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Database: UniProt
Entry: A0A0B2WEP5_METAS
LinkDB: A0A0B2WEP5_METAS
Original site: A0A0B2WEP5_METAS 
ID   A0A0B2WEP5_METAS        Unreviewed;      3890 AA.
AC   A0A0B2WEP5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:KHN94311.1};
GN   ORFNames=MAM_07840 {ECO:0000313|EMBL:KHN94311.1};
OS   Metarhizium album (strain ARSEF 1941).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHN94311.1, ECO:0000313|Proteomes:UP000030816};
RN   [1] {ECO:0000313|EMBL:KHN94311.1, ECO:0000313|Proteomes:UP000030816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHN94311.1,
RC   ECO:0000313|Proteomes:UP000030816};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000256|ARBA:ARBA00004685}.
CC   -!- SIMILARITY: Belongs to the NRP synthetase family.
CC       {ECO:0000256|ARBA:ARBA00029454}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000256|ARBA:ARBA00029443}.
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:KHN94311.1}.
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DR   EMBL; AZHE01000037; KHN94311.1; -; Genomic_DNA.
DR   STRING; 1081103.A0A0B2WEP5; -.
DR   HOGENOM; CLU_000022_37_9_1; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000030816; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0046483; P:heterocycle metabolic process; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:1901360; P:organic cyclic compound metabolic 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   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd20483; C_PKS-NRPS; 1.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 4.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
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; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 2.
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; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030816};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..434
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2232..2309
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          3372..3446
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          2312..2338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3890 AA;  427681 MW;  F743890971C483C8 CRC64;
     MAARVNGRAD DPSVIVGLAC RVPGANSPSK LWESIAEQRD VQQKMPEDRL KVDSFFHPEP
     THKGTTNARF GYFLDQDIGD FDAGFFGISG KEAEAMDPQQ RLLLEVVYEA LENAGITLQE
     IRGSLTSVFC GSFTNDYNAM LTKDLEYYPK YTVTGTGDAI LSNRISYFYD LHGTSVTIDT
     ACSSSLVCFH LGSQTLQNGE ADISIVVGSS LHYDSNVFVT MTDLGMLSTN GRCAAFDASG
     SGYVRGEGIA CAILKRKSDA IANGDNIRAV VRATGSNHDG KKNGITLPNS VAQEQLIRTT
     YERAGLNPNH TQYFEAHGTG TAAGDPIEAR AIGAVFSPGR NEPLFVGSVK TNIGHLEGAS
     GLAGLIKTTM ALENKYIPPN MHFKTPNPKI DFQNWKITVP TKLIEWQVPD GVPRRASINS
     FGYGGTNAHV VLEEYARDEK LPVPVPSEPI ANGVHSRPYL VPLTSHSPKA GELSEENLKA
     YLNSGEDVTI ADLAYSLSTR RTLHQQRSFV VANDKAGLVD QLSSPRPAAP WTLAKNAVPK
     LGFIFTGQGA QWFAMGRQLI EECPHFRQTL QRCDTVLKSL PDAPEWSIVA ELNKSKETTL
     LGETLYSQTI CTALQLAIID LIECWGIKPS AVVGHSSGEM GAAYAAGILS FESALIAAYY
     RGRYMSASRT DCVPGGMMAV GLPENKCLEE LKPYAGRLTI AAVNSPSTMT VSGDEEAILD
     LKEKLKEKKI FVRQLIVKQA FHSHHMSPLA PAYENALKNN YSFKTKAPRC RMFSSVTSRV
     ADHEKMGASY WAANMVQAVR FSDALTGVLF NEEDEQNVDI LVEIGPHPAL KGPARQTVQS
     LKLDVPYVAS LTRGVPDFEG LLTMAGTLFS LGYPVDIVAA NQNLSQNSQG ALVAAPTGTM
     LNDLPKYTWE HRRYWSETRY IREHRQREFR HATLGHRVAG SVVRHPLFRN YFRLSELPWL
     NEHVVENKVV FPGAGYISMA IEAAIRTEDI ESVKMIYLKD IVVKNALLIP PTDEGVEVLL
