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Database: UniProt
Entry: A0A0A1V471_9HYPO
LinkDB: A0A0A1V471_9HYPO
Original site: A0A0A1V471_9HYPO 
ID   A0A0A1V471_9HYPO        Unreviewed;      3883 AA.
AC   A0A0A1V471;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Hybrid polyketide synthase-nonribosomal peptide synthetase {ECO:0000313|EMBL:EXV04383.1};
GN   ORFNames=X797_002056 {ECO:0000313|EMBL:EXV04383.1};
OS   Metarhizium robertsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=568076 {ECO:0000313|EMBL:EXV04383.1, ECO:0000313|Proteomes:UP000030151};
RN   [1] {ECO:0000313|EMBL:EXV04383.1, ECO:0000313|Proteomes:UP000030151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXV04383.1,
RC   ECO:0000313|Proteomes:UP000030151};
RA   Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA   Gibson D.M.;
RT   "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT   ARSEF 2575.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:EXV04383.1}.
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DR   EMBL; JELW01000002; EXV04383.1; -; Genomic_DNA.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_37_9_1; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000030151; 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   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          3366..3440
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          2315..2339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2318..2333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3883 AA;  427287 MW;  14B9E5F30CE8B086 CRC64;
     MASRINGRAD DPSVIVGLAC RVPGANTPSK LWQSIAEQRD VQQKMPEDRL KVDSFFHPEP
     THKGTTNARF GYFLDQDIGN FDAGFFGISG KEAEAMDPQQ RLLLEVVYEA LENAGITLQE
     IRGSLTSVFC GSFTNDYNAM LTKDLEYYPK YTVTGTGDAI LSNRISYFYD LHGTSVTIDT
     ACSSSLVCFH LGSQTLQNGE ADISIVVGSS LHYDSNVFVT MTDLGMLSTN GRCAAFDASG
     SGYVRGEGIA CAILKRKSDA IANGDSIRAV VRATGSNHDG KKNGITLPNS VAQEQLIRST
     YERAGLNPSH TQYFEAHGTG TAAGDPIEAR AIGAVFAPGR DEPLFVGSVK TNIGHLEGAS
     GLAGVIKTTM ALEKNYIPPN MHFKTPNPNI DFEKWKITVP TKLVEWKVPD GVPRRASINS
     FGYGGTNAHV VLEEYTQNEQ IPAAIPPEPV ANGVHSRPYL VPLTSHSPKA GEMSEETLKA
     YLNNTEDATI ADLAYSLSTR RTLHQQRSFV VANDKAGLVD QLSCPRPAAP WAIAKNPVPR
     LGFIFTGQGA QWFAMGRQLI QECPHFRQSL QRCDAILKSL PDAPEWSIVA ELNKTKETTL
     LGETLYSQTI CTALQLAIVD LIECWGIKPS AVVGHSSGEM GAAYSAGILS FESALIAAYY
     RGRYMSSSRS DGVPGGMMAV GLPENKCLEE LKPYAGRLTI AAVNSPSTMT VSGDQDAILE
     LKEKLTEKKV FVRQLVVKQA FHSHHMFPLA PAYENALKNS PAFKTNPPTC RMFSSVTCRR
     ADHEKMGASY WSANMVQAVR FSDALTGILL DEEDEQNVDI LVEIGPHPAL KGPARQTVQS
     LKLDLPYVAS LTRGVPDFEG LLNMAGTLFS LGYPVDIVAA NQNLSQTSHG ALVSTPTGTK
     LHDLPTYTWE HRRYWSETRY IKEHRQREFR HATLGHRVAG SVVRHPLFRN YLRLSELPWL
     NEHVVENKVV FPGAGYISMA IEAAIRTDRA ESVKMIHLKD IVVKNALLIP STDEGVEVLL
     QLKPVTLSAK SHSDTWYEFN VFSYDENSNC TSHCYGLVSV ERGDAAPVNY TCRYPEGTNL
     NELRKKTYRS MPAGTFYKNM AELGLAYGDK FRLLKGSIES GVGFAVSDLV FDPGHLPLEA
     GDETVLHPTL LDSFFHVIFH AVENCLGRPL DEPYVPSFFR ALRISGDFFH GRYSPAVKKF
     QVASFTKLPS PRVAINDMIM QNDRGELMME IAGLEVTSLG REAPDGQGPR TLFYRQRWQP
     FFDMMTKVEG KPVSDIVDVF AHQYPNTKML HITSDVNKTR DFIQHLGCGK GERRRFKQLD
