ID F2PXM4_TRIEC Unreviewed; 1579 AA.
AC F2PXM4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=6-methylsalicylic acid synthase {ECO:0000313|EMBL:EGE06642.1};
GN ORFNames=TEQG_05640 {ECO:0000313|EMBL:EGE06642.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
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; DS995750; EGE06642.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:TEQG_05640; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_35_3_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; 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; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
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; 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; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF46; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
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 SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 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; PS52004; KS3_2; 1.
PE 4: Predicted;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 30..436
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1500..1577
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1477..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1579 AA; 171489 MW; 0D5A7DB450B3C600 CRC64;
MSSVITNTPC SSSDVCTDYP VTAYSTEDQY KDVAVIGMAC RVPGGIQDPE SLWQALLEQM
VACGDIPVHR WEPYHKRDPR NKKILGQTTS RGYFVDNIED FDYQFFGVSP HGKHAGIPSK
SLSGSDTAVY WGVNSNDYSR LVLEDLPNID AWMGIGTAYC GVPNRISYHL NLTGASVAVD
AACASSLVAV HHGAAAIATG ESRIAIVGGV NALCGPGLTR VLNKAGAVSP DGQCCSFDED
ANGYGRAEGA GAVILKNLSQ ARLDGDHILA VIKGTAVGHN GRTNGIMAPD SKAQQLVARN
ALQAANVDPD TVHYVEAHAT STALGDPTEI NALTEVYGEK HSIDKPCYIG SIKPNIGHLE
AGAGVMGLIK AILIVQKGLI PPQANLKTPN TKIKWNESGL KVVQELTDWP DDTGPRRAAV
CSYGYGGTVS HAVIEEFQEF SPILHNETSD SFNGHLLLLS APHEQRLAPL AQSLKTWIEQ
QDKTKFDLAM FCKTLAGRRS HYEFRTSAVI HDIEGAIAAL DCICKGANNQ WITRSRVLPS
DLAKDVVWVF SGHGAQWTDM GKGLINNRIF HDAIQPLDKI VEGEINLSPI EWLQCGDFDS
SDRVQILTYI VQIGISALLK SRGIYPQAVI GHSVGEIAAS VVAGALSPEE GTLIVTRRAI
LYRQVMGKGS MSLISKPYQE VREELGKASE VAVAIDSSPT SCVIAGAKDS VAALTRNYQD
HGVKTYTVKT DIAFHSSMLD PLREPLAAIL QGALNPARPQ VRLYSTSLLN PRGTNPRDST
YWVNNMTNPV RLTSAVLAAI DDGYRRFLEI SSHPLVSHSI NETLMEAGIE DYSIIHTLRR
DQPAEKSILH AIGQIHCSGV EISWNSQMKG LWMQDVPLSP WVHRPIAQKQ PVHSTMGMVA
DVHDVDTHTL LGRRTAIAGT DLVVHSTTLD SSTKPFPGSH PVFGTEIVPA ACLLNTFLKA
AGNSSLQNII LKVPVATSGS RTVQIVIQGD EAKLMSQLIQ NESVEESSWV THTESRCAAR
TEAIAEVIDL SEIKTRIGTR LDDDFTIDYL AKVGVAAMGF PWKVTEHYGN ADEMIARVDV
SPNSVNPDWD QSSWAPLLDA ATSIGSTIFF SDPRLRMPAQ IQQVDIWTSQ DPPKIGWIYV
KRDTSIDYSG HVYILSEDSQ LLAKFTSMRF SEIEGTPGAS GSMSSLVHRV AWPPAYPAED
PIPIQRVIMV AMSNTIRDTY ARTLPAKIQL DQLTTIEALR EALTAIENKK GTAIVYIPED
VQSLEEIRDL EKQGVCVHIS ALDLSTSQAA GRLLEKLDQL NLPPVLGVVH AAGVLENELI
QDATQDAFAR VFSPKVAGSL ALHEAFPPDS LDFFVLFSSC GQLFGFPGQG AYGSANTFLD
ALATHRRNLG EDAVSFQWTA WRGMGMGSDS DFVAAELESK GITDVTRHDA FQAWLYLIQF
NTDHGVVLRS RSFEDGEPLP TPLLNDIAIR RARSITDSPS AADGNSSSGT CKKLPSSGPE
LKAYLDKQIR ECVASVLHLP STDVDSRIAL SDLGLDSVMN TALRQLLQRT FKVNVPPTLV
WSYPTVKHLV GWFSEKLAK
//
