ID A0A100I8U2_ASPNG Unreviewed; 2433 AA.
AC A0A100I8U2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GAQ36799.1};
GN ORFNames=ABL_01862 {ECO:0000313|EMBL:GAQ36799.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ36799.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ36799.1}.
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DR EMBL; BCMY01000002; GAQ36799.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:An15g05090; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1104411; -.
DR VEuPathDB; FungiDB:ATCC64974_28870; -.
DR VEuPathDB; FungiDB:M747DRAFT_369040; -.
DR OMA; KDVQHYT; -.
DR Proteomes; UP000068243; 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; 3.40.47.10; -; 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; 2.
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; 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; 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; 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; 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; 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.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..435
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2345..2421
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2433 AA; 264462 MW; BE4DF0F95CD07FEE CRC64;
MQTTQSPQQP LAVVGMACRL PGNSNSPTAL WRFLEQGGIA STEPPSSRFN LHGHEDGTKR
IRTMRSPGGM FLENIDPADI DAQFFGLSRA EATAMDPQQR QLLEVVYEGL ENAGITLESL
RNQPVGCFVG SYASDWGDMQ GRDPEDRVPN ATVGVGRAML SNRLSHFLNI KGPSMTIDTA
CSGSLVSLDI AARYLQTGEI DTAIVAGCNL YMSPEHCIDM SNLSGAASPS GRCHTFDAKA
DGYIKAEAVN MVILKRLPDA LRQHDPIRAI VRGSATNSDG WTAGIASPSP EAQAAATRQA
YRNAGISNLN DTSYVECHGT GTRAGDPIEV NSVASVFCAT RTAERPLLIG SIKSNVGHSE
PAAGLSGLIK TIMSLEKGCI PGNPTFETPN PAINFEALKT RAFQRTIQWP DVPFRRASVN
SYGYGGSNVH VILDEASTSV PPSEASFKSS YLTDDDDLFA DQEQESFHLL VFSANDEASL
KATVQRLQMH LVRPEVRVSL PDLAYTLSER RTRHFHRAYL VSNTPTVDQH ALIYGKLRSN
VPKVGFIFTG QGSQWPQMGK ALVDTFPSSQ RLLRQLDAVL QALPHPPQWS LYEELTCPRS
SDHVRQPELS QPLVTALQLL IIDLLKTWCV QPASVVGHSS GEIAAAVAAG LLEPEDAIQI
AYYRGKAAVD LRDDSRPKLG MMAAGLSDTS PLLQQILQRH SGAVALACIN SPQSVTLSGH
VSALETVCHQ LHEHGHFARL LQVDLPYHSP FMADIAAHYK SLLDARGPDS SSPASPRRRG
AKFFSSVTGC EMQGSVDNAY WEANMRLPVR FSEAVEAMLT DADPVDFLIE VGPSGALAGP
IKQILKALPS NSAGIEYHAA CRRNTFEPTA LFDVAGRLFL ADGPININQV NATARAESAR
DSKPAVLVDL PNYMWNHATK YWWESQASRD WRFRRYPNHD LLGGKVLGTP WTAPVWKKLL
RLPELTWLLD HRIGGQVLFP AAGYIAMAVE AAFQMGQSRG FIDQNLQVHN VAYRLRNVTF
MKAMVLEEGT DQRIMLTLTP EDESADSWHH FTVLTLHEDA TTTRHCSGMI MLETPYDEDA
PWEAIKPLEY PMPAQAWYKA LRDVGYSFGP SFQSQLEVEA VAGQRTNRGL VSFSEPPSSY
PQSPYSIHPV AIDGCLQSGA ASLWQGIRSA VGGALVPAVV DDLLINARDV AAVPVAVAAA
SAAFSGVGSP EEAHNYHSHI QVFDPASKRL LLKVTGLWYH NLDASPESPE RQHTFMRLHW
KPQMSTLSDG QVRALVQARR SLQKPRPHHD PSSPSQKQWT LMELLLHEKH FLQVAEFSTL
PFEESVGRDM FDGDLSFAEG NCKYQFMPKN LASMRASQAL LSETYPQAQM NMLDVTKPDV
DLSMLPDMLD LAILQLGPVS SADLANALAN VRRAMTPTAY LLVLGTSLVD ITEDTGSASV
ISGEDSDSGS SDWSMVGGSS SQILDFLRGQ GFERVVPLAQ ESLSEDTVFL AQLSSDKTIV
SPPLATTSEV TVLHLTPEDK PLVKQLAIAG KAPSEQHLPL PAATIAPSSV VVIVDEVYSA
TLTEVTPIQW QAIQHLTASG CKILWVTSGA QLDVTHPDRS LAYGMSRVIR AEDPCVNFTL
LDVESAVSTG SLEAICRTIL SLQQGHQTQD HEFVERDGVV HVSRVYPDTQ MNADAEKEDA
ITTTAAALPP AQQTQNLHEH PSCVRLVCRQ PGKLQSLCFA EVSSSPVPLP DDFIEVEMHA
AGLNFKDVAT CLGIVPENPY LLGLEGAGVV CRLGKGVTSF RVGQRVLVNR RGSFGNKVQC
PVQGAHAIPD SMSFEEAASL PVVYLSVIRG LFDLANLQRG QSVLIHSAAG GVGQAAIQIC
QAMGADIYAT VGNDAKRAVL TQQYNIPPER IYSSRTAAFA PRIWEATRGR GVDVILNTLT
GRLLDESWRV VAAGGCLVEL GKKDILGRRS LSMEPFNRNA SYRALDMSHD SVTPQITAQL
MTKMFELLAS GSIRPIEPRT VFPYRDIAGA IRYMRGGEHI GKIIISREAP DNDPNVPEQI
VPAPTQLRLR DDATYLIVGG LRGLCGSLAV YLACHGAKHL AVMSRSGFED SRSRSVIRDL
ISLGTRIELV QGDVSCIKDV RRAFRQAVKP VRGIIQGAMV LKDKIYTSMT VDGFRDVLPC
KVSGTWNLHA VAQEQGGVDL DFFTLLSSIS GLVGQKGQAN YAAAGAFQDA FATYRRDRGL
AACAVDLGVI EDVGYISERQ EIATRLDINI WTPINEALLH RILRASILDQ HNVQARGDPT
ATAQIITGIP FPQPEGAMLL RDARFGALAA KEGSAATAAG KHGGLSQEMQ TLLMLLQTST
ADRSEQLAAT IEVVNRHFMH SLGLAEPMEA AKPLSVYGLD SLAAVDFRNW LRQELKVVVS
TLEVVGAKTL SALCERILSR LLENADATVG ERG
//
