ID   A0A1C5CQS9_9ACTN        Unreviewed;       143 AA.
AC   A0A1C5CQS9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain {ECO:0000313|EMBL:SCF72817.1};
GN   ORFNames=GA0115254_11393 {ECO:0000313|EMBL:SCF72817.1};
OS   Streptomyces sp. Ncost-T10-10d.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839774 {ECO:0000313|EMBL:SCF72817.1, ECO:0000313|Proteomes:UP000198750};
RN   [1] {ECO:0000313|Proteomes:UP000198750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ncost-T10-10d {ECO:0000313|Proteomes:UP000198750};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMDF01000118; SCF72817.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5CQS9; -.
DR   Proteomes; UP000198750; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR   PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198750}.
FT   DOMAIN          30..136
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   143 AA;  15227 MW;  51FD5B01B44F928C CRC64;
     MCPTSGVKGP IAVRDILGQP GPGADYRALP RVTFAEPEIG AVGLTEQQAR ERGLRVRTSV
     LPIAFSTRGW IHGPGNEGLI KLVEDADRHV LIGATSAGPA GGEVLYGLNV AVHAEIPVDR
     LQHMIYTYPT FHRTVEAALG ALR
//