ID G7XJ69_ASPKW Unreviewed; 3493 AA.
AC G7XJ69;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAA87094.1};
GN ORFNames=AKAW_05208 {ECO:0000313|EMBL:GAA87094.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA87094.1};
RN [1] {ECO:0000313|EMBL:GAA87094.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA87094.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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DR EMBL; DF126458; GAA87094.1; -; Genomic_DNA.
DR STRING; 1033177.G7XJ69; -.
DR VEuPathDB; FungiDB:AKAW_05208; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR InParanoid; G7XJ69; -.
DR Proteomes; UP000006812; 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: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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd19532; C_PKS-NRPS; 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; 1.
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; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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; IPR045851; AMP-bd_C_sf.
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; 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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049552; PKS_DH_N.
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:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 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; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 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; 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; 1.
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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..438
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3412..3490
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2350..2407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2364..2391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3493 AA; 384014 MW; 8AA5AA592FD331FB CRC64;
MDKSKEPIAI VGSACRFPGG CDTPSKLWEM LKQQRDVLQK IPKDRFNTDP FYHPEPTHHG
TSNAQFSYLL EQDIGEFDAN FFNILPKEAE CIDPQQRLLM ETVYDGITAA GLPMETLRGS
NTAVYVGQMC DDWPGMLQTQ LDESPPYMAT GSSRSIVANR VSYFFDWHGP CMNIDTACSS
SLVAIHEAVQ TLRSGQSGIA VAAGVNILIS PMYYISESNL RMLSSEGRCR MWDAAGDGYG
RGEGIACVVL KTLSQAQRDN DHIECIIRET GVNQDGRTSG ITMPSNIAQA QLIRDTYRRA
GLDVHNPLDQ PQFFHAHGTG TKAGDPQEAT AIYHAFFTKE TEPEQKLLVG SIKTHIGHTE
GAAGLASVIS TSLALQHGQI PPNMHFNELN PDIHPFYGAF EVPTSVKEWP ALKPTQVRRA
SVNSFGFGGT NAHAIMESYV PPETIMSAPS QSTTLYTPLL FSANSVTSLR KMISKHRDYL
VDRPETSLRD LAWTLQHHRS TLPYRKAITG RDYESIIAQM GSVLHAEPAD LSVRSTQSTE
PRLLAVFTGQ GAQWPRMGAR LLESSSFVRD KIAFLDECLA TLPEDDRPDW KISDQILATG
ESSRVLEAAI SQPLCTAVQI VLVDLLQAAG IKLDAVVGHS SGEIGAAYAA GLLSTCDAIR
VAYLRGVCAK LAASPSGAKG GMAAIGVSAE DVQEVFDQEE IREEIKGKIS IAALNSGSSI
TLSGDEDVVQ TVVDVCTSQG KFARRLRVDT AYHSDHMLPC ANPYLEAMER CGISVQQPLG
DRPTWFSSVY RDTIMDANNL TPDYWVHNMV QTVLFLPAIT RAAKEIQTLD IAIEVGPHPA
