ID A0A443HYZ1_BYSSP Unreviewed; 3946 AA.
AC A0A443HYZ1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Hybrid NRPS/PKS enzyme {ECO:0000313|EMBL:RWQ96983.1};
GN ORFNames=C8Q69DRAFT_518882 {ECO:0000313|EMBL:RWQ96983.1};
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951 {ECO:0000313|EMBL:RWQ96983.1, ECO:0000313|Proteomes:UP000283841};
RN [1] {ECO:0000313|EMBL:RWQ96983.1, ECO:0000313|Proteomes:UP000283841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075 {ECO:0000313|EMBL:RWQ96983.1,
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 -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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:RWQ96983.1}.
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DR EMBL; RCNU01000003; RWQ96983.1; -; Genomic_DNA.
DR STRING; 264951.A0A443HYZ1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000283841; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd19532; C_PKS-NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013120; Far_NAD-bd.
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; IPR013217; Methyltransf_12.
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; 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:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 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; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
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; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-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; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..420
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2374..2449
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3497..3577
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2468..2513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2474..2510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3946 AA; 436699 MW; 805218705F61117F CRC64;
MTPPREPIAI IGSGCRLPGD ASSPSKLWEL LRDPRDVSRK IDRFNAQGFY HHDGHYHGAS
NVTDAYLLSE DPRAFDAQFF GIQAGEADAI DPQQRLLLET VYESLESAGL PLEEMRGSTT
AVYVGVMCDD YGGIVILSNR VSYVFDWHGP SMTIDTACSS SLVAVHQAVQ VLREGTSKVA
VAAGANLIFS PNMFIAETNL NMLSATGKSQ MWDANANGYA RGEGTAAVVM KLLSTAVADG
DCIECIIRET GVNQDGHTTG ITMPSQEAQT KLIQETYTRA CLDLRNPADR CQYFEAHGTG
TKAGDGVESK AIYNAFFQTG HSNISDERLF VGSIKTIVGH TEGTAGLAGV LKASLAVQHG
VIPPNLHFKE LNPEIAPYYE KLRIPTEPQE WPPLPTHAVR RVSVNSFGFG GTNAHAIIEC
YDPEYHGCNT VLPQLQPGGS SVNTLPLTLS ATSEKSLSNL ISRYLEHIKN NPDEDLRRLS
WTLHYRRSLF PFRASFAAPS TDSLIPKLQS ALDDKGDFLT RRTPERKSLL GVFTGQGAQW
ATMGRDLITT SPFAEQVVER LEQALLGLPA ADRPRWSLRE QMLASTAESR VSEGELSQPL
CTAIQVIIVD MLKQADITFD AVVGHSSGEI GAAYAAGFIN ATDAIRIAYY RGRYAHLAHG
PQGQRGGMLA AGTTLEDIQE LCGVPAFEGR VVMAACNSAS SVTLSGDMDA IDEVKEVLED
EHKFNRKLKV DTAYHSHHMV PCSVPYQQSL DACRIDIQDP NGRCRWYSSV HNGKRMDVCD
ELKHQYWVKN MVNPVLFSQA LEAALTHGPT PTMVIEVGPH PALKGPATSV IEEILGLNLP
YVGTLVRGQD GIDALASTVG SVCRYFGRSA VDLRSYDRLF GHGEDPLFLR GLPSYPWDHD
RSFWFESRES RSHRLRNNPA HPLLGVRLST SNDREYRWRN YLKPDEISWL HGHKIQGQTL
FPAAGFLVMA VEAARFVAGH RSQPLNIVEI SNFNIHRALG FYDDEKGVEI LATLSNVTIN
SADDDATAVS ADFTCDTCPQ KDNGSFISVA NGRIKLLLGE SSSSTLIDRP DMDSSMIDVD
