ID A0A1L9N6M0_ASPTC Unreviewed; 2239 AA.
AC A0A1L9N6M0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OJI84774.1};
GN ORFNames=ASPTUDRAFT_28505 {ECO:0000313|EMBL:OJI84774.1};
OS Aspergillus tubingensis (strain CBS 134.48).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767770 {ECO:0000313|EMBL:OJI84774.1, ECO:0000313|Proteomes:UP000184304};
RN [1] {ECO:0000313|Proteomes:UP000184304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 134.48 {ECO:0000313|Proteomes:UP000184304};
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; KV878198; OJI84774.1; -; Genomic_DNA.
DR STRING; 767770.A0A1L9N6M0; -.
DR VEuPathDB; FungiDB:ASPTUDRAFT_28505; -.
DR OMA; ALDSLYW; -.
DR Proteomes; UP000184304; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; 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 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; 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 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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; 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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF13; POLYKETIDE SYNTHASE 1; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 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; 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; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
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:UP000184304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..433
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2147..2227
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1279..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2239 AA; 243918 MW; 2F0EDB678FAD0CCC CRC64;
MTITESSLTP IAVVGMSCRL PGEVRTLDDF WTLISRGRDA WGPIPSDRMS SASYYHPDPQ
RKGCFNPKGG YFLQEDFSQF DAPFFHITQQ EAIAMDPQQR LLLECAYEAL ENAGFPQQAI
AGSRMGVFTS LCSSDYRRGA FRDLDSVPIF DATGNQESIQ AGRLSHFFNL RGPCMAIDTA
CSSSLYALHL AVQSIRSGDA DSALVGGARL RLQPDEMVSM SMMGLYNEQG KTFAFDDRAV
SGFACGEGVG CLVLKPLDQA LKDNDPIYSV IRNTGANHDG QTVGLTNPNG EAQEQLMREV
YARANISPTE TGFVEAHGTG TKVGDPIEVG AIHRVFGDGR TKRTPLYLGS VKSNFGHLEY
ASGIVSVMKA SLMLHRGFIL PNANFKRANP AIPLDQWNIK VPTSLRPWPQ GKKYISINNF
SFGGSNCHVV LERPPRSRGQ APISPHDAPR LFVLSGYDDE AAKRIARNLV FYLEQHPGVF
ERRLVHDIAY TLGERRSHFP WRVAVTASST AELVETLNGP ASVPQRVKLG ASSSPAIAFA
YTGQGAQWPR MGVELTDTHP AFAATMEESA RALEDLGAEF SLFEELKREA AESRVSQPQI
SQVVCTAVQL ALTDLLASWG IQPNMVVGHS SGEIGAAYAA GAISVSEAIA LAYHRGRLAA
QVRVRFPDLN GCMMAVGESA DEVRKTIKQL QLGEDITVAC ENSPRSTTAS GDATAMDLLA
KDLQARQIFH RKLHVDVAYH SPHMQLIADD YTSAIQQVAP STKKENVQFY SSLLGKEIEQ
PGALGASYWV DNLTHPVQFS TALGQLCADS RPDFIIEIGP HAALQGPIKQ ILQGIQNMHT
QYFASLVRNE HATKAALQLA GRLFLAGQQL DFRAVNQTHQ DQSVPTVLPS LTPYPWSHRS
YWRESRIAVN HRLPRFPRHD LLGRLEASAR EDEQPVWRNS FSLDSLPWLR GHRMQSMATF
PMAGYVSMAV EAASQRAQLR GILTSQIAGY RLRELHASSA FTLEENIEYE TLLSLSSFTE
GTRSYSSEWD EFRIASWVAG RGWREHCRGL IGIRRQELST SNPVSQRRPF HASLKRREEA
RQGDHQPLLL ETFYTELERR GAGYSDAFTL SPESGVTVEG AGVETGRCAR AKLTVPNTAQ
IMPSGHETPL IVSPAFLDLS FQLSFVVLGA GYGALPCLFM PSFIREINIT ANFPSQPGET
VEALVNGLPA DTSRPRPVDH TIDVWSPSAS TEQPVLTIHG LRLTPVNSDT LIDSSTYPWC
YTVQWEPLSS AGAANGIAQS ASKSNGHGET NGNDIVHANG SHDSSNGSRH MSPEDETTII
IITEKQIYDP LIASLLKAIE VFAGYRATVV PLSRVPISPK CLYICLAELD APMLQSLTSE
TFKLVQELLA TCSYCLWVTS GAYMAVDHPE LNIIQGLLRS VRSETGNTAV TLDLDPSSRQ
DVAGRAHLIL DAFRASTKIG QAATSDKEAR MSDYEFTEAG GRLMVPRIVE HSGLNKALFQ
ETHPSLPYAQ DFEQGGRRLK IAVGTLGALD SLYWTDDLVQ PLGPGEIEIK VACTGANFKD
VVITMGQVAS PYLGIECSGT VVRVGDKVDS LKPGDRVCAM SHGAYSTYAR CPATSAAVIP
DSMNFETAAS LPVTYSTAQY GLVELAKIEA GESILIHAAA GGVGQAAIQL AQLIGAEIYA
TVGSEEKKQM LIDRYCIPES RIFYSRDTEF GPCVREATGG RGVDVILNSL AGDFLRETWD
CLAPFGRFIE IGKRDITSNT RLEMAKFEYN CTFSSLDLTL VADQRGKVLN RVLTSVMRMF
AQGRLTSVYP VTTVGIAEVE SVLRKLQSGK TTGKVVVDHR INGKVKATHP LPPTDLLASD
ATYIIVGGTG GIGQSITRRM VQRGARHIFL LSRSGVVTDA VQKVISEGQT MNASIHVRSC
DVSEVSQIKA LISELQEELP PVRGVIHAAM VLKDVFMEQM TFSDWEAVLR PKVAAAWNLH
YALLQQPLDF FIMLSSVSGI IGNRGQAAYA AGNCFLDALA RYRRQKGLSA VSLDLAAVGD
VGVLSDDAER KAQVMKNLAS GNAMQEAEVL ALIEFAMQGQ ELPEQCITGV HWPSSSATPY
YAADARFTHL VEAVKQEEGG ADTTAHGGLT KSLSITQQVR RATSLQEALD VTALGLREKL
GDILMLPREV VEAHAQTTPI ATFGLDSLNA IELRNWIGKE LKGHLQVLEL LSAGSLGDLA
LLVLKKSSLE GAWKGEIPS
//
