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Database: UniProt
Entry: A0A1Y2EIB5_9PEZI
LinkDB: A0A1Y2EIB5_9PEZI
Original site: A0A1Y2EIB5_9PEZI 
ID   A0A1Y2EIB5_9PEZI        Unreviewed;      3872 AA.
AC   A0A1Y2EIB5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Polyketide synthase 3 {ECO:0000313|EMBL:ORY71044.1};
GN   ORFNames=BCR38DRAFT_479572 {ECO:0000313|EMBL:ORY71044.1};
OS   Pseudomassariella vexata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX   NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY71044.1, ECO:0000313|Proteomes:UP000193689};
RN   [1] {ECO:0000313|EMBL:ORY71044.1, ECO:0000313|Proteomes:UP000193689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY71044.1,
RC   ECO:0000313|Proteomes:UP000193689};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORY71044.1}.
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DR   EMBL; MCFJ01000001; ORY71044.1; -; Genomic_DNA.
DR   STRING; 1141098.A0A1Y2EIB5; -.
DR   InParanoid; A0A1Y2EIB5; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000193689; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
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:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd19532; C_PKS-NRPS; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; IPR029058; AB_hydrolase.
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; IPR020845; AMP-binding_CS.
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; 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; IPR013595; Pept_S33_TAP-like_C.
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; IPR013968; PKS_KR.
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; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR   Pfam; PF08386; Abhydrolase_4; 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; PF13489; Methyltransf_23; 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; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
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; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193689};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..434
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2384..2461
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          2468..2520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3125..3144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3872 AA;  424756 MW;  7CE89A5AD814F559 CRC64;
     MYEPLAIVGT ACRFPGAAKS PSRLWDLLKA PRDVLKEFPP ERLNTANFYH NNGDMHGRTN
     VEHKSYLLDE DVRHFDAAFF HLNPKEAADM DPQQRILLET VYEAFEAAGW SLSDVDGSQT
     SVHVGSMTED YTSIQSRDPD MSGSHVATGV SRAILSNRIS YAFNLQGASL SLDTACSSSL
     VALHLAAQGL HRGEATQAVV AGTNLLMDPF WYIAESSMHL LSTDSRCRMW DKDASGYARG
     EGCAAVVLKT LAQAVRDGDH IECVIRGSLV NSDGATNGIT MPSPAAQSAL IQQTYRNAGL
     DPITDRCQYF ECHGTGTQAG DPVESQAIRD TFFPDNKHED DSILYCGSIK TIIGHLEGCA
     GLAGVIKASL AIQNKAIPPN MHFNQLNPKV EPFYKNLEVP TSLMPWPEIH DAPRRASVNS
     FGFGGTNAHA ILESYEPSET IVSSLNSSTS EIMDDSVYQS MVGGRIGGPF VFSARSRTSL
     VNWLKQLLTY LRENQSLDLD SLSSSLYSKR TAFPYRVAIP AASDLDDLVQ KLEDQINTIS
     TSMDGSGAGA GFAAPKSLRI LGIFTGQGAQ AARMGCALLE HCKLFKESII ACEEALKCIP
     EPPPWSLSEE LAADATKSRV SEAKFSQPLC TAIQIGLVDL LRACGIKFSA VVGHSSGDIG
     AAYAAGLLTR KDAMGISYYR GHVAHLARGD AGESGGMMAA AMPFDAASAL CSEPRFKNRI
     NVAASNSPSS VTLSGAKDAI VEMKEHLDRI NIQARALQVD VAYHSHHMLA CADAYLGHLK
     QLDIRIQTPP TDQECHWYSS VRANTNILER PFESGLEAQY WVDNMVQPVL FSEAVKLAVQ
     VVSARFSAAM EIGPHPALKG PVNQTFKQSI DYTPQYTSCL SRGNDDIETF SEMLAMIWTI
     DPSSIDFASW RKAFGLAAQP QVLKNLPPYA WDHTQIHWRE SRVVRNYRLG KQPPHDLLGR
