ID M3DD78_SPHMS Unreviewed; 609 AA.
AC M3DD78;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=FAD-binding domain-containing protein {ECO:0000313|EMBL:EMF15779.1};
GN ORFNames=SEPMUDRAFT_61001 {ECO:0000313|EMBL:EMF15779.1};
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:EMF15779.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF15779.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF15779.1,
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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; KB456261; EMF15779.1; -; Genomic_DNA.
DR RefSeq; XP_016763900.1; XM_016909547.1.
DR AlphaFoldDB; M3DD78; -.
DR STRING; 692275.M3DD78; -.
DR GeneID; 27906684; -.
DR eggNOG; ENOG502QU1B; Eukaryota.
DR HOGENOM; CLU_018354_4_4_1; -.
DR OMA; APPANCF; -.
DR OrthoDB; 1641938at2759; -.
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; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
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; PTHR13878:SF171; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR Pfam; PF08031; BBE; 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:UP000016931};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..609
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004033230"
FT DOMAIN 131..315
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 609 AA; 64535 MW; 6E90A6E663339EF1 CRC64;
MASLLGFTAS LACLFSYALA TPLAGRASTP ISQITPSQWQ ALNSTVSGRL QTATPVAKPC
YSYYNGVFTT PDLQQCKAVQ DGYTTEDSIV ANFGGYQYPN WASCQAKGQS CGLDFTAPQN
PAYYAPPANC FQGSVASYYI NVQAVSDIQA ALKFANQYGI PLVVKNSGHD FKGRSSAPNS
LALWTHNIQP PIALTRGFTP DGCSAPVADA VTFGAGQGFA GVYEFAEAND ITVVGGSSRT
VGPAGGWISG GGHSALSNTL GLGVDNVLQI RTVLPNGTYI TANRCQNQDI FFALRGGGGN
TFGVNWEMTT TAHPKMQLEV AYITFAGTNA SSIRRFIDIC TQLGDRWATD GWGGYIAPGA
VTSLVSGMIM MTPKLTHDQA IASMKPLTDY VASLGNVATH NSVTTEPSYY TAYQKYIAPN
QEKVGVGIAM GSKFVPRSML QSSAGQQKVA DAIEKSSSMV IPVTGQGGVD YRSLTYGSPF
QILVTAPSSY QTDGSSSVTP AWYGANGAAW HVCLGQGITN DASADTITAA FRNANQATQV
LRDAVGSPGA YLNEADTFEP DPVSTYWGSD NYNKLLALKK QLDPNNVLTC WQCIGWDSSD
ARYGCYPRI
//
