ID A0A428PNL5_9HYPO Unreviewed; 418 AA.
AC A0A428PNL5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Acyl-CoA dehydrogenase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CEP53_007396 {ECO:0000313|EMBL:RSL54566.1};
OS Fusarium sp. AF-6.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL54566.1, ECO:0000313|Proteomes:UP000287544};
RN [1] {ECO:0000313|EMBL:RSL54566.1, ECO:0000313|Proteomes:UP000287544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL54566.1,
RC ECO:0000313|Proteomes:UP000287544};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-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:RSL54566.1}.
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DR EMBL; NKCJ01000158; RSL54566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428PNL5; -.
DR STRING; 1325737.A0A428PNL5; -.
DR Proteomes; UP000287544; 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:UP000287544}.
FT DOMAIN 40..132
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 256..392
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 46446 MW; FFB21F60E4F20CDD CRC64;
MQSFKAEQAR VQANKRWAEE PKPDTPLGWV KRAREVADIL KLDAAERDAA GKTPFAEVQL
LKDAGLVNLL GPREFGGGGE TWQTSYKVTT EIAKADGSIG HLLGNHYSWF WSSQILGTPL
QARRWLREFT EGNYYLGGAV NPRNADMIAR DEGDSLVFNG DKFFSTGGVI SDVTVLEGVL
EDEAKTHVFA YVSTKDPGIS FKGDWDVIGQ RLTESGGCVI RNVRVSWEHI AGYEDKELTP
RDAYHDFILP PVQLQFAAVH VGVGIGALEA ATEYTRTRTR AWPYGGDDKA KATDEWYIRE
GYGRLQASLW AAEALVDRTA ERISKLIHAP REELTQEARG EIAVQVAASK ATAIEAAINV
SSKFFELTGA SSGLSKYGFD RFWRNTRLHS LHDPIAYKFR EVGSWALLGE IPEPSWYT
//
