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Database: UniProt
Entry: F0XE00_GROCL
LinkDB: F0XE00_GROCL
Original site: F0XE00_GROCL 
ID   F0XE00_GROCL            Unreviewed;       970 AA.
AC   F0XE00;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Flavin-dependent halogenase O-methyltransferase bifunctional protein {ECO:0000313|EMBL:EFX04254.1};
GN   ORFNames=CMQ_1182 {ECO:0000313|EMBL:EFX04254.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFX04254.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC   -!- SIMILARITY: Belongs to the flavin-dependent halogenase family.
CC       {ECO:0000256|ARBA:ARBA00005706}.
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DR   EMBL; GL629765; EFX04254.1; -; Genomic_DNA.
DR   RefSeq; XP_014173736.1; XM_014318261.1.
DR   AlphaFoldDB; F0XE00; -.
DR   STRING; 655863.F0XE00; -.
DR   GeneID; 25974032; -.
DR   eggNOG; KOG3178; Eukaryota.
DR   HOGENOM; CLU_305659_0_0_1; -.
DR   InParanoid; F0XE00; -.
DR   OrthoDB; 1599601at2759; -.
DR   Proteomes; UP000007796; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR43747:SF1; FAD-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43747; FAD-BINDING PROTEIN; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EFX04254.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000313|EMBL:EFX04254.1}.
FT   DOMAIN          8..364
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          807..948
FT                   /note="O-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00891"
FT   REGION          555..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   970 AA;  105819 MW;  EB6D1BF228E32225 CRC64;
     MASVPQSCTV LVVGGGPGGS YASAALALEG IDVVLLEAEV FPRYHIGESM LPSMRHFLKF
     IGAYEKWDAH GFNIKKGGAF RLNWSRPETY TDFIAAGGPG GYAWNVIRSE ADDLLFKHAA
     DCGAKTFDGT KVTSIEFAPQ DQVGEAGANT VGRPMSATWS RKNGSSGTIT FDYLVDASGR
     AGMVSTKYLK NRSFNQGLKN IASWGYWKGG GVHGVGTHKE GAPYFEALKD ASGWVWFIPL
     HNGTHSVGIV QNQEMAIQKK RQMAEPSSLG FYKEVLELVP GIKELLANAE LVSEIKSASD
     WSYSASSYAL PGVRIVGDAG AFIDPFFSSG VHLALSGALS AAATIAAAIR GDCDEETASS
     WHDKKTAESY TRFLVVVSSA LKQIRSSDQP VLHDFDEESF EKAFELFRPV IQGQVDADTK
     GGLTQAEISK TLEFCFKAFA HVSFDEKEAL INKLKELGLD GDVHDENNRK ALDELEKELT
     PEERAILTTL KGRRMIRPED SLNIDNFTLD SIDGLAPRLE RGKLGLAAAK KAEVKYTTHD
     KLSYLNGEAR AANKLGKNDY AEPQGNSMTN GHKVTNGHNG VTESGPDNMN INHVADLVAS
     WKQSSKTALD ELTRHGLMSS LHEAAEELET PYDTLTRLVN AGRQVALVKL GGDLGIFKTL
     AESKTPLSSG QLAEYSMAEP LLVARIVRYL VANRLVYEVE PDRYVARKAT YALADPHIES
     SLRFFHTVSN PSFQALPDYL RETGYRNQTA GSALQKGLAA EQGLFPWLKE NPDVLGDFQH
     LMSIPKEGNG WDVIPLELSV SSTHQGPMLV DIGGNTGQQA RLLVAKHPEL AGRVIVQDRE
     ETIKSAPEVK GVQLMAHDFF GPQPVRGARY YYLRAILHNW DEDHAVQILA NIVPAMTADS
     LVLIDEVVIP NKGAHVWPAG LDLQMLTLFG GSERTALQWD AILEKAGLKP VVVKKYAPVM
     ESCVIFAARK
//
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