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Database: UniProt
Entry: A0A137Q4L8_9AGAR
LinkDB: A0A137Q4L8_9AGAR
Original site: A0A137Q4L8_9AGAR 
ID   A0A137Q4L8_9AGAR        Unreviewed;      1095 AA.
AC   A0A137Q4L8;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Polyketide synthase HetM {ECO:0000313|EMBL:KXN82193.1};
GN   ORFNames=AN958_02938 {ECO:0000313|EMBL:KXN82193.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN82193.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN82193.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN82193.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ963052; KXN82193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137Q4L8; -.
DR   STRING; 1714833.A0A137Q4L8; -.
DR   OrthoDB; 2230730at2759; -.
DR   Proteomes; UP000070249; Unassembled WGS sequence.
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; 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   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   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249}.
FT   DOMAIN          86..387
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          734..980
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
SQ   SEQUENCE   1095 AA;  121040 MW;  49457B7F18F362C2 CRC64;
     MIDVSTLPTL QAAASKTFTR PPFDHSLTIP EIYAFHALKS PDHPIFIYAE DSAGTNRTIY
     YPEAYAAIQR GHNIVTCKHE ELAQGPKGPN VVGILANIDS ITYVTFSVGI MHAGLAAFPI
     STRNSVVGIA HLIRTTGLRL LFVSPDSAMQ RLASDACTLL ENEGIDVHIL PVPQFNDLYN
     QDKSCSELAP VRSSPDPVVL ILHSSGSTAQ PKPVPFLDSN FLKWGLLPYY GEIDMGGMAI
     AAHSVPIFHA MGAVQIIWTI CAGTVMACFR PVSPPIIPTP DIFLREIVAT KSQIVFCVPI
     FVEAWARSPG NIPILRNLSA LIYAGAPMTR SVGDQLVAAG INLVPFYGAT ESGCLTIFCP
     KSTSTDHWSF FRISPHLTME MALQDENEDG EIVEPIVISS EVFTPNVINT TYQGRPAYAT
     SDLLLRHPTN KDLYSVYGRV DDQLMLSTGE KTNPVPLETL FLQNKEIAAA IMFGRGRFQN
     GVLIQPTTPF DPEDEEKLVA YRNLIWPTVE KVNEFAPAHS RLFKEMIMVT NPKKPLEFTP
     KGTPRRQMIM VTNPKKPLEF TPKGTPRRQV CLKTYEKDIN ALYEAVKDSS QTDISIPELW
     TPDNAVAFVS SAVRRVIRQP FAADQDIFQH GCDSLQATWI KNSLLRAVRS SKNKANVHCI
     PLNFVYAHPS IQQLGDYFWM VLTGTASMNE QSRAAQIETR CLQMQSLVTK NTVEIPTPAW
     TASPASVDPE IVLLTGSTGR LGCHILKQLM ERPDVLKVYA LNRPSVTGQT REQRQQEACS
     RWGIDLQSNF EKVVFLDYDT SKERLGLTDG DYRCLQTTVT TIIHNGWRVD FNIGLGSFEN
     LITGTRRLLD LSLQSTVSNG PKFVFVSSIS VFSNIEPGQE APETSVSPSL AAGFGYGESK
     WVAEAICAKI GEATSLSVSI VRVGQLSGDR LTGRWNVKEW VPAMIKRGKA VGSLPSRNEY
     FEHSLTAVTW LPVDDAAKAI VHLLKSPSAS PSCSYISLVH PSPVDWNKLF GAAAKSLQLD
     FIAYEDWLKK LQSHRENLAN GAAEAPDDLT EFFLQGNLGD GRFTMDRTLE LCPSLRTVEP
     LEPTDILKYL AFWKF
//
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