ID G9MY54_HYPVG Unreviewed; 3989 AA.
AC G9MY54;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Putative PKS-NRPS protein {ECO:0000313|EMBL:EHK20476.1};
GN ORFNames=TRIVIDRAFT_192717 {ECO:0000313|EMBL:EHK20476.1};
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:EHK20476.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK20476.1, 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 -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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:EHK20476.1}.
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DR EMBL; ABDF02000079; EHK20476.1; -; Genomic_DNA.
DR RefSeq; XP_013954673.1; XM_014099198.1.
DR STRING; 413071.G9MY54; -.
DR EnsemblFungi; EHK20476; EHK20476; TRIVIDRAFT_192717.
DR GeneID; 25789679; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_192717; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_37_4_1; -.
DR InParanoid; G9MY54; -.
DR OMA; ETDVHHA; -.
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:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd19532; C_PKS-NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013120; Far_NAD-bd.
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; 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:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 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; PF07993; NAD_binding_4; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-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; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..445
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2344..2425
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3538..3617
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2432..2492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2517..2548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2462..2492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2531..2548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3989 AA; 436747 MW; 582B8D334B34EFB2 CRC64;
MDQRQQQDTR FREPIAVIGS ACRFPGGASS PSKLWKLLQQ PRDVVKEFDP SRLNLSRFYH
KSGDTHGATD VGNKSYLLEE DTRLFDAAFF GISPVEAAGM DPQQRILLEA VYEACESAGM
TLDELKGSFT SVHVGCMTSD YANIQARDTE TVPKYNATGS ANSILSNRIS YIFDLKGPSE
TIDTACSSSL VALHNAARGL LNGDCNTAVV AGVNLILDPA PYINESKLHM LSPDARSRMW
DKSANGYARG EGAGALLLKT LSQALKDGDY IEGLVRATGV NSDGQSPGIT MPFAPTQTAL
IQQTYARAGL DPIKDRPQYI ECHGTGTPAG DPVEARALSD AFIAEHEKST NNPIFVGSIK
TVIGHLEGGA GIAGVIKVLL SIKHRVIPPN LLFKELNPDI APYYGPLQIP TKAIPWPELP
PGTPARASVN SFGFGGTNSH AIIESFDEDS VPQHNSTDEE GTIGPFVFSA KSGASLLRSI
KDNLEFLEQD SSIDLRDLSA LLQSRRTTHR VRAHFSGSSK SDILDKMAEF VRIHEKSSSD
QIGHQPQLIN PKEVPGILGV FTGQGAQWPA MGRELIKKSS LFRKCIQECE AVLSALPEQD
IPKWSLMEEL LKDDTSSRIS EAAISQPLCS AVQLALVRLL EVAGVKFDAV VGHSSGEIAA
TFAAGIINLQ GAMQIAYYRG LHAKSARGIN GVKGAMMAAG LSFMDAKAFC SRPEFNGQIK
VAASNAPKSV TLSGDVDAIT KAYEILQAEN IFARRLQVDT AYHSHHMVPC SQPYLDSLLA
CNIKVMQPAA DKCTWISSVR GDTQLLRGDL SSLKGQYWVD NMVRTVLFTQ AVESSIWHGG
PFDLVIEVGP HPALKGPTEQ TLKASYGAIP VYTGVLKRGG NDVEAFSSAI ATTWAQLGPG
FIRFAGYRSL FYETDAPLLK IPKGLPSYSW DHDKVYWREG RLSRRFRLGK DKSHELLGRR
TLDDNDTELR WRNVLKLTEM SWLRGHEVLG EVLLPGASYI SIAVEAAKSL AMTVDKGIRL
IEVENVNILR PVVVPEGADG VETLFTTHVV KATKDYIQAK FIYYVCPDET LGSMLQTCNG
