ID M3AIZ7_PSEFD Unreviewed; 459 AA.
AC M3AIZ7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
DE Flags: Fragment;
GN ORFNames=MYCFIDRAFT_134411 {ECO:0000313|EMBL:EME84571.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME84571.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME84571.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME84571.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; KB446557; EME84571.1; -; Genomic_DNA.
DR RefSeq; XP_007925195.1; XM_007927004.1.
DR AlphaFoldDB; M3AIZ7; -.
DR GeneID; 19330917; -.
DR KEGG; pfj:MYCFIDRAFT_134411; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_018354_1_2_1; -.
DR OrthoDB; 879734at2759; -.
DR Proteomes; UP000016932; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF34; FAD BINDING DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_3G02770); 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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016932}.
FT DOMAIN 20..191
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EME84571.1"
SQ SEQUENCE 459 AA; 51228 MW; 2256CA0EB22E976F CRC64;
SSNTTQFDLE KSDFWSSFQA EVSPSCFVSP RCPEEVAKIL DILKHTECRF AVKSGGHAAF
QGASNIDRGV TILLKELDAL ELDRDAGIVK VGTGSLWIDV YEYLTPRKLS VVGGRVTGIG
VGGLVLGGGI SFFSGRYGWA CDGVRNFEVV VASGEILQVN QDSYPDLYWS LRGGGNNFGI
VTRMDLEVFE QGDLWGGSIT LPWTVKDEVI DALYDFGRRQ SSENEEVDVD ASVWAAFGYT
QQPQPGKFIS IEPVYAKPVE NPVVFENFTK LKPVLMSTAK IRNLTDISKE LNQSNPNGLR
ETYWTHNFIL TREVMTKCLE IFEEELKSIE DVEGIVPVML FQPLTTAVIR KFARNGGNAL
GITDKDGPLL LMSVPIMWSD SSRDDEVLAF ARTVIDRCVE ESRKLGAFHP YIYQNYAAKE
QRVFESYGKA NPERLRAVSG MHDPDGVFQR LQPGYHKLW
//
