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Database: UniProt
Entry: A0A1C4PCF0_9ACTN
LinkDB: A0A1C4PCF0_9ACTN
Original site: A0A1C4PCF0_9ACTN 
ID   A0A1C4PCF0_9ACTN        Unreviewed;       423 AA.
AC   A0A1C4PCF0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Reductase C-terminal {ECO:0000313|EMBL:SCE08271.1};
GN   ORFNames=GA0115251_14016 {ECO:0000313|EMBL:SCE08271.1};
OS   Streptomyces sp. TverLS-915.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839763 {ECO:0000313|EMBL:SCE08271.1, ECO:0000313|Proteomes:UP000198957};
RN   [1] {ECO:0000313|EMBL:SCE08271.1, ECO:0000313|Proteomes:UP000198957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TverLS-915 {ECO:0000313|EMBL:SCE08271.1,
RC   ECO:0000313|Proteomes:UP000198957};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; FMCE01000347; SCE08271.1; -; Genomic_DNA.
DR   RefSeq; WP_010268439.1; NZ_FMCE01000347.1.
DR   AlphaFoldDB; A0A1C4PCF0; -.
DR   Proteomes; UP000198957; 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   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; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198957}.
FT   DOMAIN          8..314
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          334..419
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
FT   REGION          401..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   423 AA;  45032 MW;  0C052FE0EB7B3994 CRC64;
     MVDADQTFVI VGGGLAGAKA AETLRAEGFT GRVILVCDER EHPYERPALS KGYLLGKDAR
     DSVFVHEPGW YAGAEVELHL GQPAVSLDAA NHTLTLGDGT PLHYDKLLLA TGSEPRRLEI
     PGTDLAGVHH LRRLAHAERL RRTLANLGRD NGHLLIAGAG WIGLEVAAAA REYGAEVTVV
     DAAPTPLHHV LGPEVGRLFT DLHAERGVRF HFGARLTEII GQDGMVLAGL TDDGEEHPAH
     DVLAAVGAAP RTALAESAGL ALAAPEHGGG IAVDAGLRTS DPDVYAAGDV ASVPLGLFPG
     APLRVEHWAN ALNGGPLAAR AMLGRDVTYD RVPYFFSDQY DLGLEYSGWA PPGQYDQVLV
     RGDAAKRRFL AFWLLDGQVR AAMNVNVWDV TEPLQKLIRS GSRPDPEALA DPNVPLESFL
     PSP
//
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