ID N1QLL2_SPHMS Unreviewed; 447 AA.
AC N1QLL2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=FAD-dependent monooxygenase {ECO:0000313|EMBL:EMF12191.1};
GN ORFNames=SEPMUDRAFT_46179 {ECO:0000313|EMBL:EMF12191.1};
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:EMF12191.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF12191.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF12191.1,
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).
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DR EMBL; KB456265; EMF12191.1; -; Genomic_DNA.
DR RefSeq; XP_016760312.1; XM_016908986.1.
DR AlphaFoldDB; N1QLL2; -.
DR STRING; 692275.N1QLL2; -.
DR GeneID; 27906123; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_3_2_1; -.
DR OMA; SLTIHWA; -.
DR OrthoDB; 1776894at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase 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; PTHR47178:SF1; FAD-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47178; MONOOXYGENASE, FAD-BINDING; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000313|EMBL:EMF12191.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 151..377
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 447 AA; 49959 MW; 3EDDE249EA73581F CRC64;
MGAPTAQQPQ KEQKHIHILI IGAGLTGLIL AQALRKLQHL ASLNSNNTNT TTPPPPLITY
EIFERDPRAF FRGGGWSLTI HWALTDLQNL LPDEIMQNFE SCLVNRDAAA AGQAGNFQFL
NLCTGERVEA WPIPRGAASR VSRERILELL MRGVDVRWSK HLTSLDFSHP SSVTATFADG
SQAQGNLVIG CDGARSAVRR TLCATTWQNN RLPVRLLGLR VKFPLAKVAK CLAIDPHFFQ
GGDPLSNVYF WFSFIHLPRA VDVEGKGEEE EYATCQMMVS WPYSGEAADE MPETQTARRE
RIRQLATNWN ETFRDLVYSI PETTELREIV LEDWPPVQGR WDNHNGRVTL VGDAAHCMTM
FRGEAANHGV IDVSHLIKTC FPTTANTETM QPTRSCDLAQ AVKSYEEEMI TRTFPAVLKS
RQACLDANNF ASVNKESPLI AKRAMKE
//
