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Database: UniProt
Entry: A0A093VC14_TALMA
LinkDB: A0A093VC14_TALMA
Original site: A0A093VC14_TALMA 
ID   A0A093VC14_TALMA        Unreviewed;      2127 AA.
AC   A0A093VC14;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Conidial yellow pigment biosynthesis polyketide synthase {ECO:0000313|EMBL:KFX49730.1};
GN   ORFNames=GQ26_0093000 {ECO:0000313|EMBL:KFX49730.1};
OS   Talaromyces marneffei PM1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX49730.1, ECO:0000313|Proteomes:UP000029285};
RN   [1] {ECO:0000313|EMBL:KFX49730.1, ECO:0000313|Proteomes:UP000029285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM1 {ECO:0000313|EMBL:KFX49730.1,
RC   ECO:0000313|Proteomes:UP000029285};
RX   PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA   Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA   Lin X.;
RT   "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT   of Dimorphic Transition in Penicillium marneffei.";
RL   PLoS Genet. 10:e1004662-e1004662(2014).
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFX49730.1}.
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DR   EMBL; JPOX01000009; KFX49730.1; -; Genomic_DNA.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_6_0_1; -.
DR   Proteomes; UP000029285; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
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:SF37; FATTY ACID SYNTHASE; 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; PF16073; SAT; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
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; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          410..822
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1648..1725
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1759..1835
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2127 AA;  233382 MW;  356578A0742D9A77 CRC64;
     MDGLVNHQQP KGDYPLPLFE TRQYDRLQGK MLRERSIVFF GDLSLPIHPA LSQLLRAQTE
     YSILSRFLTQ AKTALQAEAT NLSVVERKSL PSLTDLYTLS ETENSHGSDH PILAPALLVI
     LQLGQFISWH EEHPEKRYPE SDSTIFAGIC VGQISATAIS LAKSLTELLP LAVDAVRIAF
     RLGRLTTEAR NDLELSLEET WAIVTPRDTS IPTEDVLDRI IKESGILGRR KPYATAYFPK
     TVTIQGPPST LRLVSDSLQK ARGSSHTYFA SELPIYAPYH APHLYNQDTV VEILDGVEFV
     DKKNDTWATG QVKLISPTTG TFYDVSNRLD IMSKALHDIL LKPINWEKLC EGCTSVVASS
     EPARWSIRPF GPSKATKSLL SAISSVTNAD IILDETFISS STSQTPTTAK EPIAIIGMSG
     RFPNSTNTDE LWKLLEQGID CHKVIPADRF NASLYVSQDR NSRNKSKSPY GCFIEKPGMF
     DPRFFNMSPK EAAQTDPQQR LALVTAYEAL EMAGYVPNGT PSTQLDRIGT FYGQTTDDYK
     DLNTSQDIDT YYVSSVIRAF GPGRVSRSNQ LACTSIWSQE CDTAVVGGML LLGSPEMYAG
     LSKGHFISET GPCKTFDDSA DGYCRGESVA SIVIKRLDAA KADNDNILAV ILGAGTNYSA
     YAASITQPHG PTQEMLYRKV LNQAGLDPFD IDYVEMHGTG TQLGDAIEMS SVSNIFAPVS
     PRRPIERPLH VGTVKPNIGH GESASGITSL IKALLILREE RIPPHIGIKS GVLNHTFTDL
     QRRNVHIPLE TAAFPRSQSR KRRLMVNNFG AAGGNSAFIL EEGPIYEGHG VLDSRPDHVI
     SVTAKTAFSL QKNISNLIAH LEQYPQVSLS DLSYTTTARR VQHPLRASAI ASNVDELKGR
     LVQLLETIPP KPASGKFPGV AFAFTGQGSV YLSLGQQLFE TSSQFRADMR RFDQICQGYE
     FKTFLPVIDG SATNLNDLSP TQAQLALVSV QIALARLWAS WGITPNFVIG HSLGEYAALN
     VSGVLSISDT LYLVGIRASF LETLCTKNTH SMLAIHATLD AVKSAAENKL GRLELACVNG
     PEDIVLSGLF KDIQELSQHL KQQGFKCTVL QVPFAFHSSQ TDPILDSLEK AAQSVRFLKP
     EIPVVSTLLG AVVDEIDVFG PSYLRRHARE PVNFDGALRQ ACFDGLTDAQ TIWLEIGPEP
     ICLAMVKSIL GSEIKAFPTL RKSEAPWKTS AKTVSALHSL GFDITWKEYH RDFEGGQRLL
     HLPSYAFDEK NYWIDYRNDW LLHKGKDIVK QMDTPRINSG PATTTVQTLI TEEVKDGTVF
     VVFESNLSEP KLNALIAGHS LNGLALCPSH QAKLPASSGS NIVDMQIVKP VTITVPRVDT
     PELLRISGTA NLEKGIVEVT FGTYSSKSGK TDQNAKCIIE FGDTKLWLNH WSRSAYLIQK
     RIEDLERGVK NGDVDKLFEK TIYRLFSAVV DYDPRYHGMK EVMINSNELE AVALVKLYEG
     TDAGDFFCSP LWLDNLAQLA GFIMNGVNVV DPRKFVYISH GWGSYQLADD IDPTKPYHVH
     VKMHPAEKNV VVGEVSIFQG DTMIGLCSSI KFQKVPRSLM EMLLAPPSHQ QQSSVQIPNQ
     RPTLSSAKQA RVIPPRKAAV LPEYSSGKST PGIKSMALET IAQEIGVTAA ELVDSATFVE
     FGLDSLMALT ILSKLRESLQ LDLPSDIFQE LTTIGDLRGF LDKFDNTNEG NVDTPSTDAM
     SPILATPEPL FEDETSIAGD MLNSVYSIMA KQIGVEVEEL LAVDDLSSLG LDSLMSLSIQ
     GSIQEELSLK LELQFDGSAK LPTLVNIQEA LGLSPAEPLI IPQPLIPATS HRAGLGPSAS
     TLLLQGNPRS STKFLFLFPD GSGSAAAYAA LQEISPDLVV YGLNSPFLKS ADKYTCSIEE
     IATIMVQAVR SIQSHGPYTL AGWSAGGMYA FEAARQLIQA GELVSKLILI DSPCRSTYEP
     MPANLLEFIM SSTILKGFTD KSAPNRIVDH FKSTIRALQI YSPTKLDASR APEVFIIWAK
     NGLSEDLGNN ERGNVDWSRG VANWLFHREA NAGPLGWEKL LPGRPISVAD VAGNHFSMVN
     KSNSKSLSLA ISDVLRDDLR KQQWRIF
//
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