ID A0A2P4ZDD3_9HYPO Unreviewed; 2831 AA.
AC A0A2P4ZDD3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PON22308.1};
GN ORFNames=TGAM01_v208791 {ECO:0000313|EMBL:PON22308.1};
OS Trichoderma gamsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=398673 {ECO:0000313|EMBL:PON22308.1, ECO:0000313|Proteomes:UP000054821};
RN [1] {ECO:0000313|EMBL:PON22308.1, ECO:0000313|Proteomes:UP000054821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6085 {ECO:0000313|EMBL:PON22308.1,
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 -!- 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:PON22308.1}.
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DR EMBL; JPDN02000039; PON22308.1; -; Genomic_DNA.
DR STRING; 398673.A0A2P4ZDD3; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000054821; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance 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; 3.40.47.10; -; 3.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 1.20.1440.110; acylaminoacyl peptidase; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR010520; FrsA-like.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF06500; FrsA-like; 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; SSF53474; alpha/beta-Hydrolases; 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; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 2.
PE 4: Predicted;
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 20..132
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 135..310
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2316..2393
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2831 AA; 312140 MW; 6B5EE82335F4F388 CRC64;
MRLYESVLNG DVAHHPAYDD KSIAVVGLSC RFPGDATNPE QFWELLCKGR SAISHIPRDR
WNSDGFYCAS KGRQNTSITN RAHFLKEDVS VFDAKFFSIT QQEAASMDPQ QRLMLEVSYE
AFENAGVTLD KLAKSKTGFL SPDGLCKAFD ASADGYGRGE GFAALVLKPV EKAIRDGDTI
RAIIRGSATN QDGKTRSMTM PNGEAQEELI REAYRSAGLD FKDTSYFEAH IGHLESVAGL
AGIIKSIQIL EHGLIPPSLH FHNPNPRIPF KEWRISVPTE EVSWPEEGIR RISVNSFGFG
GSNAHIILDD AYHYLSARGI KAPHNTIPTS PKGREVLRSH KEDSSPSLPY MMILSSSDQS
GLTRQRQTLL KYLKDNAQIR HESGQEFLRD LAFTLSERRS RLPWKTAFMA STVSELTRAL
EASTSLEVRS NSEPRLAFIF TGQGAQWAGM GIELLQYRIF RESVESAERY LRKIGCPWSV
MEELQREDAI SNINQPLYSQ TICTVLQVAI VQLLTSWNIT PRSVVGHSSG EIAAAYAIGA
ISQEDAWKVA YWRGKLSSEL LKSSPDLTGS MMAVGASAEQ AQKWLDELTE GKCVVACVNS
PSSVTISGDE AGIDELAAKL KEREIFARKL KVDTAYHSHH MLAVKDPYTK ALANMKTKQG
