ID R1GRD1_BOTPV Unreviewed; 2371 AA.
AC R1GRD1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Putative polyketide synthase protein {ECO:0000313|EMBL:EOD48494.1};
GN ORFNames=UCRNP2_4817 {ECO:0000313|EMBL:EOD48494.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD48494.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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DR EMBL; KB916202; EOD48494.1; -; Genomic_DNA.
DR RefSeq; XP_007584097.1; XM_007584035.1.
DR STRING; 1287680.R1GRD1; -.
DR KEGG; npa:UCRNP2_4817; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_1_1; -.
DR OMA; KDVQHYT; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion 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; 3.30.70.3290; -; 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; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR013154; ADH-like_N.
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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF18; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 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; 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; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..445
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2287..2364
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 51..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2371 AA; 254203 MW; CD2B873A084EBF00 CRC64;
MSVQAEAGPH PASKQYVQEP VAVVGMACRL PGDSNSPRAL WEFLQKGGVA GTEPPSTRFS
LKGHHDSSDK PTTLRNPGGM FLEGVDPADF DAGFFNISRT DAVSMDPQQR QLLEVVYEGL
ENAGIPIETL SGAPYGCFVG SYESDYAWMH ARDPQNRPPS CAIGVGRSIL SNRISHFLNI
KGPSLTLDTA CSGSLVGVDV ACRYLQTGEI SGAIVAGANL YLNPDHSIEN GALRNAHSAS
GRCHTFDSKA DGYIKAEAIN AVVLKRLADA VRDGDPIRAV IRGTANNHNG RTPGIASPSS
EDQAAAIRAA YRNAAITDYS LTSYLECHGT GTNAGDPIEV KGIASVFAES RAADKPLVVG
SVKSNIGHSE PAAGISGLLK AILTIEQGII PGNPTFERPN PAIDFEALRV RPTRTAIPFP
RAPFRRASVN SFGFGGSNCH AILDEPKALI KDFAPAHTSS FKSTEDDEDD FFSDDEAASR
PYVLLFSAND ESSLKAYTKE MSKHLSNLAV KADLRDLAYT LSERRSHHFN RGYVIARKSE
LDENAIVLGK KEASTPKIGF VFTGQGAQWP RMGKEVFETF PGTAQVVKEL DTVLRSLPTP
PDWSLYEELT APRSSEHLRQ PEFSQPLVTA LQLALLSVLS GWGIRPQSVV GHSSGEIAAA
YAAGFLTQAD AIVVAYHRGL AAKHRQHDGE ASLGMLAVGI GKADIGPYLD GLESVHIACY
NSPKSLTLSG VVSNLEQVRA RLTQDGHFAR MLQVNLAYHS TFMDEIGKEY ESLLLRDFHG
QSCKPGPFGD VTMFSSVYGH ALAEDQTTDV GYWKSNMVSP VRFDDAFREM TAGKDGANFV
IEIGPSGALA GPIGQIKDSL ESGSAIQYCT ALKRGAESVG ATLDVAGKLF LKGVPVRMDR
VNADEEHGRP LVITDLPNYS WNHSTKYWYE CSESKEWRYK QFPSHDLLGS KVLGTPWRSP
SFKRILKLAE VPWLRDHCVG SDIVMPAAGF VAMAVEAMFQ TYCSLRPDGG VRSVEELCYR
LRNIKFDKAL VVEEDVPAEY MLTLNPLAGT KDSWHEFKVS SNKEGVMMDH VGGLILATTE
EIAPLKHTSP GHLWYKISSE VGYAFGPAFQ KQVLVEAVAG QRNSRSHISF TEPPSAYTPQ
SPYSIHPAVL DGCFQSATPS IWAGGRSTMN AVLIPAIIDD LVINPVSAQQ RPELGVAVAR
AEYSGRGRPE IAKNYKSSCA VYHPQTGALL VQMTNLSCHQ LDVGADLFSK HTFMQSVFTP
DLSRIRTQEQ AQGLSCTGVQ DVLDIAAHKK PALAVLEINV AVGDASCLWF EGRERANRLT
YSKYAFMASD ARDLVSVQNE SSSERSAAFS LLDATKSDLG TGAADFDFVI IKTRPALVEA
TAQVLRAASS VLADAGRVLV VEQVEQTLSR SSDIVIVEKE DIGAESRLQT TIFDSGFGSA
VRLSCGDQVR AVYLCAPASE TAAVNEPQEL YVVHLTSTSR LGEGLRAALA STGWRIKEQA
CPSVDVPAKS AVLILDELYS SVLSTVTPAQ WQIIKDITTR GCRLLWVTQG AHLHIASPER
AMANGLFRTI CAEDPSAHCT TLDVEQAEGA ATSSAIVDIL STLRKPRPKT AVEAEFFQRD
GVLHVNRILP DAAVNAAKAG AAAEPVPQRL HDAQSIVRMR AERIGTFDAL QYSAITPAEQ
PVAPGCVEIE LFAAGLNYKD LVVTMGVVPE NEHLLGLEGA GLVRRVGAGV KGFSVGDRVA
TIEKGLLANR IQAPVKRVVP IPEAMTYEEA ATMPVVFATS VYSIFDIGAL KKGQSILIHS
AAGGVGIACI QLAKYIGAEI YVTVGSEAKR QFLQEKFGIP PARMFSSRDP SFGPAILEAT
GGKGIDLIIN SLTGDLLDAS WRICADGGTM VEIGKRDIVE RNFLSMEPFD RNCSFRAVDI
SYSKHITDDV LLTKVFDLVK KGAIGPIQPI TTFSFSQIPE AFAYMRSGRH VGKIVISDGP
SGNVEVPVRP FAHDARLRGD VAYLIVGGLK GLCGSLAIHM ARRGAKHIVS MSRSGCSDGR
SQAVVVNCNS LGCKVYEAKG DVGNPEDVHT AFAVAPVPIG GVIQGSMVLR DKPYEDMSVQ
EYHDCIACKV SGTWNLHKAS LSLPAPLSFF TLLSSVSGVV GNKGQANYAA ANTFLDSFAA
YRHSLGLAAN SVNLGVIQDV GYVAEQGGME THLGSSQWTG IAENALHVVL DTSIAQQQHA
INPASVSQLV TGIALPQSPA DSDLTRDARF AGLFLPSNSS GGSSGKNTAD AAVQAFLALH
ASGASPDTVL PVVLDVINAQ LTKTLRLSEA LEPGKPLSVY GLDSLSAVEI RNWIRMELGA
EITTLEIIGA ASLVALAEKV VAKLPVVSGN E
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