ID A0A2V1DVA9_9PLEO Unreviewed; 2073 AA.
AC A0A2V1DVA9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Polyketide synthase-like protein {ECO:0000313|EMBL:PVI02111.1};
GN ORFNames=DM02DRAFT_653865 {ECO:0000313|EMBL:PVI02111.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI02111.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVI02111.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVI02111.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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DR EMBL; KZ805347; PVI02111.1; -; Genomic_DNA.
DR STRING; 97972.A0A2V1DVA9; -.
DR Proteomes; UP000244855; 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; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
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; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
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; 1.
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; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000244855};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 370..803
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1706..1782
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1676..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2073 AA; 226263 MW; E359400D2FFB255A CRC64;
MSSPANVFLF GDQSYDFVPS LRELLKTNNN PILSAFLDQA HYVLRAQAIK SLPPSTHKAC
RTTSLAQLLR KYVEGTLPAS FTTPLFCLAQ LGCFMRDHSG GHYPTADYNF NLGVCGGALA
ASAISCSRSL SELLPVAVQT VLIAFRLGIC ITERRDQLET AESERSRPWS VTIPLTRQDA
TTAIQTLSTS LALPPPRRPW ITTTSKSNTT VSGAPWVLEK LLQVPQIAGL RTKSIPVYIP
VHNPALFTLE DVEQILSPLT GSACMATPFV IPFISSASGQ STAAENYGAL IEIVLKQILL
ETIAWDAVEE SVPKLLKAQG NHSSVRIVPL NTNAGPALRS ALDPYFDSVQ IDRSSASGKS
ENSHRPDDQK NKIAIVSMSG RFPESPSTES FWDLLYKGLD VVKEVPLRRW NVDTHVDPSG
KTRNKGATKW GCWLDFYDQF DPKFFSISPK EAPQMDPAQR MALMSTWEAM ERGGIVPDTT
PSTQRNRIGV FHGVTSNDWM EVNTAQNVDT YFITGGNRGF IPGRINFCFE FSGPSYANDT
ACSSSLAAIH LACNSLWRGD CDTAVAGGTN MIFMPDGHTG LDKGFFLSRT GNCRTFDDQA
DGYCRAEGVG TLFLKRLEDA IADGDPILGT ILATQTNHSS MSDSITRPLA QAQIDNMRAV
MDMALVDSNS ISYVEMHGTG TQVGDAEEMK SVLTCFAPNE KTRENNPLFI GSAKANVGHG
EGVSGVTSVI KVLLMMQHNT IPPHCGIKPG SRINRNFPDL KARNVNIAFE PTSWMSKDST
KPRRAMINNF SAAGGNSALL LEEAPVIPQS YEGVDPRKSH IVTVSAHTGK SMVGNLENLL
TQLQNEECSL PQLSYTTTAR RWHHAHRVAL TGTSISDIQS SIRKALENGN GVTRPKGKAN
VVFAFTGQGS QFLGMGKELY YSCPSFKDDL ERLDRLAQKH GFQSFSHIYA PENSVQKIEN
MSPVQVQLAI TSLQIALGNL LISWGAQPNT VFGHSLGEYA ALHFAGVLSA SDTIYLVGTR
AQFLEKACQP STHAMLAVRS STAALEQILR DHAGEVACVN GPSDTVVSGK LEDMLAAQNV
LSAAGTKSTL LKLPYAFHSA QVDPFLEDFK SASRGVSFQS PSIPVLSPLT GEVLQAEDTI
TPDYLANHCR KTVNLVAVLE KARQQSLIRD NTIVIEIGPK PIICEMVKAT LGHSLVFPTL
DAKGNAWSNL QAVLSSLYTA GLNVNWVAYQ APFKSAHKVI SLPSYAWDLK SYDIPYEGEW
ILHRHKIHCD CADGEKQWET AKYVPGQHTF AKNILVPEEA SAVVNGKVKK PSKLDPTVEA
YPSIQLTTAV HKVLSEKTEP LGATLVFETD LSRKDINGIS RGHVVDSIPL VTPSVYADIA
MQIGKYAMDR IRAGHHQAID GIVDVSNMVV DKALVPHNLE PQLLRTTLSL TWPPKAAATT
RSGQVKFETY YSDGKLDTVH GSCTVRFSTE SQLKTLRRKV PEYRAAIQRL KERSSDLTKF
SGKRGYKLMS SLASFHPDYK LLDAVILDEE ANESTCTVRI DGCQDQGNYV AHPAHVDALM
QLSSFSMNAN DDTNIDEHVF TNHGWGSLQI YKKLQKGVSY EIYTKMTQKG DHATGDVVVL
DGDEVIAFFG DLSLRKVPRR ALKAVLEAAS QRAARHAGKA DLSPVPIIPQ VTFKHTNGAS
SPTSSDSEGR NFHDSAIGTP MEEKPAYIFE KALKIIAEES GIAEDDLTDD TAFADAGVDS
LCSLVIGSRL REELDMDLDP DFSLFESVTT VGELRGMFTG SEKDAPDESE IKSSEATPIE
TGDKPLELVP ICRPTNSVML QGTPKTARRT LFLLPDGSGS ATSYTGIPRV SSDIALVGLI
CPYSRDAQNM NCTHGAMMES FVTEIRRRQP KGPYHVGGWS SGGAFAFMVA ELLINQGEEV
HSIVVIDAPV PQPMEKLPYE FYDYCNSLGL FPGQGGEGSD SGAPDYLIPH FVAVVDVTMG
YRSSPLKTHR MPKLGLIWAS DTVLDEAKAP KMKGMHFMVN KRTNFGPDGW DEVLPGGEHE
IIVAEGANHF TLMRPPYVDL VREIINRVVG EQE
//
