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Database: UniProt
Entry: A0A066XMT8_COLSU
LinkDB: A0A066XMT8_COLSU
Original site: A0A066XMT8_COLSU 
ID   A0A066XMT8_COLSU        Unreviewed;      4028 AA.
AC   A0A066XMT8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Putative beta-ketoacyl synthase domain-containing protein {ECO:0000313|EMBL:KDN70187.1};
GN   ORFNames=CSUB01_07850 {ECO:0000313|EMBL:KDN70187.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN70187.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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:KDN70187.1}.
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DR   EMBL; JMSE01000380; KDN70187.1; -; Genomic_DNA.
DR   STRING; 1173701.A0A066XMT8; -.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_37_2_1; -.
DR   OMA; HRERITH; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000027238; 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; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.366.10; 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; 3.
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; IPR007110; Ig-like_dom.
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; 1.
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; PS50835; IG_LIKE; 1.
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:UP000027238};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..439
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          170..282
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          2398..2480
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          3534..3611
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          2492..2529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   4028 AA;  440484 MW;  42F0E5E98C909797 CRC64;
     MASRNEPIAI IGSACRFAGG VDSPAKLWEL LSNPRDVRTE IPSSRFSADG FYHVDSQYHG
     HSNVRHAYVL EQDPGVFDAQ FFGVKPVEAK ALDPQQRLLL EVVYEGLEAA GIPAEDLRGS
     NTGVYVGLMS NDYESLMLRD VDTMANYHAV GTQRSILANR ISYFYDWHGP SMVVDTACSS
     SLVALHLAVQ ALRTGEARTA LACGSNLLLG PENFVGYSKM KMLSPDGKSM TWDRDANGYA
     RGEGVATVVL KTLRAALEDG DHIECIIRET GTNQDGATPG ITMPSAESQR ALIRDTYRRA
     SLDPRDPADR CQYFEAHGTG TQAGDPIEAE AIYRSFFDDD SGDADSLYVG SLKSIIGHTE
     GTAGIASILK ASLALQNKQI PPNLWFNNVN PKILPFCKNL RVPTINPKEW AEPLNSQPRR
     TSVNSFGFGG ANAHAILEEF QGPQAADVPS DLERNAQCFT PCVFSAHSEK SLLANLAAYL
     DFLDKHPSVG LRDLAGTLRQ RRSALPVSVA FSVSSIQELK SAISAKVQQQ QEDEVGRRLL
     AGSPGTREAK RGILGVFTGQ GAQYARMGAE LVEKSAYADK LLQVLEGHLA DLPVQDRPGW
     SLKAELLADA ATSRLGEAAI SQPLCTAVQI LLVDLLRLAN VRFSGVVGHS SGEIGAAYAA
     GYLSARDAMC IAYYRGLHSS PPPGSKGAML AVEASFEEAQ ELCGRADLPG KISVAASNSS
     SSVTLSGDED AIAFIEQALG EQGTFRRRLR VDRAYHSHHM LPCSGPYLKA LGSCNIQVQE
     PSRDCTWFTS TRSFESSSEL KGVYWADNMT QPVLFSQAVA AAASSGGFDL ALEVGPHPAL
     KGPATQTVLE VSGHQIPYHG TLSRSADAVR ATSDALGFLW SLLGKAEVDL DTYESKVSGL
     TSFDVLKGLP GYRWDHDKTF WHESQVSRNM RLRRLPVHPL LGHLSPTSSP HHLSWRNVLR
     LKELPSLAGH ELQGQVVFPA AGYLSSALEA ASFLSDGRSI RLIQIRDFDI YHPIVLDSDD
     VEVVISLTEV DKAGPDTLRS TFTYSSSGLG KDSGTLTLVA KGKVEVSFGE PSMSILPPDG
     GPTPNMIPVD RERFYESLSE LGYNYSGPFR ALSSLNRSLG RASGSIGNEG LRAEDKDETP
     LMAQPGILDS AIQSILLAHS YPGDGHLWSL QVPTSIRQLR MNPSLCGSAW RGSNGLSFRS
     TADDLTGSGG LRGDVSIYVQ GSAHAAMQLE GVKIVPLAAA TAADDIRMFS RTVWGPGHPD
