ID A0A2P7YC51_9PEZI Unreviewed; 649 AA.
AC A0A2P7YC51;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Acyl-CoA dehydrogenase family member 11 {ECO:0000313|EMBL:PSK33559.1};
GN ORFNames=B9Z65_7446 {ECO:0000313|EMBL:PSK33559.1};
OS Elsinoe australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK33559.1, ECO:0000313|Proteomes:UP000243723};
RN [1] {ECO:0000313|EMBL:PSK33559.1, ECO:0000313|Proteomes:UP000243723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:PSK33559.1,
RC ECO:0000313|Proteomes:UP000243723};
RA Cheng Q.;
RT "Draft genome sequence of Elsinoe australis.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSK33559.1}.
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DR EMBL; NHZQ01000448; PSK33559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YC51; -.
DR STRING; 40998.A0A2P7YC51; -.
DR Proteomes; UP000243723; Unassembled WGS sequence.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 2.40.110.20; -; 1.
DR Gene3D; 6.10.250.600; -; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR041504; AidB_N.
DR PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42707:SF2; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF18158; AidB_N; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000243723}.
FT DOMAIN 59..167
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 455..521
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 71255 MW; E65F459439042F6D CRC64;
MSRHADAHRR SQAAPPAIDV DLTTPPIHAA RPSSGTEGFF QEPPRLINPY DDDFSFQRVL
QQLSRFGALT LDPEILRLNS DAENNPPKLE QYDSFGRLKN LLITAEGWRT LTAIHHQEGL
IALGYVNKYG PYDRLHQHLK TFLWSPSSGG VTCPAAMQDG AAALLTRLLA NPTANNVNNE
TEQVLRSALT RLTSRDPTIA WTSGQWMTER PGGSDVRNTE TLATFSPDTT PSPTRSTASD
GLPLGPWSIT GFKWFSSATD ANMSVLLAKT PGYATPSLFF APVRRTTTYP STASPAPPKQ
TYNGIHPHRL KPKLGTRSLP TAELILHDLR AHLLGAEGQG VKEISTVLNI TRLHNAIGAV
AAWSRALAVA RAWSRVRSSG GRRLDQWPLH VRGLAGETVE YHVATLGAFW GVGLLGGSEH
SAGSEGGKGR REEGEEGRGR LSPANGKDVL RLLRLVTPVL KAVTALKAIE GVRSRMEGMG
GVGYIENVEV EINLAKLYRD TNILSIWEGT TDVMGLDVVR VLKGRDGKEV LGALKMWVET
VSKEWKEGQL VVQARDLVKR RVEELTALVA RDVEQVTYEA KRLLELIFDI IGAVLVVEDA
LSDRNDRVMR MAERWMSARV ERTQSSGWRE CAAVDRQIVF GVDSTSSKL
//