     ELKPVTLSAK SHSDTWYEFN VFSYDESSNC TSHCHGLISV EKGHAAPVDY TGRYPEGTNF
     NELRKKTYRS MAAGTFYKNM AELGLAYGEK FRLLKGSIES GVGFAMSNLV FDPKHLPLDA
     GDETVLHPTL LDSFFHVIFH AVENRLGRPL DEPYVPSFFR ALTISGNFFD SRYSTDVKNF
     RVGSFTKLPS PRVAINDMIM QNDKGELMME IAGLEVTSLG REDPEGQGPR TLFYRQRWQP
     CFEMMTNIKG RSLSEIVDIF AHQYPNTRIL HITSDLNKTR ELIEKLGAKN GERRRFRQLD
     IWHSQSYDFG EEADKLAKEC RGLVNVTEPA PGLYDLVIVS EAGVNAVPLM NNAGCILFDG
     RKDFSAADFQ LLFSSPTCTA VRKAAEPFGL SSELSIIMPT GKPSARTSSI LKELESTHGG
     KITLTDFSEL SSKGTAPLAK DVVVLAGLDE AISDKTAFKG AQALLTSLEK NVIWPTEGAT
     LEANRPDNAM YIGLVRAARS ENDTLRAVTF DFGIDSPAKS VAVNIVRFLD TRITEDELTE
     RNGTIYIPRV EADDERNCKL RNGPNQEPHL EPFGTAQTRT PLALRIGKVG LLETLYFDED
     TQVIDTEIND NEIEVETKAS SINFRDVAAS MGIIEDFNLG DECAGICTKV GAKVKGFEVG
     DRVVALRPGQ GAHRSLVRNP ASWCYKLPDT MSFTDAAAMP LILGTAWFAL DHTARLATGE
     SVLIHAAAGG VGQMAIQIAQ RAGAHIYATM GSPAKRQLLK DVYGLKEEQM FSSRDASFAK
     GVMDATGGKG VDVVLNSLAG PLLHASWACL APFGRFLEIG KRDIHENSKI AMDPFRRNVL
     FASIDLVTMF EKNEALGEKL FKECFALLAN GEIRTPATIK EVPYSEVVKG FRLLQMGKHT
     GKIVLVPHPE DMVPVMRGGY RHVRLFSSSK TYLLVGGLGG LGRALSQWMV RKGASKLAFL
     SRSGADKTEA KATIDWLLER GVDATVYRGD VSKLADVQSC VDQIGSSLGG IFQAAMVLQD
     KPLETMTYEQ WQRCCQPKVE GTKNLHEASL GYNLDFFICF SSVAAVVGSK AQANYSAANC
     YLDAFMRHRR EIGLCGTTMN VGAVTGVGVV AENEELQRIM LRMGMDTINE EELLYQLEEA
     VLADKPANAM TARGCNGNQI ISGVGLISPD VYWASKPIMK NLYANHDFGA EGAGQSSKNL
     LALVSEEPDM EKKTGILLDG FLEKIAGVLA TPRESILPSN PLSAYGLDSI VAVEFRKWFR
     KEVQVDIALF DILGAASINA LVSKTIRMVS TTSTSKATTS DRTEKKVAAE SESTGADSNV
     SAMATGQLKK AQHAGVVPLS TFQSRLWFVH SFLEDKSFLN LPIVLRIRGK PHYPTLQKAI
     QEMAVRNPAL RTAYFEGDEF AVQEPLEDFE LGVDLRDLSN EADVEKALEE FVKYNRKIEM
     NVEEGEVATY SLAKLSEEEW AVVGMTHHIS IDRASLFPMM SQFVAIYDAL RTGNDLATVS
     APEFNYVDFT LWHNARLASN LMKPDLDWWK KTLQGIPQSG KVLPFAKGER PARSDPRRQA
     VRAKLNAKLF ARMKRIAAQS NGTPFHFVLA AFRAFLYRYT EDKDLVLLMV DGNRPHPDTD
     PLMGFFVNLA PVRCNDDCEV AFDQLFQATK SRALDAMAHS GVPFDTIVDI MNVKKTSSHM
     PVGQIAVNYQ IHGPVPTYTT CDFVVENIES DDIPTAADIQ LEAIETSEHS LDLKIEYSTA
     LYYNPDMERF LDNFSTFLAS CIKDHRQPVD EISMCGPLEI EHLKKEYWNM ETKANQWAEQ
     SVLDVITKMA RQHPQTAAIK TSDCRSITYK QLIENAESVA SELLDAGARP GDRIGLVALP
     GVEAVTGMLA ALMTGSGYVA LDTDFAQDRL SFMLSDSGAR ILLAGPGQEH LVADLLSKMA
     TGLKVIRIEE AASAGRSVAH PRARRPDDPF YMIYTSGSTG TPKGVVLKES NTQAMLATLS
     KDYALSHRDN FLAHTTTSFD LSVVQIFGGL TAGATVSVAS WETRKDPVAL ADFMMKEGVS
     VTYFTPTQFA LLMEFNSEAL RKCSKYRVAY FAGERLPVRV AKAFYDLGTP ATLYNTWSPS
     ELVVQTSISK IDYPGEGVVS LPIGYPMDNC RHYLVDVKGN PVPAGHIGEL VVGGVQVGAG
     YLNRPEANAR SFVEDPFASD DDRKRGWNKM FKTGDRGRFR PDGQLEFHGR IAGDKQIKLR
     GFRIDLGEVE QVIFRKSQSL KKTGSLTDIA VVARTVDSDE LQLIAYLVPK AKVISDADKM
     AIISQLHRKI KPHLNYYMLP NGYQFLPELP ATLGGKVDRR NLLERRLDLL FPSSITTQPS
     DNVPATTKTS TGSTQDLEAT VLALFRTTLG GEIELNDSFF EKGGNSILLV RLQARVKKLF
     KIAPPLPVLI REPTAAAVCA YLRRAKGGDA TIKGGLGNRV SWNVETNLPN TSQYMPRYGI
     PRIDRDELKS ILLTGAETFI GVHLLAEILR TKRDATVHVL GSTEELASQG LTDLLLRLDL
     VTDNLTLDDI SNRVKFVPGS LSQSHFGLSR SAFRELGQTV ESIYHLGGHV SLLKPYSSLK
     PVNVSPVFDI IKLAGLGSRL SDINYLSTWS VAHLQTWSAS RRTREEYVTG EEDSSHFSPP
     TEDECGYFKT RWVSEGLLTK AAQRGFPVTI TRTSGVTAAV RGSGVPNPGD EFITRIVVSM
     IESGMVPQIG RADQPSFAVD VVPVDWLVSS FFALTSRKEA LSHVPSSEMH SAPQIYHITN
     PLPLRLKDLP RIIAQLQSEQ TTPRLVSLDQ WLSSMESAED EDADSQVVRS TVLRQYLSTG
     AVMFSLDNKK TMDVLDVLNP GAAAGCPAVD AELLGTLLRK LRRAENAFSG
//
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