ID A0A0M8N737_9HYPO Unreviewed; 2221 AA.
AC A0A0M8N737;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Nonribosomal peptide synthetase 14 {ECO:0000313|EMBL:KOS22054.1};
GN ORFNames=ESCO_002363 {ECO:0000313|EMBL:KOS22054.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS22054.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS22054.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS22054.1}.
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DR EMBL; LGSR01000006; KOS22054.1; -; Genomic_DNA.
DR STRING; 150374.A0A0M8N737; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000053831; 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:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 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; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; 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 PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; PF21089; PKS_DH_N; 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; SM00825; PKS_KS; 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; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 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:UP000053831};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..333
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2136..2217
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2221 AA; 239580 MW; DD72BACA5E852673 CRC64;
MLLEVSYEAL ENAGIRKEDV DGGDCAVFVG SFVKDYEQIC LRDPDWSPQY AATGNGIAIM
ANRISYALNI HGPSMTIDTG CSGSLIAVHL AAQALRTGES SLAIAAGAGM ILSPNTIMPM
TALNFLSPDG KCFTFDSRAN GYGRGEGIGA VIMKRLSDAL RDNDTIHAVI RSTSTNQDGK
TTGITLPSKE AQVANIRNAY TIANLDFAQT GYVECHGTGT QAGDWRELKA ISETIAEGRP
ADRRVVVGSI KPNIGHLEGA AGIAGLIKGV LTLKHGKIPS QINFEKGNPN IDFDSWGVRV
PTSTLDWPLP GIRRVSVNCF GFGGSNAHVI MDEAPGYLTA RGLRGNHSSV DVNEDTSSPP
ENDSHARLFV YSANDKSGVA RVMNSHLPVL DKFSVGADFL NDYAYTLGCR RKKPKLGFIF
CGQGSQWAQM GKDLMSYHAF SASITGASTY MKSVLGSPFD LLEELFKNAA GSLISSPKIA
QPATTALQVA MVDLLSSFGI LPENVVGHSS GEIAAAYAAG ALSRESAWKV AYYRGLAAAS
IPIRAPKLRG GMAVVGMSVE KTQEYLDSVG KSARVACINS PRSVTISGLE EAIQWIVNDL
KEKRMFCKVL EVKTAYHSSH MKLVEYDYKD SLGILPTNAT YENVRMFSSV TGQLAHGGEL
NAEYWARNLV SPVQYVAAVE SLMSLPSDER PDILIEVSPS AALRSPTSDI LGSVTSNAPK
YLSVLERKQT GPVSLLTMIG ELWARSYAVD MEAVAARGLA HVQLRCLSDL PKYPWNHSKR
YWYETHLSRA NRFRKYPRQD LIGAPTADSV PFEPRWRGFL RISESPWIQD HQVQKTIIYP
AAGMVSMVLE GAKQMAAEHS SSHAELLGYE LSDLVIEKAI LVPNSAHGLE VALNIRSDSS
RTTEKGLVGT HEFAIYSKPQ EKPWERHATG KLQFRYKLGD WRASFKHHEG DYGVLKEKCT
ESLIPRQLYE TLDAVGLNYG SSFQNLVEVS KSDNASVSKI RIPDTRSKMP EKFEYPHLLH
PVTLDAMFHS LLAIEPVPMV PVAIKNIFVS ANVKSEAGSV FTGHSTTSMS GIRGAEADLV
MKQANGEDSA FVIINGLRLT RLSSPSPGTF GFLANHRNLT TQIVWKEDAQ FASPSSIVEQ
IDVLAHKYPN LSVLQVGANI NLTAAILKAV TPNKTDTARL ARLTIAVPGD EKFASDVRAL
VDGTSVAPLV EMVSDASSRG VAYHLVIVGQ SSSAANLRSL LQPGGVLLEE MKPERELGLV
NDDSHVWEEV SSEALGAQRV QIKAFKNKAP IAEESSLGEV VFLVPSKTES AEVGAFISAI
QERSGDNGQP VIRLRDLRET PEVVSGRVVV SLLETSLSET EDYIFNWEED DFVAFHALQA
EAAAVLWVTR GANMTPHNPK GAPIIALART LMSEDPLKHI VSLDLGHKSK FLDTSVVESF
LSVFKASFCT KPGPGPREVE YAEQDGRLYI PRLTTVEPLN RVIEDENFGT IVKRQFDRKE
DDVSGLELDA SKLQIFEDKE ACFVESKPKE LPEDEVEIAF LEAPLSFLDV ETLLGRTSDT
SIGMDVRGTV KRVGSAVSGF APGDEVMALV ADNAIRNTLN AKASLTKRSV PGFVPSMIVS
AVYALVHVGR ISRSRKVLIH AGASGHGLAA IQVAQNAGVE IFATVLGSDM ASQRDILKQR
DVPRDHILDA EADGFVMALL ALTNGRGVDV VYNPTLAHSD SNMKIIRKGG TIVSFADKSP
APQARPSISG SMTVVTFDLR SLMEQDAEFV AELFDQATQL SGALRPLPES LVERCDVGSI
KDLLSHIQRN PFSRYASAVA NLRAESRVSV FSSGATRSLD QSIDANGTYL LSGGLGGLGK
SITELLVKNG ARHIAHISRS GASSEGAKAF IADLQARGID ARAFAADICD SAALEAVIRG
TVAKEMPPIR GVFQCAAVIR DAVFDNMTFE DWDTAVKPKT VGSWNLLHAM DATGHKPFYV
FLSSSAGVIG NRGQANYASG NCFQDALARH LRLKGERACS LDLGPILGAG MLAKNDSLLD
ILRASGFYGI RHGDFLKVVE HAITGEVGHP AAAMPAQVIL GVGTGGIIRQ NQPADPYWSR
TALYTYLNLV DMPPADLSAS SGTSNMDMKS MLARAADIDA ATAIVCTGLA SMLAKSMNLH
VEEVDVNRPP SNYGVDSLVA VSVRNWVLGN CGVQISVFEI LGDFTIVQLS HTIAEKSGCG
Q
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