VNMFYSSLQS LGYNYAGLFR SITSLRRTTD AAMGEILTAE TVNGTEYASE DFLLHPAALD
VAFQAIFAAV SYPGDGALWT LHIPTTIRRV TINPAGCLRN GGLNVPLAFS ANSQISPGGQ
ISGDVDIFPH NGQNAFCQVE GLEVTPLSPS TEKDDRQMFA ESLQYIASPD ADIVFRPILS
TSEDQIEAIQ VERLALYYLR KFLGSTVNKP GFRIWAQRAV DIIASGEHPT CRQQWLLDTW
DDVESALGAI RPSSIYQSDV RRIKALGETF EPTGDAEIST EINRLRDFYE ASFGVSQSRQ
YLASLTFQIT RRYPQTSILE LQTVNGSATR TIINHIGNSF SAYTCTDSFD TSFDALHEEF
GSLDRTLFST KKINIDEDLQ AQGFSGGSYD LIIAPNGIHG VQEYSQALRN LRALLRPGGY
LLVLQVTNPD TLRVGLTVGA LDRLPESFHS HGTPFLDLSE WDTLLRTTGF SGVDTATPDG
PVPFSVFVTQ AVDTQINTMR QPMGNSSIVI DHLLIIGGHR FPVSRTVREL QELLGPFCKS
ITTIKSMDEL DAATLVSRPL VLSVTELDSP FFLSLTRRKF QALQKLFDRC KTVLWAVEGA
NGELPHGNMM KGLVRCLLPE MPHIFAQIFN FQPSTAVKDR SRILAQAILH LHIASTWRDG
YGPLWSTERE LTIDDGKVYI TRYIPNEFLN RGYNAIRRRV TAEASLEDRT IAVITDKESY
ALQQYRVPPV PRYMLLQGGL CTVKIHYSTL CSLKVGNLGY FYLCSGIDRE SNSSILILSE
QHQSVLTVPR TRVVACNLPR NHERNMLISV AGVLLANSIT EKNGANSTII VYEPPPLIAY
FVARKATQKG IHPVFTTTRR DDAVHNNWTY IHPHTPDRHL RKLASSKVSA FISCSEDAVK
SRITDHLPIG VHGLSITDFL KSCSYVYPGL MEKSIHEALL DAYNEASSVN ISDVSLDTLE
DIALHDVAKQ PVTAGRNLQA VNWTSAAPVL ARVTSAMEEV TFSDCKTYFL IGMTGNLGLS
TCLYMISRGA KYFALASRNP KVDQQWLDHV SLTYGVIVNV FSLDITSRES LIEVYQTISR
TMPPIGGVTN AALIMRDGAF MDMDSDDMNQ ALQPKVDGSI YLDELFSDHT DLEFFVLFSS
LVYITGNAGQ VAYAAGNAFM VSLIHGRRQR GLVGSVMNLS GIKGVGYITR TDHGILNRLD
ILGYGVMSER DFLYFFAEAI LAGPPNSGRN PEISAGLRFC DPHKDAAPPA WIEDPKFSHY
RVHHNQNDGQ EGGHQVTSVK NRLLGAQSEK EVFDIILDAL LAMLHRKLRL QPENAVPADV
AIVELGVDSL VAVEMRSWFT NEFNLDIPII KILGGATVSA LISDAIPELS HETIPNLAKD
APAKPADAIP PSMYKSSDSG SGSFGESESH LDSNSTPDES TDTTASIPDV EEKTSPLVFQ
RKEKMSYGSS RFWFLRQYLD DKTCFNIVFR ARITGKINIK KFEEVVRQIG SRHEAFRTAF
YADKERQDEP TQGVMVESRL QLEVNKITHE DEALIVTNDL LDYSFDIEGG ETIRMLMLSL
SPEDHILVFG MHHIAIDGFS FNVLLTEIDM LYRDQPLPII RRQFTDFAVQ QRREVENGQT
DKERAFWRNM YPDIPEPLPL FPLANVSCRK PVMRYEHEEA SIILDRATAE SIRTRCRENR
STIFHFFLAT LQVLLFRYLD VEDLCIGIAD ANRHDVNTLT TVGFLLNLLP LRFNAPNGAF
DSVLAAARNL VYSCLEHSRF PFDVLIEDLN IPRSSTYSPL FQVLLDYRQF AVKSPPMLNC
RAEGERIMGR TAYDLLLDIT DFSGSDISIK LQTQKSLYSR QHTETLLRSY VHLIHFFAND
FKAETSNAPL FSENEKWKSI RHGRGPTFTS EWPETLSHRI DDISTQYPED VALRDGLGVV
MTYRDMSLKM DAIIDQLQQA RIEPGSRIAV FQEPSALWIC SLLAIWKVGG IYLPLDSRNS
LSRLASIVTN CKPDAVLCTT DTLAHAPSLG FNGSMIDVRT AARAPLLARH TNKAAGSFTA
VILFTSGSTG TPKGIEISHS SLRNLFEGYQ KTGDLSRHTV LQQSAYSFDL SLDQILTGLT
GGGSIYVASA EQRLDPRELA RIIAQEHITS TTATPSEYSS WITYGKPMLL SARKWTRAII
AGERWTSALR KAFQDLHLPG LRLLSCYGPA ETTIYCTKMD LPSDDTGIIP VGCPIPNSSI
YVVDNQLNVL PPGVVGEIVV GGAGVAVGYF DNAELTNDKF FTDPHASSEF VAAGWTKIYR
TGDIGYLQED GSLVFVCRVD GDTQVKLRGI RIELEDIENT IIKASDGAIS QAVVSVRGEG
NESRILLAFV EFAPGQSLSQ EELSHLLGRL SLPQYMIPTM LIPLDDGIPL TPHKKVHRRA
IDNMPLPQTH HIDGEQNCLN ATEVALREIW VEMLPKEITA AVPIDKKTDF FYVGGNSLLS
VRLQARIRDI FGVFLPLVDL IESSTLEDIA IHINNRLNEH AIDWDAEIAA DEDILSIIPG
EATQNSGQPQ TVLLTGASGF VGSSILQKLI SDDRVSRIHC VAVREGAARE KMRSMTSETT
KVIIHEGNLA SPALGLPENT FALLSKETDV IIHSGANRSF WGRYDSLRAV NVLSTKELVR
LAAYARRDHG KAIPIHFLST SSSCYRDANS RPPTDGSMGY VASKWVSERY LENAAARHLG
LPVYIHRMAP PASSEGLEGH RNDDDKNTEK ERIFQEFISI ISRIKLIPSS DTWGGQWDLI
PVRQLAEDIV EGAVVSQIYS TANSAASQQN PLVRYQMHFS TVRMTMDEVV QALEEAIPIR
QKGYQEIPAH IWVGKAKSAG FSYHFASMDM FLLKDQNGDV VGELRR
//
