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Database: UniProt
Entry: A0A0C1MW80_9CYAN
LinkDB: A0A0C1MW80_9CYAN
Original site: A0A0C1MW80_9CYAN 
ID   A0A0C1MW80_9CYAN        Unreviewed;       545 AA.
AC   A0A0C1MW80;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:KIE06527.1};
GN   ORFNames=DA73_0234705 {ECO:0000313|EMBL:KIE06527.1};
OS   Tolypothrix bouteillei VB521301.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE06527.1};
RN   [1] {ECO:0000313|EMBL:KIE06527.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VB521301 {ECO:0000313|EMBL:KIE06527.1};
RX   PubMed=25700407;
RA   Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA   Adhikary S.P., Tripathy S.;
RT   "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL   Genome Announc. 3:e00001-15(2015).
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:KIE06527.1}.
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DR   EMBL; JHEG02000059; KIE06527.1; -; Genomic_DNA.
DR   RefSeq; WP_038081766.1; NZ_JHEG04000001.1.
DR   AlphaFoldDB; A0A0C1MW80; -.
DR   STRING; 1479485.DA73_0234705; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR48105:SF5; BLR1248 PROTEIN; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          9..128
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
SQ   SEQUENCE   545 AA;  59326 MW;  B199BF3B6E9433F1 CRC64;
     MALEHHPIAF PKLDDEQIVA LGKFAKLKAF QAGETLFAEG TPNYQFFAIK RGEVAIVDRS
     SGHDRIVTIH EPGEFTGDVD ILTGRPAVVR AIAHSNCKVY EIAADDLRRI LNEMPRLSDV
     LLRAFLMRCQ LLEESGFVAV RVVGSRYSPE THRIREFLAK NKVPFTWIDL ENDPQVDTLL
     TQFRISEDET PVVICGNDKL LKNPSMAELA DCLGIKKPIE HTIYDLVVVG AGPAGLAAAI
     YGASEGLKTL VLDKMGPGGQ AGSSSKIENY MGFPTGLSGS DLANRAAIQA EKFGAILTAP
     AEVVQLSRET GYYALRLESG EEISAKCILI CAGASYRKLA VEGYDRFEGS GIYYAATTVE
     ALLCQDAQVV VVGGGNSAGQ AAVFLSEQTQ KVFLLIRGGD LGKTMSHYLV QRIEQTPNIE
     VQCYTEICKM YGNKWLEAVE VFCSQTGQAD TIKCLAIFVF IGAVPHTKWL PEAIQCDRNG
     FVKTGLRVME SGEWTLRRQP FLLETSLPGI FAAGDVRLGS IKRVASAVGE GAMAVQFVHE
     YLASS
//
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