ID N1QEK3_SPHMS Unreviewed; 578 AA.
AC N1QEK3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=FAD-linked oxidase-like protein {ECO:0000313|EMBL:EMF10835.1};
GN ORFNames=SEPMUDRAFT_143451 {ECO:0000313|EMBL:EMF10835.1};
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:EMF10835.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF10835.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF10835.1,
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; KB456267; EMF10835.1; -; Genomic_DNA.
DR RefSeq; XP_016758956.1; XM_016903044.1.
DR AlphaFoldDB; N1QEK3; -.
DR STRING; 692275.N1QEK3; -.
DR GeneID; 27900181; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_024402_0_0_1; -.
DR OMA; NVPTIRH; -.
DR OrthoDB; 5474593at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748:SF114; ARYL-ALCOHOL OXIDASE VANILLYL-ALCOHOL OXIDASE (AFU_ORTHOLOGUE AFUA_3G09500)-RELATED; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT DOMAIN 85..280
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 578 AA; 64529 MW; AEDFE465212EBB64 CRC64;
MKQIDELQGE APIAFRAPVG GGTNTAPLTL PPNTSLEKFN DFMSSIAGIV GTENATVVSS
DAELQQEDYL DPSKAHDMYH ITEKEYFVSS AVVAPRNVGE VQAIMKLCNE FEIPVWPFSI
GRNVGYGGAA PRVPGSIGLD MGRNMNKVLE VNEDGAYAVL EPGVTFLDLH NYLVEKNLRD
KLWIDTPDLG GGSVIGNTVE RGVGYTPYGD HWMMHCGMEV VLPDGSLWRS GMGGLPNPKA
DPNARPEDQA WNETFGLFNY GFGQYNDGIF TQSSLGIVVK MGIWLMVNPG GYQSYLITFP
KDSDLHKAVE IIRPLRVGMV LQNVPSIRHI LLDAAVMGNR KAYKESDELL TDDEMDAIAK
KLNLGRWNFY GAVYGPEPVR QVMLSVIKQS FLSIEGAKYY EPEDMPDNLV LQTRHLTLQG
VPTTTELKWV DWLPNGAHLF FSPIAKVSGD DAVAQYEVTR RRCEEAGFDF IGTFVIGMRE
MHHIVCIVFN RKDPESRRRA HWLIKTLIDD AVARGWGEYR THLAVMDQIA KTYSWNDHAQ
LRLNEKIKEA LDPKGILSPG KNGVWPKQMN AEDYKVPF
//