ID A0A2S6C5L2_9PEZI Unreviewed; 2483 AA.
AC A0A2S6C5L2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PPJ55018.1};
GN ORFNames=CBER1_01452 {ECO:0000313|EMBL:PPJ55018.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ55018.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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:PPJ55018.1}.
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DR EMBL; PNEN01000549; PPJ55018.1; -; Genomic_DNA.
DR STRING; 357750.A0A2S6C5L2; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000237631; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; -; 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; 3.
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; 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; 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:SF50; HIGHLY REDUCING POLYKETIDE SYNTHASE SRDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; 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; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000237631};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 30..458
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2405..2483
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2483 AA; 271282 MW; E74F12C1F65A67EA CRC64;
MAQKVSTNEA LRVSPNAQTS SPQPLQDAGP QAIAIIGMGC RFPGDSNTPD ELWSMLLEKR
NGFSRPPPSR FNIDGFHSKK RRPGSIRPEG ACFVSDTIHD FDSPFFGITK SEAEAMDPQQ
RKLLETVYEA LEQGGITLEG VSGSKTGVYV GNFNYDYGVQ NLRDADYPRD YSMTGQGVTI
LANRISYVFN LTGPSVTLDT ACSSSMYATH MACRALSSGE IDGAIIGGTN LIQSIENHMS
TDMMGVLSPT SHSHTFDASA DGYGRGEGVG AIYVKRLSDA LRDGDPIRGL IRGTAVNSCG
RTSGITQPSA TSQSAVIRDA YTFAKISNLD ETGYFETHGT GTAVGDPIEL HGIADVFASS
KGQRRRHPLL LGGVKPNVGH AEAASAIASI LKAAYILEKG TIPATIGIRK LNSQLDFRGG
ELEVVQENRH WPTEHEIRRA SVNSFGYGGA NGHAIIEAVS SVLPGYQSFK TRETSRQNVT
TEKITGTMGS GEFTFSTKER TQFLLPFSAH DLDSLRANIA ATRDVADQYD TEDLAYTLAA
RRSRFAHRGY AVVNETSTAH DLEEQAISIG KRGHGGNIIF VFNGQGTQSA QMGKDLMQDF
PSYLHTIREL DKVLKSLEKD APPWSLETEL LKAETASRVQ EAQLSQPLCT AVQIALVDLL
DSWNLRPKAT VGHSSGEIAA AYAAGTISRS EAIVFAYFRG VAVVDGNDKG QMIAVGLGAE
ECEPYLEDGV VIACYNSPNS VTLSGGADAV AHVQAKLESD NIFTRAINTG GRAYHSHHMG
EPAISYLDNL QHALKLTGST AQRSGKLAHA AIFSSSVYGT VMETGFHPGP EYWTKNLKSP
VRFSQALHAL LSSANHKLDT IVEIGPHCAL ASPIRQLRDK LDRKHEELAY LASLVRGHNS
TLKILDLAGA LFIRGHDIDL AAVNSIERMV DGTLKRFAGK PLVDLPPYKW NYENGRNLRL
KNRFTEEHRL RHFPRHDLLG SKITGGIRDR PQWRNLLDTK DLPWLEQHKL SVQPVFPAMG
YIAIAVEAAR QFFSEFLIFR NRFRYVFPQI TIKAALNLPT AGTHVEVLTS MQFQQISDST
ASKETAVFSI HSCSNGVWTE HATGKVKIER GEPMQPLFEE AKLQEPKAAH TWYRGFSNVD
LNYGAPFRGL SDIRSDPWEN EVTALTKLLP AGIDQDDSRY LVHPATMDVC IQAALIAAHH
GSLKDLRQSF IPVSMDNLVI WNYNGRDIPA LQPADGRILA VGSKSGERKL VGTMQLFDSE
ARPLFAIDRI NCVTYAEKLT SDTQPDSHPH LRVVWKPDVD HPNAFATPTR APQALLRMWA
GSLVSTAKTR PTQPIAKAIL EALPGSYASQ VVQEPSLDFG SEGMGEEMLE LESLVLSTFQ
HLGNDYQPPN DGVMPETFQK ALDLVTHKRP NLDILLLVDG NNTDIFRTLE STLKSRSSLK
RYRTLDIVVT NGKANPSLVR SLADFRQVQF TESNIFAFPD EMATAYDLIV IAQPPSYLQK
PIILNEFLND MKRHLKERGR LLIAEGHDLD ADTGHILDTI ASGLGESFSS QPFDNWSEAI
QKQDFDVRFA ESQPTGWTLL TAEVSSQQQT ADLILLSRQE DCNVTEVFHK GLKKAGFQIS
RASLASQKFV AKDNATYVSI VEFGDSLLDT LDPVEFGNLQ AIANKAGTVV WTTTGNLLGE
TNARAAAILG LARTLQNENV ALRFYTIDLD HKNAKLGACQ VAYLLHSIDA EDAAGDNEFV
VKNGAYYVSR LSEDVTLDAE VQKKTSNKLT KKSLTAESPV RLAIERVGAF DTLHFVADDR
DPSLKIGQVE VAVKSVGLSM KDIAKFQRDP DFESHCYEGT GIVRRVAPGV TKVAVGDCVT
WIGKGAFADV ERFDAIHVHK LSHTDKLEVV AAMPLAFATC VYGLMHRGRL RWRERVLIHS
ATDGVGLAAI QVAKMVGAEI FATVATEKQK AFLMKHYGFD NAHVFSSVDN GFASEIMGTT
KGYGIDVCLS SLEGELLHAS WGLMAVDGRY VNFESHHSLD HGSLDFEVFK RSATFTAFDL
GALAEERPHV LAGVMQEVLQ YFREGKIKPL HPTYTCSAGD IDVAFQQASH GDNIGKLVVN
FDSQMLKVKE NPEGVKFRSD GTYLLVGCLG GLGRCLSRWM VEKGARNLTF LGRSGASSKA
AAQFVCQLQA RGVTVNVIKG DVSSKADVAR AVTSAAVPVL GVVQGAMALQ DFRFDKLNLD
QWNAAIRPKI HGTLNLHEAL FGQPLEFFVM LSSIAATTGN ATQSNYCAGN AFMDFFARHR
KQQGLPATTI ALTMVQEIGF VSQDEKLEQG LAHTGLVAIN EKEFIDLMET AMLPQPKPTW
SGDDNATALL ISGLDPAKIS PDVLTSGNRF WHQPRLGPLT VALEEKLAES SGGNDTEPAP
GHDLPSLLEA VQGYLAKTFG VPTQDVDELK PLNDFGMDSM IGIALRNWVF ATYDVKIPTS
EIMGVTLSAR TLAEQIHDGL QAS
//
