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Database: UniProt
Entry: F0NMY1_SULIH
LinkDB: F0NMY1_SULIH
Original site: F0NMY1_SULIH 
ID   F0NMY1_SULIH            Unreviewed;       323 AA.
AC   F0NMY1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:ADX81587.1};
GN   OrderedLocusNames=SiH_0215 {ECO:0000313|EMBL:ADX81587.1};
OS   Sulfolobus islandicus (strain HVE10/4).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=930943 {ECO:0000313|EMBL:ADX81587.1, ECO:0000313|Proteomes:UP000006395};
RN   [1] {ECO:0000313|EMBL:ADX81587.1, ECO:0000313|Proteomes:UP000006395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HVE10/4 {ECO:0000313|EMBL:ADX81587.1,
RC   ECO:0000313|Proteomes:UP000006395};
RX   PubMed=21278296; DOI=10.1128/JB.01487-10;
RA   Guo L., Brugger K., Liu C., Shah S.A., Zheng H., Zhu Y., Wang S.,
RA   Lillestol R.K., Chen L., Frank J., Prangishvili D., Paulin L., She Q.,
RA   Huang L., Garrett R.A.;
RT   "Genome analyses of icelandic strains of Sulfolobus islandicus, model
RT   organisms for genetic and virus-host interaction studies.";
RL   J. Bacteriol. 193:1672-1680(2011).
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DR   EMBL; CP002426; ADX81587.1; -; Genomic_DNA.
DR   RefSeq; WP_014511862.1; NC_017275.1.
DR   AlphaFoldDB; F0NMY1; -.
DR   GeneID; 78427338; -.
DR   KEGG; sih:SiH_0215; -.
DR   HOGENOM; CLU_031864_5_3_2; -.
DR   Proteomes; UP000006395; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
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; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   NCBIfam; TIGR01292; TRX_reduct; 1.
DR   PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT   DOMAIN          16..305
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   323 AA;  35201 MW;  1223FD0D73DF7847 CRC64;
     MSLLPRTASV KPGEKFDVII VGLGPAAYGA ALYTARYMLK TLVIGETPGG QLTEAGIVDD
     YLGLIEIQAS NMIKVFNKHI EKYEVPVLLD IVEKIENSED GFVVKTKRKG EFKADSVILG
     IGVKRRKLGV PGEQEFVGKG ISYCSVCDAP LFKNRVVAVV GGGDSALEGA EILSSYSTKV
     YLIHRRDSFK AQPIYVETVK KKPNVEFVLN SVVKEIKGDK VVKQVVVENL KTGEIKELNV
     NGVFVEIGFD PPTDFARSNG IETDTNGYIK VDEWMRTSVS GIFAAGDCTS MWLGFRQVIT
     SVAQGAVAAT SAYRYVTEKK GKK
//
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