ID A0A093XN84_TALMA Unreviewed; 2575 AA.
AC A0A093XN84;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Conidial yellow pigment biosynthesis polyketide synthase {ECO:0000313|EMBL:KFX46688.1};
GN ORFNames=GQ26_0181690 {ECO:0000313|EMBL:KFX46688.1};
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:KFX46688.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX46688.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX46688.1,
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 -!- 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:KFX46688.1}.
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DR EMBL; JPOX01000018; KFX46688.1; -; Genomic_DNA.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_2_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 373..790
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1637..1711
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1597..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1713..1762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1725..1751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2575 AA; 282581 MW; DACD56F2522F29E2 CRC64;
MRSLAQEGNR LLVFGPQALS AKGNDFRALQ AKVAQLTWIT HVITDLPNVW GDFVKEFPKY
SLVSGETLLQ KLIKWVDTGD IDLGTNNHLA NIILSPLVII THITEYLKYL QNGAPKTNHE
SSTETLGFCM GFLSALVVSV SNDSIDIERY GAAAIRLAMI IGGIVDAQDG LDAQGPSKSL
ATAWNSTKAA EELQQILVHF PEAYVSVSYD DQRATITTAS KTVSTLQGQL RTAGIVANEI
GLFGRFHNDW YAEDVDEIID FVSSRPELVL PDATDLIYQT RSNSGTGLIT SGKLHDHAIR
TILVQHSNWY QTFKSIHDTQ IKSLKTSVIA FGPEPCVPPS ILREIKQNVI HASDIQAESI
APPPIVLPQQ VKEDDIAVVG MSLKVAGADD TDEFWDLLCA GQSQHREVPR NRIKFDNDWR
EVGPKRKYFG NFLNDHDIFD QKFFKKSARE AASTDPQQRI LLHVAYQALE QAGYFNSPEQ
DKRIGCFIGE CANDYADNVA CHQPNAFTAT GNLKSFIAGK VSHYFGWTGT GLTLDTACSS
SLVAVHLACK AILSGECNAA LAGGVNMMNS ALWVQNLAAA SFLSPTGQCK PFDANADGYC
RGEAVGVVFL KSMSAAIANG DQIIGTISST GVSQNQNCTP IFVPNAPSLS TLFQDVIQDA
QVDPKKISVV EAHGTGTQVG DPAEYDSIRR VLGGANLRSK PLAFGSVKGL VGHTEASSGL
VSLIKILLMI QNKTIPPQAS HESLNPHLNA TADDKMEIIT KKTTWDEDYR AALINNYGAS
GSNASAVVTE APRLHESTTS ATSFPVLDYP FHIFGKDDRA IRDYCTKLAK SLEAKGVNNL
SIANLSFNIC RQSNPTLDRG LVFTSRSVKE LVEKLNAFQT GDVNVAATIV QPQLRPVVLC
FGGQISTYVG LSKEVYENVR ILARYLDQCD YACQSLGCES IFPGIFQRSP IEDTVKLQTM
LFSIQYACGK SWIDSGVQPV AVVGHSFGEL TSLCISGVLS LEYALKMIVG RATIIRESWG
SEKGAMMAIE ADQEEVQKLL AETSLPCEEA GQRAPTIACL NGPRSFTIAG SSRAIDIAGE
TISKNPAYSR FRFKKLNVTN AFHSTLVEPL MSDLEKVGQS LQFNEPSIHL ERATEFYSSE
RLAARYVADH MRNPVFFNHA VQRISKKYPD AIFVEAGSNS TITNMASRAL GSPVASHFQP
VNITTDNGLQ LLVDSTASLW KQGLMVPFWA HSRVQTYEYS PVFLPAYQFE KLRHWMEPVP
PPTSSKQVVG GQAEEPKGLW SFIDYMDEKK RGARFRINTE TDKYKELVSG HIIAQTAPIC
PATVEVDIAV EALISLYSNF ATSGLQPRIC NVDNQSPICI DSSRSVWLDV ESQESAPNNW
SWRIVSTGES SKASTVHVTG QIIFVSTDNA EWQLEFSRYE RLIGHQRCVG LLNCDDADDI
IQGRNIYRSF GEVVDYSAPY RGLQKLVGKG TESAGRVVKK YTGDSWLDAL LSDAFSQVGG
IWVNCMTDKD PGDMYIATGF EKWMRSPDIT TDYKRPEAWD VFAYHQELPL EHSYLTDIFI
FDSTNGKLTE VILGVNYHKV AKATMSKILA RLSGLPTTST STNVKSSPAA AEGSSPVENG
ASGSGSKAKK TKSGAGQDVV NKTKGLLAEI SGMGVEEISN EAQLADIGID SLMGMELARE
LEGMFKCTLP SDELMNVTDF AGLVQIIKST LGVSDDEEGS DQEGSEASSS ESSTTFTPST
TATTVSDVED NGNEKSIGKE KSVSYTGDLQ LPSSTIIEAF EESRKLTDDF IANYRCADYM
ETVLPRQTQL CVALTVEAFE QLGCPIRSAK AGDILTRIPH DPQHQRLTNY LHKMLEEEAR
LIDTDGSKIT RTAIAPPSKS SDAILEQLLR DFPDHEWANK LTHFAGSRLA DVLKGECDGI
KLIFGSDEGR RLVTGLYGDS LLNKLANVQM QDIVARVASK MPQDQGPLKI LELGAGTGGT
TKGMVALLAK LGVPVEYTFT DLSGSFVAAA RKTFKEYPFM KYKVHDIEKS PPADLVGTQH
IIIASNAMHA THNLEISTAN VRKALRPDGF LMMLEMTSPV FWVDLIFGLF EGWWLFDDGR
EHAIGHQTLW ERIMRAAGYG HIDWTDGNSP ELEIQRVIIA LASGPQYDRQ PVAPLPQPEK
QLQPAAGRKA AVDEYVRKYT EGFSLGERVE RATSPSQYEQ CVLITGATGS LGSHLVAHVA
ALPNVKTVVC LNRRSGSDAN ARQQKALEDR GILIDAASQS KLQVFQVTTS KPLLGLEKSD
YEELLGKVTH IVHNAWPMTG KRPLSGLESQ FQVMRNLIDF ARDISAHRSK GSKVTLQLIS
SIAVVGHYPL WSGNVEVPEE RMTLESVLPN GYGDAKFVCE RMLEETLHKY PEQFRVMSVR
PGQIAGSKVT GYWNAMEHLS FLFKSSQTLK VLPDFEGDLC WTPVDDVAGT CSDLLISDRE
PYLVYHIDNP VRQPWKEMIP LLAELLDIPR TNIVPFKEWV RRVRAFPGSV EWDNPAALLI
DFLDDNFLRM SCGGLLLGTA KSCEHSPTLA AVGPVSVEVT KKYIQSWKNS GFLHK
//
