ID A0A1J7INR1_9PEZI Unreviewed; 551 AA.
AC A0A1J7INR1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Putative apoptosis-inducing factor 2 {ECO:0000313|EMBL:OIW29239.1};
GN ORFNames=CONLIGDRAFT_655167 {ECO:0000313|EMBL:OIW29239.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW29239.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW29239.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW29239.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-2016) 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; KV875098; OIW29239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7INR1; -.
DR STRING; 1408157.A0A1J7INR1; -.
DR InParanoid; A0A1J7INR1; -.
DR OrthoDB; 495825at2759; -.
DR Proteomes; UP000182658; 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:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 2.
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:UP000182658}.
FT DOMAIN 7..105
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 551 AA; 59033 MW; 7B2D6AB414FF22AE CRC64;
MAQEYKIKDL QSLDLKPGEK KEIELEGLDS KVLLLNAGGK IQAVGPRCTH YGAPLVKGVL
STNGRLTCPW HGACFNAKTG DVEDAPALDS LPVFAVTERD GSFYLTGDAE TIKAGKRKPT
FKNKSAQRTA SSDKVVVVGG GSGACGVVEG LREKGFDGPI TMITSEGYLP IDRTKLSKAL
LTDLSKLQWR DDDFYKSASI DVVKDEVTDV DLQNKTVTTE KGEKYPYTKL VLATGGTPKN
LPLQGFKVLG NIFTLRTVHD AKKIVEAIGE QKGKKIVIIG SSFIGIEVGG ATAKDNDVTI
VGMEKAPLER VLGEEVGNII RKGMEGKGLK FYMSAGVDKA EPSTSDPTKV GAVFLKDGTK
LEADLVILGV GVSPATAYLR SNNIIKLEDD GSIKTDEVFS VVGIKDVYAI GDIATYPYNG
PGGEGRYTRI EHWNVAQNAG RTVASHIVNP KVTPEFFTPV FWSALHSQLR YCGNTTHGYD
DIVMQGSPDD GKWAAFYAQG ETVVAVATMG MDPVMSQAAQ LMRVGKMPPK SELKPGLVQG
GLDILSLGPP E
//
