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Database: UniProt
Entry: A0A2P4ZDG7_9HYPO
LinkDB: A0A2P4ZDG7_9HYPO
Original site: A0A2P4ZDG7_9HYPO 
ID   A0A2P4ZDG7_9HYPO        Unreviewed;      3964 AA.
AC   A0A2P4ZDG7;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Beta-ketoacyl synthase domain-containing protein {ECO:0000313|EMBL:PON22311.1};
GN   ORFNames=TGAM01_v208794 {ECO:0000313|EMBL:PON22311.1};
OS   Trichoderma gamsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=398673 {ECO:0000313|EMBL:PON22311.1, ECO:0000313|Proteomes:UP000054821};
RN   [1] {ECO:0000313|EMBL:PON22311.1, ECO:0000313|Proteomes:UP000054821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6085 {ECO:0000313|EMBL:PON22311.1,
RC   ECO:0000313|Proteomes:UP000054821};
RX   PubMed=26893428;
RA   Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT   "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT   Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL   Genome Announc. 4:e01747-15(2016).
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:PON22311.1}.
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DR   EMBL; JPDN02000039; PON22311.1; -; Genomic_DNA.
DR   RefSeq; XP_018666266.1; XM_018800801.1.
DR   STRING; 398673.A0A2P4ZDG7; -.
DR   GeneID; 29980884; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000054821; 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: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: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; 3.40.47.10; -; 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; 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; 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:UP000054821};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          8..449
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2381..2459
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          3523..3602
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          2478..2534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2478..2528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3964 AA;  437535 MW;  5CC82B5D009E6F67 CRC64;
     MALPTFKTEP IAIVGSSCRF PGGANSPSKL WQLLKNPKDV LVKIPPSRFN PDGFYNTNGE
     HHGSTNVLHS YLLEEDHREF DHNFFNIHPK EAESMDPQQR MLLETVYECV EAAGYSIQGL
     KGSQTAIFVG QMTQDYSDLM LRDVDSAPQY AATGISRAIL SNRVSYFFDW KGPSSTIDTA
     CSSSLVALHH AVQTLRSGES SLAVAAGVNL ILGPDPYILE SKLHMLSPTG RSRMWDADAD
     GYARGEGFAS ILLKTLSQAI KDGDHIECLI RETGVNQDGR TSGITMPSSI SQTALIKSTY
     TRAGLDFNKK TDRCQYFEAH GTGTMAGDPI EARAVRDAFF GADEEEDSAN AAELDEPLYV
     GSVKTVIGHL EGTAGLAGLL KASLAVQHGV IPPNMLFNKL NPAISPFYTH LCVPTQAKPW
     PKLPPGVPRR ASVNSFGFGG TNAHAILEHW PSRGYDRALQ IPCGPFTLSA NTEKAVRARA
     QTLSAALESG QVTDLSDMAW TLQTRRTQFP HRIYISASNQ EELVKKLNDV ASQSASTTTR
     AIHVTEDLPA RILGVYTGQG AQWPSMGRRL YEKSKRFKQT IDDLEKALSN LAIPPSWSLS
     GELVASAEDS RIHEAAISQP LCTAIQIALV DLLYASGITF SAVVGHSSGE ISAAYAAGHL
     KAADAVAIAY YRGVFAHLAG GPDGRKGKMM AVGMSFDQAL FFCKEAQFAG RIQVAASNSR
     SSVTLSGDED AIEEAKQVLD EQQTFARVLK VEKAYHSHHM QRCAQHYLES LQKLDIQIRA
     DQLKCKWYSS VYGSNGRSIE DTDAYKASYW VDNMVKPVLF SQAIDRAVVE EHCHDIVMEV
     GPHPALKAPV LETLKNLTGL DLPYSGVLKR GQDDMESFSD ALGFIWSNFH TPTPIVDFAG
     FRRACLGDEA GESITLKGIP PYPWDHDTKL WKESRKSRNY RSRKNPMHEL LGYATTHGNN
     SEVIWRNVMK IKEMEWLRGH IFQGQVLFPA AGYVSMAYEA SIRLAAGETQ VRLVELEDLV
     IHRAITLEDE SSGTEVTFTI RVKSQTSDQI TAEYSCYSCK VDGGSELPDS TNFTGRAIIH
