ID A0A0F0HYS9_ASPPU Unreviewed; 2385 AA.
AC A0A0F0HYS9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJK60669.1};
GN ORFNames=P875_00053129 {ECO:0000313|EMBL:KJK60669.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK60669.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK60669.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-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:KJK60669.1}.
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DR EMBL; JZEE01000732; KJK60669.1; -; Genomic_DNA.
DR STRING; 1403190.A0A0F0HYS9; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion 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; 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; 1.
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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; 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; IPR009081; PP-bd_ACP.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF50; HIGHLY REDUCING POLYKETIDE SYNTHASE SRDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 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; 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 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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 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:UP000033540};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..447
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2300..2379
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2385 AA; 260139 MW; EBD981693EA5D274 CRC64;
MQLPMNEATP LENGHTETAA SNNKSIAIVG IGCRFPGDIS SPSDLWDFLA EERSAAGRVP
KSRFNVDSFH GSKDEPSTTV ALGGCFLQED IRNFDNQFFG IHNREAADMD PQQRKLLEVV
FESFESAGVT LDDVSGANVG CYVASFTPDF IAMQTKDVEN MTRFTHLGMG ATLLGNRISH
VFNMKGPSCV VDTACSSSFY ALHMACSALE NGECDAAVVA GVNLIQTPEV HVGTSLGGVL
SPASKCQTFD SSADGYARAD GVGALYIKRL DDAIRDKDAI RSIIRSTAVN SNGRTPGISQ
PSVDGQEAVI RKAYARAGLN PRETAYVEVH GTGTSVGDPI EVEGLSRVFR KDQRHRPTLI
GGVKPNLGHG EASSGLLSIM KASLSLERRQ IPATISVKQI NPKIKTEEWG VEIVTRMTDF
PSECSPRRIS INSFGFGGAN AHGILEEPGR QTNKVSCRQA MSRNGDLTGT MNSQSDSRIS
NGINGLNGHN VSSSLPYLLP LSANKLSSLQ GRAGRLSKMD FSAVSIADLA YTLGQRRSHL
GLRGYVIARQ ATLAQDFSVD NLILANSDSN LTDNKFAFVF TGQGAQWKGM ARELLHFPVF
ADTIRQLDHE LSTLVHAPEW KICDVLMDDS EDCPLNLAAF AQPITTAVQI GLVNVLRSWS
ILPQGVIGHS SGEIAAGYAA GLLTAREAII IAYYRGYSVT SSAPEGAMAA VGLHCDDAHE
WITRFGFNAN LKVACINSPQ SVTISGDSEC IDTILSSLHA EGVFARKLKT DGKAYHSHHM
AVIGTMYEKL LKKALSFEKQ ASLDLEQQDT HMYSTVMCQE VQSKAVRTAA YWRANLESPV
RFSEGLTFLS EMTGQCTFVE LGPHAALKMP IMQTLGKSTS YLATLNRGQD SSVSLLNFVG
QLFVQGFKVD FSKLNHTYTH GTPRFIYDLP TYPWHYEKPP WNESRISREW RNTTHPRHEL
LGREVPGGNK TTFGWRNLLQ MKNVPWLRDH KLGDTVVFPA TGYLSMAVEA LMQKALPVGA
DGAGKSVALR HVDLLKALPL PEQGSIELYT ELRPVAISNI RDSKFWWEFQ ISSISDDGPT
VRAKGSIRLE PIAACGTQLP SRECRLAPQS RKLWYESIAD SGLAFGPTFQ HMHDIHTPDP
KGVLYAEART RTLAPTIEGA HPRPRYLIHP VLLDNLFQVA LIACTGGFIH SMVGKVPTRL
GSVRISLPSS PTDEGTIRST SKVTGQSTNK IDSALFDGQQ QLVAHFKDVE VTAYIGTERM
EVRHPITRVT WKPDIAQVHD SATFSSALDH VLSQSDLGSF GSKANILAAL DLIVHKNPDT
DILCLSTDLS LITLSFLEVL DASSIYRRFN SFSLGRLSSD GGLEVAEVRN FIVPLGLRSL
QYRMASSGDH FGLVILGDDI AVVDGLGSHT DGETVFLAPD VDSTLKHDTF SVLSSRSETA
KNVQVLRPAP TTNGSSTPDF DNVVFICRSP KHPADDHLAG HLSDDLAVPI KRVALTDLAD
SPIPPNALVI STAELERSIL AGAVPQEEFD GFKQMIEHAA WIVWITGSGV HEEFNPTLSL
FAGFARAVVI EQPSTKIFSL ELDPTTDAAV ISRDVTKIVQ NGKNAINDCE YIDNGSHLLI
SRIVPDERMN REFRTRQDGL ASPMPLGSVG NAALSVRKPG QLSTTQFVKR PYPSLSILAS
DEVVVKVSCV GLNAKDVNAL AGHVQTTDAR CSLECTGHIV AIGSDVRDLN IGDKVAVMYP
GYFGTYETVP AWSCVKLRDD EDLRTMASVM MVFSTAMYAL YHRANLQPGE SILIHSAAGG
VGIATIQLAK LIGAEIFATV GTEEKKQYLI EHFGLTPDHI FNSRDSSFAS SIKSITNGRG
VDVILNSLLG ELLHESWDCL ADFGRFVEIG KRDLLDQGRL NMEMFSRGTT FTAFDMSMLA
ESTSPTQHRV YKGLVTRVIS LLRSGDIHPI EPLSVFNISD IVQAFNHFNN AKRMGKIVIS
FEDQTQMVPV VHEKFSTQLD PHKSYLLVGC LGGLGRSVSK WMMSRGARKF IFLGRSGTQK
PAAKRLIDEL EESGAQCTVI KGDITNYPDV HRAMAAAPTP LGGVIQAAMG LNEAIFKHMP
REYWLNGTEA KVQGTWNLHN ALSALDKEKE LDFFVLTSSI SGKLGTATES NYCAANNFLD
AFARYRRGLG LKAVSLGLGM VSEVGYLHEH PEIEDLLLRK GIRPLTEDEL VQIFDFGLTQ
PPTSLHPNDL MPQSHILTGL EDTGLQGHRK QGYEGYWQFL SDARFDVLTC ALRRNAGKSA
QGNSTQASVI QEAIASNDRE QLTDAVKVVL VKKLSNIILT PVDKIDVKTP LLDFGMDSML
AAELRQYIFG TMGVDVPFLD LMDKKTSIFG LAGVIADKLT ITSSN
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