ID E4UU00_ARTGP Unreviewed; 2371 AA.
AC E4UU00;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Non-reducing polyketide synthase nscA {ECO:0000256|ARBA:ARBA00018393};
DE AltName: Full=Conidial yellow pigment biosynthesis polyketide synthase nscA {ECO:0000256|ARBA:ARBA00031359};
DE AltName: Full=Neosartoricin B biosynthesis protein A {ECO:0000256|ARBA:ARBA00033379};
GN ORFNames=MGYG_03811 {ECO:0000313|EMBL:EFR00806.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS989824; EFR00806.1; -; Genomic_DNA.
DR RefSeq; XP_003173636.1; XM_003173588.1.
DR STRING; 535722.E4UU00; -.
DR GeneID; 10028919; -.
DR VEuPathDB; FungiDB:MGYG_03811; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; E4UU00; -.
DR OMA; IMMDTAC; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000002669; 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: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; 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:UP000002669};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..434
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2287..2361
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2371 AA; 256728 MW; 4E1F1F75274F5E56 CRC64;
MDCSDKQEPI AIVGAACRFA GEVSSLGSLW DMISKVKTGH CTVPGDRWNS SHWYHPDPDR
KGSIGSQHGY FLQQDISHFD APFFSITAKE AAAMDPMKRL LLEVSYESFE NAGIPVEDLM
NSRTGCYVGS MRNDYEMIST RDFYDISHPA ATGLSGAMTA NRVSWFFGLK GPSMTLDTAC
SSSLYALHLA CQSLRLRETN MSLIAGVNLM INPNTMNQLT AMHMLSPEGI SHTFDDRANG
YGRGDGIGAL IVKRLSDAIR DGDTIRAVIR GTGVNADGKT PSITQPSSEA QADLINQTYT
DAGLDQSETE YFECHGTGTP VGDPLELNAI ASTLGAARRT AGKSPLYIGS IKPTVGHTEG
CAGLAGVFKA ILLLEKGMLV PTYGVEQVNP KLKLTEWNLA LPQDIVTWPS AGLRRVSVNS
FGFGGANAHI ILEDAYHYLQ ERGLAGRHNT TIHDSGSDSG VDDAPVNGAV HDESKQLFLF
SSKDQAGTKR VSEGINTWLQ SDSTDKSCPY FLENLAYTLA LRRTHLEHRT FAVASSLSEL
TKKISQGLPA ATRAQRHGDN LVMVFTGQGA QWAAMGRGLF ENPIFRQSID DSQSHLQALG
CKWNANEELT KIPNPNIDRP EYSQPLCTVV QVALVDLLRS WKILPTATIG HSSGEIAAAY
AASFLTQSDA IKLAYVRGLS SAAISKQGAM MAAGLSEDDA QIYLEKVPQG SAVVACVNSP
SSVTLSGDVD AINQLEALIS SDGKFARKLK VATAYHSPHM REVSPSYLEM IGELSPRQRD
ESDSSSPVMY SSLTGSMVSS AEELSAQYWV DNMQNPVRFS QGFLALLKHK RVASGSTRPV
AIHWGGFLEV GPHAALKGPL RQIIDASNNK FAKSAPYASM LVRGKDARET SLDATGVLWA
AGCKIDMGAV TQHPTVNTTP QMLCDLPSYP WNHTRGFWHE SYTSRSHRFP SHERSDFLGI
PEDSPNSHEP RWRNYLRISE NPWIEDHTIT GTVLYPGAGM LVMALEGVLR TADSSKTVDG
FRFNDVMFER GLVVSLDDGL PVETRISFHP HGIKPDSWTF TVFSMTKGSP WAKHCSGTVA
LVYEKDESEV EEGRVDPFWQ KQLDLRKALL STADSMVINV DEFYKNLDSI GMQYGPVFRN
VVSLTLVPSM GASHGSIAVP DTRSTMPKHY EPPHVIHPAT MDSIFHIMLA SLNNGQPVKQ
AAVPYSIEEM YIARDQPQEP GALYSGYGRL LSQSGHEIAA ELSVSDQEWE KPKLSIKNFA
LRQVTSGDDR EMAGSILPGT TKNCARITWI PDLAFVTRDE DHTKLVSSRE TAALINSLLD
PLFLKMSSNT VLVVMFDESK SSTDLLLDLK NRTYGPKKII ALATSESGGQ LMRATLGEST
EKTTIIYNEW LPENELLQTL APEANDLVIG LGVPDVSKNA TTLMKLAPLA CLTHASQPDE
VDIVIPASKL VSHFVGDTTG VLFASSTSSP SAVLPDSVIL LLPISPSDTL RTFATTIQAK
LENCSVSVSQ KILTPCDVAS LSGQSVISLL EVDNPLVYAW DEDQFHAFKA LVSTVERLFW
ITHGSVLESW SNGIEFATSQ GLLRVLRNEY PVTSLPSLDL SAAADISSGL YVDLILNVWR
ASLAEDAEME YAESNGLIYI PRAIEDAGFD YELQLASNTA KPVMSALGAS GKPLKASDSL
NTQGCIWVPD KEAESSLQAD EIEVKVEYAG LGTSKTLSSA HHAVGIVTRR ADSAKAFELG
QRVIVFSHSA ARTHVRQAQS LVAPLPEGLG PQEAVALVEP MITAQYALIE IAHLKRGQAL
LLDNAASAVG QSLIRAAKAV GANIFALVRS KAERGMISDV FGIPTDHIFD SALDSFVPFI
QSITYNCGVD VVVNQQSGAH ISRAMSVLSD FGQFVDINGG STKALLPTSK ANFTFTRIDM
ATLMQSRPSI ISKLFQRAFN EYTFQERSPL TVLPVTNLSA STNNTSAEQV VVSLTDASSV
PMHATYQELK LDSQATYVLA GGLGALGLDI ANWMVECGAK NLVFLSRSGG SKNEDDLQKF
AERSVRAEAY KCNVNDAVSV AQLFDSLKAS GRRIAGVIQL AMVLEDGIFE NMSFAQWRRA
IEPKTKGSRN LLANIWPGDK PFFILLSSIT GVIGNTAQAN YASGNTFEDA LAHHARAHLG
INATSIDVGL VSDSSHFTAA GEFGDLSSYL SRYQHGWRGL QTNLKELGVV MQAIMRRSTT
LGQSAPAQIV LGLGDRIEHN ESAGGFSKDK KFELRVVKTG NDASDGKATQ DVGVLLSNAT
SMAEAAVVVE DNIKELVAAA MGVPPEEIDS QKPLYDYGVD SLQAVEVRNR ALKNMRGDIS
VFDILSAMPL AGVAAKIAAS SQWVNITADE D
//