PPNGPQMFTS VTGHIISAKE LGPSHWVTNL TSPVLFSDAV RELLRYKSRE DQNHGCSVDI
MVEIGPHSAL QGPIRQILSG FGALNTEYRS VMSRGKNAVD TMLTAVCDLV SRNLPADILA
INTCNDDYTA SFNSPPAPIV TLPSYAWNKT KSYWNESRLT RQIKQRSSPR LSLIGAPLPS
FAQLEKQWRG FVRIAEEPWL RDHKIQGSIQ YPTASYIAMA LEAASQVADK GRAVNRYKLR
DIQIRDSITI DEGSQTEFIT RLRASASDAT TLSEGWLEFS ITSSGSDDSL QLHCSGLLDI
EYGDSTGAAV STESTHDEQA MRDLYLLAEE ECQVSQDTET FYQDFQSVGL EYGPSFQSLR
DIRYDTRGQS YCTIEIVNHG STPAALPAAR PHVIHTTTLN GTIQAAVAAF KGDDGNIKGS
LTESYVEEIV VKADIPFEAG ARFKGCAKIS QQCSSEAVSN IFMLDEGTDQ RVISIKGLRF
VVEVVSRTLQ RDGDSTSLRE SPFTCKMDWI PAFDLLSSGK KQEMLDQIHK PDDAEVQHLM
KEQQTAHVAI REAIEKANGM RIPNLQLRNF AKWMKQQLNT SSLPLEKDLF ADNKLSKSLT
EVLCASVDPE SLLGTEKSVD KIIDSLRGMR VSQTKLIKIV AIMAQIKPNL AILELGADYT
SPFLASARDI PDTVNYTYAC PSAIGLQEVK DLTQTFLIPS QLKVLNIDLD VRKQGFEPSS
YDIIIGCNVF SNSKSLQRTM ANLKGLLKDG GKICIAELTN PGSTVLPVLG GIYEWWKKRD
DGSSRPLKLD SIQSVFNDHQ FGIDFISSDF DASPLHQTSV LVASATRPKD EVTILQTPNC
SKAAQELASK VSQLLQNDGI SSQVCAWGSD NIDHKGKRFI ALVEFELPFL ENLTQRDFEI
LKRLATEASS LQWVTALPDP ERSSALGFAR VVRNEIPAIR FQTLQLDTGC ATMLDRAAAL
IHQVESSTTT ENEFREIDGV LHVPRVVENR ELNERLSQKS PDLDTVELMP LGSTTGSQKL
FIRNDGVSES PYFEADELRN NELDEYEIEI GTKASALSRR DVIARTGPAS DAALELEASG
IVLRVGDQVT QFQAGDFVFA LAPGTHRTVL RTRASMCQRI PTGFNFEDVA CLSLVNCTAY
HALMNIVCIR EGQSILIHDA ASNFGQAAVQ LAKHKDLDIF ATIRSASERD LLKDLYNIAN
DRIFALRDSN FSNSILRMTN GTGADYILNS VVREQLQETW NCLASCGTYL EISSKDASRS
MLREMRPPLK DYIFASVNMG HIQSQRPEIM AGILRNTFEF MEQGIIKPAT PVPVYPVSQI
ERAMDLMKSA ENLENIALSF SPDDLIPVLC KPKRISLKLS GESTYLIVGG LGDLGRSLAR
FLVDSGARHI CFISRSGTVQ DVQKQLVTDL TSSGVDVRVY KCDIASFSAL EDTLALCSRE
MPPISGVIHS ALVLRDAILH NMTYTQWVEA VGPKLQGSRN LNELLPRNLD FFVALGSFIS
VIGGRSQSNY ALGGAYQDGL ADFRRSLGLR AVTINLGVIK DIGIIARNGA VGAARDWAEA
FGLDENELHT LVEHAISVQQ TESSSSTPAQ IITGIPTIGM VKQAGIPRPY YFDDPKFSIL
ASMGAKQTSL TAEREDIQPS SLSLGVQLKG VTSIAEASKL VLNALVAEVA KLMQVDTGEI
DTNKALYSHG VDSLVAVDMA HWIKKEIGAD VVLSDITATI PITSFAKDIT AKKSVSSDCR
MQRIISSEFF NFEYLRVLGT SPFQGAEVGE CLEAAHKIRS NDPESWYRAW SEAALKSEEI
AETALRTGDR EAARWAFLRS SNYRRASEFL LHHNPEDTRL SSTISQSISN FKKACQLFDD
PVHFLEIPYE NGATLPAYLF MPTSASKLPG KTPVVISTGG FDSTQEELYY FTASGARTRG
YATLSFEGPG QGIVVRRDKL HLRPDWEFVV GHVLDHLERI VGEHPEWNLD LSRVAIAGAS
MGGYFALRGA LDPRVSACIS IDGFYDLAGL TRARVSGPLM TAIEEQYIPD HIFNTLLWIV
LALDFQKQWE LGHARLATGI PSPAAAMRTW KNYSMALPDG GTRLSQIKCP VLVTGSRDTM
YIPVEAGPQR IYSELTSISG SEKKHELWIP SSPGQGSLQA KVAALAALHT KTFSWLDDVF
GIQRESITVR D
//
