ID A0A423XCJ6_9PEZI Unreviewed; 2590 AA.
AC A0A423XCJ6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ROW13683.1};
GN ORFNames=VPNG_04575 {ECO:0000313|EMBL:ROW13683.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW13683.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROW13683.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROW13683.1,
RC ECO:0000313|Proteomes:UP000285146};
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:ROW13683.1}.
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DR EMBL; LKEB01000018; ROW13683.1; -; Genomic_DNA.
DR STRING; 1230097.A0A423XCJ6; -.
DR InParanoid; A0A423XCJ6; -.
DR Proteomes; UP000285146; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 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 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; 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; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000285146};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..426
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2504..2581
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2590 AA; 283401 MW; 4D2E72A2F3068732 CRC64;
MDEPIAIIGL DARLPGDGDT AENFYESLLA GRSARTEIPS DRFNVDSFWH PDGERSGSTR
ARHAHFLKGS IAAFDAPFFS ITPAEANGMD PQQRGMLESV YKALENAGVP VSKAAGTQTG
VYVGCFAYDY NDIIVKDLDI PSKYAATGTV ASMLSNRVSW FFDFRGPSIT VDTACSSSLV
AAHEACMSLK LREINMAVVG GCNLMLSPEM ALKLDAAGVL GPDGKSYSFD HRGNGYARGE
GFGTLVLKRV SDAVRDGDVI RAVIRNSSTN QDGRSPGITQ PTKAGQAALI RHVYNRAGLD
PSLTRFFEAH GTGTQVGDPI EASAIAEIFA PHRSPGEPLY VGALKSNVGH LEGAAGVAAI
IKGVFTLERG VIPPNIWLEK VNPKIQDSWH LRFPTEATPW PQEGLRRMSI NSFGIGGSNA
HVVMDDAAHF LQQYRLVGEH RTLARPVGSN TRENNPHING VNGVDCVNGA NGHLNGRHRR
TDSGIDLSED DEIAPAQLFV LSAYDQDGVS RVRDSYHEYL STSSEDFSDA TEGTRFLRDL
SHTLASKRTH HAWRAFAIAQ SPRALKDGLS EIPKPTRTKS EPRLAWVFTG QGAQWPAMGV
ELMVYPVFRQ SILAADRYLN DLGCLWSLSY ELSKGGGSSR IDDPEFCQPI CTALQIALVD
LLASWNVFPH AVTGHSSGEV AAAYATGAIS RESAWKVAYY RGKLSSKLIR SGTLPRTSMA
AVGLDFKATK AAIERVDQMG GQGSLDIACM NSWQSHTVSG DAEKIDTLVE LLSAEKVFAR
RLNVEIAYHS QYMKAMADEY LESMGDLQPG VRQAASEATF FSSTRGALIP LSELREPSYW
VANLVSPVRF CESATAMLKG SVDEPKANGY HKDGPDSPSS SPITDVLEIG PHSALKGPLA
NIAKQLPGGG SVTYHSLLKR KSSAVQTVLE AAGSLFCQGY DINLAAVNDA ASPASHKPRM
LIDLPSYPFN HSKEYWIEGR LSKNFRLRAA GRHELLGAPA PDWNRHNAIW RNYIRLSESP
WIEDHKVAGD VLYPAAGMLV MAIEASRQVA DKDKALRGFR LKDVSFHAAL RVPDDAQGVE
SHFYLRPYRE ASLPGKSEWD EFQLWTFDND EWREHCRGLV QTEYAEEQRS DDQQLLEDCR
HVLQEARVSC TTEVAAEKLY RNFQESGLDF GTTFRTLRGV RTGADLTLLA EVNSPLPKIR
EAMPSHYIQP HLVHPAMLDG IVHANLAPLV LGSRRAQQPR VPVFAKEFWV SASPIADDDA
YIVSAQSSRC GRTETESSVT AVDRETGAPM AYASGLVFKT LPGGAPQDTA SSLHDAFNVE
WKPDPTLLSE SQAAKVFGLP MSAEDNPSSW MEDCEDLCLA YIRRFLESVT NDRIEKMEEH
HMKYVTWMEH VSRSNTRELA GNIEELEAKV KSRDTPEGVL IIAVGQALEE MLGGPLNPLD
VIFRDKIAEN VYRYGLGSQR CYEQLCNYMD ALAHKNPAMQ ILEIGAGTGG ATRPVMQTLT
RQGRRYQEYC FTDISPAFFE QAREIFSDDL GNMDFRVLNV ENDPVDQGFE ETKYDLVIAA
NVLHATKKIE ASLSNVRRLL KPGGKLLLFE ITNIEVLLSH FCFGVLPGWW LSEDKDRRWG
PLMSTSSWDH HLSQSGFTGV DAAFQDFPGS EHQMSSILLS TVPEEQETAE TTAEYIVIDN
LSAQEDDVAS RIASALSKNT STSEIVPLEG LGARDLQHTT CIVLLELQSP LLLDMTESVF
ASIKRLTSQC KSLLWVTRGG NASAPDPNTE LVSGLARVAR SERPGFKFVT VSFEQSESQS
SVVDKCVQTV LTTRNGNENS FRVADGITQI PRLVKAEYLT EHIRSQTASL EPVQQQLGED
TSRALTLQVG LPGQPDSLRF EDDILHGTPL VNDEVEFKAM ACGLNTVDVA SALGKTEDSP
VGIEAAGIVT RIGPTSTYQV GDNVFGLSLT GTVKTQVRSA DGFLAKKPDS LSWAEAASIP
VAYTTAYAIL HEHGTTRKGD TVLVHSAATA LGQAAVQLAQ LAGAEVFATV EDDDQRHFLE
TAYAVPRDHV FLTRHGGVVN GIKRITQQRG VDIALNLIGG ELLTETLSCV APFGRVVDIR
SGDEGSESRV SLSDLQRNNI RYETFDLKFR ALNDPVRTQR TFQGAVEQLR LRGPDLTIRR
TPISSHTFSE LHNVLRQLQS GSRIEKLVLE PHDEDEVSVL PQREPAHRFD HEASYVIAGG
LGGLGRSVAR WLASRGAKNL ILLSRRGPVQ AAAKELVKEL EATCERVATP ACDVTDSASL
REVIDECSKT MPPIRGCIQG SMVLKDNRLE DMTLEEWNDA LHPKVSASRN LFDNLGRDLD
FFILLSSTVG ITGGPEQANY AAGNTFQDAL ARHLATEGVH AVSLDLPIIR GVGYVEERPE
LLDHLRAMGW AFMEEDEFHA TLDYHCRPPN DEPTPIARSQ VLPRFWLPQQ TAAEGRELPS
WRLDPLFGNL AVSSATNDTA GSNAGTAKAV NYAVLLAAAK SPEEIVELTL EAFLLKVSRV
LSVEVSNLDA ANPLHAYGVD SLVAVELRSW LAKELKAEVS VFDMTNAASI LQVASMAAAR
SKLVVNIDAE
//
