ID   A0A1J9R0I2_9PEZI        Unreviewed;      1074 AA.
AC   A0A1J9R0I2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Thioester reductase domain-containing protein {ECO:0000313|EMBL:OJD34105.1};
GN   ORFNames=BKCO1_2500091 {ECO:0000313|EMBL:OJD34105.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD34105.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD34105.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD34105.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family.
CC       {ECO:0000256|ARBA:ARBA00029454}.
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:OJD34105.1}.
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DR   EMBL; MNUE01000025; OJD34105.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9R0I2; -.
DR   STRING; 236234.A0A1J9R0I2; -.
DR   OrthoDB; 2230730at2759; -.
DR   Proteomes; UP000183809; Unassembled WGS sequence.
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; 2.
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; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
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; 2.
DR   Pfam; PF00550; PP-binding; 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.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183809}.
FT   DOMAIN          563..645
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          673..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1074 AA;  116228 MW;  51FE0C8AC696CE9F CRC64;
     MPTTPDYGHR LIIPLIEQKA HTNPTGIYCT LPATLSPSSP QPTVLTWRTL AHSIDKTAWW
     LDRTLGAPPR GTHPTLAFIG LNGPLYYIVL LACAKVGYKL LLPSTRNSID AQLHLLDATG
     CDVLLRGPRS NLVQGILDAR GTVRCVTVPV EGLLGGEEEG GEEVERYPYE RTWEEGRDEP
     LVVLHSSGST GPPKPIVVTN RSMASLDAHH LVEDPAEGVR DVLRASEGST VFNPMPCFHA
     AGLMWNLFAA VYFDIHVVYA PMGEPLNAGL VEKALDSDQL RFDWMFLPPS VIEDVALEQR
     MLPKLEKLRF VCFSGGPLSQ DLGDVISKHT PVVNLLGTTE NALPPYNFVP LKEWNWILVP
     PQMKGIEMRA REEDDFAELV IVRDADTDAF HSTFSTFPND NEYHTKDLFA HHPTEPNMWQ
     HRARSDDVLV LSNGEKVVPI PMEGQLAQCP SVSGVVVLGH GRFETAALVE LSDKAQQENT
     PGENLAAITT FIDKANKAAP AHARLSRDRV LFTSPDKPMT RAGKGTIIRK ATLAAYAREI
     DDLYAGRSSI ALSSALPLHV DDPSTASTEA ALQDLFANLT DRQLGPDDDF FSAGIDSLQV
     LNVVRSLKSQ LAAEQAPVSP DLVSLSLVYA NPSCRKLAAA LHAAASDDGT AGLRNAEERA
     KAMKELYLRY AHDLPHRPRP SDADAPRSDS LTPFNNNNGS SSSSAISVVL TGSTGSLGSY
     ILGALLLSPK ISHIYCLNRG DPTSTAKKQH ALHLSRGLPT TDLDTRVTHL QSDPNLPRHG
     LTPTAYADLV AHTRYIIHNA WAVDFNITID TTRNWPSVNP GTPLVPERPI HDVAVPSAGG
     YGESKYVGER LLEAAAGVSG VPVAVCRTGQ IAGPVGRGRG GGGGGGKWNE REWFPSLVRS
     SKHLGALPGG LGSMDGADWV PVDVVAGVVV DLVGENLGRL GGGAGKEGGG EAFVQFDHLV
     NPRVSSYPEV VLPALRRRLG EGEGELFPAV EYAEWLRRLE DEAAKPDADP NKCPGIKLLD
     FFEGMGEEVK AKEKGPFAGL RLDTKETVKR SETLRNLKPV GADWVDIWCE GWGL
//