ID A0A423X2H7_9PEZI Unreviewed; 1075 AA.
AC A0A423X2H7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Polyketide synthase phosphopantetheine-binding domain-containing protein {ECO:0000259|SMART:SM00823};
GN ORFNames=VMCG_02037 {ECO:0000313|EMBL:ROW10094.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW10094.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROW10094.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROW10094.1,
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:ROW10094.1}.
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DR EMBL; LKEA01000003; ROW10094.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423X2H7; -.
DR STRING; 356882.A0A423X2H7; -.
DR Proteomes; UP000283895; Unassembled WGS sequence.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000283895}.
FT DOMAIN 571..644
FT /note="Polyketide synthase phosphopantetheine-binding"
FT /evidence="ECO:0000259|SMART:SM00823"
SQ SEQUENCE 1075 AA; 117138 MW; C9B47B7C6A71EDE7 CRC64;
MATDLHHQGP KLWPQLVDQL ARERPNTAYG LWPVASDSYE AGFHTITYGH LANIVNGLAW
WIVKELGAGQ GSQHEVLTYI GPNDVRLTAM ILASVKAGYA LFLTSPRNSP AAQRSLFEAL
KCRTLVTSDS KLPPVLPILE IVKPRCLTIP TLDELLEESF PLFAYDKAFE AGRWDPLFIL
HTSGSTGLPK PLVWTQESAV RHYASASQEV PAQQDVTSVE HLISGKRVVV TVPSFHGAGI
LQYMVWAIRA GCIPIAPAAV GIVTAHGLAD ALKHTPAEVA ILVPSVVADL AQNPDQLAYC
ASHLSLILYI GGDLPQAIGD VVAAKIPLRC WWGASEVGIP HQLIPRGLGP NDWRYIRFHS
SVGAVFDPVS DGTYELVIRK DKALAQTSFS IRGQEHLAEY RTKDLFQPHP TVADAWSWRA
RSDDIIVFLN GEKTNPVSME QHVVARNPEL SGALVIGTQR FQAALLIDPV ALNERGPLTT
SEQAALIERV WPSVQEANAV APAHARVEKS LILVVDRPLI RAGKGTIQRA TSIQQYTSQI
ESLYTHADVA VDDENSPDEP QVNLNDTESV TRFVRESVCA VTDWPYSHQA FSTGTFFEHG
MDSLMALRLI RLLRRGLHRP DLGLSTIYSN PSVDQLSTAL LAQRDERKDD DALLMKPWLD
TYRALIEQIP KPKDIHAVQK PSGASVTALL TGSTGTVGTF LLRALLDRPG IGRIYCLNRS
EDGGYAAQKL RMTERGLSVA DLDDRVTFLP ADLSQPLLGL DEKKYKELSD HVGIIIHNAW
PVNFNLRLSA FQPQLAGLVN LFRLSTAASS GHPASLIFVS SVSAVGTGGS AAGKRPIPEQ
VPTLGDAPNT NGYARSKFLS ELLCDTAAQK LGIPATIARV GQVAGAVRQP GGEWNRKEWF
PSLVIGSLSM GCLPNDLGTQ FSEIDWLPAD LLADVLVDLV QDQLSSEPEE SGSACVYNLR
NPHTTTWESL MPSVIDAAST LLGPDRVPRV VSPSSWLEKL DDAASKETGD GAIANPAVKL
VEFYRDYLWG EGEQGAGQDT PPMSVEKTYA HSPTLRGLQA VTAQWVQKWM GEWIS
//