ID A0A0L6WUX4_9AGAR Unreviewed; 548 AA.
AC A0A0L6WUX4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative flavoprotein C26F1.14C {ECO:0000313|EMBL:KNZ79211.1};
GN ORFNames=J132_09722 {ECO:0000313|EMBL:KNZ79211.1};
OS Termitomyces sp. J132.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC Termitomyces.
OX NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ79211.1, ECO:0000313|Proteomes:UP000053712};
RN [1] {ECO:0000313|Proteomes:UP000053712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA Hu H., Poulsen M.;
RT "The genome of Termitomyces.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
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DR EMBL; KQ412454; KNZ79211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6WUX4; -.
DR STRING; 1306850.A0A0L6WUX4; -.
DR OrthoDB; 495825at2759; -.
DR Proteomes; UP000053712; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR CDD; cd03478; Rieske_AIFL_N; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
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 InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
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 Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053712}.
FT DOMAIN 6..102
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 548 AA; 58554 MW; 7BCA8D33B3A17C23 CRC64;
MSTKTIAVLD DSELHDGQMK EVAFGEGKVL LSRLGDKIHA TSAFCTHYGA PLAKGVLTSD
ARVVCPWHGA CFNVCTGDIE DSPAPSALHS FKAHVSDGKI YVTANPAHAL GNNKARQPTL
LSSGTDSVGK GLIIVGGGAA AFHTSSHLPQ HGYSLPITIL SKETYTPIDR TKLSKALVVD
PMKIEWKTAG EFKIKYGTTI RLGVEVTSLD LNKKEVILDG GKDTLGYDKL VLATGGTPRR
LPVEGAQLEN VYTFRGITDA QKVEAAAKEG KRLVVIGSSF ISMEIVVAVS KKKLASIDVI
GMESHPFEGV LGKEVGAGLQ KYHESQGVKF HMETKVEKII PQEGNPNLAG GVVVNGVTLP
ADFIVMGVGV VPTTEYVKGS GIALEKDGGI KVDKYLRVQS GPDQENIFAV GDIAVYPQVT
GGYYRIEHWN VAGNHGRAIG KTISGTPQEF VKIPIFWSSQ GQQLRYCGVG HDYDDIFISG
DPEEMKFIAY YGRHGRIVAV ASMQNDPVVS QASELLRLGL MPSLEEVRAG KSLLSVDIST
TGIVNSAA
//
