ID A0A094GAW9_9PEZI Unreviewed; 2638 AA.
AC A0A094GAW9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFZ00155.1};
GN ORFNames=V498_00262 {ECO:0000313|EMBL:KFZ00155.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFZ00155.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFZ00155.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFZ00155.1}.
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DR EMBL; JPKA01000047; KFZ00155.1; -; Genomic_DNA.
DR HOGENOM; CLU_000022_31_0_1; -.
DR Proteomes; UP000029270; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
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; 3.40.366.10; 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; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
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; 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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; 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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..429
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2550..2627
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 471..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2638 AA; 289434 MW; F58D17C069F08EF3 CRC64;
MASVPNGNGH PASISDKQEP MAIIGMATRF PQEATNTEKL WGFLLKGRSA HTAFPKDRIN
PDGHYHPDPE HGGTFAVKGG HFLSEDPAYF DAPFFGITKT EVLSLDPQQR VIMENVYQAL
ENAGLPIAKV TGTNTSVYVS GFNHDHLATL NSDPETTLKY KPTGTTNSLL SNRVSWFFDF
KAPSLTLDTA CSSSMVALHL ACQSLRCGAD AEFSPCMGHH GFLSQEGRCF SFDHRADGYA
RGEGVGTVIV KRLSDALRDG NTIRAVIRGT GVNQDGRTAG ISLPSSAAQE RLMRTVYASA
GLDFNDTMMV EAHGTGTAAG DPIEASAIAR TFASRSKDIP LFVGAIKSGI GHLEGGAGIA
GIIKSVLVLE SGIIPPNVNF EKANPKIPIE AWNLQFPLVN TPWPTPGLRR ISVNSFGVGG
TNGHTVLDDA YNYLTSRNLT GAHNTNHHTP TAEEIRVTVA EIDGSIALET EMDAPPNGHA
NGTSNGATTN GNHDTTEITN GNGVQNGNGV NNNGHFAPHV PRLFVFSSFD EKGAKRNATT
YAKYLKNIQP PNEDDYMKDL AYTLSEKRSV FPWRSYAVSN SLSELIENLS SDQGMPSAVR
VGTPPRIGFV FTGQGAQWYA MGRELLIYTI FRKSLEDAES YMKSIGAEWS LLEELSRSKE
ETRLNEPHLA HPSCTAVQIA LVELLTSWNI RPTRVVGHSS GEIAAAYCAG KLSKEAAWKV
AYFRGYVSAK QRGAKGAMIA VALSETDLQP YLKTINELHE GEMIIACYNA PKNHTISGDE
HKIDALKTLL DDKKVFARKL NVLNAYHSGH MKALADEYLE RMSDISFGDR LSVADIHLFS
SVNGHKVEKD TLDAQYWVDN MVSPVRFTDA LLAMSFTRLS KGQASLRLNA GTENIFVDAI
VEIGPHAALQ SAIKDTLATK VSSSSFSYLS VLNRTTPGAQ IILNSAGVLC SRGSPVNIQA
VNDSANPGAT APRLIVQLPP YSFNHSDKVW YESRLSKNYR LRKYPRHDLF GAPVSDWNSE
RPHWRHIIRL YEQPWLRDHM VTDAYVYPGV GYIIAVIEAS RQIADPEMTI TEFRLRDVSL
KRALIVPDNK EGIEINLSFA RMDESSLWGS SVWKKFVISS WNPTGNDWIE HCTGYVSVDY
ETSPNLVDAG RESVAEALKW KDTLEGVKQR CVIPFDIDTT YDNLITSGLA FGPLFKNLSD
VRGTADARGE VFGLVTVPDI AASMPKGFTH PHLIHPATMD SMMHFFIASV MDHTGKNTLR
TAMVPTFIKD VWISAQVDNN PSHTFRGHGK STFLAYDKYQ SDVMVWDGAT DEARISIKGI
RAAPLESIDS GSGESRKLCH NIEWGLDADL LSPASFPAVV HATHEDNLDY KYWINRFQLA
TLLRVTDALS ALGDFNTDVL EGHFLKYWNW LKQLEEWLHA DQISGMKLSD WTEYNNDPSL
KAQLFEEVAA HNADGALAMR MGSNITAVLR KEVDPLHLMF GQDDLLNHVY EQVVKLGDLP
NLQKAYLEIV AYNSTNLRIL EVGAGTGSST AAMLDGLSQS TDGGKNMTSR IETYTFTDVS
SGFFEKAQEK FKAYKNILEY RILNVEKDVS SQGFDVKSYD FIVAGNVIHA TADIKKSLTN
LQELLKPGGK LILHEGIRQD YLWSGISFGQ LPGWWLGVEP IRQWNPWITA VQWNVILKEA
GFSGVDLDLP DRKDPNLHTQ SLLIATAVEP SGAMPQTVIV TTTPSCDSEL ITALKSHLEF
TLKIPNVCTV HYLDLGNTDL SKAVCISVME LERSVLSTLA MTEYNNIRHL LVTCVGMVWI
TGDTLTNPSF NMITGLTRTV RWERDIDEVN LITLSVCEPR PAVSDLVSSI GRLYSQQFIA
TLPADKINGE YMLRHASFLS ARLMDSDTGN DYLSSKTVRP TPVLQELSKA GRPLKLATAS
PGQLDKLEWV TDSIYAEPLS ETQVEIEIKA VGLNFRDLMI AMGEHMAYSL GNEAAGIISR
VGLGVTAFKP GDRVVYMCGL ESTGCFQTYG RVDQNVVVLI PDSLSYEIAC SLPCVYSTVI
YGLMDAARLL KGEKILIHAA AGGVGQAAIN LSKMIGAEIF ATVSTPEKRA LLVKEYGINE
EHIFSSRDLT FVQGIMRVTN GKGVDVVLNS LSGEALRRSW DLIAPFGRFV EIGKKDAQAN
GKIELHPFLR NVTMTSVELP TMMRHRPHLI QRLTADTIKL YDEGKIKEAI PTNVMGYDRI
EEGLRMLQSG KGMGKMVFRP SPSDIVPIVP EQTTPYRVEA DATYVLAGGL GGIGRSMAKW
LVERGAKSLV FLSRSGRVTD AVGKMMLDLK TAGCNVKVFT CDVTDKMRLA EVMDECKVTL
PPIKGCIQGS MVLKDVMFEN MSYDTFEAAV KPKVQGSWNL HELLPANIDF FVLLSSATGI
LGNRSQANYA AGNTYQDALA RHRISKGLPA AVIDLGTVMS VGYVAENKER ASMAKHLGTV
LEVLREDEIH TLIEYLMDPR SKLSELSCQL VSGLTTAAIY RERGIPTPTY LSYPLFTHLR
TASSSRSEGS EEDPSFLVQA QLRAATSLEE ATAVAANGVR AKLSSLLAVP QDNIDPTKSI
SSNGVDSLVA MEFRTYLTKD LGADVPLLDI MGTSSIMVLS QKIASVSKLV LISDEKET
//