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Database: UniProt
Entry: A0A2T3YUM7_9HYPO
LinkDB: A0A2T3YUM7_9HYPO
Original site: A0A2T3YUM7_9HYPO 
ID   A0A2T3YUM7_9HYPO        Unreviewed;      3087 AA.
AC   A0A2T3YUM7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PTB36239.1};
GN   ORFNames=M441DRAFT_84067 {ECO:0000313|EMBL:PTB36239.1};
OS   Trichoderma asperellum CBS 433.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB36239.1, ECO:0000313|Proteomes:UP000240493};
RN   [1] {ECO:0000313|EMBL:PTB36239.1, ECO:0000313|Proteomes:UP000240493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB36239.1,
RC   ECO:0000313|Proteomes:UP000240493};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232}.
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DR   EMBL; KZ679271; PTB36239.1; -; Genomic_DNA.
DR   STRING; 1042311.A0A2T3YUM7; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000240493; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase 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:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 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; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039551; Cho/carn_acyl_trans.
DR   InterPro; IPR042231; Cho/carn_acyl_trans_2.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF22; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF00755; Carn_acyltransf; 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; SSF52777; CoA-dependent acyltransferases; 2.
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; PS00440; ACYLTRANSF_C_2; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
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:UP000240493};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..431
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2436..2513
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   ACT_SITE        2842
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   3087 AA;  340505 MW;  F9FE0A96B36E7FBD CRC64;
     MRSQGPVPVA IIGMGCRYPG GANSPEALWN VVAEGRSGWT EVPSDRFNHQ AFYHPDPEIP
     GTINQRGGHF IDQDIATFDA GFFGIAQQEA DTLDPQQRVV LETTWEAVEN AGIPMHKFKG
     SDTGIFVAMF GHDFAQIIHK DPEAISKYHN LGVARPLLAN RVSYVFDLQG PSVMVDTACS
     GSLAAISLAC QSLRSGETSM ALAGGVNLVF SPDQMALMSM TGLFNDQGRS YTFDARGNGY
     GRGEGVGMVV LKRLDDAMRD GDSIRAIIKS SGINSDGRTN GIMLPNQDAQ ERLAKRLFQN
     LPIRPSDVQY VEAHGTGTKA GDKVEINTIR NVFCEGRNGQ NPVFVGATKP NLGHSEAASG
     TAGLIKTVMA MEKGFIPPNI LLENFKPGLE PDERYMKVRL AFHSNSAPTN RKAVVNSFGF
     GGTNAMLLLE SADGYNATQN GTQNGNADLR KDDPNLQHFF PISARSEYSL QNAINNLGDY
     LKNHPNVPLN HLSHTLVKRR SKFQWRSCIV AEDIDSLLQG LGAKDLVRNK APNKQATAFV
     FTGQGAQWAR MGYNLLLSEH TAFARSIATS EKLLQGFDAQ WSLVEELSRD ESSSRLNNSA
     YGQPASTAIQ IALVDLLKSW NVLPTAVVGH SSGEIAAAYA AGAISQSAAM FASYHRSFLA
     EKSKQRSVQS GTMMAVGLGH EDVQKYIKQF NIQGVTVACI NSPSSVTTSG DLDGITVLKD
