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Database: UniProt
Entry: A0A250VQ77_STROL
LinkDB: A0A250VQ77_STROL
Original site: A0A250VQ77_STROL 
ID   A0A250VQ77_STROL        Unreviewed;       558 AA.
AC   A0A250VQ77;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Fused response regulator/thioredoxin-disulfide reductase {ECO:0000313|EMBL:GAX56236.1};
GN   ORFNames=SO3561_07803 {ECO:0000313|EMBL:GAX56236.1};
OS   Streptomyces olivochromogenes.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1963 {ECO:0000313|EMBL:GAX56236.1, ECO:0000313|Proteomes:UP000217446};
RN   [1] {ECO:0000313|Proteomes:UP000217446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3561 {ECO:0000313|Proteomes:UP000217446};
RA   Dohra H., Kodani S.;
RT   "Streptomyces olivochromogenes NBRC 3561 whole genome shotgun sequence.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC         H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00000849};
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:GAX56236.1}.
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DR   EMBL; BDQI01000024; GAX56236.1; -; Genomic_DNA.
DR   RefSeq; WP_067381225.1; NZ_KQ948474.1.
DR   AlphaFoldDB; A0A250VQ77; -.
DR   STRING; 1963.AQJ27_41770; -.
DR   Proteomes; UP000217446; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR48105:SF5; BLR1248 PROTEIN; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217446}.
FT   DOMAIN          11..134
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         68
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   558 AA;  59732 MW;  393C52B7FDA842CB CRC64;
     MAQAAATART VILTVDDDPG VSRAVARDLR RRYGESHRIV RAESGDAALD ALKELKLRGD
     QVAVILADYR MPQMNGIEFL EQALDVYPGA RRVLLTAYAD TNAAIDAINV IDLDHYLLKP
     WDPPEEKLYP VLDDLLDAWR TSDYRPVATC KVVGHRWSAR SSDVREFLAR NQVPYRWYSS
     DTPEGQRLLS AAGQDGERLP LVITPDGTPL VEPDDPDLAA RVGLATTPTS EFYDLVVIGG
     GPAGLGAAVY GASEGLRTVL VERSATGGQA GQSSRIENYL GFPDGVSGGQ LTDRARRQAA
     KFGAEILTAR EVTGLEVTGA SRTIRFSDGS AISAHAVILA TGVSYRQLQA PGLADLTGCG
     VFYGSALTEA AACQGHDVYI VGGANSAGQA AMYLSRGAKS VTLLVRGTSL SASMSHYLIQ
     QIEEASNITV RTCTVVDAAH GTDHLEQLTL RDVTSGHTEL VDAQWMFVFI GAAPLTDWLE
     GTVLRDGRGF IPSGPDMTID GQPPKGWELD RPPYHLETNI PGVFVAGDAR AESAKRVASA
     VGEGAMAVML VHRYLEQS
//
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