ID A0A0G2DVP9_9PEZI Unreviewed; 438 AA.
AC A0A0G2DVP9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Putative salicylate 1-monooxygenase {ECO:0000313|EMBL:KKY14251.1};
GN ORFNames=UCDDS831_g08312 {ECO:0000313|EMBL:KKY14251.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY14251.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY14251.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY14251.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY14251.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY14251.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKY14251.1}.
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DR EMBL; LAQI01000239; KKY14251.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2DVP9; -.
DR Proteomes; UP000034182; 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; PTHR46720:SF4; FAD-DEPENDENT MONOOXYGENASE AFOD-RELATED; 1.
DR PANTHER; PTHR46720; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 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 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:KKY14251.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..376
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 438 AA; 48469 MW; D372720A6E11658E CRC64;
MSSDEASFHV AIVGGGIVGL SMAVGLLRRN IEFTIFERAA SFQELGAGIG FTRNVERAMQ
LLDPRIHAAF RTVAAQNTED YFYYVDGFNW DESNPEHEET ILKLYLGERG FEGCRRSDFL
KELVRHIPEE KVKFAKELIS TADMGDDGKV LLTFQDGTSA DADIVIGCDG IRSKMRRIML
GDTHPASRPS YSHKYAIRGV VPMEKARAAL GEWRTSNRMM HLGPNAHAVT FPVAFGTLLN
VVAFVTDPNE WQAEDGKLTA PAKKSEATHG FANFSPVVRT IMDLLPDQLD KWAVFDTYDH
RVPTYVAGRL CLAGDAAHAA SPHHGAGAGC GIEDCLALAV LIEAAVHDSS MERSASVRTA
LQVYNHVRYQ RSQWLVDTSR VVGNVYEFSH LESGSDHKQI AREIEVRSHQ VWFYDVDGMV
AEALSQLHQK TADANTDP
//