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Database: UniProt
Entry: A0A1L9VR98_ASPGL
LinkDB: A0A1L9VR98_ASPGL
Original site: A0A1L9VR98_ASPGL 
ID   A0A1L9VR98_ASPGL        Unreviewed;       401 AA.
AC   A0A1L9VR98;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=O-methyltransferase domain-containing protein {ECO:0000259|Pfam:PF00891};
GN   ORFNames=ASPGLDRAFT_72738 {ECO:0000313|EMBL:OJJ86443.1};
OS   Aspergillus glaucus CBS 516.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Aspergillus.
OX   NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ86443.1, ECO:0000313|Proteomes:UP000184300};
RN   [1] {ECO:0000313|Proteomes:UP000184300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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DR   EMBL; KV878892; OJJ86443.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9VR98; -.
DR   STRING; 1160497.A0A1L9VR98; -.
DR   VEuPathDB; FungiDB:ASPGLDRAFT_72738; -.
DR   OrthoDB; 1067404at2759; -.
DR   Proteomes; UP000184300; Unassembled WGS sequence.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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; 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; PTHR43712:SF11; O-METHYLTRANSFERASE (AFU_ORTHOLOGUE AFUA_2G17820)-RELATED; 1.
DR   PANTHER; PTHR43712; PUTATIVE (AFU_ORTHOLOGUE AFUA_4G14580)-RELATED; 1.
DR   Pfam; PF00891; Methyltransf_2; 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   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184300};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022603}.
FT   DOMAIN          174..374
FT                   /note="O-methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00891"
SQ   SEQUENCE   401 AA;  44276 MW;  162778C45CD8F61D CRC64;
     MSLSGLIGSI NTAAANTGSS HVNDNECREL LQACERLRSA YETPLDVVTR LYYSIPQAIV
     LRLGVDLKLF NAVVKLSGKS ANGEFSVQQL AGETGAEPLL LARILRFLAT MGIVREVSKD
     TFSSTPSTAA FISSSSLASV VIHGTHFLNI LSKLPEYFAQ KGWNSPNDAD DGPFQFATGT
     QSHYFDFLSS EPYYQQAFNT TMTASFRRKG QSWFKFFPVE EKLRVEDPMA PLLVDIGGGQ
     GEDILAFRDK FPHLPGKLIL QDLPVVVEGI QGTISPVEAQ GYNFFDEQPN KGAKAYYLRT
     VLHDWPDKQA LQILARVRES MTPESLLLIN EVLVPETNRS LSSVVADLAM MTSYAALERT
     QAQFEAVLNE AGFELVNVWR PDGVEVQSAQ QAVLLEARLK R
//
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