ID A0A0V1MRX6_9BILA Unreviewed; 1293 AA.
AC A0A0V1MRX6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=thioredoxin-disulfide reductase {ECO:0000256|ARBA:ARBA00012610};
DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610};
DE Flags: Fragment;
GN Name=TXNRD1 {ECO:0000313|EMBL:KRZ74545.1};
GN ORFNames=T10_5673 {ECO:0000313|EMBL:KRZ74545.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ74545.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ74545.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ74545.1};
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:KRZ74545.1}.
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DR EMBL; JYDO01000049; KRZ74545.1; -; Genomic_DNA.
DR STRING; 268474.A0A0V1MRX6; -.
DR Proteomes; UP000054843; 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; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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:UP000054843}.
FT DOMAIN 174..439
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 105..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ74545.1"
SQ SEQUENCE 1293 AA; 141933 MW; 694E4F49A2C85ECB CRC64;
LISKHCYSRM LTFTVRANRD SSMPPVDNVK EPEDFSSLLE LIVNSKTIAV VNGHRIELNK
INDYLLSVDS KPCQIADIKS ISVRLRCSYL CITDRIVMDQ QTNIKREEPQ QQQQQQQQQQ
QQPQPPQQQQ QQPPQPQGQQ QNKQATSGRE SDSDDEDSNS PLEESPCGRW QKRRERVQRR
NVLGIDATYL AMDNELGVEV AWNEVHFNDR RQLMLQQRSI CAMFDRLVEL DHPYLVKVHS
YWLDEDRARV VLITDYMSSG SVAQFLRRTA QGGVSAKPPS SGGRSWRKWC LPVLLALDYL
HSFEPPVVHG HLTNSAIFIQ QNGVIKVAFV MPEGASVELH GLRSAAGRDT ARQHHQHMYY
VAPECRAPGS RGTVQADIYA FGVCALEMAA MGLLGDGDQL TRALQSLENP SQRQLIEQCL
STVASNRPTA HQLIFHPALF EVPSLLLLAA HEMLRGPDSF SEFDPAAAAG ARGSRHASIS
GGRLPGRRQS GVLAELVGAD GTRHVLVYRE DVSTQDLEKL LEDVRNGIYP LAGLQHRSSV
DGSYVAGDDV GNGDGVDESA SAGGGGCGDV GAGDNGDGGG GDAAAVRVGS SSTYDVVSGR
GLGVAGDHRG CSLSPSRLRP FGGDSLANGL QHGASASLLE PKHEGRKKPP SRGGEFEETR
ELVELSAEVR PAEQSGAYVL AMMLKFDDRM NRELTGQFTD DESPEALSDE LVEYGFVRPR
DHHRLVDLIG QAMALCRQSR ATVDEESSSS STAINRDRVI SNLFDISGRK ELPLIFVKGD
CVGGVEDLRK LVENGVLKEW LADHQYDLVV IGGGSGGLAA AKDAAVAGKR VAVLDFVTPT
PLGTTWGSLG GTCVNVGCIP KKLMHCTSLL GKNLADARNF GWKYGEEVKH SWKDMITAVQ
SHITALNWNY RVQLREKAVT YLNAFGTFVG SHSIKATDKR KKEQIITSDR FLIATGLRPR
YLDVPGVKEY CITSDDVFSL PYCPGKTLCV GASYVSLECA GFLRGLGLDV TVMVRSILLR
GFDQDMANRI GNHMQTVEGV RFIYQCIPTK IERLQDGQPG LLRVTAKKED GEEVVDEYNT
VLIAIGRDAL TDALNLDKVG VQTNARNKKI VCYSNEQSCT TPYIYAIGDV LDGGLELTPV
AIKAGRLLVK RMFGLSSNLC EYHLVPTTVF TPLEYGCCGL SEEKAIEKYG EKNIEVFHSY
FTPLEYTVPK RDDSEHCYAK LICNKQDDMR ILGFHLLGPN AGEITQGFAI GLKLKATKHD
FDQLVGIHPT CAEVFTQLTV TKSSQQVLKK TGC
//
