ID A0A2V1DUA4_9PLEO Unreviewed; 436 AA.
AC A0A2V1DUA4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Acyl-CoA dehydrogenase NM domain-like protein {ECO:0000313|EMBL:PVI01807.1};
GN ORFNames=DM02DRAFT_704192 {ECO:0000313|EMBL:PVI01807.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI01807.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVI01807.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVI01807.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ805352; PVI01807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1DUA4; -.
DR STRING; 97972.A0A2V1DUA4; -.
DR Proteomes; UP000244855; 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:UP000244855}.
FT DOMAIN 45..135
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 266..410
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 436 AA; 47865 MW; 1F12061EA6DF3AF2 CRC64;
MTDSSQTNGT SFSSRDPAVY QGYASKWSSL PQDEAGWLKR AQEVADVLAV DAVQRDQENK
SPLAEVALLK HSGLLKVLGP KKYGGGEQPW SVGYKAIRKV AEADGSLGML LGYHLLWSTT
ANVVGSPEQA ERYQKLIIEN NYFIGGAVNP RDSDLKIQSS GDKIVFNGFK HFNTGGVVSD
LTVLEGVLEG TEDHIFAFAE TRQPGIVFSH NWNNIGLRLT ESGSVKIDNV EVPWTDALGW
DPESKKPDPE VLKIPFASLL LPTIQLVFSN FYLGIALGAL DYASKYTTKN TRAWPFGGDN
KEQATDEFYI LSTYGNYHAH LRAAVALADR SGLQIDAIYS TYSGDTATRA KLTAQERGEV
AEWVASTKVV TTDTGLRVTA GVFEVTGAKA TSTKVGLDRF FRDVRTHTLH DPVAYKNREL
GRFQLLGEVP EPTWYT
//