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Database: UniProt
Entry: A0A1J9RT51_9PEZI
LinkDB: A0A1J9RT51_9PEZI
Original site: A0A1J9RT51_9PEZI 
ID   A0A1J9RT51_9PEZI        Unreviewed;       486 AA.
AC   A0A1J9RT51;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Monooxygenase fad-binding protein {ECO:0000313|EMBL:OJD30709.1};
GN   ORFNames=BKCO1_5700013 {ECO:0000313|EMBL:OJD30709.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD30709.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD30709.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD30709.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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:OJD30709.1}.
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DR   EMBL; MNUE01000057; OJD30709.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9RT51; -.
DR   STRING; 236234.A0A1J9RT51; -.
DR   OrthoDB; 2332834at2759; -.
DR   Proteomes; UP000183809; Unassembled WGS sequence.
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; PTHR47356; FAD-DEPENDENT MONOOXYGENASE ASQG-RELATED; 1.
DR   PANTHER; PTHR47356:SF2; FAD-DEPENDENT MONOOXYGENASE ASQG-RELATED; 1.
DR   Pfam; PF01494; FAD_binding_3; 2.
DR   PRINTS; PR00420; RNGMNOXGNASE.
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   Monooxygenase {ECO:0000313|EMBL:OJD30709.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183809}.
FT   DOMAIN          8..174
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          290..352
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   486 AA;  52832 MW;  C5C53B2B96A620E2 CRC64;
     MAASESKHQV IIVGGGITGL TLALMLQRLR IDYVLLEAYQ SVTPNVGASI GLYANGLRIL
     DQLGVYRDVC AISQSAKAHI VRDGETGRRL SRMPCGPILE ARHGYAPKFM ERCELLRVLY
     GHVAEKERIL VDKRVRRIET YEDRVLVHTD DGATFEGQIV VGADGVHSTV RKEMWRNADE
     KDPGAIPKED RQNIKCEYAC VFGLAKPTPG IAPGDVIAVS RAHSTAGCMG GKDREVFLFW
     FWKLPQAQHS CGIDAIPRFT DAEGRAELER GGDAVVAEGG VRLRDVAARL ERSAVTALPH
     YVLRRWHYGR VVVVGDASHK FNPLVGQGGN SCIESCAGLV NALAAALEEA SSGVAAPAWP
     LDVVRGVFAA VEAERVPRLV DMVERCQQAQ YVAAWDTWGI KLLSKYIVPL QSDSKATDFY
     SSFITGGLTL KTLDLPRVEH EWAYDDEKES GGSATANNKL VLAGASFALF AGILAVRAVR
     NGRIGA
//
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