ID K2S3T4_MACPH Unreviewed; 502 AA.
AC K2S3T4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=FAD linked oxidase {ECO:0000313|EMBL:EKG21558.1};
GN ORFNames=MPH_01152 {ECO:0000313|EMBL:EKG21558.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG21558.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG21558.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG21558.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG21558.1}.
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; AHHD01000047; EKG21558.1; -; Genomic_DNA.
DR AlphaFoldDB; K2S3T4; -.
DR STRING; 1126212.K2S3T4; -.
DR VEuPathDB; FungiDB:MPH_01152; -.
DR eggNOG; KOG1262; Eukaryota.
DR HOGENOM; CLU_025883_0_0_1; -.
DR InParanoid; K2S3T4; -.
DR OrthoDB; 2783952at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0050614; F:delta24-sterol reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR040165; Diminuto-like.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR10801; 24-DEHYDROCHOLESTEROL REDUCTASE; 1.
DR PANTHER; PTHR10801:SF10; FAD BINDING DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_6G14300); 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 1..168
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 502 AA; 56868 MW; 9FE3006B786BC5AF CRC64;
MEEHKRHVEA IAAKVRSFRE QGVKFRISHG STNSTRPSAT RRDHNVINLS ALSNVLKVDK
ESRTAWVEPN VPMDRLVEET MKYGLVPPVV MEFPGITVGG GYAGTSGESS SFKHGFFDRT
INWVEMILAS GEVVKASRLE RADLFHGAAG AAGSLGTTTL VELRLKDARK FVETTYHPVS
SIAEAIAKCR TVIEDPELEY VDGILFSKSH GAIITGRLTD SPPEGTPIQC FSDAKDPWFY
LHVQERTKSK AESITEAIPL AEYLFRYDRG GFWVGQSAFD YFCFPFNDFT RWWLDEFLHT
RMLYTALHAS GQSKQFTVQD LALPFSAAEK FIEYTSEATG IWPLWLCPLK QSPSPTLHPH
NSSVLEADGQ TLQPLLNIGL WGKGPTNHDA FVALNRSIED KVHELGGMKW LYAHTYYAED
DFWKDFDRGW YETLREKYGA TSLPSLYEKV KVDVEAEKRM IASSWLMCIR ETWPISGIWA
LVRAIQSGSY LHARNSTWKY RR
//
