ID G3JBQ2_CORMM Unreviewed; 2173 AA.
AC G3JBQ2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Polyketide synthase, putative {ECO:0000313|EMBL:EGX93678.1};
GN ORFNames=CCM_01947 {ECO:0000313|EMBL:EGX93678.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX93678.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX93678.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX93678.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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DR EMBL; JH126400; EGX93678.1; -; Genomic_DNA.
DR RefSeq; XP_006667164.1; XM_006667101.1.
DR STRING; 983644.G3JBQ2; -.
DR GeneID; 18163976; -.
DR KEGG; cmt:CCM_01947; -.
DR VEuPathDB; FungiDB:CCM_01947; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; G3JBQ2; -.
DR OMA; IGLNMKD; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000001610; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; 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:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF50; HIGHLY REDUCING POLYKETIDE SYNTHASE SRDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2092..2173
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2173 AA; 235637 MW; 3662F4272FB66311 CRC64;
MTPWPANRLR RVSINSFGYG GANGHAILDH PSVVIPGYRH HGVPLVSEAV PRALIPIEAN
GKSNSNGHAD SIGPENGHAY ANGNGHANAG VPSWCQLAPV AQVQGAGVRP YMLLPISAHD
ETALKHKFAL TESLLGQYEW ADVLYTLSAR RSNFARRAYA VVKSGSLLPN GIKPNATSKA
PSAVAKRIGF IFTGQGAQWP QMGAKLFSEF AVVKQTIQYL DQVLGALTLK PSWSIEGALL
EPAATSQIHD PAFSQTICTA LQIALLALLR QWNIVPAVTV GHSSGEIAAA YAAGHLKACE
AIVLAYFRGQ VVSMNTRSGL MMAVGLGVGE AKSHLDGIED AVKIAAVSSP NSVTLSGEPD
AIQSLNTTLS DKGLFTRVLK TGGNAYHSHH MAALGQTYED LAAQGLLEIK SFVQQEPALP
ISEWISSVTM KKEAVSVHPT YWRRNLESSV LFSNAVERLA RESPVDLLVE IGPHPALGGP
LKQIRANLEA NGSSLPICCV SLRRGEDDVV SMLSLAGDLF INNAEVNLPA VNATEEMKYG
KLELQHGFFC LNMPPYKYSY PESPLYYENR FNKEYRLRKH LRHDILGARV PGGSKNHPQW
RNILRQKDLP WLEDHKLLPH AVLPGAAYIT MAIEAVTQLH YEIYDAPPIK SFKLRQVAIN
SALRVEDTEL GVETFLNMER LPLTNTAAMS QWYKFSIGSI LPNSDVWNQH CTGTICVATT
DTVIAKSKKL KIDDRAKSLD ISRWHKRFHT AGLGYGPAFQ GLSDLKAYRG ANIASANVSL
RPTRSSEMES QYVIHPATLD TCIQLALISC HAGQVENFEK AFVPIFADEV SVWLPDFPEE
QALGVASGCL VGLRSVYAKV QLHDSAGAPL LDIGELKCVS YEGIEDTSTV QTTRELYWRP
VARPDVGTLT PSIAKAMFPP KEIASYISTH DALDRLSVHV LVSIAEKLQT VRLTEGVGEN
HDLFSDWVKN WVASTKHQAA NAFSNGNKDA EIQRLANNLI SVPEARCLVA LHRNLDKVLA
GETNSLKVLM ENDLLNDLFD SGIFVQAAYS QFQNILDLLA HKNPRMRVVE VGAGSAGATL
AALGTLRRSP SKRFQEYFVT DSQGWCVTDA KSRIDDHSHV IFETLDIMQD PVAQSFETGS
FDLVIAAGCL TQFESPETAL RNIRALLKPS GSLLLLETTH LTLASEVLFR TLTGQWGREH
VSTDEKSWDS ALKKSGFSGI DISLQDYSGD QQQTTVMLSK IVQSSADTVQ RKKGAEVFLV
YSQTTPLAAD VTFDLLIDQG FSPVLVDLFS AQEIPPKSSV ISFVDANGST FTCRDEAYFE
AVREVILLAS SLVWLGADLM IPAESSIMKG FLRSIATENA QSRYAFVELD HTSYTRPSRV
AELLIHKLIE LEEAPSLHSV ERECVLSGGS FYIERLLADA TLNDQFFQRN TEEDVGQATL
GSQGPIKARY RQPGVLSSLY FSSDPDFDEP LETDWVEIKT EAIGLNMKDL AVATSRFDLN
NLSTEGAGVV TRVGSAVQTL REGDRVFGMI PGNMGNHLRS PASLLAKVPS RISSQGAASM
PVAYLTSIYA FRHLARLEKG ESVLIQSATG GLGMAAIRIA QHLGAEIYAT VGTDNKRRVL
TEEFGIPADR IFNSRKLSAV DDIMRATGQN GIDVILCSSA GDSMHETWRL IAPLGRFVDV
GRTDVLGGGS LGLEVFKRNA TFSSFDLGLI YRQKPRLITK LMDEMMALLD QGVVGPIQHL
SSFCISQLES TMSSFSKGVH TGKFVITFDD PAAKLKVAQS AVRAKFDPTA AYLLVGGLGG
LGCSLAMWMV ERGARHLVFL SRSGADRPEA VSLVQNLKAV GANPEVVRCD VTCKAAVASA
VGNISARFKV KGVIHAAMVE GDAFFSNATW PQIQKVLLPK VTGSVNLHYA TEKLPLDFFL
MTSSIVGTVG TPSQGAYTAA NAFQDAFARF RRSQSLPATA LGLGLILEVG SVSGSLAFQQ
MLQRNATYGV SETEFLQLFE GALCDGSVAS ESSLLSNADP DCLGQIVTGL EPGRFLSYLD
NGRINELVWY SNPRFQAVAQ AISDQAQALS SGSGAADGQG SSVSIQVKNA STPVEKLAIA
RCAITTQIGE LIGVAADDID SDQPVSRYGV DSLVAGELRN WLIRTFGIEI SMLQLLNKST
KIESLVQEAV KIS
//