LKGPALDSLG EVQTQIPYTG LLGRGKDDVD ELSTAVGYLW TQLGTGVVDF DGLESALAGD
KEPKTLLVDL PSYPFDHQNR YWVECRTWKA NRLSDAYPNT LLGSCLTTTR SPGNAQWKNI
LKPTEIPWLQ GHRLQNQLIL PATAYIVMAL EAIKAVAGDA AIALFRLTDL VLKRPIVFDD
DSSSIECISS LQNLAFNDSH IKAQFTVESA PQGELSLRVN VEGSIEVELG RSNPEKLPLL
EHDDYYNMNE QNPGRFYSEM RNVGYHFLQA EGIVLAPFSP AQAQDDNQLL GHIKWLPALP
NGANTGDGKA SVSLNPAVTG DVERISLYYL RRLCEMCTPT HRSKALPHHQ QLLKWAASVI
DRVSVGKHPF IAKEWISDSE QLIEQLSCRH PDSVEAKLAA EIGPSLPGLV HEQGILAHYI
SMNEEAPTIK RVHERLADLV KQINHRYAHM HILEIGSGNG AMTEMIVSSL GTSFSSYTFT
DVSDNLFSEA EFRFYQYADR MIFKTFDMYQ APTAQGFTAG KYDLVLVGNG LQTARNQEQV
LSNIRQLLKP GGYLISASPL ADDSLRLGLI MSDCPEWWSG ADSGRLTLDS WNNLLGQCQF
SGIDTCTPVE DVLHDIPVWA AQAEDERVRL LRNPLGASVE LPEEMPPLVI IGGRSLATVQ
LVEQIATLLS TKFPVVTRLH SLEALITSSI PSKATVLSLA DLDGPVMKLW TANKLEALKL
LWNQAARVLW VTKGARFSDP YSTMISGIVR VVRMEKIDLN VQLLDVDSIN PGTACLVCET
LLKHQLLLTW SADNSTEKLL WSYENEVAVE GQQTLIPRLY SNEVENLRFN SVRRPIMHEV
NPFVSTLRLA STGESYQLEE VSSLRVAATL PTIRVCQSIL QFLKLGSNGS FMLCIGTRQD
DSQAMVLALT QSSESPTPVE PGWEIELPFS PEVGRLALIT VATHIVTQQM LAMVPKNGTL
VVHEPDDLLH AALLDAAEKD RLDVWFTTCQ SGRNSNWTYL HPALPARLVR EKMPSEVSAF
VNLEAPNGLG ARVADAIAGC VPPHGVHASA TTFFANQLYT RSGIGPAVLS ELLQNAWQSA
STSSLALELI DPIPLGEVSF HNPVREAIQL VDWNVPAVPV HLRQLDADPI FRRDRTYLMI
GLTGEVGQSL CHWMARKGAG CIVLASRNPK ITPAFLRKAE DLGATVRALS LDITCRDSLQ
RCLRQIRRSM PPIAGVANGA MIMEDVQFDH VEFESMERSM KPKVLGSKLL DEAFYDTALD
FFIMFSSIAG VVGNTGQSTY AAANMYMAGL ALNRRKRGVV GSVIAYSPLM GLGYIDRTDE
TMGDKFLSMG VSLMSETDFR YAFAEAIKEG QSSCHDRAEL ITGCAPKVLS DITRNRYRSD
IRFSHINLER TNGQAGAGAG DSSIRGLLKQ AGSMEEVEGI VLGAFTARLK TLLRMSTEQP
LDANSSLVGQ GIDSLVAIDI REWFDRELEI DMPVIKILGG SSIVALVKGC LQDIPETVLD
IRNLDQSIGG KPAAPAAATS GVESAIPLSD SKDSISSSSD SESVDTSSHY GTSDTEPEEE
STCEPSIDLD LRQSTIQSAT EKVVPMSFSQ ARFWFMQHAL QDPSALNMGR CWHIEGALDL
PRLRKAVITV ADRHEAMRTR FFWGGQDHDV PMQGILSRSI VQLETKRITN KEEVYRELDA
MRHHAYDLGD WQLVRTRLLT LSNREHYMII GNHPITFDDS SASLLLDEMN QAYLGQSLPR
LPQEAQYSFF AEAQFRDYKE GRFQKHIDYF KALIKEENHP LELFAFSKAP VRPVQTQYRT
HRSDMRLSSK QASLLKQISQ DRHSATSDLY TAVLGVLLFR LLPNTNQVLL GIDADRNDLA
LGRSMGCAHN TLPVRLERPG INTKLGPYLN TVRNAIEGVL EHSALPFDVL INELKLDRSA
NVPPVFQAMI QHRVERQDQV TWCNATCNPD KSLNSCTGLD LYLDITENCA GETAVGLEVQ
QGLYSLEHAD LLVKSFVYLL EQLTTNLDVP LATSELWPPE DISRALELGT GPVAPMQWPR
TVVHRIDQMI QQNGSNLALK DGSGKSLTYN DMSRRIDSII AALRQAGTPK GSFIGVMQEP
SVDSICSMLA VFRAGAVYMP FDHRISIDRA QGAIHKAKPL LLLVDQSTVD KARSLQAPMP
RVLDISSVAT RQHIPRTPNL ADGSSPAIIL LTGGSTFEPS LVKHASIIPQ LEASSMQYNF
SNERPLVALQ HSANSTDLSL TQTLDVLCNG GSLIILSANR QGDPVEIAKT MQEENISYTL
AAPSEYQNWL SCAAEQLRDC PRWTLAITTG EIVPQKLLQS FRALESPSLQ LLNLYSPAGT
CFGSTWQGLV EYRKSDAKSP VAAGYASPNQ AIYIVDVELR PLPVGVPGEV LIGGAGIADC
YGNMDSTMKE RFIESPFSQW DSNFTSTKWE TVYRTGDRGY LQKDGALILV GRSDGATQVN
VRGFQVDLEE VENALIEASG GFLTNAAVTL REHGEDQFLA AHVVFSNQTS QKNSQEMLLD
NLLMRLPVPD YMVPSAIVVL EELPLDSHSK VDRTAICQLP IDESNVVTPT SREMTSMEAS
LAEVWKGVLS ASASPTLTPS SDFFQVGGTS LLIVILQRAI KEQYKVALPV TELVATKRLA
DMARLIEGKG VFV
//
