ID A0A423VXB5_9PEZI Unreviewed; 2589 AA.
AC A0A423VXB5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ROV95678.1};
GN ORFNames=VMCG_07565 {ECO:0000313|EMBL:ROV95678.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROV95678.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROV95678.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROV95678.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:ROV95678.1}.
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DR EMBL; LKEA01000035; ROV95678.1; -; Genomic_DNA.
DR STRING; 356882.A0A423VXB5; -.
DR Proteomes; UP000283895; 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: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; 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; 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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
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; 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; PF08242; Methyltransf_12; 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 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:UP000283895};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..435
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2505..2582
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2589 AA; 282076 MW; 034686D0D554ABC2 CRC64;
MAETYGDATM PIAIVGVSGR FPGDASSPDR LWELISEGRS ALTEVPKERY NIDAFYHPSA
EHQGSQNARG GYFIKEDVAT FDAPFFRITA QEAHAMDPSQ RLALELSYEA MENAGVPMES
MAGSQTGCYM ATCLRDYANL RATDPHEYPR YEANGSMGTA MISNRISWFF DLKGPSLSLD
TACSSSLVAL HLAVQSIRSG ETTQALVGAT NLILMPDTSN HLSTLTFLSP DGKSKAFDAN
ANGYARGEGV CVLLVKSLAK ALEDGDSIRA VIRGTAVNQD GRTPGINLPS TTAQETLIRT
AYKDAGLDFS GTGYFEAHGT GTAAGDPLET AAVGRVFADS RKSDQPLYIG SIKTNIGHLE
GGAGLAGLVK AMYILEKGKI PPNLWLQKVN PKIDLEAWKL AIPTSLTSWP TSGLRRISVN
SFGYGGTNAH CILDDAHTYL TSHGLTGRHN TVLTRAISEH SEPTTPSTPS TTANFSEADI
ASSARDSRLS EITNMSDYVE LTTPQLLIWS SHEQNGINRM AESIASYLSK HHSGPDPNLL
KRLAYTLSNR RSRLDWTSFA IANTIPSAIA SLATPAKPIR PAAEAPSALF IFTGQGAQWA
GMGRELMVYT TFKQRMDEAT AHLKSLGCTW DLIEEINGPR VNEPQVSQPA CTALQVALVD
LVAEWGVKPA ITVGHSSGEI AAAYAKGALS REAAWTVAYH RGRLSAGLKA GGLELGMLAV
ALGEEETQEY IDQVKAEHKP VVACVNSPVS VTVSGSAEGL QEVQDLIGSR AMNRRLVVKT
AYHSPFMQEL AQPYLESLSG IEDQKGEYGY SAKMFSSVTA GEITDEALRQ PQYWVDNMTC
PVKFRHAVDA ALSYASSAAL PLVLVECGPH GALKGPCQQI MTAHPTAEPT KIPYANFLTR
KENAITTTLT AAGSLFQHGM PVKIAVANSR TSVPEDLTQL VDMPSFAWNH NTRFWYETPR
TQAYRLRADA RHDLLGTLDE SCPDTTGEPV WKNYLRVAEV PWLKYNQLQG QAILSFSGML
ALVLEGVRRT SDPLKSIVGY QFRDVFPGPP LVLDEVDSSS VETRLTMRAW RAGSRSLTTY
WREFSLSSRN RQGAWTQHST GLVQIQYAAL DDSTKEALMK EWEGVQAENC RERNVEEFYE
TFSELGMQWS QAYQSLQTAK ISASRRAITG SIQIQDTAAI MPDNFESKHP VHPTTLEGAF
QLLSACDGGS GDKIRVPKYI ESIYVSASIS PLSPGTVLNA FGKINEKWAD GTNSTLVVSD
TSASEPLLVF EGFKTVDLET ENGADTASAE ATAQALTKLG AFPAWGLDVE NSPVEAVKTV
LRKAWTEGSN ADYESIHDLE WAAYILCKRA VQKFTPEDAQ TMAKHHQVFF RYMTRQVALA
QDPATPLPCQ KPDWLSADEA TEDEVLSRAA ATSLEGRMMV RILDNLGAIL KGEVEPWELM
NGDGLLEDMY RSGLSDEKTP ATQCEFISLL SHKRPLRILE VGAGTGSATS KILKKLGRAN
VQKYTYTDIS AAFFPQAAEE FKEWAANGVM DFKVFNAEQD PQAQGIDIGS YDLVVAFQVL
HATSKMDETI ANCRKLLTPG GHLVVTELTS KVARRSAVFG VLAGWWLGED DGRMNGPEML
EDEWDLRLKR NGFSGVEWCF RDREDEGWSS SVMASRATIE QEESSAPSKA IIVTTQTPSP
LVQELSEKLS ASGMEIQQKS LGEISTIERD ELAATKCIVA MELDQPLFSR ITSEEFDTVK
HIILTAHSTV WLTCGGASLD CKNPEDAMFT GLARSIRGEV PGIKLMTVDL DSDSSNSESV
DNILRVVKLQ DEESNSEHEF VERKSGLYNV RVMPDERLSK LLSSAVQKPD TIADEEIPTP
QPIKQDDRPL KMELRKTGDL ESFVFRDDDG TSAPLGDDEV EIEVKAVGLD PYDMAIAVGQ
IWDTHLGLEC SGVVTRVGGE VLDVSVGDRV VTFGISTNWY KTYFRSHRDI VQKLPEDMSF
EDGAGIMRSY GAVKYALVDA ARLEADESVL IHDATTALGM AAVNIAQHIG AEVFATVAGE
AERSLLIEKC GVPHNRVFSV AEFAQGIKRA TQHRGVDVVL NGSMTGENLR QTWHCIAPFG
RFIELGMKDI RSNTGLDMVP FAANATFVGV NMKCMLFSKP KLFKRIMSDT LQYLSERIIK
PAPLHALKLS EVAEAFRILQ SKSKLEGGRV VLKDEDSDVV PVIGEKPKQP LQLLSDATYF
VPGGLGGLGR PLLRWMADKG ARYFVTTSRS GAKDPKATAL IDELSEKGVQ IKVFACDISE
EASLESVLSD LSTSDFPPIK GTIICSMSVQ DTFFETMTHN DFVAATRPKY NVSHNLHRLL
PDNLDFFICI SSAAGQIGSI AQGNYNAGNN YQDALCAHRR SLGLAGTSIN LGWMGEIGFV
AESDRAKVPQ VVRDGVRDLK ASQFFAIVEA AMRDEEVSKN QPVLGLASGG LIKHAGRDEP
YWFGDARFAA MRVYDTHQSK SDGPAQSENA ADVKTALASV KSIEEANRVV LAGLMAKLAK
GLMMDLGDLD ASRPINTYGV DSLVAVDIRA WAMKEAQSVV HVSEILKSMP MADLAGKIAE
ASKLVAGLK
//
