ID C5FYP9_ARTOC Unreviewed; 2225 AA.
AC C5FYP9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
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_07466 {ECO:0000313|EMBL:EEQ34647.1};
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:EEQ34647.1, 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).
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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DR EMBL; DS995707; EEQ34647.1; -; Genomic_DNA.
DR RefSeq; XP_002843683.1; XM_002843637.1.
DR STRING; 554155.C5FYP9; -.
DR GeneID; 9225770; -.
DR VEuPathDB; FungiDB:MCYG_07466; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_3_1; -.
DR OMA; KDNIGHT; -.
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:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR049492; BD-FAE-like_dom.
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; IPR001375; Peptidase_S9.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF21; NON-REDUCING POLYKETIDE SYNTHASE AUSA-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF20434; BD-FAE; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
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 418..834
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1688..1762
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1794..1871
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1768..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1768..1783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2225 AA; 244440 MW; AAB4120D3C7057E1 CRC64;
MQNTEDGSDG NRRVCSAWFR PQGMITSKMM MESRTLLRET PGLVFLLNAI FELPELWPVI
VEAMPQLCKL PAQEKLTELC RFFKGGQLTV LTEPISNLLQ SPLSVIIQIV GYLRKFNHGF
GNTSHLVDVQ GFGLGFLTAI VISCSKSEAD FRELAPKAVR LALCMGAIVD ADALENGHGP
VSAIPFRQGS ATQPQDLKDI LDIYPKAYIS CISYAGGVTI TAPETDLASL IVDLAKHDIK
ADDSSDFMAR VCHFGPRVQR LTQNASSISL PLRGRWHHRD NLNGAQAISA LCERDNRFRL
PSADAVKAFL LSNISGTTIT EGALHNIALR SILTDPSRWD LMVKPLLNLA TMLNIKLVAI
IVGETADTNE PVSFGVQGAT VNPKEEDYET FDGDFQVSSF TEPVPKGLDF KDADVIPESA
IAVIGMACRY PDADSIDEFW DLIRDGKCAV RQMPKNRFDP SELVREPKGP FWGGYIRQLD
LFDHRFFGIS GREAKSMDPQ QRLCLEVAYE AMESAGYYGL HADGFDTEIG CYIGSANDDY
LDNVCSHPVN AFSLTGTLRS FISGRVSHCL GLTGPSMVID TACSASMVAI HAACQALQTK
DCSVAVAGGA NSMTSSRMTQ NLIGAGFLSP TGASKAFDED ANGYCRAEGI GIVVLKSLRD
AVRNGDFVLG VITGSAVNQG RNDSAIIVPD GPSQCSLYQR ALARSGVAAK DVTYVEAHGT
GTQVGDPIEF KSIRKTFGGL NRNDNVYVGS VKDNIGHTEA SSGVASLIKT VLMFQHQMIP
KLANFKSLNP KIEPLGKDHV LIPTESLEWK IAKRIALVNN YGAGGNNAAL VVEERAITPK
MYTQITNFPI FISGKTAEAV RCYCDILKAS LGGKRLADVA YNLAIKQNRD FENMLIFGSA
NIEDLSQQLE NAASGAIELQ KLPRRKSSVV VCFGGQNGRR AHISKELYDN SALLQCHLDE
CESVLVEQLS LPSLFPEIFD ATPIDDIIKL HCTLFAVQYA CAMSWLSSGL KVDKLIGHSF
GQLTALCVAG SLSLVDAFRL VSTRARLVEE RCGPENGIML AVKGDELDVD QLLLLARQQT
KDLVADIACY NGPRSFVIAG DEASIEAIES TAASLSAGFQ FKRLENSHAF HSQLLDAIIP
IFLQDMGNLH FEAPKIPIEA CSNEDDWSSI TAEKVTRHTR MPVYFMNAVR RVETQFDGPI
IWLEAGSGSP IIPMVKKCVN SMHQHTYIPT ALQSLDAFAN LTKAICQLWS NDMRVQFWPF
HRSQHTSFNW INLPPYQFAK TSHWVDYKPR ASLVEISTTT STPMASNPDL VTLLSHNPSQ
GEALFEINPS HDLYQSNTRG HIFVDQTLVP ASMYTEFVLI ASLMISNAET GYMPQISKLA
MISPLIANPT GKVLLKLVRR ELKLGSWDFD IFSKIDDYNS LTHSTGYVTI SNPDIPVSIN
HLQALQSLML RRCEEIESSP TSIGFKGPTA YQAMRRVVTY LDYYHGIQSI YSQGNEAAAR
VALPFTRPRG MGTSFCDPVL IDSFSQVSGI LANCFSLPDD GEMWVCNYIE DMVFTQRFIA
SAREENKTWI AYSKFNIPSP KRLKCNIFII EPDTGDLVLT IMSIEFQRVS TKSLRKVLGK
LNNQPASMQN GSNQKVTVKK APIQLDSTEY SSDQADKKQI STPILPTAVP SPVPQLLHGA
SEKPQHSLGP LYDVKDMLKD ILEIPVEEIK TDSTLEDLGV DSLLATELFS EINKRFGLSI
LQSDFATVTD VWGLSKLLPG ENESLVNNST LTPVSTPRSN PSPDGTLHHP VKATRKHQLV
DKIKDMLADV LEIPIEEIEP GSILEDLGID SLLATELFSE MNKRFGVSIS HAEFAAIADV
QGLAQLLTGS RTPPSSSKIN CYPTQVDIET VVFAERDGIA LSADIYYPTD PIKSHMPLPI
ALMIHGGGHV IYTRKDIRDD QTEILLKAGF LPVSIDYRLC PETTIREGAM QDVRDALYWS
RKTLPFLPLR RGDIRPDGDR VVAIGWSSGG HLAMSLGWTS PSLGIKPPDA VLAFYSPTDY
EDPFWSSPNL PFGQKSTPPP EDGYSFLYNG LHDSPVVGYT PRVSRRALGG WMSLDDPRCR
IILHMNWEGK SLPVLINGLK RTSIKSVTNP PFPSTEQIQA ISPLAQIRAG NYKTPTFFIH
GTRDDLVPCR SSQKCYEALQ EVGVPAGLVV IEDALHLFDL YPSSKKDPVA MKGVKDGYSF
LSECI
//
