ID C5FNH3_ARTOC Unreviewed; 2214 AA.
AC C5FNH3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=MCYG_04406 {ECO:0000313|EMBL:EEQ31587.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ31587.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
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).
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DR EMBL; DS995704; EEQ31587.1; -; Genomic_DNA.
DR RefSeq; XP_002846669.1; XM_002846623.1.
DR STRING; 554155.C5FNH3; -.
DR GeneID; 9229780; -.
DR VEuPathDB; FungiDB:MCYG_04406; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_2_1; -.
DR OMA; VWHVYAR; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; 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; 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 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; 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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF14; ITERATIVE POLYKETIDE SYNTHASE AFOE-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 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 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; 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 Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 389..812
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1670..1744
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1647..1666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1750..1787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1768..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2214 AA; 243544 MW; 5541E2699E5D7B5A CRC64;
MQNIGHNLLI FGSQIAYSEQ AINGIKKTLQ SKLCRQWVLD IVAGLPNYWD ALNKELPMFL
GAASYEGRQL LENFHVWLES DGHKGIDIQG GTLPAAVFVP LIVLAQLTEY RQYLQNKSKG
AMSDPQVDQV TRKEPVLGFC MGLLGAYAVA SAHNMEELDH YGAVAVRIAM LAGALSDTQH
KRNPHRTYAV AWTNAKQQQD LWNIVGGISP DAYISLLFDE ARATVTVSER AAARLVRKAR
AAGIVLSDTG FQGELHSPNG NYKKEIQHLI VFCNKRQDFQ FAKVNRLALM TFTNAGNGKH
LEPGDNTLHS HVLETLFARQ CDWYGTFSAI KSAYLDSSEA SMIIFGPDRC LPPTLVRDIG
SRAVYFADVQ EQPDLWRNDN PTNGNIDDDN AIAIVGMSIK VAGADDLHEF SQLLRKGTSQ
HEKVTRERLN FDSLFRKPDT RDYFCNFVHN IDAFDHRFFK RSPRESAAMD PQHRLLLQAA
YQAADQAGMF TEIMRARREG IDRSHVGVYI GSPSVDYEHN VATHPLNAFM ATGNLQSYLP
GRVANHFGWT GPAIAFDTAC SSSAVAIHTA CNNLRNGECY AALAGGVCIL TNPHWFQNLT
EASFLSPTGQ CKPFDEKGDG YCRAEGVACV FLKRMADARA DGNPILGRLA SSAVYQNQNH
TPIFVPNSPS LAQLFGDVVR KAGVSPKDIA LVEAHGTGTA VGDPAEWAAL RKAVGGPIRS
QPLPIGSVKG HIGHTEGSSG VISLIKVLMM MHEGYIPPQA SFSKLNSTIK AAADSDMMEI
VTSLRSWDSR NKVVLVNNYG ASGSNAAMVV AAPTTSIVSE HQGQGVAPSI KMLEGRFPFF
ISGFDARAVK EYAVKLAALI RTQPRSALAD LSFNINRQSN PDLPQRCTFR CHSVNDLQRT
LDSVSEAGMV ETQAERPVVL CFGGQVSTFI GLDRKLYDCI AIFRHHLDEC DKMVKGELGL
PSIFPGIFSR TPLPDPVTLQ VALFSMQYAS TQTWIGCGLA GKVVSVVGHS FGELTALCIS
GILSLKHALK LVSCRAQLVR DEWGDETGAM MAIDGNESLV QGLLEHLRQQ LPNNPATIAC
YNGPRSFTVA GSVTVIDALV EAIAGDRFSG LKSKRLNVTN AFHSTLVDPL VDRLEQVGND
IEFNEPLIPF ERATETAFTG PLTSKFVSEH MRNPVFFSHA IQRIAKKYPS AIFLEAGSSS
TITVMASRAL TEQVRKFHHF ESVNLTNDKG LDGLTDTTVS LWNQGLRVAF WAHHALQTKD
YTHILLPPYQ FEKSRHWMDF KSASELVASL AQNESVNDPK SLPLWEFVGY QGNDTKHPRF
RVNLVSETFK RLVSGHVFAH TAPVLSGTVQ SDMAVEALLS LHPAWREQGM IPTMLDANIP
TPICVDSSRK VWIDYEAVNV EHTMWQLNVS STSAEGTLPR RHLHGRLHIR SPADPTFVAQ
FARFERLVPY EQCARLLAEA GGPDVDVLQG RQVYRAFSEF IEYSDQYNAM HAVVGKKTEC
AGRVHRKHAG ESFLDIALHD SFKQVSGLFL NCMSDAKPGE IHIGSDVELV MRSPRGILQP
GQTQDIWHVY ARHSQVSAKV YMADAFVFNA ANGELVEVIL GLQYTRMSIG SMKRLLMNLT
RDEWALNMNA NGATEIPTLK ISRSVVESDS KTRREENKEA KGVSSQPQKS ALTVEIKKVL
ASVVGAEVDT VSVNTIAADI GIDSLMGIEL LREINTAFDC KLDLPELLAA ITVGDIVTLV
TSALSQGAWR AAATDDSNED SVGDSSREKS HPTTPASASE PETPISTDDF LAIKSKNGDF
EEQMRTDIRS REAEAEGYVR EYTAGWMSAK PTHTSEFVTN SNDAATVIVT GATGSLGAHI
VATLSLNSSV KTVVCINRRR PMPAETRQEN AFSSRGITLT PEARSKLRIL ETDSSLPNLG
LEISEYQWLT RHGSHIIHSA WPLSGSRPMS AFTSQFQTMR NLLDLARDMA ASRRVGFQMV
SSLSVVGCSK ESVVPEDRVD MDSVLPPGYG EAKWVCERML EETLHKHPTL FRTMAVRPAQ
IAGSSISGVW NSVEQIPFIV KSAQSLGAWP KFSGTVRWIP VDAVAEILVD LLYIGDKLAP
EPWPIYHIDD TVGRPWDDIS SIFTSDLGIP ESRLMPFKEW LDVVASSSKS ETENPAARLV
NFLEHNFERL SCGRLILDTM KARQHSPAMR ALAPVGVEVA RSYIRAWKET GFLD
//
