ID A0A0N0NI03_9EURO Unreviewed; 2468 AA.
AC A0A0N0NI03;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Lovastatin diketide synthase LovF {ECO:0000313|EMBL:KPI35158.1};
GN ORFNames=AB675_10165 {ECO:0000313|EMBL:KPI35158.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI35158.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI35158.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI35158.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-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:KPI35158.1}.
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DR EMBL; LFJN01000043; KPI35158.1; -; Genomic_DNA.
DR RefSeq; XP_017995121.1; XM_018138918.1.
DR STRING; 1664694.A0A0N0NI03; -.
DR GeneID; 28730798; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000038010; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 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; 2.
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; IPR013154; ADH-like_N.
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; IPR013217; Methyltransf_12.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF46; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PF08242; Methyltransf_12; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 19..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2377..2458
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 51..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2333..2353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2468 AA; 269325 MW; 271D92441B44BF11 CRC64;
MPSAKDTSAG DSRPQPSFYE PLAIVGLACR LPGNINSPSQ FWELLKQGKD ARGPIPESRY
ASASFDDHRR RTTGPATTPE GYFLGHDLEH FDAECFSMNR TEAAHLDPVQ RQLLEITQEC
LDSADVSDSS GRKIGCFVGT FGEDWQDLRR KDTLDHGPYR MIGSSDFAAS NRISFEYDFR
GPSVTYRTAC SASMVALHSA CQALQMQDCD AALVAAANLI FSPTNTSGLA DLGALAPDGS
SKTFDASASG YARAEAVSAL YVKRLDDAMR DGDHIRAVIR ATASNSDGRS SAFANPNPDA
HVELMRSAYA ASGLAPQDTA FVEMHGTGTA VGDPLEAEAV ARVFGGSQTY IGSVKPNVGH
AEGASGLTSI FKAVLALEHG VIPPNIKFNL PNPKIRFGEA GLIVPVAPTP WPAHKARRVS
VNSFGLGGSN AHAIIESWSS NSNGALNTAE PSTGSHLIAF SAFRDESLKQ MIDQTREYVS
KNADSDVNVA YTMNTRRQHR RKRGFTICRD GQLIHTHMAP ETLTNPRVVF VFTGQGALSL
GAGAQLAERY PSFDADLVSM DRTLQATSEP PSWCLRKMVR DRSGHVAKIT GVISQPLCIA
VQIALVNLLE SWGTRPDAVV GHSSGEIVAA YASGALNMKE AILMAFWRGQ SLPVRQSDGS
MAAVEMSEED VQPYLSERVC VACVNSPSNV TLSGDKTALA KLVAKLKQEK PTLFARTLPV
DHAYHSHHME AAAEVYAKKL GSEIRPKKRS VPFYSTVHGR LLRPEEHLDA TYWTKNVVQA
VLFAPAVAPI LKDQTRPTVF IEIGPHRTLF SLGMPVDLET LTPHGRHLHD LPSYPWHRER
LWNESRISRQ WRMRPFPRHE LLGVPILENN ELEPTWRNVL RVNEVPWIAD HQIDANIVFP
GAGYIAMVGE CMRQLAGGNS DAYTVKDVSI KNALVVHENQ SAELITSLKP FSWSKNQPSS
GWEFCISSYQ NSRWTLHCTG TVREGFVEKR GSVHSQRYTR VVDEQRLYRT MAKSGLKYGP
CFATLRNISA DVHGKRAAAS IATAISSSDP GSAQPYAVHP TSIDAMFQAL MVADVKGHPR
DLSGICVPVA IAEMSVRRNG GKSSTLHLNA DVEAQRSEWQ GLHGSFDAFN GASDGAPVVA
VQARGVQLAQ VGEPAASSRF ESNYSSAELA YRPCLSLMKA EQRASLLRPE ADIAALQDEL
EQLTLDIIRQ RATLLRNIKG KTPSLERYRQ WILSVADFDN QDDEAGWVTV QDSLDTSAVS
PPACQRDHSH SAATLISRVG KNLIDIIEGR SSLLEHVLDE TLLAMYYQWG ERFDYSRFIQ
LFAHENPGCR ILEIGAGTGG TAAKVLSHLY AASPSNHPLC SEYAYTDVSE GFLTTAKERF
AEHAFMTYRT FDISQDPASQ GIKLADFDLV IAANVVHATA FLQGSLANIR KVMKPGATLL
LQELCSQKNS TSFIMGGFAG WWLGAEVGDA ERMTKPYVSP ERWDQELRAA GFGNGAESVV
FDSKSEEAQL CAMISSRFLG HQQAESRLLA SLVVAPDHND ELIQNVSEAL QQSGFSVAVS
ALGSVPTGDY VVSLLDMAPQ RSVDSAPWAV SESKSAEVDS FRQRKALIVG LRERQRMVWI
TPGSRSTKWD PRHSMVLGLA RTLRLERDMD FSILEVNDDE VAELSKCLPG FLQGQRRRQD
RGDKFLDETS RDYEYRLENG HIHVGRYQWH SIEEALASAA SLPSNDEENV NRLAIRQPGV
LQSLEWQNQK LLSHIGPDEV KVKVAAVGVN FRDVLTAMGV ISSPSLGIEA AGIVTATGAN
VVDLSIGDHV AVLTEGAFAT SLIVSRLRCA KLPEYIAFEQ AASIYSVFCT NMLALHYVAK
IDRGMTIMIH SACGGIGLSA IRLCQNAGVE IFATVGSAEK AEYLQTRFDI PADHIFGSRS
TSFKDDLLRA TNGRGVDVVL NSLSGELLDA SWDCLAEFGL MLELGKRDMQ DGGALRMANF
SQNRGYRGVD LAHVVAERPE LCASLMKDVT KILNMGLIEP LAPIKTYEAA EIEQCFRYFQ
KGEHMGKVVV TMPTNVNEAS IVQPTRSPGV SFSADAGYLL VGGLGGLGQA VAVWMAEHGA
RHFVFISRTG RSTATDAFFE ELSAMGCAFD IVKGSVVDPE VVSNVVRMSR KPISGILQMA
MELQDVTFAN MSEQEWLAAT EPKVTGTMNL HKACLTLPTP LDFFVMFASQ NGLHGWHGQS
NYAAANTFLD AFAQYRRNQG LAASVIDIGP VEDIGFVSGR KDVQSKMAPL FRFTPEHEFL
AALELAIIQS TPTSTSAQVI PGFHPRSVGG AGRAPWSGDA RFSAYQNLED IERRRQETRS
PGQAHSTSRS SSTRMAALSK LLAAPLIGTM SRQEAFDVVA QAILERLCIT TGMDLEPLLS
RDSTSIGLVK IQDVGMDSLI AIDFQSWWRQ VFRAKISVLE IMDLGTIGRL TERALDLVEA
AEGGSQAL
//
