ID G9MUA5_HYPVG Unreviewed; 2459 AA.
AC G9MUA5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:EHK21975.1};
GN ORFNames=TRIVIDRAFT_53633 {ECO:0000313|EMBL:EHK21975.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK21975.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK21975.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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:EHK21975.1}.
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DR EMBL; ABDF02000050; EHK21975.1; -; Genomic_DNA.
DR RefSeq; XP_013956168.1; XM_014100693.1.
DR STRING; 413071.G9MUA5; -.
DR EnsemblFungi; EHK21975; EHK21975; TRIVIDRAFT_53633.
DR GeneID; 25795348; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_53633; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_1_1; -.
DR InParanoid; G9MUA5; -.
DR OMA; EKCDPQQ; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000007115; 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: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:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 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; 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; 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; 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:SF28; SYNTHASE, PUTATIVE-RELATED; 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; 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; 2.
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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..430
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2378..2452
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2459 AA; 269350 MW; 1C40799842A1E296 CRC64;
MVSNASDSSE QFLVAVCGLG IRAPGGIRNA AGFWDLLVNG KDARGPIPET RYNIDGFNDS
LGGANTIKTR FGYFIDDDLT CIDTSLFSMS RKEVERCDPQ QRLLLEVARE ALEDAGEVNY
RGERVGCYVG TFGDDWAQIA GKETQHQGGL GYVATGNGDL MLSNRISYEY DLRGPSMTIK
TGCSASLAAL HAACQAIRQG DATAAIVGGS SLIMTPTMTA AFTAEGILSP EGSCKSFDAS
ADGFARAEAI NAIYIKPLTA AIRDGNAIRA VIRATGANSD GHSQGLFTPN LEAQEALMRK
IYQDAGLDPA LTGFVECHGT GTATGDPIET SAVGNIFGEK GVYIGSVKPN VGHSEGASGL
NSLIKAVLAL EHKIIPPNIK FNNANPKIPF AERKLKVPTV PTPWPKDRAE RISINSFGIG
GTNAHVVLES YNQPAPASSG DTELRPELLI FSANTAVSLK DQVNQYQEFV RSNPGLSNRN
LAYTLSMRRE KLPHRAYGII QDKEFVEISS LVKAPAKAPN VYLIFSGQGA QWPEMGKELA
LTDAPFCDDL RKMDGILRQL AHPPSWSLIE ELLKPAETSK IGTAELSQPL CTAIQIALVN
KIRSVGIKPA AVTGHSSGEI AAAYATGAIT MEAAIIFAYY RGYVAKQQTL RGSMAAVGLG
PQEVNKFLVD GVVVACENSP KSCTISGDLE KVFTVISQIK AEMPDTLARP LKVDMAYHSH
HMTALGKVYI TLLKDELEKL GKWSNNATTA FISSVTGGSL DDNFIFGPEY WRTNLISPVH
FTAAVTKLLD LHGDGVFLEV GPHSALAGPL RQICADASRT CNYATCLTRG ENAVKALFSS
FGKLFQEGVD MNFASLYPGG KVLTDLPTYA FDHSLTLWYE SRVSQAWRLR KYAHHALLGS
RVAESPETAP QWRNILSLDH EPWIIDHKVK QDVVFPFAGY VAMAGEAVRQ MTGIETGYSI
RHAVAHAAVV LTLEKGIELM TTLRRHQLTD SDHSEWFEFT ISSYNGATWM KHCEGQVKAL
EEECTSDLTR QNYPRRVPSS QFYDYMSDVG INFGPEFCRL ENITASPNEA LASADITVPS
KEQNKPYIMH PTAIDACFQL LILSYAKGLG RNVTQLSVPT LIGNLDIRRG GGSLVAKAWG
STQTTTEGVE CVSDGKLALR LTGFKLTALE DGNDVSYDEY AAARLEWLPD FDFVDVAPLF
KAPPSNREEI AMIEELTLLC IIESAEKLEG LSPAQPHFLK LRDWLHREVQ SAKEGKNLLV
PDAVKFLTMP RAERKALIIS HHRKLSNGSK SGLAEGMKRM VDNYERVFTG EADTIDILME
GGVLAELYNA MSFGYSDFVK LMSSTKPKLR ILEVGAGTGG TTELILRDLM HEGGLPRYSS
YTFTDVSAGF FPLAKERFAY ASNMEYKVFD ISKDPLEQEL PESSYDVIFA ANVVHATPSL
KDTLSNLNKV LKPGGILVLT EICTELRSPT YIFGNFIGWW LGEDDGRRYT PYVPPSRWHD
ELLASGYTGV ETAVYDEEAP YMCCTTIMSR KVRELQPRAK TVSLITTDVK GDIATALAQA
LKNAKYSVTP VRLGDQLPEG QDIISCVDIE RNFFENIQED DFYAFREIIR SQTTEQNLLW
LTSPVQIKCK DPRSAQTIGA ARTIRTELAV PFHTLEISIA EPNFNDLVLK VFNKILQEED
DDYLVSDKEF VVDNGTICIG RYHPFSLQDE LSQKSIAGHE TIKSLQIGKI GSIESLYWAE
QALPKEIPAD TIEVEPKSIG LNLKDVLTAM GVINPVGSVQ MELGIELGGV VTRVGADVDE
FKIGDRVFAF APEGCLATKA ILQRYHAAKL PDSLSFQDAA GVPVVFATVI HGLINIGNLQ
KGQTVLIHAG CGGVGLAAIQ ICRMIGAEMF VTVGSQDKVD YLVKTYGIAR NRIFNSRDET
FLDGIMKETG NRGVDLVLNS LTGPLLHASW KCVAEFGIMV EIGKRDLLGY GKLDLNPFIG
SRQYVGFDGV QFARKRPRYF RQLLEQFLKY REQGHIHPIS EQTHFHASDV INAFRHLQHG
SHIGKVIVSM DDATACVEAK PLAKGITFDP KARYLLTGGL GGLGKAMSTW LVEHGARSLT
ILSRSAGVTE ESKSAIKELE SLGAEVITIA GGVEDMKIVE AAVNSSTKPI KGVFHLAMVL
RDSPMVDMTW NQWDEVTKPK VNGAWNLHHA LKDHSLDFFW LASSVVTVVD QPGQGNYSAS
NTFLEAFTQY RVRLGLPTAI LNICPIKGVG FVAESAVAQR NTKAQGIYFL GERKYLDYLE
HSIFAAKGNT SDHESAPSSQ PPKAWKNDSQ IVMGLRSELH LEDPNNRCNW RRDRRMGAYH
NIRSQQDEAA GGDSNALKAF LAKASENPDI LADKSNHEFL ALEIGAKVYD FMLKPGEEVD
TSLSLTQIGL DSLMATELRR WFRQLLGLHI SVLEIMASGS LLRLAEIASE SLKNKYTGA
//
