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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//