ID A0A316YZ24_9BASI Unreviewed; 445 AA.
AC A0A316YZ24;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acyl-CoA dehydrogenase NM domain-like protein {ECO:0000313|EMBL:PWN94004.1};
GN ORFNames=FA10DRAFT_270904 {ECO:0000313|EMBL:PWN94004.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN94004.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN94004.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN94004.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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DR EMBL; KZ819634; PWN94004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316YZ24; -.
DR InParanoid; A0A316YZ24; -.
DR OrthoDB; 2264654at2759; -.
DR Proteomes; UP000245768; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000245768}.
FT DOMAIN 60..141
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 277..415
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 48450 MW; D36A4C15DB27E638 CRC64;
MAPTASASAV PPPPASAKGA SRIQPDPELV SYPSFNARPK TPEEYYERAK QVADLLHQDE
AVRDRGNVVP NRQVQLLKDA GLVTLLGPTS KGGGGQTWNE AYHVVRLVAQ GDGSLAQLLG
YHYIWFWAAA LVGTDEQRAR LEAEFTEKNY FIGGAVNPRD SDLKVRQHPQ DKAKIVFDGK
KTFSTGSKVS DVTILEGSFE GAAADAPHVF VPVLSKQPGI VYGDEWVDVL GMRGTQSGGV
TISNVEADWR DALGFVDGKF TPLGPYNTLN LPAIQLVFTS FYLGIAEGAL QRGIEYTRNN
TRGWPYQPHP PSRGTDEVYI QDGYGTLQAR LWASSAQIAQ TIKLASSILG TNPRQNVTAA
QRADLAVQVA AAKVNIVDFG LDVTSKLYEL QGARSVSGKY GFDVAWRDLR THSLHDPIAH
KRAEVGRYAL FGPGQDGWPT PTWYT
//
