIFV NGDCVGGVEE LARLVEKGIL
KEWLADHQYD LVVIGGGSGG LAAAKDAALA GKRVAVLDFV TPTPLGTTWG LGGTCVNVGC
IPKKLMHCTS LLGKNLADAR KFGWKYGEEV KHSWTDMVTA IQSHITSLNW NYRVQLREKS
VTYLNAFGTF VGSHSIKATD KRNKEQIITS DRFIIATGLR PRYLDVPGVK EYCITSDDVF
SLPYCPGKTL CVGASYVSLE CAGFLRGLGL DVTVMVRSIL LRGFDQDMAN RVGNHMQTVE
GVRFIYKCIP TKIERLQDGQ PGLLRVTAKK EDGEEVVDEY NTVLIAIGRD ALTDALNLDK
VGVETHPKNK KILCYANEQS TTAPYIYAIG DVLYRGLELT PVAIKAGRLL AKRLFGLSNI
LCDRYLTPTT VFTPLEYGCC GMSEEEAIEE YGEINIEVFH SYFTPLEYTV PKRDDSEHCY
AKLICNKHDD V
//
