ID A0A139IAG3_9PEZI Unreviewed; 2252 AA.
AC A0A139IAG3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KXT11738.1};
GN ORFNames=AC579_5038 {ECO:0000313|EMBL:KXT11738.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT11738.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT11738.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT11738.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-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:KXT11738.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFZO01000184; KXT11738.1; -; Genomic_DNA.
DR STRING; 113226.A0A139IAG3; -.
DR Proteomes; UP000073492; 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:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 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; 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; 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:UP000073492};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..439
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2158..2235
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 455..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2252 AA; 243387 MW; BA04D5A5C222B94C CRC64;
MACNTDDKLM EPIAIVGMGM RFPGESHSSD SFWDLLSKGR DGWRTMPKHR FNLDGYYHPD
GARAGSVFVK GSHFLSGEYE KSAKQFDAPF FNITASEVEG SDPQHLHMLE VSYEALENAG
IPMQSVIGSD TSVYVGCFTR DWEAKGGRDP YTGPFYAATG NGMSMLANRV SWFYDMRGPS
MTIDTACSSS LYAVHLACQS LRTGEAKMAI AGGTNIICDP CYMRDLTTMG FLSPDGRCHS
FDHRANGYGR GDGIGAVVLK TISQALKDGD TIRAVIRNTG LGQDGRTPGI TMPAPEAQAD
LIRLVYKNAG LTMDQTAYFE AHGTGTPIGD PYELSALGAT FGKTREPTNP LYVGSVKANI
GHLEGGAGIA GLIKAALVVE RGQIPPLADF EKVNPRLKLD EWKVALPLKL TPWPVSGVRR
ASVNCFGYGG ANSHVIIDDA YHFLQEHGLK GHHQTILGPH DIPEISDGSD SGFSSAAPST
PADNTDRELS RPLLMVLSSV DQAGLGRSAA ALTDFISQQA DREAQDKQLE TASAGVDMES
FLPDLAYTLS HRRSTFDHRT FVVARSVSEL QAQLSAPLSK LRRSAKNSNV FFVFTGQGAQ
WATMGKSLLA FDTYRRSLER AQAQLSRLGC AWNLVSELCA PKGQSHIDQP EFSQPLCTAL
QVALVDLLEE WNLRPKSVVG HSSGEIAASY AAGFLTHEQA VKVAYCRGLF SADVNRRLGD
KRGAMMAVGL SEADVKPYLD QVPKESVVIA CVNSPNSVTL SGDEPSINVL EKTLQDASVF
ARKLRVTTAY HSPHMRVIAD DYLAAMDDIQ QSTEPPKATM FSSVTGGTVL KAVDVDASYW
VKNMLGCVRF SDAVQALLTQ PANPNAKGRR RAPVVYSAMV EVGPAEALKG PLLQILNATD
GRLASSLPYT ALLSRNVDGG QSALAAAGKL WASGLPIDLH RINFPTEPEQ PLQSLACLPP
YKWNHKVYEH ESTYGKTVLR RAKPRTDLLG FVDETADESE PRWHNYIRLT EQPWLGDHRV
QNMVLYPGAA MVVQAIEAAR TLQDASRTLK AVEVRDIAFK KGLVIPAGDA AAETAIHLKP
EKVPSSDETA WSFSVFSKTG EDPWNEMCTG SVSLLYSGED YGESVRQWTS ESSLYDDIRK
RACRVVKAAT FYKLFDDKMN LQYGPLHRNV TEATAGFGEG YGVVTIPDTK SVMPSQFEYP
HLIHPATLDS IFHMQALGYL HSLSGDESLV PISIDKIYVA ANAPTEAGTQ LRGYSKGTQS
SSGDTVGDIV LSDDAWQEPK VIVRGFLSRD ISAAAPSSAS AIDNAPRKCT RLDYVPLHPE
ESSGSSAQSD DGVELASPAS RLDQLIVLHA STESLDLPLV VAEISARLAT SCEHIVQMHP
EQVTFGEKSN IKDKTVLSLL EAEESFVDGW SEKQFSWLRD LASTAETILW VTRGADVGSP
ETIKFSATNG LLRTIRVEKP QLRLFQLDLD TTSALYSDTS IDLIVDAFET SVLSTAKAVE
QEFVQIGDKL HVPRLVTDES FHAELKSGAT NSAPILQALT AMPYPVRAIV SQGGRSLCFV
KDDQYEAELA EDEVEVAPCV TMLDAAAFEA GLSLGRDAVG TITAAGAAVK DYSVGEKVLV
CAASCLRTRL RVKSSFVRKQ PDFIGDAVAV TLPTALTLAW LSLLELGFLK TGESVLIAAE
PDATTGAMIY LAQHLGAKVY ASFTTAYHHR WLVEQIGLEE EQVIKADRGD NFKETLLRRN
KGKGVDVVVT SNAHQSFNVL APFGRCVCLG SNQTLSSTAQ LALGVSIHNL DIEHFRAAAP
DRVARAYQSA WSLASKGVFH TLPPKRALSL ADFAAQTNLP DAVKAPGGVA VTVDPASNVW
TLPPPPAVLH LDAEATYVLA GGLGGIGRSI AETMFAAGAR KISFISRSGA KTEEAKKLLS
SLQQRGCVAK AYAVDVSSSS AVEAFVQASI ERGESIKGVV QAAMVLQDSV FDNMTFEQWT
RSTAPKIQGS WNLHQHFPRD MDFFIMLSSM AGIIGNPGQA NYSAAGTYQD ALSVHRRKQG
LNSTTIDLGI VSDVGYIAEN PEQFERLRYL KPLFISERDL RLLLSAAMLG KTMDGNDVPP
QVVTGVGKEL MQDGSIGSAM AADLKYSSLH GSSGNDAGDA GEDEAAQEAL KTATSLQTAT
EFVEAVFASN IAKATGMEPE DVDLDRPMHA YGVDSLAAVE VRNMIYRKFK SDISVFDLLS
TLALHKLAIR VVAKSKLVKN EVQVVAQEEN AE
//
