ID A0A443I807_BYSSP Unreviewed; 2509 AA.
AC A0A443I807;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:RWR00193.1};
GN ORFNames=C8Q69DRAFT_513018 {ECO:0000313|EMBL:RWR00193.1};
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951 {ECO:0000313|EMBL:RWR00193.1, ECO:0000313|Proteomes:UP000283841};
RN [1] {ECO:0000313|EMBL:RWR00193.1, ECO:0000313|Proteomes:UP000283841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075 {ECO:0000313|EMBL:RWR00193.1,
RC ECO:0000313|Proteomes:UP000283841};
RX PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA Urquhart A.S., Mondo S.J., Makela M.R., Hane J.K., Wiebenga A., He G.,
RA Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA Grigoriev I.V., Idnurm A.;
RT "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT variotii (Eurotiales).";
RL Front. Microbiol. 9:3058-3058(2018).
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:RWR00193.1}.
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DR EMBL; RCNU01000001; RWR00193.1; -; Genomic_DNA.
DR STRING; 264951.A0A443I807; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000283841; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; 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; cd05195; enoyl_red; 1.
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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 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 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; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF28; SYNTHASE, PUTATIVE-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PF13489; Methyltransf_23; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 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; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000283841};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 64..484
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2422..2499
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2509 AA; 273759 MW; 0791867AD2C1A9E5 CRC64;
MTIDNSNTFE GRRVPVASTN GFTNGHSSDD VANVPVNGES TNGVSADINS RNGVLGTATH
TNGQIPIAIC GMACRLPGGL TTPEELWDFL IEKKDGRCRV PESRYNVDSY YSNTKKPGTV
STEYGYFLDE NVDLGALDMS FFTMTRTEVE RADPQQRLML EVAREAFEDA GVTNWRGKTI
GTYIGNFGED WLEMLGKESQ PWGIHRISGS GDFVVANRIS YEFDLQGPSM TIRTACSSAL
VALNEACAAI NRGDCGSALV GGVNLILAPG MSMAMQEQGV LSSDGSCKTF SADANGYARG
EAVTAVYIKP LADAIRDGNP IRAVVRSTSH NVDGKTPTLS QPSTQAQEAL IRRAYELGGI
TDFGETAMVE CHGTGTPTGD PIEANAVARV FGEKGVYIGS VKPNLGHTEA ASGLVSLLKM
VKALEHRTIP PNIKFTTPNP SIPFDEAKLT VPTEPMPWPK DKLERVSVNS FGIGGANAHV
VLESAATYNV PDAIYETPEE PQLLLFTANS AKSITRVVDN CKEWIEKNPD KISDLAYTLA
RRREHLPHRA YAIVTNGAIE SVSQPANLKS TKAPNVVMIF TGQGAQWPQM GRELLQSNKT
FKASIRALDA HLQTISGEKP QYSIEAELKK PAKKSRIGMA EFSQPMCTAI QIALVDTLAA
AGVVPAAVVG HSSGEIAAAY ASGALTAKEA ITAAHHRGAV TTKQKRPGAM AAVGMGWSET
EKYLIPHVSI ACDNSPKSVT ISGDVDAVKS VITAIKQKQP QMLARQLQVD KAYHSYHMEE
IGSDYQALIG EQVVGKTPSK LFFSSVSGRI LGAEDTIGPK YWQDNLESPV RFREAVTAIL
KHEVGQNAVF LEVGPHGALA GPLRQILSQA RSSAPYISTM ARNQDCTASF LSAIGGLHSL
NVNIDLEALF PSGICLPDLP RYPWNHEGSY WYESRLSKEW RNRKAPHHDL LGVRVAESSD
TEPAWRNLLH VTNVPWIRDH KVGENIVYPF CGYIALAGEA IRQLTNVNGG FSIRNIIVST
ALVLSEGKPT EIMTNFRPHR LTNSLNSSWW EFSVSAYNGR NWTKHCSGEV CALPSTPEDA
VEPEPLPRKI NVRKWYEKMI KGGLNLGQSF QTLETIATST SEQQALGNIA NGRQGDEGNY
FIHPTALDGT LQILGAAAVN GYARKTKTWL PTSIDKVTIH RCSSDMLISS AAKLSSNFSV
VGDSRCIAEG KEVVEATGIR MSLADGAGSA DSNDDHAASR CEWKPDIDFL DVNDLIHIPS
DHSEQSRLLE ELGEICLLLS QRHFTETASH STLPHLQKYI AWIRAQSTSI VTKLPSTWTG
LDTQAISARI ESIKAQLADT SAAPVANVIH QICNKIDALL AGEPLEGVLQ EGDLARVYGF
LGQLERGEFI RALGHSKPNL RILEIGTGKG VSLHGEIIAE LTHANGDVLC SNYTLTAPGY
VVSESQEKLF PNMVFASLDI SRDPFDQGFE EVGFDLIVAS NVLYETKNVQ ESLVNIKKLL
SPEGRLLLQE LCPSSKWVNY VLGLLPTTWG ATDERTDIPY LRQSEWETRL IAAGFGNVQA
VTADGEEPHQ VTTTMIVRNV LEKPSNKITV LFEQEGPAVI QVLRELEKQG YEVSKCQLGD
EAPVGQDVIS LLDIEKPFFH DMDEDRFLSF KTFLLSLQGR DAGMLWATHL VDIGCHDPRY
AQVLGFARTV RTEQLADLAT CQVDSFENPK SVEYLIQVLG KFQTRQGDQE LNPDFEWVIS
NERIQVARFH PFVLTDNLLV PEDSNEMATL NVRTPGRVNS LHYQRHARQD LDKDEVEVEV
YSAGLNFRDI LVALGIVELP VRLFGIEAAG IVRRVGADVS PDNLQVGDRV VCFCRKDAFS
TYTTTLADVC VRIPDSLTFN QAGTMLIPYF TAIHSMINVG RVTKGQSVMI HSACGGVGLA
AIQVAQMLEV ELYVTVGNEE KVKYLMDNYN IPRNRIFNSR DKSFVDGVMR ETRGRGMDFI
LNSLSGELLH ATWSCVAEFG TLLEIGKRDL IGSSKLDMKP FLANRNYCCV DIDGLWKRIH
IARALIFTIL DLYGKGHISP LPTTIFPAAQ TQDAFRFMEK GLHIGRVGVA IKEAAEETGI
AFPTTKRALA VSFPGSASYL MIGGLGGIGR AVSTWMVDHG AREIIYMSRS AGLTNKDDAF
IHELQSMGCS VKLVSGDVTK LEDVNEAIAA ATSPLKGIVQ MSMVVANENY TRMSFSEWTA
SVAPKVQGTW NLHNASVAAG LDLDFFLMFS SVSGIVGQAG QANYASGNSF LDAFAQYRND
MGLAASVVDM GAVEDVGWIS EHQGMMGKMS RSGFKPVSEQ EVIDAMAIAM LAHNKPDQAA
KKVLATSSKN NFYFLHKNTF LVGLALLIPL HDPSNYVIWK KDRRMASYHN NSVVGITAGS
TDVLKSFLAN AQADPSILKS AEASKLFAVE IGKKLLDLLL KPQEDLNTSL PLLDLGLDSL
VALELRAWIK QVLAFDLPVL EMMSIGSLDI LGQHAANEMF RIATENNQG
//
