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Database: UniProt
Entry: G9MRS4_HYPVG
LinkDB: G9MRS4_HYPVG
Original site: G9MRS4_HYPVG 
ID   G9MRS4_HYPVG            Unreviewed;      2210 AA.
AC   G9MRS4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:EHK22793.1};
GN   ORFNames=TRIVIDRAFT_53926 {ECO:0000313|EMBL:EHK22793.1};
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:EHK22793.1, ECO:0000313|Proteomes:UP000007115};
RN   [1] {ECO:0000313|EMBL:EHK22793.1, 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:EHK22793.1}.
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DR   EMBL; ABDF02000006; EHK22793.1; -; Genomic_DNA.
DR   RefSeq; XP_013957004.1; XM_014101529.1.
DR   STRING; 413071.G9MRS4; -.
DR   EnsemblFungi; EHK22793; EHK22793; TRIVIDRAFT_53926.
DR   GeneID; 25795379; -.
DR   VEuPathDB; FungiDB:TRIVIDRAFT_53926; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; G9MRS4; -.
DR   OMA; ALDSLYW; -.
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; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 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; 1.
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; IPR013149; ADH-like_C.
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; PF00107; ADH_zinc_N; 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   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          12..437
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2124..2201
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1266..1305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1277..1297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2210 AA;  241587 MW;  3A0570F010701DB8 CRC64;
     MSSSQDSNRE RPMPIAIVGM SCRLSGGVST LDDFWTMLSR SRDGWRPIPE ERFTPKAFYH
     PDPQKKGSFN NKGGYFINGD LSNFDAPFFQ ITRQEAEAMD PQQRHLLECT YEALENAGIP
     KNTISGSNMG VFIGGASSDY RLGTLKEVDQ IPMYDATGNH QSIQAGRISY YFNLHGPSFS
     TDTACSSGLY ALHLAVQSIR SGESDSAIVA ASSLHLQPHD MVSMSMLGLF NEHGKTFAFD
     HRAKSGFARG EGTGCLILKP LHKALEDKDK IRSVIIHTGA NQDGKTTGLT NPSGEAQERL
     IREVYARAGI SPEDTGYVEA HGTGTRTGDP IEANSIYRVF GAGRTKRMPL YMGSVKSNVG
     HLENASGIIS VIKASMMLEK GFILPNINFE KANEAIPLDE WNIKVPTSIR PWPRNKRYIS
     VNSFGFGGSN AHVVLEKVPF SLRDSPHDNQ NVTPRLFVLS AHDEGAAKRV VEKLGIYIEQ
     HPEVFQKRLV RDMAYTLGER RTHLQWRIAI TASSCDELAN ALNGVGATPV VASNEPKVAF
     VYTGQGAQWA GMGKELMESH PVFANTIKAC SDYLQEIGAE FSLLAELAKG EKETLVNEAH
     ISQPACTAIQ IGLTKLLESW GIAPSAVIGH SSGEIGAAFA AGSINIEDAM SAAYWRGKVS
     SDMRLKHPDL RGAMLAVGAG AEEVKGIIKT RGLQNVTVAC ENSPDSITAS GDEEDVDKLA
     AELETRSIFK RKLRVTVAYH SAHMQLVADD YKAAIKNMKD KTTSKVEFYS SLVGRKLDSA
     MSLGPSYWVD NLTKPVLFSP ALKELYEGTK PDVIIEVGPH SALEGPIKQI LKNISSQAAM
     GVKYLSCLIR NQHATSTALD CAGSLFVKGH PINLRKINHP NASLRLPAVV SDFYPYPWSE
     HKYWFEPRSS KQLRQKPFMR HDLLGLLEDS YSDIEPKWKN VISTDDVPWL KDHRMQSLAT
     FPLAGYICMA VEAASQRAQL RDIPAEQIDG FRLREIQVSK ALILDDGAPY EMIFSLKPYA
     EGTRFNSSDW DEFRISSWTS ARGWLEHCSG LVGIKKAAPI NPVSDGLLRA ASIRRQHTLG
     MSCHQLPMDG FYSELESRGA GYSGVFRISP DADVKIHEQY STASLTIPNT ATVMPASFEP
     ASIAPAAFVD LLFQLTFPIL GAGSGEMPSL FMPSAVKAIE ISSKFPNTPG ERVQVVAHGC
     PDFTAPGPVD FFIDMWYQDA IEPVTKISGF RMTPVNGDID DGVSPRSICY KVQWESLDEV
     NEKAERGAKE NCAIENGHEN GDSSGKMSAS SEANGTKSHA ISHRDGSDPL VGTLLDLLEL
     RTTKRPRLID FSNLIPESGC CYICLSEIDE PLLANMTEEI FEKMQNLLVT CQSVLWVTSG
     AYRFAEQPES NISQGLLRTV RSEANKAVAS LDLDPHSTLD VLDTAELILR AVKVSIATPE
     DDTPVDYEFA EEGGKLMVPR VVKQEDMNLA IFHDTQATAA PPYLQPFEQP GRRLTVAVGT
     YGALDSLYWK DEDETPLGPH EVEIKVACTG MNFKDVVIAM GQVASPYLGI ECSGTISRIG
     SCVSCLKVGD RVCAMSLGAY STFARCPASS AATIPDDMSF EVATSIPVVY CTAYYGIMDL
     ARLEYGEKIL IHAATGGVGQ AAIQLAQMVG AEIYATVGSA DKKKFLMDTY GIPETRIFYS
     RDVSFGPAVR EATSSHGVDV VLNSLAGDLL RETWECLAPF GRFIELGKRD ITNNTRLEMA
     KLEYNCTFSS VDLTLLAARR PKLMQRTFAS VMHLLENKTI QPIGPITPVN IQNVEGALRK
     LQSGKTTGKL VVTHSGQSQV KATHPAPRSD MLERDATYLI IGGTGGLGRS ITRRMVRLGA
     RHIILLSRSG KVTDDLTKLM KESRKLGASI YVVPCDVADE KSVQALVEEL QDDLPPIRGI
     IHAAMVLRDV LFEKMTFEDY EAVVRSKISG AWNFHKALIN TPLQFFIVLS SVAGIVGNRG
     QAHYSAANTY LDALVLHRRR KGLAAASIDL AAVEGVGYLA ENAAKMSQVM RNLSDNTVGE
     AEVLALIESA MTGRVDFFCQ GQVITGLGFD NASAMPFYAS DAKFSYLRDA LLATSGDVDI
     SLRSEILTIC QQLRRCTTVK EAQDVVTLGL RDKLGAILML PEEVMAARQG NTSITAFGLD
     SLNAIELRNW IGKELQAHLQ VLELLTSGRV ADLAGLVLRK SRIEGVWTEK
//
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