     VWSLLGNEFG EEAERLSKEC RGLVNVVEPA LDSYDLIIVS EAGVNAVPFM NDTGCILFDG
     KKGVVTAELQ ELFSSPFCTA VRNAVEPFTL NSELSVVMPT CKPSARTSLI LKELESAHGG
     DISFTSFPEL AHKGTRLLAK DVVVLAGLDE SISDKAAFKG AQALLTSLEK NVIWPTEGAT
     LEASRPDNAM FIGLVRAARS ENDTLRAVNL DFGIDSPAQT VAANIVRLLD GRVTEDELTE
     RNGIVYIPRV EADDERNCKL RNGPDQEPRL EPFGTAQTRT PLALRIGKVG LLETLYFGED
     TQVMDTKIND NEIEVETKAS SINFRDVAAS MGIIEDSNLG DECAGICTKV GANVRGFQVG
     DRVVALRPGQ GAHRSLVRNP ASWCYKLPDN MSYADAAAMP LILGTAWFAL DHTARLAKGE
     SVLIHAAAGG VGQMAIQIAQ RAGAHIYATV GSPAKRQLLK DVYGLKEEQM FSSRDASFVE
     GVMEATGGKG VDVVLNSLAG PLLHASWACL APFGRFLEIG KRDIHENTKI AMDPFRRNVL
     FASIDLVTMF EKNEALGERL FKECFALLAN GEIRTPATIK EVPYSDVVKG FRLLQMGKHT
     GKIVLVPHAE DMVPVMRGGY RDVKLFSSSK TYLLVGGLGG LGRTLSQWMV RKGARKLAFL
     SRSGADKAEA KATIDWLIER GVDATVYRGD VSKFTDVRSC VDQIGSSLGG IFQAAMVLQD
     KPLETMTYEQ WQHCCQPKVE GTKNLHQATL GNQLDFFVCF SSVAAVVGSK GQANYSAANC
     YLDALMRHRR ELGLSGTTMN VGAVTGVGVV AENEELQKIM LRMGMDTINE EELLYQLEEA
     VLADKFGHPV TARGCNGHQI ITGVGLISPD VYWASKPMMK NLYTNHDFGA GGAGQSSKNL
     LALLSEEPDI EKKTEILLDG FLEKIASVLA TPRESILPSN PLSAYGLDSI VAVEFRKWFR
     KEVQADIALF DILGAASINA LVSKTARMVT TISASKHTAG DKPEKKSAVE SEGTEEDSNI
     SAMATGQLTK SQHSGVVPLS TFQSRLWFVH SFLEDKSFLN LPIVLRIRGK PDYPTLQKAV
     QEMAVRNPAL RTAYFEGDDF AVQEPLEDFE LGVDFRDLTK EVDTEKALEE FVKYNRKIEM
     NVEEGEVATY SLAKLSEEEW AVVGMIHHIS IDRASLFPIM SQFVGIYDAL RTGNDLATVS
     APEFNYVDFT LWHNARLASN LMKPDLDWWR TTLKGIPQSS KLLPFAKSER PARSDPLRQK
     VRTNLNAKLF ARMKRIASQS NGTPFHFVLA AFRAFLYRYT EDKDLVLLMV DGNRPHPDTD
     PLMGFFVNLA PVRCNDDCDV PFDQLFQATK TRALDAMAHS GVPFDTIVDI MKVKKTSSHM
     PVGQIAINYQ IHGPVPTYTT CDFVVENVES DDIPTAADIQ LEAIETSEHS MDLKIEYSTA
     LYDNPDMERF LDNFNTFLES CIKDHRQPVD EISMCGPLEI EFLKKNYWNM ETKENQWGEQ
     SVLDVITKMA RQHPQTAAIK TSDCRSMTYR QLIESAESVA SELLNAGAQP GDKVGLIALP
     GLEAVTGMLA ALMTGSCYVA LDTDFAHDRL SFMLSDSGAR ILLTGPGQDG LVAELLSKMV
     MAPKVIRIED AAAAGRTVAH RRARHPDDPF YMIYTSGSTG TPKGVVLRES NTQAMLATLN
     KDYAFSHEDN FLAHTTTSFD LSIVQIFGGL TAGATVSVAS WETRKDPVAL ADFMMREGVS
     VTYFTPTQFA LLMEFNSEAL RNCSKYRVAY FAGERLPVRV AKAFYDLGTP ATLYNTWSPS
     ELVVQTSISK IDYPGDGVVS LPIGYPMDNC RHYLLDIKGN PVPAGQIGEL VVGGVQVGAG
     YLNRPDVNAR SFVEDPFASE DDRKRGWNRM FKTGDRGRFR PDGQLEFHGR IAGDKQIKLR
     GFRIDLGELE QVIFKESQSL KKAGALVDIA VVARTVDSDE QQLIAYLVPK ASITNEADKI
     AIVSHLHRKI KPHLNYYMLP NGYQFLAKLP VTLGGKVDRR NLLERQLQLL FPSSITTQPG
     NTASGEPTED LEGTILALFR TTLGREIELN DSFFERGGNS ILLVRLQAKV KKQFKIAPPL
     PALIREPTAA AVCAYLRRAK GGDGADKGGL ASVISWNVET NLPNTSQYIP RYGIPRIDRD
     ELKSILLTGA ESFVGIHLLA EILRTKRDAT VHVLGSMEKL EPQVLIHILQ KLDLLQDSLT
     LDDINSRVKF VPGSLNQSNF GLSRSAFREL GQTVQSIYHL GGHVSLLKTY TSLKASNVTP
     IFDIIKLSGL GSHLSDINYL STWSVAHLQT WSASKRTRED YATGEEDSSH FSPPTEDESG
     YFKTRWVAEN LLTKAARRGF PVTITRASGV TAAVRGPGVP DPGDEFIMRI VVGMIESGMV
     PQIGRADQPS FAVDVVPVDW LASNLFALTS EKEALSRVAP SEVYSAPRIY HITNPLPLRL
     KDLPRIIAEL RSEQTRPRMV SLDEWLDSME SAEGEDAAGR VVRSTVLKQY LSTGGVMFSL
     DNRKTMDILD GLHPGVAAGC PAVDAEFLRA LLERLKGGEK FSS
//
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