     ALDADGVFSR RLKVDTAYHS HHMQLVSSDY LHQLEGLESG PVNTAIRYFS SVTEQEKVDG
     FGASYWVDNL VSPVRFCGAL QNLYQELRQA AVNIVEIGPH AALSGPIKQT LAGLQANGSS
     YNYIPTLVRG ENSVKSLMNT GSTLFRSGND DLDIGAVAAL CKSESSPLTV LRDLPSYHWD
     HTETHWMESR LSREYRCRKH PSHDLLGSRV IASPDSQPSW RILLSTERLP WLQDHVVDNF
     IVFPAAGYMT MAIQAIQQLD QDRRQDLKPK GYRIKNVSFK KTLTIPKDDK SVETILTFQY
     SDSNENWNFS VSSMSDQGKW QDHCNGIIST ITENDKDEVV QQREAEFDRK TQASRLEDAA
     KACTNVISHK DLYSQMAATG NQYGPTFAIN NEVRMAAFQS LNDLIIPDIA TKMPSGYIQP
     HLIHPTTLDG IIQSCLPVFQ QHSNKGSVMP IFISDIFIST SIANQAGNHL QTLCNLSNVF
     PTSTNFSTTV FQTEVDGTPQ CVLTMNGGEI RVVGESQATE VLHNDNIFKL EWGVDSSSIT
     PEMLERVQIP LQSDEAGITQ AEKVNLTFVA CARYIDWAVK EMHERGLAVK DDHRVNWWRL
     LENFASSDMG KSLIDKSPNT KDELDKLTSR LGVEGEAVAR IGPELIPLLT GQTDPLTHFL
     KDDLLFRVYH SDEGARPNQY MADYVKMLTF QRRDLRILEI GAGTGGTTYR ILKACSPNGD
     TFCSEYMYTD ISSGFFEAVR TTRLKDWAHL LTFQTLDLEK DAASQGFEEH SYDLVVAANV
     VHATRSLDKS IRTIHKLLKP GGVLGLVELT TSTPYINMTF GSIPGWWAGV DEGRTDSPLQ
     SAEQWNVHLQ KAGFSGVDLA AYDLPEPERH CALLLSTALA LPSATNGHIP PRFRILDGFV
     GGNPPSSPFS EKLASALTEK GFGASLEEWT NVEVDNSGSY IILDSAKQPL LTKASAEQFS
     SITRLLSKAT KVYWIIFATN DNRGILPDNA LITGVSRTAR NENPHLDCFT IDVQDSLQQH
     PDQIQNAILE FIYATEARIK KNEPREFELM YRDGRMQIQR FVADNKLSKV VAASSDVTET
     EETTFHQTDR RLRIHVDKPG LLNSLVFVDD DSPTLGPDEV EIKSYAWGLN FSDVFIALGQ
     LPPTQPMVGE SAGIITAVGS NFASQFTPGD RVTAMFGTPY ASRTRTNGHL VYRIPDKLSF
     TDAASIPLTF ATAYYSLFDC ANLRQEQTIL IHSASGALGQ VAIKIAQRLG ATIFATVGSA
     AKRQLLVEQY GIPESHIFSS RTTDFAAGIN RLTNGTGVDV VLNSLSGPML HASWECVAAF
     GTFVEVGKTD ISRRSQLNMK PFERNLRFMS VDLVGLSKQR PADCQKLLQR IFADFDAGLF
     TPLEVTAMPM GDIEKAFRLM QSRKHTGKIV LEASDHSTVQ AKEQPFHLRS DGTYIIVGGL
     GSLGRHLCRH LQEKGARHIA LFTRQSYQEA AKAEMEKELT VVLEAIVKIV TCDVGDTKVV
     QQVAAELSQA MPPVRGILHG GMVLSDRTLS QITQKDFEIA LLPKYHGTVN IYNAFYHKDV
     DFFVNLSSLC GIVGTLGQSN YAAGGTYQDM FTHAQVSAGY TKFATIDFPL IKSTYTVTQE
     HTHSLGRQGV QFLPIETALP VVDYVMSGRA FKDGNHQIAF GLDPQSFINQ TTPGGRVPPL
     VSHLLSSQDR GLAHQTGQEN ERTAEEKVAL ASTIEEAEQM ILIAIREKIA SLTVLESQEL
     DLDQAVANMG LDSLVATEIK NWITNKLQAP VQTSDILDAP SLRSLASFVT KSSILVKNKF
     KPEGVNGHNE TKAEVNGNSY RVKEVSLPKY PMQSLEGTLD IFLDSVSHIA NAEELSRTRE
     AINAFQDPDG LGQKLQARLR NMSGGEGENN EVVDMYVRNK WLRGRDWRPR LRNFFATLPG
     QDTARQPQAQ QAAQLSLAAY AYKLALDAGT VKQDFYHEQA LDMATVYWLF SSNRTPALGC
     DGYDRFPESD YIVAMRRGHA YKIPLTDHNG QTIAYDKLKN VFEAVIQQTP EETNWTGLLT
     TANRDDWAKA RDEILSGNES GRNYVKTIEE SLFIVYLEDV SPETADGRAE AFLLDDNSNR
     WLDKTLSFVI CLNGVTAIWG EHTMVDGTTF GGLIKALNAP AVEHIKLSSG SSNSTSVVDG
     DFKYFEFTLS PTLSKVIPAL QTQHRSAHDG YTLANLTQTS CAASYLRQHK LPPKTVIQLL
     IQVAVRRLFG YNPSGAVDVI SQRPFRGGRT DMIYVMTPPV EAFCAAAEDA SVSSVEKRRL
     FLEAVKSHAR LVALSTRGRG FRWHLMALRE MLEPGEELPV FYKDEVFKRT SERPVCTSFT
     EFGLPEMGRC QPHKEDVWVG VQVFDER
//
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