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Database: UniProt
Entry: T0LRW0_COLGC
LinkDB: T0LRW0_COLGC
Original site: T0LRW0_COLGC 
ID   T0LRW0_COLGC            Unreviewed;       485 AA.
AC   T0LRW0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Thiol-specific monooxygenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CGLO_09553 {ECO:0000313|EMBL:EQB50950.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB50950.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT   gloeosporioides as revealed by transcriptome analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:EQB50950.1}.
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DR   EMBL; AMYD01001925; EQB50950.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0LRW0; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006909_5_3_1; -.
DR   OMA; FRHREVM; -.
DR   OrthoDB; 2453855at2759; -.
DR   Proteomes; UP000015530; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 2.
DR   PIRSF; PIRSF000332; FMO; 3.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015530}.
SQ   SEQUENCE   485 AA;  55046 MW;  1CE3B35DD0C6E470 CRC64;
     MAKEIRRVAV IGAGPAGAIA TDALVKEQAF DVVRVFERRD LAGGTWVYTP ELPSRIPSLR
     DLVEQRANPP VDLPKTFPTW TPKTEKINSH QLRYADTGVH ETLHSNITPE IMAFTQEPIP
     KILSERTIAQ YGPGAPFRHR ELIREWVEAI FTRGGHDKLV EFSTTVELAE KKGDEWILTL
     RKVVPGKSKD YWWQETFDAI VVGSGHFYLP YIPDISGLIK YDEKFPGRVK HTKHFRSPEE
     FRGKKVVVVG GSVSAFDALH DIRLVSQTPV IASLREPLPA FGWAPFTHPD ITIKPQITHF
     CHKTGRITFS DKSTVDDVDV VLFATGYDFS FPFLPKLKVE NRRIPRLYQH VFHTDDPSLA
     FVGMVTGGFT FRVFEWQAVA AARVFAGRGQ LPSTTEMERW EADRLVKRGD GVPFFTLSPD
     FEEYFEALRA IAGEPAPGST GRILPKFDPK WLEAFADVIN ARVDWWKKET EKAEKQQKTL
     YKSKL
//
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