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Database: UniProt
Entry: A0A0C3K2A1_PISTI
LinkDB: A0A0C3K2A1_PISTI
Original site: A0A0C3K2A1_PISTI 
ID   A0A0C3K2A1_PISTI        Unreviewed;      1086 AA.
AC   A0A0C3K2A1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Polyketide synthase phosphopantetheine-binding domain-containing protein {ECO:0000259|SMART:SM00823};
GN   ORFNames=M404DRAFT_1001160 {ECO:0000313|EMBL:KIO03672.1};
OS   Pisolithus tinctorius Marx 270.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO03672.1, ECO:0000313|Proteomes:UP000054217};
RN   [1] {ECO:0000313|EMBL:KIO03672.1, ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|EMBL:KIO03672.1,
RC   ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN831975; KIO03672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3K2A1; -.
DR   STRING; 870435.A0A0C3K2A1; -.
DR   HOGENOM; CLU_002220_1_0_1; -.
DR   InParanoid; A0A0C3K2A1; -.
DR   OrthoDB; 2230730at2759; -.
DR   Proteomes; UP000054217; Unassembled WGS sequence.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
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   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   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:UP000054217}.
FT   DOMAIN          582..663
FT                   /note="Polyketide synthase phosphopantetheine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00823"
SQ   SEQUENCE   1086 AA;  120115 MW;  E7D7D7EF66055EA2 CRC64;
     MEHSTERIYP PVDGSLFVPE MLEYNARHCP DHPFFVYPDE QSNELRSISH LEFYRASQRV
     AHAVRPGRQG QDREVVGIVA NVDTILYQAL FMGVIYAGLI PLPMSPRNSP AAIINLLKTI
     KSRRLIATQS SLGSLIAEVK RESASQGDQA YDLQIDEPPT LATVYPYMSE ETIDSPFSPY
     PKGEISNDHV MFYLHSSGST GFPKPIPITH VTGKHYCIMP TMIEHRALGY DVRVAAGHLP
     PFHFMGVFMQ IFVSITSLQS MSVYAPTAYH DHTKPPVVAN TQNALENAIL TKSGALLVVP
     SFLEEWASSP ESVKQLTKFV YVSYGGGPLA KKAGDALVNA GVKLGSVYGA TETAAFTTCI
     RTPEDQKEWE WVRPGPNTRL RWAPLDDGAF ECQVLSSETH QVSVENLPDV KGYATSDVFI
     KHPTIEGLYK VVGRLDDVIM LSTGEKTVPA PMESVIRTSR YVSGICMFGR GRSQAGILVE
     PKPEYAIDVQ DEKQVAEFRN LIWPVVEEAN KDAPSFSRIF KEMILVTSKD KPMLRASKGT
     VTKKATLSLY ESEIDALYES VEASATAGIE VPLPSEWTIP KVEDWLMVHV TAVNSNEPVI
     PDVDLFEQGF DSLSATFLRN RINGSLKASS DQNIREAVSR ISQNIVFANP TLRALAEQLV
     NIITHKQDTV DPKVEIENMI KKYSSGLPGK RIGGVPTRRD GNEPHVVLVT GSTGALGSYM
     IASLLQREDV ARIYTLNRRS KTTTSQERQF STFQDRGLDT SLLESQKLVY VEGDTSREHL
     GLEDQTYAEI RDSVTVIIHN AWRIDFNLSL ATLEPNVRGT RNLIDLALAS KKTPKPRFMF
     TSSITSTQNW DTKRGRVPED VIADATVAVG NGYGGSKYVS ERIMAMSGLP ATSFRIGQIT
     GGAPRGAWSV TEWVPITVKS SVTLGGLPSL GGSIAWLPMD AVSGAVLDVT LGDDEPPIAI
     NVVHPRPVEF EAVMKPISDA LFEKKITKER LPLLHSTEWF HRLEKQAVNA NEEKIRRVPA
     IKLVDYLRTF DQQSSGQDTS VLAVTFATDT AERVSKTMAK LPPLSRSDAI RWVDYWVSVG
     WFRDVV
//
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