     LGTPRLDSLP SREAPKLPMK PVSVNRLYSY MEEVGLRYTG EFVVEGVERR LNTSTVKLQR
     LDNSKTKLHP ATLDAAFHGI FTALAFPGDG QLWTPYLPTN IRRVRINPAA LDAPVSSSDI
     SDLVADCYLT NANSKTICGD VNVSSSTTGI TQIQLQSLTC SSFTKATPQN DRKLFAKTVW
     MRDISSGIEP DKVQYLSEEE VDYGDICERL AYFYLRKLRK EISPEEIPRM DEHFQIQIDW
     ILNYLLPKIE AGNHPRIKKE WVTDTEEDAH KWMAKYSGKV ELQMISALGE VQPSILRGQL
     PALQVMMQKD MLTRLYAEAV PFRQTYSHLI TVTSQLAHRY PRMRVLEIGA GTGGASIHML
     KGLAGHCHSY TYTDISAGFF EAAQERFREY SSLMEWAVLD IERDPCEQGF EKHSFDVIMS
     SNALHATKSL AQTLTHCRAL LKPGGFMILN EVTNDGVLPQ FISSHLPGWW LGRGDGRLYH
     PTVDESRWHQ ELLATGFSSV DAAYRDYHDP KRYLASLIVS QAVDDRISLL RSPLSSKENI
     PRVKHLFIVG GESDEVQNLV RKVEPLFRHI ALTVTLVTTL EEVGEVIPGS AVLILSELDK
     PTFEQITPQK FRGIQLILQD AKYVLWVTQK CRDDNPMSNM VVGLGRSVLH ELPDLRLQFL
     DINAAQAGAV EPSLFVETML RTICLDSPEF DGILWHEEWE LSINGDGLYI PRIVPVEHMN
     DRLNSTRRDI VSPVSLGEVC IELGRSNGSR SLQQVRSKME ATTSTDTVQI RVHYSSLLPI
     QTRDNLLLHL CIGSIGQSSQ MALVFSPHAR SIVDVPKVEV LLLQQQFATS SDAERLMATI
     IAESIVQSSR GNIWIHDSDI PLAKVISTVA GMRGLDVFFS TSSEANSQSN FDQAFIHPYA
     TERDARNIIP ADIQSFVNLG KFNSVLHRIV LSSQRINQLA IYDEHSIHGR FTKKDMADIA
     IRHILSLSDD LGHHQSAIPL DQVMDMPSLP ETPTAMISWH SSDSMDLKIN PVDPNDLFSA
     NKTYLLVGLA SELGLSLCDW MVTHGARNIV VTSRNPGRVD AEVLKHLRRK GAKINIFALD
     ISDKEELLKI YKEVCDTMPP IAGVANAAMV LNDKLFNNMT LADFEVALKP KVTGTQNLDD
     IFYSTPLDFF ICFSSLTCVM GNGGQSNYAA ANMYMHSLVR QRKKRGVSAS IIDIAFLLGV
     GFVARNLEQY EDHLKKVGYM RMSEPEFHTV FAEAIVAGKS TSDEDPEIII GIGQAPNAPW
     YTNPRFATYV PHENTTENSD REQVQSSDSV QGRLAAAGSG KDALTVLQIV CAEKLAMILQ
     VHSDSIDHAA PLLKLGIDSL VAVEIRSWFL KEVNVDMPVL KILSGASLAD ICQDALVMLP
     PTLVSSANED LISSNVAPKA QNHQAPTVAA TSKETQLSIP PTTVASNSDR EGDSSTELST
     VSPKPSSVSE ETFEDRSYVR MGEMTPGQSR LYFLHVYLED KTTYNVTMSG KLSGPLNIDN
     FSNALDALSE KHEGLRTSFY LDSASGKAMQ GVNRRSSIIL EHANIPGDSS VKIQESLDDM
     KRFKFDLNRG KWMKIRILSL SPSDHRIIFT FHHIALDGVG WSIFLKDLND AYAGKGVRTP
     RQQAIDLSQK MQREAASGTL AEDLQFWKDT YDSIPEPMPL FPTSKVQHRQ LLKSYDTETL
     DLILQRPLVH QIKQASADLQ LTSFHFYLSA IAAFVSKCLN IGDFAVGILD ANRTSAADMT
     TIGYFTNLLP LHFKTNASES FADLAVRTRD ITLAALSHSR VDFDQILDTL NIFRSGDQNP
     LFQIAVNYRL GGSRTMPLGE CEIQWTSTHD ARNPYDLIID ISEIAEGTII SFTTQSYLYS
     TCDTDMLLKW YTHTLKEFAA DTSKLALDCT LAPSTDIQRA ISVGRGSRID IEWDAPTLAH
     RIIEMAETSP TSMAIKDGYS RQLTYSNMMR RVQQFAEHLS NLSPGSYVGV LLEPAADTIC
     SLVAIMILGL VYVPLDLRNP EGRLAAIIAD CKHAAIICQN ETLGLAQKLT LTVGNTLITL
     LNTSDVPTAT TRGNSPTHCL AQPHAPGFAI YTSGSTGTPK GVLLTHHCVL NQIWGISKMF
     EIKKENVLQQ SSFGFDLSLE QVFIALANGG TLIVASKEAR GNALEIANLI LSENITYTVF
     VPSEYLHLLH YTSNILKACS SWKFAFSGGE KVTAQLRRGF KKLDLPNLRL INLYGPAEAS
     LSCTRYEIPY RTDKTTTASP AGFVMPNYTV IVVDQIGSPL PFGFPGEICI AGAGNSIGYV
     NQPQETASKF TPDRVSPVED INRGWNTLYH TGDKGRMLDN GLLEFIGRLD GDSQVKIRGM
     RIEMDEIAKT IVDASQGVVD DASVSLRGSD LLVAYVVFSD GFAGDTNLAV ERIRNDLPLP
     SYMCPAHIIA IDEIPRNPNG KKDKSKIDAL PIPDALEVKT QTGDLSDFEK AVVAVWRDVL
     PNTMKLSQFG SETNFFFVGG NSLLLLKLQA ELEMAFGRNL TLSELFQAST IREMAAKIQA
     VSDKPLRQHI DWNKEIRSLC DGLSRSAFTK PVNVSSSKSG LSVVLTGATG FLGRNILKCL
     VNDDRVSEVH CIAIRPDVNG LPRHVDVSSP KIIEYSGDLA DHDLGLSPEQ LESIASRANV
     IVHNGADVSF MKTYQSLRRS NVLSTRRLAE IAAAVSIPFH FVSTASVAHL YPGEHLSEVP
     LEAQADLPAD GQQGYAISKW VSEALLEYLA DNHDLQSCVH RPTSIIGDGA PDTDIIASLH
     TYSEILGSVP KLSGVITGNL DFVDVQNVAK EIATQALAST SANQMDPSPK TFYINHCNEE
     KVSIPNLKEY MEKAKGKLFS ELELNDWLQK AREAGLNELI CVYLKNMVDK KEPLYLPSLV
     KGKV
//
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