ID A0A395HAF1_9EURO Unreviewed; 2426 AA.
AC A0A395HAF1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Polyketide synthase 2 {ECO:0000313|EMBL:RAL04559.1};
GN ORFNames=BO80DRAFT_398869 {ECO:0000313|EMBL:RAL04559.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL04559.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAL04559.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL04559.1,
RC ECO:0000313|Proteomes:UP000249402};
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; KZ824423; RAL04559.1; -; Genomic_DNA.
DR STRING; 1448316.A0A395HAF1; -.
DR VEuPathDB; FungiDB:BO80DRAFT_398869; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000249402; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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; cd05195; enoyl_red; 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; 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; 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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF18; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 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; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 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; 3.
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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2346..2422
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1414..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2426 AA; 263255 MW; C2B6097526443113 CRC64;
MTKSQFRQEP VAVIGFACRL PGGNHSPQKL WDFLERGEIA SNQVPKTRFN IDGHYDGSHK
PGTMRPKGGM FIGDVDLADF DASFFEIGGT EAIAMDPNQR QMLEVVYEGL ENAGIPLEQI
DGKPVACFVA SYASDYGDMQ NRDAEDRPAN CAIGVGRSIM ANRLSYFLNV KGPSVTIDTA
CSGSLVGLDL ACRSVQSGEV DTAIVAASNF YLNPDHVMDA GNVGQAHSPT ALCHTFDADA
DGYVKAEAVS CVIIKRLSEA VRDRDPIRAI VRGTASNSNG RTGGIASPSS EAQAAAIRAA
YANAGIENFH ETAYLECHGT GTQAGDPTEV RGAGSVFAAT RTTENPLFIG SIKSNIGHSE
PAAGNSALLK VILSIEHGMI PGTPLFIKPS PKIDFHGTKT VAFRTAIPWP DQGYPLRRAS
INSFGYGGSN AHAIIEQPHV DMREFHVSSY KSGGDQDPFL DEDELTDRPY TLVVSANDAH
SLKENIRALS NHLINPRVSV KLPDLAATLS QRRSRLWHRA FLTTRTTQID EKDFTVGKNR
GQPPKIAFVF TGQGAQWPQM GKELVQFFPW TRAILDELDQ ALQSQPDPPE WSLVSELTEP
RSAEHLRQPE FSQPLVTALQ LCILAVLASW GVNPSSVVGH SSGEIAAAYA AGYLDRASAI
KAAFYRGRAA VNSKANARVD SDVGMLAVGL DPDSALQYVQ NYRGSAWIAC FNSPNSVTVS
GKKPALAALA EEIKAAGHFA RALQVDLAYH SELMGPIGEE YDRLLNEDPK FQPQNDASSP
VRMFSSVTGE VKDTPADALY WKTNMVSPVR FAEALTALVT QDSPSMIIEI GPSGALAGPV
SQVLKSVPLG GDVQYCAAWA RGINSGKALF DVAGQLFTTG APIDLSRVNQ YDTTAVRTIV
DLPNYSWNHT VKYWHENAAS RDWRYKQFIT HDLLGSKIPG TAWESPTWRK HLHLADVPWL
RDHKMGPDVL VPGAGLATMA LEAMYQKHCA LHPDQAVGSP NELAYRFRNV KFDRAVVVEE
NKPTTLLLTL TPVPGSKDWH EFRIRTTAAG VIYEHCSGLI RVQDPIGDEE ALQGEDLAPL
KHPQSAKLWY KAQREVGMGF GPTFQTIKSI ESVSGSRTCR TLVSLEPPAS KWDPQSYYPF
HPAILDGCLQ TATPANAAGE RSLVKDTMIP ALVDDMVVNR IPKDLVEGLS VAESVYTGRG
RREVAKSWIA NIAIHHPETG ALLLRVRGLN YIRLDVDEKP DAHVFTTTTW TPDISLLTPD
QLMYLQPTDA ASTRLDRVID LIAQKKPLLQ VLEINVDETD ASTRWFQGDE HARAAYALYH
LASPSANTIL EWKTAHQTKR NTDCHVLDLA APGLGLPTTD PTYDLVILKP GPQSDDPTTI
ESISERLQPL LRPGAYVLLI PQFTPLHPID DLIPSSPGAI SPDDPLSRSG SHTPSGDSSA
TSIDLTLSPG NAWKSLGKLH GLSQFPSILQ IPAEPGHATA FLCRTTNPTP STPGAHPPTL
IIARFHPDTP ALPSTLHNLL TTSGWSIRTV PITTLAAEAP TTDPTAVILI LDELSKPVLT
QITEPHWDSL KTVISTGRPL LWVTKGSQTT QVTDPDTALV HGLFRVIRRE DPQVQLTTLD
VQSATSPATG QAIERILQRL MAGMDPDLET EYAERDGVVL LPRLRPEPAV NEFKAAERGG
RGWEPVVKSL HGTKAQVRIQ AEKVGTLQSL RWCETAVGEV AMEPGMVEIE VMAVGVNFKD
VATTMGIVPE NEHTIGCECA GYIKRIAPGL TTPFQVGDRV VAMRSGTYVN RVQCPHERVH
RIPDTMSYED AATIPLVYLT AIYALYHLGN LQPGQSVLIH SAAGGVGLAA IQLAQHKHCD
IFVTVGTDAK REFLSRTFGI PRTRIFSSRS GRFAEEIRRE THGRGVDVIL NSLTGELLDE
SWRLTADGGV MVEIGKRDIV DRNRLAMEPF DRNCSFRAVD LSYTKEISDA LIGQLLREIF
ELVNAGHIGP IRPITRYPFD EVIPALSYMR RGQHMGKIVI ANPDAEDVQL PIRPALPTLQ
LDPNAAYLIV GGLRGLCGSL AVHLARHGAR QVIAMSRSGI DDEASARVIA NCAAYGCRIT
EAKGDAADLD FVRGVFRSVQ PRRIAGLIQG AMVLRDKPYE TMTHDEYTTT LPPKHHATWT
LHRASQTEQP THPLDFFTLL SSISSIVGNK GQANYAAGNA FLDAFAHYRR GQGLRAQTVN
LGMIEDVGYV AEQGGKLEAR FDPRQWTPVN EDMLRRIVSY SILVQTPGGI SGGVNPAQLV
TGLACPLGSG SELGGEARFG YLVRRGGGGG PGDEDEEVGG DGNDDATAAA VKGFQMLYAS
RADAGVLSKA AVGLLQLQVT RILRLETEME PGKPLMAYGL DSLSAVELRG WVRQKTGAEL
STLDITNASS LVALGEKLVA KMPVVG
//
