ID A0A066X0Z1_COLSU Unreviewed; 1016 AA.
AC A0A066X0Z1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=O-methyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CSUB01_02712 {ECO:0000313|EMBL:KDN62803.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN62803.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
CC -!- SIMILARITY: Belongs to the flavin-dependent halogenase family.
CC {ECO:0000256|ARBA:ARBA00005706}.
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:KDN62803.1}.
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DR EMBL; JMSE01001300; KDN62803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066X0Z1; -.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_305659_0_0_1; -.
DR OMA; YEKWDAH; -.
DR OrthoDB; 1599601at2759; -.
DR Proteomes; UP000027238; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022603}.
FT DOMAIN 8..365
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 853..994
FT /note="O-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00891"
FT REGION 137..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 110511 MW; BCE0CD5513339D0F CRC64;
MASVPQSCTV LVVGGGPAGS YASAALAREG IDVVLLEAEK FPRYHIGESM LPSMRHFLKF
IDGYEKWDAH GFNVKKGGAF RLNWSRPETY TDFIAAGGPD GYAWNVIRSE ADELLFKHAA
ECGVKTFDAT KVTSIEFSSP GEGSEADGKK LGRPVSATWS RKDGSSGTIS FDYLVDASGR
AGLISTKYLK NRSFNQGLKN IASWAYWKGG GVHGVGTHKE GAPYFEALKD ASGWVWFIPL
HNGTHSVGIV QNQEMATKKK REMDEPSSLG FYKQSLDLVP GIKELLSKAE MVSEVKSASD
WSYSASSYAF PGVRIAGDAG SFIDPFFSSG VHLALSGGLS AAASIAAAIR GDCDEETAAS
WHDKKTAESY TRFLVVVSSA LKQIRSSDQP VLHDFDEESF ERAFDLFRPG TFPVARGMKK
FNQHSLTLYR PAVIQGQVDA DTKGGLTQAE ISKTLEFCFK AFAHVSFEEK EALVNKLKEL
GLDGDAYDET NRQALDELEQ KLTPEEQAIL KTLKGRRMVR PEDSLNIDNF TLDSIDGLAP
RLERGKLGLA PAKKAQVKYT THDKLSYLNG EAGAANKLES NGHHKPQGNP TVTNGHGATN
GHSATNGHSA TNGHSATNGH SMTNGHNGVT EHTSYNATHV ADLVASGNES GKITLDERTR
HSLMSSLHEK AEELETPFDT LTRLVDAGRQ VALVKLGSDL GIFKSLAEST TPLSSGQLAE
YKEADPLLVS RIVRYLVANR FVGEVAPDRY VSRKATHALA DERIASSLRF FHAVSNPSFQ
ALPDYLRETG YRNRTAGSAL QKGLAAEQGM FPWLKQHPDV LADFQNLMGI PKESNGWDVI
PLDMSLSANH QGPVLVDIGG STGQQAKLLV AQHPELAGKV VVQDREETIK GAPAIQGVDL
MAHDFFKPQP VKGAKYYYLR AILHNWDEDQ AVQILANIVP AMSNDSLVLI DEVVISEKGA
HVWPAGLDLQ MLTLFGASER TGPQWDTLLD RAGLKPVSVR KYAPVMESCV IFASRK
//
