ID M7SK55_EUTLA Unreviewed; 2595 AA.
AC M7SK55;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative polyketide synthase protein {ECO:0000313|EMBL:EMR64557.1};
GN ORFNames=UCREL1_8471 {ECO:0000313|EMBL:EMR64557.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR64557.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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DR EMBL; KB707045; EMR64557.1; -; Genomic_DNA.
DR RefSeq; XP_007796340.1; XM_007798149.1.
DR STRING; 1287681.M7SK55; -.
DR KEGG; ela:UCREL1_8471; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000012174; 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: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; 3.30.70.3290; -; 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; 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; 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: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; 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; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..427
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2506..2588
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 442..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2595 AA; 282197 MW; EE333F546CECF467 CRC64;
MLPGDDVAVV GFSYRLPQDV NDDAAFWDVL QSRRNLMTSW PESRLNLESF TNKKQQKING
PGGHFVTDDV AAFDAPFFSV TAKEAASMDP LQRWSLEAAY RAFEKAGIAT ASLRGSRTAV
FSASMIEDFA RMSAIDPENV ERTAATGNVV SCVIPNRVSW YFDLRGPSVH VNTACSSSLT
AVDMACKVLK CGDASCALVL GSNLLLDPAV SQMLSTANFL SPNSLCHSFD DRADGYARGE
GVVAIVLKPV SAAVRDGDMI RAVIRSTASN QDGQTPILAQ PSPQAQEDLI RHVYSQANLP
LDQTRYFEAH GTGTPVGDPI ETKAIGRVFR KYRSADEPLY IGSVKANIGH LEGASALASI
VKCIMILEKG IITPNALFEN INPAIDADFY NIAVPTQCVE WPGMGLRRVS VNSFGFGGSN
THVVLDDALH YLHDRGLSGN HCTSRLPRPT TNGTNRTTHA NGATNGVNGY TNGVDKAIAN
GSTPALPLDT GTKPPTLLVW TAADEKAVAR MIAAYETYYK DRVLGHPDKL ESLAFTLAAR
RSCMLWRTFA VVAGDDGPLP KEGEKALFPA KPTRSSAFGD LGLAFVFTGQ GAQYVDMGWD
LVQFPVFAET LRRIDDIYRG FGCGWSVFDE LRNKDNIDKP EYSQPLSTAV QIALLELLKT
FGVVPKAVVG HSSGEIAAAY TAGALDLSSA CKVSYYRGQL AGKLRAANTS SPGAMLSVNL
AENQVPAYLE AVPGDTTSVG VACINSPGNC TLSGPEAAID ALKAQADKEG MFAVKVKTGV
AYHSVSMLEI ADEYRSLMGT LEGAARKADA KAPAAICPMV SSVTGKPIRL PELAKAQYWV
DNMVSTVRFA DAVQVLTQKS STIKIGLGNI TDLVEVGPHP ALKRPVQDTV GQEGNKKKVR
YANTLHRSQP AAQAVLELVG RLFCHGYDVS VAGANQHSTK KDNASAFLVD CPEYPFDHSN
RYWTESRISR DYRLRGTVHG ESLGQRVSDW NPLEPRWRNF LSVESTPWIG DHVISDTVLF
PAAGMLVMAI EAVQQMVPSE MSVAGYLVKK AEFLNPIVVQ QAWEDRTETQ VRLQPGKSGF
DVTIFSYSRD RWTECCRARI QVEYGGPGKE EAAAATARLA DHQDISHRYD VAMTSCRRPL
DSNAWYREEA ELGLRYGESF HLLQDIAWDG ATTAVTRVDM SKARYQLNSL VHPAVLDTLF
HALRVSAGQQ PVTNVPVRLH DAWFASSGWQ HPHTASIRWL AVSNYVSIPG HYGEQGSVFA
LGDDGKVLCV IQKAVTATIS VETKKQEKKL LYNIEWKPQI SMLNPQQLAD MCDADVFSRD
QTAVVQKFTE IYRILELVVA RVLKGVDPAK VPRVLVRHVE WMQCVTDKLP RSQVQEAETI
SDAELETKLK RVESLVPSWE LYTLCARKLL AILAGELDPL QVVFGSGLAD VFYEDLFVSL
CADGRFGTFL DLASHENPAL RILEVGAGTG GMTGHFISIM EAREKRTGAP AFAEYTYSDI
SPMFFERAHA RWPHLEAQGR MLFKTLDLDR PVADQGFEPE SYDMVVAASV LHAAADLEAN
IRHVRRALKP GGRLVLLEAI NPNTVATNFM AGLLPGWWIA NETWRPHSPA ISESMWDTYL
KKNGFSGNDL IIRDYHQEEI RMMSIIITTA VGENELTPRS PVKGPGRVLL VVDEDQSEIA
SAIQSRISAI NSPIVSSCNF TTDSLSEAVV GMTVNDIVIS LVEVDNKPLL SNLSAEKLQC
LQQLMKKASN ILWASSADRS DPQYPDHAVM QGFFRSLRAE QPASHLVSVF IEEKADIPRY
SDLIVDVFKA SFISTESPSS QEVDYIVRDG VMTTGRAVEN VSGNATLRSL LSQQLQQRPW
SEGPAVQLSA GTRSSLDSLQ FIRDETHKTD LGTSEIEIEA SAWGLSNIDV QVALGNVDGV
QNKFGSDCVG VITRFSRDCK SSNIQPGDRV YMIGRGCMRK FPRAPETSVV KLPASIPLEI
ALSTLVPAMT ALHALINIAR LEDGDTVLVH SAASSTGQVA ARIAQMYGAE VFTTASAENK
QFVVDELGIS QDRVFDNQTT SFARDILRAT GGQGVDIVFN LLPGEDALQA SCSCLARNGR
FVEVGRNNIE ADGTAALPMT VFAKNITFAA VDVMQLSPKV TSRLLAKAVQ LLEEGKVQSP
QPMRVFKVSE IGQAFKELRS SETVERAVIV PNPDDVVPQL LQERRSWQFN EDASYLISGG
SGGLGRAILK WMAERGAKHL IVPSRSGATS KAAVSLVAEL SALGVKVFAP KCDVSSEQDL
ANVLSECTRR GMPPIKGCIN AAMVLQDAIF QDSMTFAQWE LTMRSKVQTS RNLHRLLPED
LDFFIMLSSL AGVIGQMASA NYAGGCAYQD ALVRHRLSRG QRAFSLDIGW MRNVGIIAEN
SAYQRQRVSW NDMQPIDDVD LLALLTMCCD PSVPAPVPAE SQGQILFGLR TPADLLAQGK
EPPALLLDKP LLAAFSFLPD AGVNASRAVG GGDELAAAAS SFRRSSDSSE RIQIVLRALA
AKLARAMGTI TADDVEPGRP LSAYGVDSLM AVELRNWFGR EFGASVAVFD IMGGAPISAI
AYLIVERSTL GKASP
//
