ID Q2TXJ8_ASPOR Unreviewed; 2580 AA.
AC Q2TXJ8;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAE66025.1};
GN ORFNames=AO090010000114 {ECO:0000313|EMBL:BAE66025.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE66025.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE66025.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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DR EMBL; AP007175; BAE66025.1; -; Genomic_DNA.
DR EnsemblFungi; BAE66025; BAE66025; AO090010000114.
DR VEuPathDB; FungiDB:AO090010000114; -.
DR HOGENOM; CLU_000022_6_2_1; -.
DR OMA; CHPASAY; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000006564; Chromosome 8.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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; 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; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
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; 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; IPR032088; SAT.
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; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 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; 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; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000006564};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 394..810
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1652..1726
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1729..1770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1729..1755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2580 AA; 286220 MW; 323843211CC818EF CRC64;
MSRPYRNSNM LSQLEPPPGG NTVLIFGCQC LSFNIDDFHR LRATVLETPE HRWIQDVLSE
LPVYYRTAST TYVQKLKNIP GTQQLRNLAE WFHTGKVPTD SFPLPYIQLA PLLVITHFTE
YWQYLRIRHH KGPTSVKESS AESPVVEIVG FCIGFLSAAV VSAARNQEQL SKYAAVALRL
ATLMGALGDA QEREEEYTSL ATVWKAAELE NRLPLVLEAF PESYVTVRFD TNRVTIMTPR
RTIKQLENEL QSAGFNTTQV EFNGRYHWAG HEDTLHALGR MCDSDPALQL PDTSQSVVPT
RPNIPMDTPP KGPLHELVLW SILAKQCQWL DTFSKVYRAH LEDTASLIIE FGPERCIPPT
YMRKLQGRTV HFADLDLNTL SRTPPLYQTP RSYDSDIAVV GIACRVAGAD DLEEFWRLLC
SGASQHQEMP LERYKDYETP WRPSAIRPWY GNFVRDIDAF DHKFFKKVPR EAMSQDPQQR
LLLQVAYQAV QQSGYFHRPN INRNIGCYIA SCTVDYEHNV NCHPASAYSA TGLLRSFMAG
KLSHYFGWRG PAFCVDSACS GSAVALHQAC QSIIRGECTA ALVGGANAIM SPLAYDNLAG
ASFVSPTGPC KPFDASADGY CRGEGFAAIF IKKMSDALAD GDIVLGTIAS TAVEQNNNCT
PIVVPDASSL AGLFTQVTKK AHLHPRDISV VEAHGTGTQA GDPAEYVSIR QTLAGPRRTS
PLSLGSVKGL VGHTEGVSGL IALVKILLMI NEGIIPPQPN FQTLNPHINA SPDDQIHIAV
TLEQWRENFR AALINNYGAS GSNASMVITE APYASEHRMS SSIHTFTVAL PILICASDEG
RLSDFAKRLR QFLHHQAISA APATDLGNLS FNICRQSNPT LDSQVAFTCC SKSELSSKLS
SIIDGETSHI FRFIKSPRSI VLCFGGQVST FVGLDRTVYD CISLLRYWLD QCDSLAQSFG
YGSLFPGIFE HNPIIDQIQL HIQLFSLQYS CARCWIDSGL AVEAVVGHSF GELTALCISG
ALSLGDTITL IARRAAIIRD GWGHDHGAML AVEGNKDDIM RLIDEACRNT PTNVAPATIA
CFNGPSSFTL AGTTAAIDGI QATLKTPSYI SLKAKRLFVT NAFHSDLVDP LLPALEDVMC
GIHPQEPIIP CEKATENACT GTVTSDMVAK HLRQPVYFHH AVQRLAEKYG PCVWLEAGSN
STITYMVNRA LVPSSGHHCQ AVNITTERGM QSLSDATVSL WKASVSVAFW GHHSQQAQKY
VPMFLPPYQF EKSRHWLSNK KLPGPAHEAG ATPAVSASAL RFVGYQDTQQ LVARFSIDTA
HPQYQESIAG HVVSHTSPVA PASFMLDYVV EALRSLPECK GKIPQVQNVT SDAPLCLDMS
RDLWIELYAQ DTHKHIWDLR YLSEQLQIGR RSQVLHCSAR FTMFDPDDSQ IRSEFTRYSR
LVSHRHCKEL LNDPNISDII QGRNVYRTFA EIVDYSEPYR GVQKLVGKDN ESAGRVIKRY
TGQTWVDTYL CDSFSQVGGF WVNCMTDRAP SDMYLASGME MWMRSPIYAD PTTPRPDTWD
ILAKHERGDD CYTSDIFVFN PTTGQLVEVF LGMQYTRVKK ATYSKIIGKF MPQCAAHSSD
VNKLETAVPH AAVPVPQAAK AKSDSSGPKS RINLTARIKE VVAEFCAIDP SEITEDGNMA
DAGVDSLMAM ELAREMEEAF HCTLPAADLM EADTFRDLVN CVKGAVGECD SDEHENSSRS
SEEISFKDRS PDGDYNTPDT EPPTSVASDT LDLELPLESV LEAFGETKAL TDHFLADNKC
SGRIHIFAPL QNELCVTLTL EAFEQLGSHI RTASRGQRLD RIPFDPQHQE LTNYLYKRLE
EARLVHLDGN TVIRTAISAP NKSSLSILEE IKCSYPEYAG ASKLAYFTGS KLASVLCGEQ
DGLQLIFGTK EGQELVSWMY GDEPHNVVGY MQMLDFIKRL IQKVPRTGAE AGALKILEMG
AGTGGGTKWF LPVLSKLDIP VEYTFTDISP AFLAQARRRF KEYSFVQYRI HDIEKPPPDD
LVSTQHIIIA SNAVHATSSL QESTRNMRKA LRSDGVVLML EMTRPAFAID IVFGLFRGWW
VFNDGRNHAI TNEHRWETDM HTVGYGHVDW TDGHSPEVSV QRVIFATATG TQSERLPLGK
PLEKVHPVQK VDNASRRKVI DKYIRRSIET FTLPVTSQNG FGSDGQVVLL TGATGSLGSH
IVAHLAQRQS VKTIFCLNRG NPNEEPFQKQ TSALKKRGIP LATHEMCKVK ALTATISHHK
LGLSSELYDT LKTTVTHIIH NAWPMNGGLK LSGFEKQFEA MRHLVDLASD IACHLPTESK
VRFQFVSSIA TVGHYPIVTS QNNVPEQSTN IEFVLSNGYG EAKFVCERIL QETLQRYPSR
FQVMVVRPGQ IAGSSSSGCW NTAEHFPAMV KSAQTLRALP DLQGDLSWTP VNDIAASIVE
LLLTDNTPYP VYHLDNPIRQ PWHDMIRILA SELSIPTGNI VPFSEWIQRV RSFPGSREDN
PAGMMADWLE ENFERMSCSG VLLETTRARE HSSTLAGVGP VSEEVTRRYL HCWKQCGFLH
//