     AAEAADGDMA MADELEFASV LERISSFYLR KIDENVPTDH PAREAGPLAG YLNFARHVND
     LVKSGEHPYT KKEWLNDTLD HIKAASLRFA DTPDVKILHT IGEQMPHVIE GKTTILEHAR
     PNGLLDDYYV NALGLPQVSR WLANTVAQVT HRYSDMNILE VGAGTGGATK SILGRIGRDF
     SSYTFTDVST GFFENAASTF ERHGDRMIFK KLDAEQDPIE QGFVANSYDL VVASFVIHAT
     SKLRETMTHL RRLLKPGGFV ILAEITDNEQ IRTPFIFGTL PGWWVGVDEG RTLSPCVSPE
     SWDSILTDAG FSGIDTITPD SFKAVHPFSV FVSQAIDDRL TFLRSPLSSP PTSAVPRVPI
     EHLFVVGGNT LREKRLVTEL GKILRPYSRA VTVFKTLADV NHSLVTPEST LLSLVDLEKP
     VFKNITKAEF DSLKNLFGTE KTLLWVTQGR REKDPFANMS VGFGRTAVCE VPELRLQFLD
     VESDRVDARA VAEAVLRLQL GSFWAQQEVQ NDQLWSLEPE VVIDDAGRLL VPRLEPSAVL
     NSRYNSARRS VVRNASLQEE AVRVCKIGDK FVLQEDVPQA PDTKPAVESP LVQLRATHTL
     VSAIKTPLGH YFLSIGVDPD TQSRYFVLTD SPSSTIRVPL SAAVPVPASA HHDDGQLLVL
     LGDAIISLTV LDGVFPGQMV LVHNATPELH NALSRQAAEK GVNIVFTTSS TSSALPTSWT
     RLHPYMTAAE IKTILPHGNV DAFVGFSGPD LSSQQLESSV IDTLSPKSRV ETTGTIFSSS
     SSPLPSSDLA PAIGEILRKG VSSASAIDSA ASLEGVSTVA IADLAAGKEP AENMTVLVWP
     LSSSSSPSSV PVGVSRLDSR MLFKSDKTYW LAGLTGTLGL SLCKWMVEHG AKHVVITSRS
     PKVDPTCDIS SYDDVKSLYE HIRTTLPPLA GVAQGAMVLR DTSIRNMTFD QMTDVLRPKV
     DGSINLDSVL GEHPLDFFVF FSSILEITGN MGQANYTAAN AFMSTLAAQR RKRGLAASVI
     NIGVITGVGF VTREASTVQE KALHRSGLML LSEKDMHQIF AEGIEASRLD SSPSGQQLQI
     TAGLRSIPID SADLPTWRSD PKFSRFIVQE TDTGAGEANV AARASSMSSL KQQLQGTKSS
     AEAEHILVEA LGRKIRSVLQ TDTPDDALMR MSTDEIGLDS LIAVDIRSWL LKHFELEVPV
     LKLLGGMRLT DLVAKSVQGL LGAVSDSTSQ SEVDEMSASI HSSGDTSSQQ ASSTSDDLPE
     PTLTSTSLAG SELFTKPEAV AERSLAISFS QSLFWVVDSL VEDKTAPNHT VLMRVVGQPR
     LSVLRNAVEM VGRRHEALRT RFRMDGEQHT VQEVLESPTL ELEEVRVSDE ADVMLEYDSL
     KRHVYDLGSG RLMRIILLSR SPSDNWLLVG FHHINVDGMS FQVVMQDLDK LCRGQQLNPK
     TMQYPDFSEA QRTALSSGAW VEDIEYWKRE FATIPEPLPL TRARITTRRP ITRFSVHTKE
     LRVDGALSGR IREVARANKV TSFHFYLTAF QILLHRFTGA EDMAIGVADS GRNDQGEVLD
     SVGPFLNLIP LRFEVTPAQT FGRLIADTRR KSYAGLAHSR VHFEVLLTEL QVPRVATQSP
     IFQAFVDYRQ GAQERQPLAN CTLEMMELQM GSTGYDLSLD VIDNPEGDAR IALMGQAHLY
     SVSDMDIIGG LFEDILNEFV QSPAKRISEG WQYRQADVER ALQVGQGQIR KSEWPETLIG
     QFEVSAEKHK RNTALIHADG TSLTYAQMQQ RIDTIAAALE ENSIKPGDSV GVFQESTTDW
     VCSMMALWKR GAVFVPLDPG TKTERLAMVV KDCKPAAILI DDATKGLHTE LGATERTVFI
     NVSALTTKTD APSSKILASP DDLAMVYYTS GSTGNPKGIA VRHEGVRDVF ESACWLYGVN
     EKVVTLLQSS LGFDITLIQM FISWPVGGTV CMISRDMRGD SVALMEFMTK HNVTHTVGTP
     SEYNSWLRFG DQAKLRSSAW RVAICGAEAF PPTLLEKLRE LNKPDLQLFH MYGTTETTVY
     ATQQELNWKQ EGFYDDGVMP AGFSLPNKSM YIVDEDMHLL PVGLPGEIVL GGVGVAQGYN
     NNELMTKASF VPNTFAPNGS PFHRKGWTTM YRTRDRGRLL PDGSIVVEGR IGGDTEIKLR
     GLRIDLKDIE HAILRSADGV LSEAVASVRS TAGTDTQFLV AHVVFSPANA PKDRQSFLSD
     LLDNLPLPRY MCPSVLVPIE KMPMSMSSKL DRRAVATLPV NRPDRLTAER GASQALNEAE
     IRLKEVWEQV IPQGMFDIAR DSDFFHVGGT SLLLVELQAR IRQRFDCTLR LADLFANSML
     CTMSKLIPQQ ESVATVAADG DDDGNGNEMP SMEIDWEWET RPAPELQIGT ADLSVVVPPS
     PNPKSVIITG GAGFLGRSLL KSAIENPHIE RVHAVAVRKL QQRLASGLLP QHPKVTYYDG
     DLREPLIGLS QEDADAIFND IDAVIHNGAD VSHLKSYFTL RRANLNATKE LARLCLPRRI
     PFHYVSTAGV SMFTFWQSFG EETASAAEPP TDGTNGYKAS KWASERFLER LNEKLGLPVW
     MHRPSDMVRQ DDEEASWDLL HTLLGYSRKL RAVPVSENLW GWLDLVAVYN VSHDIVQMVH
     DNRPRSTDGR VSYVHQTGDM AIPIDEMKEF FEEECGYTHV FEKLPIKEWA RRAELAGMRP
     AVAAVFGNVP RLPRALCFPR FVKTWRPSEG QDGGMLLMKK CDCGGLVSPV WGEGCEGCGK
     SPVMPVWG
//
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