ID A0A2V5INL9_9EURO Unreviewed; 2322 AA.
AC A0A2V5INL9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Ketoacyl-synt-domain-containing protein {ECO:0000313|EMBL:PYI35874.1};
GN ORFNames=BP00DRAFT_195412 {ECO:0000313|EMBL:PYI35874.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI35874.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI35874.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI35874.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ825467; PYI35874.1; -; Genomic_DNA.
DR Proteomes; UP000248817; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; 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; cd00833; PKS; 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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 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; IPR013120; Far_NAD-bd.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..426
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1285..1359
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1392..1466
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1464..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2322 AA; 254704 MW; D0F212AE093C7DB2 CRC64;
MASSTSISNN DIAVVGYSLK VAGADDPEEF WNLLCTAESQ HREVPVDKIP FKSHWRKVDP
NRRWYGNFLN DSDAFDHKFF KKSPREVASQ DPQQRLMMEV AYQAVQQSGY FSLHDVDQHV
GCYLGVCNSD YETNVACHEP NAFTTTGNLR SFIAGKISHY FGWTGPSMTL DSGCSTAAVS
VHMACQAILA GECTAALAGG VNVMTNGLWF QNLAGASFLS PTGACKPFDA SADGYCRGEA
AAVVFLKKMS QAVSDGDVVL GCISGTAVYQ NLNCTPIFVP NSPSLSSLFA HVTQKAGLDP
QQISLVEAHG TGTAVGDPAE YSSILEVFGG LKNRQTPMTI GSVKGLVGHT ESASGAVALI
KVLLMIQEQK IPPQASFQSL SPHLKASSSD MLEIATSMKD WNVNHRAALI NNYGASGSNA
SLVVTQPRQH DGAGLTAIHA EGLKHPFRLS ALDERSLLEY VTKLRGLIRS KAVSARYITL
ANLSFNANRQ SNHILPTNAI FSAHSISDLE EGLTAYMEGT NRDFSNTAKA NPTRPVILCF
GGQISRSIGL DRNVFDGVRV LRDHLNHCDS ILQGMGYDGL YPEIFQTSPV EDAVKFQTIL
FALQYSVART WIDCGVKVAA VVGHSFGELT ALCVSGALKF EDALRVIATR AELLRKLWGQ
KRGAMMAIEG DLNSVERLLA AAHQLTPVEN AATIACYNGP QSFTLAGSSK AIDAVFETLS
GDPDFSSMRT RRLNVTHAFH STLVEEPLLE ELRKLGQSIT FSHASIPMER ATETANEPLT
SSFFAQHMRN PVYFDHAIQR LAKKYPSAVF LEAGSNSTIT GMARRALGAP AESHFQAVNI
TNGAQGLNNL TDMTTCLWKE GMNIIYWPHH RSQTYEYGPI LMPVYQFERS KHWLDVKIPQ
EKASSIPEHI PDESVPECLY TFLGYQDSRQ RVARFGINTA TQMFRDHLKG HTIAQTAPIC
PMTLEIDMAI EALGSLQPAL RDPKHIPRVH NIQSKSPLCD DPSRTVWLDL KESEGSAPGT
AWEFCLASSG GSGSADTVHV SGEITFGLTE SPDAHAEFAR YGRLIGSHQR CLQILNSSDA
DDIIQGRNIY RAFSEVVDYG VEYQGLQKLV GKGNESAGRV LRKHAGESWL DMHLSDCFAQ
VGGIWVNCMT DLQPTEMYIA NGLEHWLRSP KLGSRYGQVE AWDVIARHHN LDDEKAYMTD
VFVFDSVTGE LAEIMLGIKY TRVSKQAMSR MLTRLTPRLA TKATTPLEMA LPITSDVGTV
SAAASAKISP ILKPHILANL PFSNIDVSSG VKAVLAELSG LDAVDIKDST QLCDIGIDSL
MSMEMGQDLE HKFHCSIPMY DLADLTTVRS LVDYIRGTVT AISSEDDQSS SAESVSDVFS
DSATTVSSDL DVSIAGGFGA FLAEFLGVAE HEIRNDVSLG ELGVDSLLSM ELSADLECKF
GLHFPHGQIL QELTVSDIER KMNKSVPATP GFPTPSELAS PTPAPETAKS YFPDRDLRLP
SEAVMDAFTE IKGLTDEYIA EFNGLNYMQT IYPALVQMCV ALIVEAFEQL GCPLRAAVHG
QVLPRIEYLP KHERLVEYIY QVLQNEGNLV KVEGNTIIRT HAPAPVESSG SILNRLIKDY
PDHTKAHQLA YFTGRRLADV LSGKADGLRL IFGNEEGRQL VSSLYGDFLF NRLHYKMMDD
YLRRLIGRLP SSDGPLRIME MGAGTGGTTK QLVPALARLG ISVEYTFTDI SPMFLASARK
EFKQYPFMKF RVHDIEKAPA DDLLSSQHII IASNAVHATR SLTESTKNIR KALRPDGFLM
MLEMTQPLVW IDMIFGLLEG WWLFDDGRRH AVADPVRWET ALHAAGYGQV NWTDGRCPEV
GIERIVVAMA SQGPRYEGRH CSLPQSPSPP ADADLVTRQA VADGYIRRYT QGFSAKAPKA
SIKKPPSGAV ILVTGATGSL GCQLVSHLAH QSSVATVICL NRPARSSKTP SERQQEALST
RGIVMGAQAL SKLRILETDT SKPFLGLAQA EYAQLAPKTT HIIHNAWPMS GKRPVEGFEP
QFQVMRNLLD FASYAYSGSK IHFQLISSIA TVGHYPIHAG NPNVPESRLP LQSVLTNGYG
LAKFVCERML DETLHRYPDM FQPMAVRLGQ VAGSRVSGYW NPQEHLPFLL KSSQTLGCLP
DLKGTVSWTP VEDVAATLGD LLLSGEGLEM ANRYPFYHIE NPTGQSWEDM IPLLAEGLWF
NPATARLQEG QDSSAKNGII TTVSFEEWIH RVRTFAGPGE ENPASLMVDF LAEHFRRMSC
GGLRLETVRC REHSATLARV GPVDAEVVRR YLQNWKKMGF LR
//
