ID A0A1L9UAK3_ASPBC Unreviewed; 2249 AA.
AC A0A1L9UAK3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=S-adenosyl-L-methionine-dependent N-methyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASPBRDRAFT_77659 {ECO:0000313|EMBL:OJJ68593.1};
OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767769 {ECO:0000313|EMBL:OJJ68593.1, ECO:0000313|Proteomes:UP000184499};
RN [1] {ECO:0000313|Proteomes:UP000184499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946
RC {ECO:0000313|Proteomes:UP000184499};
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).
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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DR EMBL; KV878690; OJJ68593.1; -; Genomic_DNA.
DR STRING; 767769.A0A1L9UAK3; -.
DR VEuPathDB; FungiDB:ASPBRDRAFT_77659; -.
DR OMA; CASDYND; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000184499; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF21; NON-REDUCING POLYKETIDE SYNTHASE AUSA-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000184499};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..426
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1284..1361
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1388..1469
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1252..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2249 AA; 246189 MW; F6F33A4344B6BC7D CRC64;
MVLSEQQGNG PAREVAIIGM GCKFPGADSV NDYWRILDEG LSMVQRPPEG RFPTEKHHRS
SDKSVFLGNF IDDIDCFDNR FFKKSSREAA SMDPQQRLLL EVAYRTLESS GYFGPDQQDT
DVGCFVGVCA SDYNDNVAGH PPNAFSTLGT LRAFLTGKIS HFFGFTGPSV SVDTACSSSA
VAIDAACKAI LNGDCTSALA GGVSIFTSPH FYQNLAAASF LSPTGATKSF DAGADGYCRG
EGVALVMLKE YSQAVEDGDQ ILATILSSSV KQSSNKTPIT VPYSPSQTAL YRRVLQKAGV
AARDVTFLEA HGTGTPIGDP QEYLGIQEVF ASEDREQPLY FASVKGNIGH TEGASGVAGL
IKTVLMMQKQ LIPRQASFTK LNPKIDLVPG RVEIPTRTIP WTAKTRIACV NNYGAAGSIA
AMVVREPISS TATMTPTQVQ ETALSKYPIF ISANSPKSLA ENCHKLREQI SQLHPSSSTN
ILADIAFNLS DKQNRGLPNT LIATVGSMAE LDDQLRIAAS NPESSPCVLS SPSPPLVLAF
GGQTNRSIGL SRDVFNSSAL LRKHLNRCDK LLRTLGNAGI YPGIFDPTPM DDVVALQCMQ
FALHYASAMC WIDCGLKVDY VIGHSFGQLV ALTVAGVLSL LDGLKLVHGR AVLMRDMWGD
ERGSMIALDG NQENTMQLIA SVRSQTGQTL SPEVACYNGP KSHVLVGSAA DIGTVVEVLK
QSTAIKHKVL NVTHGFHSQF CDPILPELKK LAECLTFNKP VIPIETCSND QSWTSTTPQF
IADHTRTPVY FGAAVQRIAD RFGPCTWLEA GSNSSITSMA RRALSSTDSR DSLFLPINLS
RDNAMGSLAE TTASLWKRGH QVQFWPFHRT CRAAYQPMNL PPYQFEKTRH WLEFRQIEPS
KQPEKAPEPI VPEKEPVLIT FVGFHETSPP VATFTIDPRS EQWTKLVQGH SVLAQPLCPA
PLYIELVLQA ARDIAAAKGI TAHPFARVEG LEITASLGIA HDKVISLILT QADHTGRSWN
FAFHAVDRNR QQNASSADPV HATGKVDIIA ADDSSVPAEF ARTGRLLQQH HGLDNNSLHP
DGEVVQGLAI YQLFSRVVQY HDFYKGIRRI TAHGDTAVAR VSLPSGQPPA TEGLCSCPVA
VDNFLQVPGL FANCLAPCPG DEVYVCSKVD RIQVAAGFGG SMHNDWTVIV TSTRVSDKEM
QNDVFVTDRL TGELLMVVFG ARFSRVRITS LTKVLARAND DVSNKATLPF TVSSETKPQA
PTDVTQTTPS VPTTLSEAKV PPPRAPTSVE GPLRELLSKI TDVKTDRFQG DITLEELGID
SLMATEIVSE VDQVFGVSIP PEDLQYLLTF SALRDYLDAR GPRVAAGFSS GSSDSAIDIS
SDDHHRPSFA NEDEEELVSR LAGLLSSHLE CPTSTFQRTT NLANTGLDSL LCMELATDIQ
TTFGVTIDVS QLTTESTFHE LVNMVVAAGT PNLGSSSTLT SQAMTPEPAT PALEKEDPWT
NGSPDALLPD AQSAFESIKA DFDPLADEYK FSGFYKNVYA KNAKLVLAYT IEAFADLGID
LSQLKPGDPI PELPCLPKHH NLKDVLYEVL RDGQVADYNG QHYVRSEIAI DPTHSSVLFK
DLVDAFPQHA KEHMLLNVCG SEMAKLLSGA KDPLTLLFGS KANRDILEDV YSTGPMYVIM
SQLLTSFLER TLSTATPGPS GKFRLIELGA GTGSTTKWVV ERLVKRGIPI EYTFTDISSS
LVNAGKRKFA KYDCMKYATI NIEKTPPAEY HGQFDVVLST NCIHATSNLP NSLQNIRTLL
RPNGFVSLVE FTTRMFWFDL VFGLLEGWWL FNDGRKYVLA SPEFWEECMQ NTGFNHVSWT
GGSTRESQVV RIITGFVQPA TDPNFRSIPQ VTKGGIETVV FKHTDKRLPL RADIYLPSAE
QATKHDTWTV ALLVHGGGHV MLSRKDVRPR QIQLLLDHGL LPVSVDYRLC PEINLLDGPI
TDVRDAYKWA RKTLPSLRLT STNLQIDPSK AVAIGWSTGG TLAMSLAWTV QDVEVNDKED
DDDPVPPPDA ILAFYCPTNY EDEFWRTPNI PKHSEPFVDR SYNILSAVHP SPITAYNVPP
AMMAMSGWMA PQDPRSQLIL HMNWRAQTLP VLFRGLPSQV DDYGGNNIAQ YHDLEQPSTE
EIIRASPYAQ IVRGTYRSPT HIVFGTEDDL IPWQQAMETV EALQAVGVEA GMTLIEGQPH
LFDLFRDADG KRWEAIQPAY RFVFERVGR
//
