ID A0A364KVL7_9EURO Unreviewed; 2318 AA.
AC A0A364KVL7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RAO67597.1};
GN ORFNames=BHQ10_003609 {ECO:0000313|EMBL:RAO67597.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO67597.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO67597.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO67597.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
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:RAO67597.1}.
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DR EMBL; MIKG01000005; RAO67597.1; -; Genomic_DNA.
DR STRING; 1196081.A0A364KVL7; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000249363; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; 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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; 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; 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; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
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:SF54; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 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; 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:UP000249363};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..427
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2235..2314
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2318 AA; 251093 MW; E4E2C626ED80F283 CRC64;
MPYVESPESC PPDEDVQLEP IAICGMACRL PGAVDGPSDL WQMLLDKRVG NSEKVPKSRF
NINAFLHSNE DRPGSIKIPG GYYLDGNAEN FDPTFFNMTP VEAMWLDPQQ RKMLEVCYEA
LESAGVTLSH VAGSNTAVFC GSFTADYQQM TFKDHDFRHN YAATGVDPGI ISARIGNIFD
LRGPSGLINT ACSSAVYVVH NACHALRARD CDAALCGGVN IIISIDQHMN TANLGIMSPT
NMCHTFDASA DGYGRAEGAG ALYLKRLDDA VRDGDVIRSV IRSSACNTNG KVPGYGITFP
SIEAYFETHG TGTPVGDPIE VKAVSRAMND TRSPNKPLLL GAIKPNIGHS EAASGIFAII
KASLMVEKAV IPGVAGLKNL NPAIHEKEWN VVINRDARAW PDGFESRRVS ISSFGYGGTN
AHVILENVEA LVPNYSHVAL KAQGPITEVV SEVSEDRPLL LTMSAHDKTT LTKNIRAHAA
VVDYYNLHDF VYTLNNKRSV LSTKGFIITT EQAVAKDLNG ENFRFTSSST PVEKVAFLFT
GQGAAWPTMG REAIKHFPLF RRVIKKLDIV LGGLRHPPNF LIEQQLSCSK EESKLHDPNV
AQATLTAIQI AVVDLLASWG IVPEATIGHS AGEIAACYAA GLISAPAAIV ASYYRGYCLR
TFGPSGGSML AVGKGVDDLD LSKLGPNLSV ACENSPNSVT LSGPAAEIEE AREMFAAQQV
FAREVRTGMA YHSNYMQNFA EPMANYIDSA VAGLDSPDHQ WRQDPKPMLS TVTNKMLNSL
DVDGRYWAKN LTNPVKFNTG VSLLASSGSL KDVQGFIEVG PHSALGGPFK QICQSNKLRF
AYVPTIVRPE GNAAISLLKT AGVLFVEGYP VNLLAVNKSE LKGLSSPQTV VDLPRYQWNY
EKIFWAEPRA NFEYRHLTHA RHDLLGRRIL GLSDNNIAWR NVLRLKDVPW LEDHKLGGSI
IFPCAGHLAL AIEAVRQRCD VIGLESIGTT LRNVELKETL VIPPTDAGIE IQVRLTSSSS
KTEPTSYSFA VESVNDNGIW TIHCTGTCTA QTVGSEPPSE KHPVNFDNLT QRHSGKTWNE
TFQRVGFEYG RQFGALDRIR THGKYESQAA GKIPITTKSE LMKDESRYFL HPATVDSLLQ
LIIIAIHGGD YQEMLWGVIP VGIDEVTVRQ AGESEGTVGD AVAWLPEGRK DRLRRFLSDG
KIFGKTGEVV LDIKGLHTLA YEAALPPRYE ATLPPMPYSG VSWKLDLDHL VLSNAYDQPN
SMQAVSAVVA LVGXXSHKHP LKYLLLLDED GEIPEMELLR NTSLITTISL VSNKEGVKED
SRLGKLSIPE GQFALEAVNV DKQDFVILGT KESAQLLETG SASSLRKHLS ESGHAVLLLE
SSEMTKALKI LDTAGFKNSA VSFADKSLIW SKATKNSRTN ELVSATAPTV DLVYSPRHSA
SPEGLAVNLK ACGILVTIQT LEGYTNASTS NKPIVVFNPN ANLITAADCE NFEHLKKLLG
TSSPILWLTT GVNQGQNPSA STVAGLLRVV REENKTSIAS VLDYDTNTTF KSLATAIISI
FAHEDRPRYF ESEYWLHNGQ IHVSRVVPNN SLNMRMIGSA TSDKPIQRLL KRGEYLQGVP
KYGALTFSQN GRLQRSQIGV GEVDIQVEAL EFQKKDMQSP PSDPRLVYGT VIEVGSDVKQ
SLKNKPIIAY TSSAYDTIVR VQAAAAVELS AVPEDVTKLI RSLPTIMQAM SALQAASASA
QKIVFLMPSS DALKTSTIAI CRSLGFQLVI IQDDPNFRTT DHLTTFHSND LEGINQALKR
AGSAGVVIVE NFSNTSQRIW KDIPAGASFV VSSPASDNTL EAAPDITPYY RGARFIVTNV
AYSLALDPTV IGGNLQTAIA VATQENSDIG ENSMITLNHL LASSETLPDA SVLSFNYGKD
TIRSVDPEYS IRFSSEDAYL LVGCLGGLGR SLTTWMVDRG AKHLIFISRS GADKPVAAKL
IEDIKAAAID AVTKGDGARK IKGVVHAAMV LNDVMFHNMT LDMWNDTLSP KVDGALALHE
ALASNGIDAD LDFFVITSSI SATAGPPGQT NYAAANSFLD NLAWSRNLSG KPGTSLALPM
IIGVGVIAEK ESQAAQALVT RRGLYGDNER EMLRGFGAAM SQPRPTLGSE PLTQANAAII
MGLDPTKIAR SMHATQETEN SDVDWFSLGR FSEIRALSEL SRGGSSSSAN KKSGNGASFV
EQLSNLHAKH ADPAVALEFT ARHIMAKCSA ILMIPIESME LDSKSPGAYG LDSMIGVELR
NWLFKELGLN IAFQDLLATT LTFQALAAKV LEVHEIVV
//