DISVYFETHP GSLSEEVLPP RDATPTNLTS IDTERVYSLF KDIGLNYSGL FRGISTIDRQ
LDYASTTSTW AEGLDTSYVV HPAMLDVAFQ TMFIAKAHPA SRQISSALLP SHIDRVRINP
AVHFTQSNGG AETTAEFETW AVKQTANSLI GDLNIYDAAT GKTFLQVEGL SVNSVGEQDA
SSDRSMFSRT IWGQDVSLGL PDPVRDPVKD AEGLQMAHAV ERVALFYVKS ILNEVKEEER
KGLQWYHQRM FEAFEEHIRV VKVGEHPIIL AEWLDDEASI LDELDASHGD TIDFKLLHAV
GKDLADVVRG NKQMLEVMTK DDMLNRFYME GYASVPTNKA VGDALRQLSF KYPRAKILEI
GAGTGGTSWS VLNSIGDAYD SYTYTDVSSG FFHLAEEKFS KFAHKMIFKV LDIEQEPKDQ
GFAEHSYDII VAALVLHATH DLEKTMRHAR SLLKPGGFLV MVELTGTMSV RATLVMGGLP
GWWLGEGDGR RLSPLVTAIE WDRLLQDTGF SGADAVIHDL ANEDKHCTAL IMGQAIDDDF
QRLRSPLSTA VELPIPTEPI VVIGGKRLST SKIVREIQKL LPKKWDRQMR LFKSIDEIDM
AKLTPGMDVL CLQDVDEPPF AQTMTDKRMT IIQSLLMNAK NLLWVTCAGE SQTPRANLIH
GIMRVVPSEL PQLNVQVLGL ETGEIPANVA KKAVEMFLRL RETGTDGGNS HRDMLWSMEP
ELDIIGDQIM IPRVIPDIEL NELYNASKRV ITKTVDAKKI PVNVVQRDGK LSLQIATVHN
TQYTTGSVPI QVHYSVRIPG TSGDELFIIS GQSADSSWVA GMTSVNASIV YVDGRHLIPI
DEQDCTPEKL VAMSNFILAW AIMTLAAPNA SVLLFEADDS LAVSVKAKIA AAGGKVILAA
AQTKNSSTDF IKVHTLASRR ATQRLVPRDV KLYIDCSSEK LAGSRTTSLN TTTYVTDWKQ
KSLPTTIQPL NVEGIFRADK TYFMAGMAGG LGLSICQWMI RNGAKHMVIT SRRPEVDRAT
LEEAERVGAS VKVLAMDLTK RESVEKVVQE VRDTMPPIAG VCNAAMVLKD GFFVDMDVDQ
FNNTLAAKVI GSENLDSIFG SDPLDFFILL GSVASVIGNV GQSNYHAANL FMTSLVHQRR
ARGLAASIIH IAYVTDVGYV TREERDRQLD SHFRKVRLMP TSETDVHHAF AEAVKGGKPG
STSGYYDIIM GIEPLTEAIP SDQQPLWMKN PRFAHFDQHA IHAQHERGSG ATTENVRALV
DKAEKEEDAI DAVMAAFCGK LESILQLTVG SINVQRPITD LGIDSLVAVE IRTWFLKELG
ADVPVVKILG GDTVQQLSTI ATKKLLAKNM EAGAEKKSTT EMPTDTPAPV SAPAPASIPS
PRIAVESSNI VSGDRIQTDQ TGPTLTPESG RSPFLTAQNV LDFDSVSVLT AASKQEDSIS
SSSSYTKGEA PEVDNKSERS NSIGEGKLED MRVRPEILRE ERMSPAQARL WFLSQHLENA
SAYNMAFRYR VQGPIGIARL KHALSVTTYN HECLRMCFYS RLEDGHPMQG VMASSLHSFK
HFVDASDADV DKEMSRLSTR KWDLEHGHTM EVSLLSRSPE DHVIIIAYHH IIMDVMGLGI
VLNDLNNAYN MKPLDKSAGS YVDFSTQQLE RQTRGEFDQQ LAFWEAEFKT IPDTMPPIPF
ANISNHGIEL GTDAHHQYRE LSDAQFLSLK AACQHLRISL FHFHLSLLQI LLSRYTNSED
MCIGIVDANR NDHRFASTVG CFVNMVPVRL HVPGRQTGFA AIAQKTRKSA LQALENSAVP
FDMILDKIKI PRSSGSTPLF QVALNYRTGS IWEMPLGKAK LNMEAVKDAN NPYDLSLGVA
ETRTGCMVEV YASSSLYSAE ACCTIMDAYM RLLDDFSGTP DLEIGKCKVY GETDIERSLE
IGTGPIMNFG WPATLSERFL DMVRLYSTNQ AVTDKTCTLS YAQLLERVNA VSDALNRHGC
KSDSRIAVLC EPSADTIVSM LAILHIGAVY VPLDVSLPTS RHAAMVQSCK PPVILSHSAT
GGIAKDLMDK VEFPIQQIII DDIVVEEVRI TVPCAAKPDT CSVILFTSGS TGTPKGIMLS
QANFVNHLAL KTRLLGLGKE TVLQQSSTGF DMSMIQMFCA LANGGRLVIA PFEIRRDPIE
MVSLVRSEQI SLSIATPSEY LAWANYGAAN LKENVAWRHI CMGGEPVTRQ LVAELNRLGL
PNLTVTNCYG PTEITAAASF QTIDLEGQEN ANPDMIKYTV GKVLPNYTVS ILDASGSPQP
VNYTGEICIG GAGVALGYVN PSEEAGSKFI VTEGGQKMYR TGDRGRLLPN GTLLLFGRID
GDSQIKLRGL RIDLQEIELA VVEAADGLLS TVVVSQRGDV LIAHATISAE KNTITSVTDD
DLTAVLRKLT LPQYFIPARI VILPTLPTNA NGKLDRKAIG ALPLLQSQFI ANPALEEEKM
TVGEGELRLL WERVLPQATS SKRISPSSDF FLLGGNSLLL MKLQAALKDS MNVIMSTRKL
YQASTLRDMA RSIGEQRQSQ IANDAELEID WVAETAIPKW LLNQIHERSQ TKISSSPKPS
DEEIAVLMTG ATTFLGGHLL KSLLQSDKVS KVYCIAIPAD DQHLLPEDSK IECFTGSLLS
PTLGLSTVER QRLELTADII VHAGGSGHCL NTYATLRTPN VLSTQFLSSM ALPRSIPLLF
LSSNRVVLLT GNTAPPAASV SAFLPATDGR EGHMMSKWAS EVFLENLVGQ LHASSPEHQQ
NPWTVSVHRP SVIVSENAPN SDALNAILRY SILMRTVPRM DNVEGYLDLA QLETVVAELL
ESVIHLGSGQ NTNDSTEIVY KHHSGGVKVP TGELWSHLEQ VHGVTFEEVD MKEWLRRAAR
AGIDPLITAY LEAIQSNGAT MIFPYMGSD
//
