ID E3R0U2_COLGM Unreviewed; 2667 AA.
AC E3R0U2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=KR domain-containing protein {ECO:0000313|EMBL:EFQ36730.1};
GN ORFNames=GLRG_11878 {ECO:0000313|EMBL:EFQ36730.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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DR EMBL; GG697492; EFQ36730.1; -; Genomic_DNA.
DR RefSeq; XP_008100750.1; XM_008102559.1.
DR STRING; 645133.E3R0U2; -.
DR EnsemblFungi; EFQ36730; EFQ36730; GLRG_11878.
DR GeneID; 24417241; -.
DR VEuPathDB; FungiDB:GLRG_11878; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000008782; 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:0008270; F:zinc ion 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; 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; 3.40.366.10; 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; IPR013149; ADH-like_C.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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; PF00107; ADH_zinc_N; 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; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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; PS01162; QOR_ZETA_CRYSTAL; 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:UP000008782};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..445
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2586..2663
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 474..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1919..1945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1928..1945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2667 AA; 291920 MW; 4914FBD315332B6B CRC64;
MLPATSPVSM GEQRSLQSEP IAIIGLNLKF PGEATSMQAF WAMLENGLNA SCEVPAGRFN
IDAFYHPDPA RLDSIRVRKA HFMAEDPRAF DAAFFNMSPA EASILDPQQR GLLEGAYHTF
ENAGIAMECA AGSKTSVFCA SFGRDSDAIV ARDPAFQSRY QATASGSSML SNRISHFFDL
RGPSLTVDTA CSSGLYAVHL ACQSIMAGES NMSLVCGSNT YITPECMSLP LSNAGFLSPD
GRSYSFDKKG NGYGRGEGYA FVLLKPLHKA IEDGDPIRAV IRATGVNQDG RTPSITQPSS
QAQADLIRST YRTAGLSLDD TGYVEAHGTG TPVGDPLEAA AISQVFQTAS RSEPLVVGSV
KSNIGHLEGA SGLAGLLKTV LALERGVIPP IADFEEANPA IQASVSGIDF PSRPVTWQKP
MPGFRRASVS SFGYGGSNAH VVLDDAYNYL RMRGLKGCTA SAGLVDGGVS VNGATRHTNG
TNGHLSANGT NKTSKTDSGS SVDSEADDNM PTVLLTFAAA DEAGLQRQAM ALQRYLESHS
PHLGNQPDNV FLVDVAHTIS HRSAMAWRAF AVVTSEARVR KGLVDILSPA HHAVPSKTPN
LTFIFTGQGA QYARMGVGLM RYEVFRRSIH ECDEFLRSLG CGWSVIEELG ALPESSKINE
ANLSQPLCTA LQVAAVDLLR SWGIVPRSVC GHSSGEVAAA YCAGGLDRKS AWMIAYFRGV
VSGKVSSDAT QDKTTMMAVG LSRDAVRGYL SQGVSVACVN SPSNVTLSGP VTEIDAIAEA
LDKAQVFARK LSVKVAYHSR FMEVVAAEYH DLIRDISKPT SETTKGLGDG SSGIRFYSST
YGGRLETMSA LTQPAYWVKN LVSPVLFSDA MEAIVKDQPQ GVPMFFVEMG PQSALRRPIQ
ETMTQLTSKT PKGKWRYVCI LKKDAADERS ILETAGTLWA SGLAVRLDKL NQDAMRACRK
PKHVFDLPSY PFARPRELWE ESRLSRNFAM RQHRRHALLG VRERDWNSGE ASWRHLIRHQ
ENPWILDHAL NGSPLYPGSG MLVMAIEAAR QLASASADGR IRAYRLDNVR FLRSVDANDT
ERGSEAKIVL RPRRQTTNTG SQQFCYDWRV FGINNDDWIE CAHGAIQVEM DPQQGTEAEQ
VARSEARRAR LAASLTSQVR TVADKCRLMV HPSQLYKHMS ELSGFDYGPY FQCLSDISYD
RDGHATATLR LRDFASKMAY AAEDPCVIHP TTLDAICHLQ MVALSQGGWN AVPTMMFSHL
RKLWISHKLL TAEGNPRMRA ATQETMRAFR EAECRTMVML EGSEEPVVIL EGQRGTAITS
LASSGGTAAS GPELKQWLYG LDYKPDLSLL RSEDAQSYLA SIFRRDPRCS ASPKEKIDRA
DAIALHYIEL ALDSIDREAT PLQFDDHLGR YVQWMRRIRR QRSQWTLESR GLGQLNMEDV
LRDAESEPTQ RLTKKVGQHL HQILKGSENA LQVIFEGNLA DEFYHCDVFA TNNSKMGAYI
DILAHKNPKL RLLEVGAGTG SFTGRIMPYL APGEEGGAPV PVRFGEYIYT DVSAGFFEKA
RERFSFVGDH MKFQKLDLEQ TPASQGYDDG TYDVIVAGNV LHATRDLVQT LRYVKGLLRP
GGVLLLGEAV NLDNVRDGLI FGLLPGWWLR EGQWWSTDDE YKDQGPLLTE SQWDMVLREA
GFPGVQMVFR DHEEKPHHRV SIIVSARPDE EGLPEISSLT RPVRVNPYRI VFNPASPLQK
SIAETLQDYI AREITTGVVV LWAIGEAATL DTQQIQEEGV ISLLDLEHSV LESGCDVHFS
SIKTLCLGSR FVVWLTYGAA PEASNPWAEA AVGFGRSVCS ERGDQGFITL SVASRPGSPS
EAAPLVQHVL RVLCQLEAAR SPTAENESEF SEKNGVLCIP RFIPAPGMKD TLSERWGARK
PRTYRFGQDS DGGTSTSSKP RFRSSIQTPG LLDTLYFAED PNGCSELKDG EVEIEMKATS
MNFKDVMIAL GQIPGKSFGF DGAGVVSRVA RGSELRPGDA VLYCSSDGGG YGTFVRCPEL
QTEKLPEGMS FHVAAAIPAV WSTVVYSLDY IARLSAGETV LIHAAAGGVG QAAVQLAKLR
RAEVFVTVGS ESKRELVKEL YDVPDDRIFN SRNDSFAQEV LFATGGRGVD VLLNSLGGEL
LRQSWECIAP FGRFVDIGKA DIIANNMLPM GPFDKNVTFA AVDLVVVHKE GKALMKRILK
DVVRLFEENH SLHEPRPLHV FPPSRLEDAM RFLQGGKNTG KVVIDFTCDD AVEYQPLQRQ
ERYNFDADAT YVISGGLGGL GREITRWMVT RGARHFVLLS SRGPSDRPEA VKFLKELELS
SVKILAPACD VSDRTSLESV LTQAREQLPP IRGCIQSAMA LRDDMLANMS SSAFREALNP
KCAGSWNLHE LLPRDMDFFV LLSSFCGVMG NRGQSNYAAG NAFEDGLARH RVASNLKAVS
IDLVLVAEAG WAITNYDSVT LGLRASSNGL MQAQLMALMD MACDPSYDCN AFGAAQVVSM
VESPAELARL TREGLLDWIH KPMFSNLRRI GETDSDTADD SKARKDSPVD EVDRLAAIKV
APDLETATEI VRAGLVQKLA KSLSVSSDDM DVGKPAYIIG VDSLIAVEVR YWFMKQLHVE
VPVFEILKDR SITELCKHVA SKALHTS
//
