ID M7SJ78_EUTLA Unreviewed; 484 AA.
AC M7SJ78;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative fad binding domain-containing protein {ECO:0000313|EMBL:EMR66399.1};
GN ORFNames=UCREL1_6606 {ECO:0000313|EMBL:EMR66399.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR66399.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB706657; EMR66399.1; -; Genomic_DNA.
DR RefSeq; XP_007794500.1; XM_007796309.1.
DR AlphaFoldDB; M7SJ78; -.
DR STRING; 1287681.M7SJ78; -.
DR KEGG; ela:UCREL1_6606; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_19_3_1; -.
DR OMA; DWTHPSG; -.
DR OrthoDB; 981595at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF242; FAD-BINDING DOMAIN-CONTAINING PROTEIN; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..189
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 484 AA; 53355 MW; 69F1AA01C6C73F20 CRC64;
MASPSYTEFS RQGQEKMERD DQNKLNVIIV GAGLGGLGAA IAILLAGHNV TILEAAREIG
EVGAGIQVLP NAAKVLFSWG VEEQLNRHAT RPRQCNFLGW KGNHLSKMDY HGYARAAGAP
FLDFHRANLH SCLLDRAVEL GGNIMTNAQV QNFAISEDDT TASVLLADGR VLVADLIVGA
DGINSTLREV FLGRQDPPQP TGDLAYRLLL NTTDMLDDPE LRPMVESPQV NYWVGPGAHA
VSYVLRGGEF FNVVLLVPDD LPPDVAANTA AGDVAEMRAH FAGWDPRLRK LALLGSGEKS
TILKWRLCIR PGLDPTWSHP SGAFTMLGDA VHATLPYLAS GAGMSLEDGG VLGLCLGRLA
DKSPTSKQRA LRAYEACRRE RTEKVVERGT YNQWIYHLPD GPEQEDRDRR FRAFGESDQR
WLAEGSPVLP ESQETGDDPF PWRYHGVARW LLTYDMWKDV EARWSQYALP LPVSDHPHPT
RPNL
//
