ID A0A1Y1V2H3_9FUNG Unreviewed; 2971 AA.
AC A0A1Y1V2H3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
GN ORFNames=BCR36DRAFT_414372 {ECO:0000313|EMBL:ORX45774.1};
OS Piromyces finnis.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX45774.1, ECO:0000313|Proteomes:UP000193719};
RN [1] {ECO:0000313|EMBL:ORX45774.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT biomass hydrolysis.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX45774.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:ORX45774.1}.
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DR EMBL; MCFH01000038; ORX45774.1; -; Genomic_DNA.
DR STRING; 1754191.A0A1Y1V2H3; -.
DR EnsemblFungi; ORX45774; ORX45774; BCR36DRAFT_414372.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000193719; 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:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000193719}.
FT DOMAIN 449..874
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1432..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2665..2705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2723..2743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2666..2705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2971 AA; 334644 MW; B5F91AFDEC0F9D9F CRC64;
MVVQDNILSK KYGNNIVTLV DSTGAIHIHD KSPLSSIKST NKYFNFKSSS FLSLNKELKV
KLEAEKAIKE YGLGSYGIFT PYHAELTEYI EKIYGEDCSI RTFQNDIRDI LFNSLVSSQD
FIFIDEQLNT SFKQTIKSLF LEKGHIIEYT HNTPLDLKSQ LKAIQLKFPT VNKFIITEGV
FENIGDVCYL NDIMDISKEF GCTLVLDESN ALGVIGQKGF GSYDYHQCQQ KADIIFCSMD
KTLCSSGQFY VFNNKSISIL LKNNTSLFDE SIYYPINALS AAVAKTVLNI IFENTTDFKN
ITSSIDVHTQ LVDNINYWKQ KCQSIGLKLI DSPSAITSII IDDVDAESLV ELLFKNNIKC
SFTKQINHNI NTNILKFNIL RSMTKKFINE AFNILQSVLI NYYPHLIHMS TIPKEIQIEN
MIDPTQQTSS LLNENIIDSS DVTDYPKAYP KFAIIGTGIR LPGDINNKDD FWKVMIEKKV
ITGLTPEDRW DRDEWYCKTE KPGTIQTLYG GFIENAFDFD NKFFSISQKE ALDATPEQRW
LCELTVETIE DANINIDKFK GSNTGVFVGT SGIDYGSYVF SVPEKITKYT YSGIEPSIHA
NRVSYLFDLH GPSLSTNTAC SSSLTALSIA CNSMAAGDCE MAIVAGTNFF QAPANGVAYS
QLRVVSKKGA CRPFDSGADG YARLEGAGMV LLKPYEKAIR DNNKIYATIL STACNEDGKT
ASLTTPSSKA QYKLMKRVYE KGHIDPCTID FIEAHGTGTA VGDPIEASSI GEAYGKINKA
NGNPAIPVGS VKGNVGHGEY LSGIIGLIKS TLILHKNMIV PQTAFDTLNP KIECEKLGIR
IANKIEKFPG QGRHRVAVNS FGFGGANANA IIEEEPQFDK NNISVLLKKN KNGEEIPCPY
VAFFSNSSLR LLKETLKKWL SVPEKELLPM IYLNSTTRTV LAYRIFIFAK TTEEFYRTIR