     LWNDAQYEHT WRNIFQLKEM PWVKGHVFQG QVLFPATGYI SLAVDAAKAF ITGRPIKLVE
     VLDMAIPTAL VIGEGDEVEV LFTIRSRVSP EKVEDGSILE AEFACYSYPD GREADKTCDG
     RLLVHLGEPE PEDLAPTNIS NVELTPFNVD RFYRAASDIG FGYDGTFRAL TSLNRCWGHA
     KAVASWPKDD LDVCCTLHPA ILDVALQAGL ATFVSTAERS MPSSYLPVGI KRALVHPNVD
     FLSLDGSTNI EIEAYMTSPE LGKLMEADIN VRAKKGTRDD LGGIQLEGVR FKAISEPQPS
     EDRNIFAKTV WGLDAAYGLV QPRTAEISAR SSMYTPEEYE RVALFYLQSL ARSVNARELN
     VVKHHHQDLM RFIDATVAQL RKADHPVLMR EWLNDSSDTI KHLLSRDPSD VDMAMLASSA
     EWTLTLLEGT SEYTHESLPS SFYHNRSSAT TCNEYIAQLV LQISHQFPRT NILEISAGVR
     NTTSTILGTV GDAYAHYTCA GASETVIKSL KEKLVPAETE NVSFKVFEVE ADLASQGFEA
     GSYDIVIATD VLRASRYLSR TVQNMRRLIR PGGFLIAMEF TGTSLRPTAI MGGLETWWAG
     VSDRGTASPV ITTGEWDKLL ERHGFSGIDC TLHDQANVGM HGFSVFSSQA TDDRLDILRD
     PLISMDMITP PPVILIGGET SKVSRLVRQA EKMVRGWATE IQAYSRFDQI DCSRIPPGAS
     VISFQDLDKP LFSSPPSPSE LRNLKQVLDI SRNILWVTSR RMADDPYANI MIGIGRSLRL
     ESPDTTIHYL DFDEDEPWDI QVLMAQFLRL IFSSSLGVAE GMLWVEEPEI VIKDSQILVP
     RILPDQISNE VYNAKRRQIT KLVEPAEPIE IAKDVDSADS VLICSRSLDL PENHVPIQVK
     LSVALHDGNE SPCFLCYGNV KDQGDRVVLT LSETDSSVAH VREDSDFSSL GLQECDAEDL
     ANLASFLIAS HVVSNIPGHG TTLVCGASDR LADAIRLVVA GAGCKALFVA ISKERQSEHD
     GWLYVHPQST ARSFQQMIPR GPINLYGLSK KNTDTISRWL PAGCTSVEDA VRVYSTHQES
     LASASKPAIV NIHELPQPRD SSPVRLSVVT NWKRESSVGA ILRGLEPSAL LSPDKTYFLV
     GMASELGQSL TYFMIRAGAR HIVLSSRNPK GGQNWIHDLQ AIGIEIRVVK MDVTSRSQVR
     ETVAMLRRTM PEIGGVTNAA LVLEPAIFAN LSAESIAKQM KPKIYGTANL DDEFKTSKLD
     FFLTFGSLST VCGNAGHAIY HAGNAFMMSL VQNRRRRGLA ASILNFGMLV DVGYVARSDR
     SAGPSVEEWL RTDLPTALSE ADFHHVILQG IAAGHPNSPS GEVIMGLEMF HDQGQSSKPR
     WANAPLFSHM VRVSKASKDG QADDAPSSIQ RWQQNLEDAI SFDEAIPPIT ELLSRKIESM
     IHVSLHSIHP DEPMSHLGID SINAIEIRKW LREKLEADIS MLKILGRDSI SSIIRTVAEQ
     YIAKRPATKS MSKGEISTAE VPQPNKTLAP KADPNAQKES TGPTLSNHGH DARDSEASLT
     SSQCLTGISN QIPGPQLPFI RSERLSYAQA GFFYLSAFSD SRTSFNLTGR FRIKGRLDTE
     RFCRAFDQVM HHHEALRTCF LATSGSSEVM QHVTKNATPQ ISRLQSTKET AKVDVEKAFD
     EIAKHEYSLA TGDTLRATLI SHGAQWHTLV IGFHNIALDA VSMRLLFADI DRAYRFQTLS
     QDSASYLDFT RQEIDDVQAG RLDESIDYWK RLLDPIPEPI PLLPTAKVKT RQNRRSYGYH
     LVKRELSSEL VQRVTQISQA HGVTPMQFYL AVMRVFLCRL LDIDDICIGV MSHGRDPTSR
     FGDTVGHMAN ILPIRFKGSW GECFPEVLEN TFKTLLDSFD NRNVPFAVVL EKIQALRSEG
     GMPLVQVAYD YRVGENVANS VGGCTMELEE TIYTTLYDLT IDVLQSTSHG HLLNIRCSDD
     FYSLSTTEFI AETFVNVIES LAPDPSVAVK DIGLFSDTQL QQATTVAHGA DVEHSWPQSL
     SERFEQVVAN FPGSVAVKDG NEAITYNQLK QLVEIYANIL LEAKTTAGSL IAVLCEPSID
     LYATMLAVFH IGAVFIPLDV SVPAARRNDM MKACQPDLLV FHAATAASAT EDHGEYRSLN
     IAEKARAHPR HARSPERTVS DPGSDSYILF TSGSTGVPKG IKLHQRGMMN YAAYTSKAYG
     FKQVRVLQQT SIGFDLSFAQ IYNAFTNGGT LVVASVEARG DPDMLSRFII DEMIEYTIGT
     PSEYNLLLSY ASDVLQQCRS WRFCHTAGEA LPERLIEGVR ELKLPNLTLT DAYGPAEAFI
     VTNRNIQVHA GAIQDECNNR AGSVGYVLPN TSVYITSESD GSLLPLGVPG EICIAGSGLF
     NGYLDTELGD EKFVENPFAS AEYLEQGFHT MYKSGDRGIL HADGSIVFLG RCFGYNAMIK
     LRGLRIDLNE VTGAILGAAP NDLADAAVTV RGDPQFLIIN ITGASTIEPA RGSILINFGG
     PGGDGQQNLA ATAEFLQNMT GGFHDIISFD PRLFAQIPNT ATANSSDTAL GHIWAEAMLS
     SDACLNGMNE SGTLVGTAFV ARDMMKIVDA LGEDGMLRYY VLGATVASMF PDRMDRVLLD
     GVVNPDDYYH GPDTVTFTDT DKTFRSFLSG CVTAGDACAL AHRNQTPAEL ESSIHDFLQI
     LKYEPIPVAG LVLDYSIFKA TLLGSLYWPS GWPQLAAALD SMLSNDIDTL AQHLDYLVTP
     AASIQYEALP GIKCSDKFPR LSSSKALVPI MEEFYEISEW CGETVANLVS QCAQWQFDAK
     ERYDGDFQVQ TRNPVLLVGN TFDPVTPLAA AQNVSAGFDG SVVLQHNGNG HSSWAQRSAC
     TMKAIADYFV NGTLPEPGTV CEVDAPLFSE TE
//
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