ID M3AYD1_SPHMS Unreviewed; 452 AA.
AC M3AYD1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:EMF12522.1};
GN ORFNames=SEPMUDRAFT_65681 {ECO:0000313|EMBL:EMF12522.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF12522.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF12522.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF12522.1,
RC ECO:0000313|Proteomes:UP000016931};
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 paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; KB456264; EMF12522.1; -; Genomic_DNA.
DR RefSeq; XP_016760643.1; XM_016909728.1.
DR AlphaFoldDB; M3AYD1; -.
DR STRING; 692275.M3AYD1; -.
DR GeneID; 27906865; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_2_1; -.
DR OMA; QSCLHAN; -.
DR OrthoDB; 1113861at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789:SF172; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12410)-RELATED; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT DOMAIN 13..365
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 452 AA; 50101 MW; 2E528AED6CAEC4BF CRC64;
MALPGTNWKP FNIAVVGGGI GGVAVSIALR RAGHHVTIYE RADYAGEVGA SISCAANGMK
WLREWDVDIA KGDGVYLRKL INRDWKTGEP VSVYDLGDYE QKWGNPYYMF HRQDMHKMLM
DTATQEQGTG TPVKLVVNHK CIEVDTSTGL ITFANGLQFQ HDVVIGADGI GSAIRKIIGI
HVDKRPSDSS CLHANVITSA AVSQGFVNYS LNSAIEYWGG HHSWNKIVLS PCNSGSLLSY
YCFFPREKGD FTEQKWDAES TVEDLLAPYP DLDTQVKNHL SIGQEIRPWR LWVHQPYSHW
HQSRACIMGD AAHPMMPDQS QGACMALEDS AALGLIFSKE YFPGSVEGAL ELYERVRKPR
ASRVQAASAR ARENIHERIG FSDNTSNPLY KVEDEEGKLT MKEMNGYDMR EDIRRKWPGE
WPEGLGGVGG GREEKGDDGV AMQQAGVVVA AH
//
