ID A0A1G4AW67_9PEZI Unreviewed; 1054 AA.
AC A0A1G4AW67;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Thioester reductase domain-containing protein {ECO:0000313|EMBL:OHE93371.1};
GN ORFNames=CORC01_11321 {ECO:0000313|EMBL:OHE93371.1};
OS Colletotrichum orchidophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHE93371.1, ECO:0000313|Proteomes:UP000176998};
RN [1] {ECO:0000313|EMBL:OHE93371.1, ECO:0000313|Proteomes:UP000176998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 309357 {ECO:0000313|EMBL:OHE93371.1,
RC ECO:0000313|Proteomes:UP000176998};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) 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:OHE93371.1}.
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DR EMBL; MJBS01000121; OHE93371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4AW67; -.
DR STRING; 1209926.A0A1G4AW67; -.
DR OrthoDB; 2230730at2759; -.
DR Proteomes; UP000176998; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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: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 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; 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.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000176998};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 225..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 557..640
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1054 AA; 116739 MW; AA0DB25075CFAA40 CRC64;
MAQPQYGKRL IPHVLDEVAK SEPNREFISV PRSSNPQDGW RPISYKQIAN AVNRIAHRIT
DKSGKPEPGS FPTVAYIGPN DARYTIITIA CIKAGYKALL ISPRNSFEGQ INLFEKTDCH
TICFDTSFKD VIQPLLEEHQ MEAIMVSSAD AWLSDEEVPH FPYDKTYEEA QNDPVVVLHT
SGSTGLPKPI VARVAMVAVG DAFHDLPDFM GSENCIKSIM QGSRLFLPMP LFHAAGCYMS
IFATIYWGRA VALGFTDRPL TPQTLIDAAK YANIDNVILP PAILEELSHI PEGVEALKKF
KRVNFGGGNL ARDAGDKLAK EGVPVSSVIA FTEAAPLPYY FQKNLELWQW FIVDSDRLGV
DWRQASGEDS DVYEQVIVRK DKADPLQGIF YTFPDVNEYN TKDLYRKHPT LPNHWMYYGR
SDNIIVFSNG EKLNPVTIEE IVTGHPRVKG AVVAGAMRFQ PLLILEPSEP LTSEDDIEKF
IDDVWPMVVK ANKETVAHGQ IGRAFIGITN PEKPFPRAGK GTIQRPMALK LYKDELDAWY
NKAEDGADSL SVHIDVSSQQ GLIDSIEKLF QQTLGSRALS ADSDFFSAGI DSMQVINASR
LLRKGLEAAD ANITADAIAT RVIYAHPTPR QLAAYLMDRI SNKKTTNTME SNGDRGVNHD
IQAMEAQLQK YTRDLPKSPG NKPAPNDQGQ TILITGTTGA LGSYLLDFME HNPAVAKVVC
LNRSEDSGKR QVKMSAERGL ATTWKKAEFH SVDMAKSNLG LAPDVYDRLL GEADRIIHNA
WPVNFNLSVE TFEPHIRGVR HWVDFSLRAA KNVPVIFVSS IGTVDAWQGP EPVPEKRLMD
LTLPSTGYGR SKLVSSLILD EAALRSGVPT AVVRVGQVAG PQSEAGVWNR QEWLPTIIAS
SKYLGVLPRD LGAMATVNWT PIEGIAKLIL EVSGVAAPVP LDKINGYFHG VNPRTVPWAP
LAEAVRGFYG DDVIKKLVSF KEWVEILEKS AASTEDMDKN PGIKLLDFYQ GLAMGEGQGV
EFAMERTTKS SKTMKEMQAL TPELMQNWCR QWAF
//
