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Database: UniProt
Entry: A0A0F0IHF9_ASPPU
LinkDB: A0A0F0IHF9_ASPPU
Original site: A0A0F0IHF9_ASPPU 
ID   A0A0F0IHF9_ASPPU        Unreviewed;       670 AA.
AC   A0A0F0IHF9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=O-methyltransferase {ECO:0000313|EMBL:KJK66606.1};
GN   ORFNames=P875_00128083 {ECO:0000313|EMBL:KJK66606.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK66606.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK66606.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJK66606.1}.
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DR   EMBL; JZEE01000238; KJK66606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0IHF9; -.
DR   STRING; 1403190.A0A0F0IHF9; -.
DR   Proteomes; UP000033540; 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; 1.20.1050.130; -; 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; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR43712:SF2; O-METHYLTRANSFERASE CICE; 1.
DR   PANTHER; PTHR43712; PUTATIVE (AFU_ORTHOLOGUE AFUA_4G14580)-RELATED; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KJK66606.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000313|EMBL:KJK66606.1}.
FT   DOMAIN          539..670
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   COILED          10..37
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   670 AA;  76229 MW;  767303FCEDF4B9B3 CRC64;
     MDAPLTDVER TALQTSLEAL NRQVEATRNI LRSNSQKALL QTLHTDQELP DPALEALAGK
     TINLLHETQQ LLEPGHLVLA DHFLGYVSTK CLCAAVELKL VDILADADEA GMTVDELADA
     SGAHPDRLQQ VLRVLRNDNI FDYDAVSHRY RNNRVSALLH SEHWTQWHNW VDLYGNEFYD
     IARGIPRSIR REEARWAAQI NFDTNDDMFT YFQAQGWLPR LHRTLGGGAI AQAPGIVADY
     PWHEIGSRTV LDVGGGGGGF LASLLREYPQ MRGGILDLPR TIEHACTLFH EPQGPYFDLR
     ERVPRENLIA GDFLKAVPAF EVYTMKWVLH DWKDPDVLTI LRCIRASLIP GPDSRLVILE
     SNLSDGQMGR LSRYGDINMM MTANGQERSE EQWRALAAAS GWEVSRIYPM RRAWVCAIDL
     RPSASESGDR KHNPSGAVVM GDMEYDGRVI LYIIKADETS YINYIKPLIL AEEIQFPHVL
     SVIDTRDEWF YSIHPERMVP SLKDQDPVTG EKVIVFESTA CLQYLVDRFD TDGTWSGRTV
     AEKGAILSWT AYQTAALGPT AKYWLYFKRG YPTRANPVQL PRTIEKLHAN TLRQWDILEK
     RLKEPGQQYI ALKDRPTLAD LSYFPFAMPW MFTFLGVDIK DWPHIQRWSE RMLSRPAVAR
     VLQRAPTLGH
//
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