ID A0A1L9RYT7_ASPWE Unreviewed; 2523 AA.
AC A0A1L9RYT7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OJJ40111.1};
GN ORFNames=ASPWEDRAFT_730400 {ECO:0000313|EMBL:OJJ40111.1};
OS Aspergillus wentii DTO 134E9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Cremei.
OX NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ40111.1, ECO:0000313|Proteomes:UP000184383};
RN [1] {ECO:0000313|Proteomes:UP000184383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
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; KV878209; OJJ40111.1; -; Genomic_DNA.
DR STRING; 1073089.A0A1L9RYT7; -.
DR VEuPathDB; FungiDB:ASPWEDRAFT_730400; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000184383; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 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; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; IPR011032; GroES-like_sf.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000184383};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..438
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2447..2521
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2407..2432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2413..2432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2523 AA; 276092 MW; 7B544121C7F0A32F CRC64;
MQSPPDTKGR QESIAIIGMG CRLPGSATNL SKFWDLLSRG ESAWTKVPDS RFNQDAFYNP
DSKTSGTFHS RGGHFLTGDI SRYDANFFNV NPAEAQAMDP QLRLLLEVAY EAVENAGLSL
DKLRGTSTSS YVALYNRDYE KMLLRDPENL PFYHQTGNGE AMFANRLAYF FDLNGASVTL
DTGCSGGMVA LHLACESIRN GVSSQSLVGA SNLILDPATM IGPSFLRFYA ADGRTKAFDQ
RADGYGRGEG VCCVMLKSLA AALKDGDPIH AVIRSSAINQ DGRTPGITVP SGDAQESLIR
AAYHAAALSP AKTGYIETHG SGTALGDLTE TKAIGSVLGA AQGRLSPVLL GSVKTNIGHL
ENASGLAAII KAALVIEKDC IPPTINLQKA NADISWKEWN IEIANRWQRL SELGSGSSQV
SLNSFGFGGT NVHIVLDRLQ DFDRPEQHTN GRNGFQKPNP NIYILSARSS ESARLMAVQF
QEYLQQNSCN GQDHDFLEDL AHTLYTRRPL FPWRAAIVAD SASALEQHRP ETWSFYHAGK
RSPKLSFIFT GQGAQWETMG RDLLETNSAF RESIWRADQY LSELGVEWKL IDELMKPLPE
SRLGSAVIAQ AASTAVQLAL VDMLASWNVY PTAVTGHSSG EIAAAYAGKI VSFRDAMLIA
YARGCAVGQL ARQNNNPIKG AMIAVGLDVL TAKQYFGRLS DSAGLLTVAC VNSPQSVTVS
GDEAAIIQLE KILEQESIFV RRLPVDVAYH SHHMLRVAED YRSALSSLQK PCSNPDVVFH
SSVKAKVLDG AELDAHYWVK NLVSPVLFSA AVESLTQAPK DSQSAAVSFL VEIGPHAALK
GPIKQILGTR MGEQVRYAPT IVRHKSSRHT MLDLAADLFK HGYDIDINLV NFGNAEAARP
RRCLSDLPPY PFDHSTSFWH GSRLSRNYRH RVDPPHELLG VLSVESSALE PRWRNYIGVS
TAPWLSGHKI NDEVIFPAAG FLSMAFEAGI WYHTHARGQY EQNVCSIQLS NVSIARSLSI
PESGPPIEIM FVLRPGTEQA GRDLARRHEF VIYSYPDGAE VVEHCRGFMS VVPTETISDH
EFHPNKRMNE IRVDHLYHQL KHHGIDYTGP FQRLAAVTAQ GGYCSATIDD PEDVGEGYRS
SMHPATIDTC LQTIFPAIRS LRGIQRAAMP THIQEASLCV PGQTLAHRSL NISSQVQEAS
GDRFKADIEA HLEGLGCILS VKQMEATPVR GIPSKREHDF DQVKTCQKTA LTIDPDFFTA
HDIQFLCNAN LTNASVTHRL SKLAHACRYY AKAATESIDN NDIHRMTSSQ RQYFAWIQNQ
AALYTEVEEC ASRKILDDVK ASGSEGEIVC RIGQNLASIL KGDDDPLSLM LNEDLLSRLY
RDDESMQRCA IQAAEYATVL GRKSPSLRIL EIGAGTGGTT LPILQALSVP GGSLFEHYCF
TDVSSGFFPN AKDKFASWID RMSFDKLNIE DHPRNQGFEP GSYDLVIAAN VLHATTYIDS
TAKHVRSLLK PGGKLLLLES TRPTVHRSFF LGTLPGWWLG SMERNKDNPL LTVNEWHDVL
QRTDFSGVDA AMHSYEIPEE QTDSLIVSSA SSTSTKQASD DRPVQLVLSK EQLWGQAGNQ
AIGFYVAEDL MALFGSDREN IVFLGNADFD GRVCVFLGEL DGPSILANLD NDSFAALKSM
CKRAREIIWV TCGATERCEN PRSALVLGLA RVLRRENAHV QLTTLDLDPS SRFCANRLAT
SVFDFLQRRQ PGSATRDHEW TQRDGKWLVP RIVTDDGPTQ YVRSQTIRVD QLEHRLENFY
QAKRPLCLAI GDVGTLQDLH FTDNIMLTQQ PLGLDEVEIE VRASGVNFRD IMVSLGQMPD
ELVAECSGIV LAVGSQLQND FSQGDRVYTW HVPRYASRVR AKGSLTRCIP PGFSFEDAAS
IPVVYSTAYH ALVNIARLNA GETVLIHSGA GGVGQAAVTL ALNIGAKVFT TVGSEQKKQL
LVEKYGLSPS HIFSSRSNGF VKGIGDMTSG FGVDVVLNAL AGSFLQDSIN LLAPFGRFVE
IGKNDILANS RMDLGIFSRS TTFTALDLVQ LVREKPDIAA DVFSRVDHLF RTGVARPPSP
QTIFDISKIE DAFRIMQKGE HVGKLVVSHS PAAQVKVTPP HPRPAKLRPD ASYLIIGGQG
GLGRALCTFL VHCGARSLVI LSPSGSQKPA TRALVEEMAE IGVCLHALQC DVDDRRQVAA
ALAKCNIELP PIRGILHAGL LLQDSSFDNM SVEDFCHALR PKLAGTYNIH EAFQQQQTTL
DFFVLLSSYV GLLGSPGQAN YAAASTFQDA FARWRTSQGL PTRSLDLGTV QGAGSLHEKP
EAMAHFERMG LGGIPLEAFY ALIGYAISTP LNSIDESQTA IGWAPPSSWT GSVYKALDPR
YSHLRPRIND SLGESSEDSS STSPPTTGAK NLPQALASCR SQDELVSVTS EAISKQIVSI
LGVVSEDIDF GNNIAAHGGD SLVAIEFRNW FRKELRCSFT TDQILTGCSV QDLVLKAVRE
FQV
//
