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Database: UniProt
Entry: F2PY25_TRIEC
LinkDB: F2PY25_TRIEC
Original site: F2PY25_TRIEC 
ID   F2PY25_TRIEC            Unreviewed;      2041 AA.
AC   F2PY25;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Conidial pigment polyketide synthase PksP/Alb1 {ECO:0000313|EMBL:EGE06793.1};
GN   ORFNames=TEQG_05787 {ECO:0000313|EMBL:EGE06793.1};
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; DS995751; EGE06793.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:TEQG_05787; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_6_0_1; -.
DR   Proteomes; UP000009169; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 2.
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; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR032088; SAT.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF40; NORSOLORINIC ACID SYNTHASE STCA; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF16073; SAT; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
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; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          463..712
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1548..1626
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1654..1732
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          350..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1506..1550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1746..1765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1746..1763
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2041 AA;  223150 MW;  0AA467AA1B28EDEB CRC64;
     MVNQLHLYLF GDLTYDISTK LQPFLHSQSY PLLRSFFDCV CDKLRAEIGR LPAQDKEVFP
     RFSSIAELLT WRSSHSRSNP AVENALTCIY QLGEFIHQHE GLGQEYFSPQ ETCVSGICTG
     ALSAAAVSCC RTASELVPIA VQTVLVAFRL GMCTLRASKA IDPSEGNWSM VVSCDSTDKV
     EELLCKFAET NNLPITSMPW ISAYGEDSWV SISAPASVLL ALRSSDILSG MRSRALDIHS
     PYHAKHIFSK TDIDAILEKT DSQEWERYRA VRAVVSSTTG EVIEPEGLRS RLEAALTQIL
     FEPIRWTQLT QGLAAFMSSI NATRFHVISI GTNAEATLIA SLSSKMQIEE AQAPGNGESA
     KPDQHGGEAR GNMVRGRSKI AIVGLSGRYP SAENNEEFWD LIFRGLDVHK TVPDLHWSAK
     THVDPTGKKK NTSATPYGCW LEHPEAFDDS FSTCRPARRP KLTLLSRDID TAIAGGTNIL
     TNPDFTAGLD RGHFLSRTGN CRTFDDDADG YCRGEGVGTV ILKRLEDAIA DKDPIHGLIL
     GTYTNHSAEA ESITRPHVGA QRDIMRNILS NSGVDPYSVS YVELHGTGTQ AGDAREMTSV
     LDTFAPADAR RYRQPDESLH LGSVKSNIGH GEAAAGVSAL IKVLLMLRNN TIPPHCGIKN
     KINSSFPTDL DARNVYIAKK AVSWPSREGQ PRRVFINNFS AAGGNSALVL EEKPAEAEIQ
     GTDPRTAHVV TVSAKSAISL SRNIQSLADY IEKHQDEALF LPQLSYTTTA RRIHHQHRVA
     VSGTSAADIK AALEKAAANG DGKVRARIAP KVTFTYTGQG AQYVGMAKQL YTLFDQFKGD
     INRFDGLAQR LGFPSFLSVI EDESSEQLQD ISPVTLQLSS VCMQMALSRL LMSWNIIPDS
     VIGHSLGEYA ALNIAGVLSD TDTIFLVGRR AQLLEQHCTL GTHSMLVVKA SLSAVQGALE
     GAEFEVACIN APEETVLAGP NTQIEVLKES LNSNGFKTKI ISVPFAYHSS QVDSILGHFE
     TVATGVRFRK PTIPVISPLL AEVIADEGII GPSYLRRHCR ETVNFLGALQ NVKETGFVKD
     KAFFVDVGPH PIVTGMVKAT FGTSVTSMPT LQRSRDDQKV VTELLVSLYS AGTDLRWNEY
     HRDFEASHKV LELPAYNWDL KNYWMQYVND WSLRKGDPPL IVGPSSLTST TIHKVLDDNV
     DKIVVESDMA REDFNPLVQG HEVDGVPLCT PSVYADIALS IGKYLLERYH PEIETNLVDV
     ANMTVLKALI ARAQGPQPLR TIATVDWPAK KASVSFRSYD KSGEPTVEHA TCEIRFTDRS
     RLKLLESSTA AVKARMGTMR ETLGSGETQR FNRAMVYKMI SPLAQFHRDY QPLDEVIIDS
     NSLEVSSQVN FKGVQAAGNF FAHPAYIDGL TQAGGFVMNC NDSNDLAVEV FVNHGWESLQ
     LYEPLQKEKK YKTFCHMSPG DNRKFHGDVV VFDESERIVA SYKGIVFQGV PRRVLRFFLK
     PEAPAAPRGQ ANQKTTARSA PVAPAATAMP TTTPKPIAKP TAAPATASPK SPKVKQAFQI
     ISEEAGVPVE DLTDDCVFTD LGIDSLLALV ITSRFREELE LDGELDDIFL TYTSGKSLRG
     YLAKQSGSDI PVVVEPTPLP VVAPKVEPAV ASRISIGADC AAALAIVSEE SGIAIAELAD
     ECILAEIGID SLLALVIVSR FKEELDVDID SQSVFTDSFT IRDLKAFFGK GESTITTRAP
     SILMESSDEN TMSSMTPPDS SSDYDTSEKL ERIAVPPATS VLLQGIARHA EKILFLFPDG
     SGSATSYSAI PRLSPRVAVI GLNSPYNKIP ELFRCTLDDL IDSYIDEVRR RQPTGPYYFG
     GWSAGGILAY RAAQKLIEAG EKVLDLVLID SPVPRGLDKL PQHFYDHCSK YQVFGHRAGP
     TKGNGKAPAW LIPHFNATID TLHDYHASPL PAGKTPRTTI IWACESVIDG VNVPKLQSHP
     DNTPGMKFLS EKRTDFSAAG WEAVFPGGDI ILKRMEHANH FSMMKGEHAG KLAGIIKATL
     T
//
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