NFIADDSLDN GYKVTDQMMY IETKSNRKKG TLMAFDEPLT YVNSFLKHST YYNCCRNLYC
NNKYFSDCID YCDGIFKALS QRSLLQDYGL FTTEMMDNNK FKKFNSDLRK DPLVMIMFGG
MVQLTLSALL KYYGLFPNAV IGYGAGEIVA AYVADKMDLK TTVKVLYHYG RVLSHAYSQE
NKVYTLTLIC PISKIKQTIF TKLNQDEKDG ISISGIPSPK FCLLSGDYNI MKKVSDIAKS
ENIAIYGAMQ NNYGLHSMMI NDKMKEDLVN SLKDIPLQTS DIAFFTTTKL NKDGKPYEGK
LDGEYWWMNM RNPVLYAHAL SQTVAFLPID GKNIIEIGFG FDSIVLNDAS STFYEKERIY
NLFTFDKFKM NNATNYDVSF VQLIHFMATL HGYNVTNNLD YNHLWESYVQ VVGGHNTLQQ
LYSMHYDIPT RCWNHKYLRK YFKAERNGLP GNVDVGIKTE DIVYLEKLNQ KDHSKSVPSK
EETMKKEDIT IKSEPKRIEK STSAPIKETK TVTNDTVKPL PKAHSTSKIV NLSAFQAKSS
SSSSSNINEN SSSHYNNSSN DNNKNHSVHL KQNHPSISNP IQNKISTTTV EDFATEDDEF
WSYENNQYLV DHKVNNQIVF PAAGSVSRAM YGFLNSRNSQ KIQESKGHVA LTQLEFTSLS
VFQKRAEDQL NSKGPIPMKL YEDKNHQFTL KHQDGSIISK GNFVEIAKEF TDFPNLSDVV
KSCTTVMGGK GIHKDLIYQR AAAIQLQYGP EFQLIQSGRS GRNYSYVKIR VTEEHSKMIC
HPAVLDNCFH SIITLGLGSG NRQVLPHRIK SIEMTNGGHF KPGLITCVSQ LIYQDLDSVI
INFYVYDEEG HPLSKISNME FLVRKINIVR PLDWHNVLKY EKVKASEQKS FSISCSQVVI
MGSAKQADAI NIHIVPTLSS MNLKVYLITE NHNQTIDYML QNNFITKTNT TIVDVTLLDD
TSITTAFTKI QYYVSQGLNL IIGNIIMTNA KVEENIESLF TASNTISSML RVARAESRDC
HMYSIQANSI DDFAKGLFSG CLGKDEPDVI YSKEYGLHVP RLVRETTIPT IHSKNVISEP
KRFGNINKTI FRKTYGIPDL SKHEMDKESV VVKVSTISLQ NNDILQNSLP DLSSLMKDSS
VAECIGTIVH TGSNVKNFKK GDVVFGLNLQ ANDIPSTYVK IHQDLVFPVN TMDMDKQNNL
LSSVYAYTVA IYLLNEIPTG ESVLISTDAS DLMQALATIA QQKGINLFID DTSSKYSKAN
SNAFKNIKAQ MINTRQASEY VRLVKQHTNG EGVGVIIDIN VKFDKENTLE KCLRIDGEYI
KVGNIDQSTK KRTTHKIVQM SHFKDNVITP VVRQAVEMII HGKVEAIDLK TYPVSKINSA
TLEILSGRLQ GKSCLEMCKK GEDDIEFECL PSRVFKENKS YLITGAFGGI GLKVGLWMQL
RGARHIVLTT SSDPESKYKH PIVNALRQKG VHVTITKCDI SKYDEVEKLF METTPAIDGV
FHFANKFGPK LIRDSSLDSF NTAFEPKARG ALNLHKISQK GFSLSSFVLF SSVLDILGNS
GQMAYGAANS YLNNLIYYRR RKGLSGQCFS LPAMKGSGYL SQWNQITQSR EFSEVIEFLD
SEDLPDILDF FLRDDVDPCL QLLSGIQIND KVINKHIAPI TNIVKYKIHS EIDVPQLIQN
QFPPLKFRKI LEDKEQYILD KYVRNTHHSP PSSTNSSETE GEQVSDHSSY SSVSSTIGDN
SNGDSSAIES NVEYISVDES IDSDKTLRNH EDKNKNSSSK KKYMKNVNDN KHVFYKHIKN
GIYSLEMKNH YMDIEYAEEL GQVITKLSQL KKMQALIIEY EEDFSKGLEP SLKDELLKKN
PSKSKMNEVY KIYFNCLKLT NLNVPVISCL NGEITDHIIL ISLLSQWKIA TRRSVFASYN
NPVNISWMKE LAKNSNNKNS MKLIKQVETE KISAITAYKH KYINDIAANF EQAKKNALEY
VEKLINNSEN IVPVISIKTE DIVKINKAIK I
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