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Database: UniProt
Entry: A0A094CSY4_9PEZI
LinkDB: A0A094CSY4_9PEZI
Original site: A0A094CSY4_9PEZI 
ID   A0A094CSY4_9PEZI        Unreviewed;      2075 AA.
AC   A0A094CSY4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY50435.1};
GN   ORFNames=V496_09344 {ECO:0000313|EMBL:KFY50435.1};
OS   Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY50435.1, ECO:0000313|Proteomes:UP000029302};
RN   [1] {ECO:0000313|EMBL:KFY50435.1, ECO:0000313|Proteomes:UP000029302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
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:KFY50435.1}.
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DR   EMBL; JPJY01001845; KFY50435.1; -; Genomic_DNA.
DR   STRING; 1420909.A0A094CSY4; -.
DR   HOGENOM; CLU_000022_6_0_1; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000029302; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; 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; 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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
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: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; 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   SMART; SM00823; PKS_PP; 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; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029302};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          364..796
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1663..1737
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1606..1649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1737..1759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1610..1643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1737..1756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2075 AA;  224973 MW;  967AAFE4BAEB5418 CRC64;
     MTGQFQFVVF GDQAIPYHKE LQKLIANKES HTVAVFLAEA YHALKRDISR LSSSQRAQFP
     TPSTLAELLV AYQSSPGPNC ALDSALVCLH QIASFISYIS ETQNEYPQSS SSTVIGSCVG
     LLAATAASCS QNVVDLLTLG PEIVVVAFRL GLLVQTKTNS VASNSDKSTF YSSVVGGIDK
     DSAAHLIDEY CLSKGLSASS RIYVSAVGHG SITVSGPPAH LRDFCSQNSS LKSVNVPVGG
     LFHSPHLYSV IDAKNLVETL SVGSQKRVAR LDVLSNSDGQ KIPSTTCKGT LEIALWNILS
     KQLRWDLVTE NASSKLAQLG GLSVRILPFA SGSVQSLATA IGQSGSRTVE TTDTAVRLEQ
     ESKRSKIAII GFSGRYPEAE SNEEFWNLLV SGLDVHKEIP KDRFDPWLYY DPTGKGKNTS
     GVTKGNFLKN PGLFDARFFG LSPREAEQAD PAQRLAMMTA YESMEMAGFV PDATPSSQRD
     RVGVFYGTAS DDYRECNASQ NIDTYFVPGG SRAFLPARIN YQWRFSGPSF DVDTACSSSL
     AAIHIACNSL WRQDCDTAIA GGTNVLTNPD NWAGLDRAHF LSHTGNCNTF DDGADGYCRA
     ESVATVLLKR LEDAEMDGDP IFGTILGAYT NHSAEAVSMT RPHSGAQRAI FSRIMTGAGV
     DSSDVSYVEM HGTGTQHGDA CEMDSVLSVF APEGTQRSQS LHLGSTKANI GHAESASGAS
     SLIKVLLMME KGWIPPHVGI KTRINRNFPT DFAQRNVHIA LKPTRWTRPL DKPQGRRAFV
     NNFGAAGGNS SVLLEDAPLL QPAVQDPRPL HMVAVSAKTP TSLKRNIRAL REYLDVNPDL
     SVSSLSFTTT ARRIHHGFRA IVSGASIYDI RNALQVAEAT EGYTSTATVN TTVGFCFTGQ
     GPQYLGMGQQ LLQIPQFRTI VMGLEDILRV QGFQSILPIF EGSCTTPLED LPPPTLQLSI
     TCLQIALAKF WKSLDITPQV VIGHSLGEYA ALNFAGVLSD SDTIHLVGTR AKLLEKHCTI
     GTHAMLAIKA SLSTVASLIA PHPGLEIACI NGPEEIVVAG SNGDIETFSN ALSRVSIKGT
     QLKVQFAFHS AQIEPMLEAF QHSCRSVTFK DPAIPVVSPL LSKTITSASE FGLPSVYLSR
     HCRETVQFGL ALQASCASGA VTEKLVWVEI GPHPICSNMI KNTVGQDVRA FPSLRRNENP
     WKVFVSALTS LHACGIAVNW NEYHSGFKAA LRVLGLPAYQ WELKEYWIPY MHDWCLTKGN
     APAQIQQALP SPVEEAPQPI ITASVQRIVE ENHSGNEAWV TARSDVKYPD LLAILNGHRI
     NGQPLCPSSA YADMALTLFT RLLEKSSLAD KSDFGVSVCD MAVDKTLLVN GDPSQLIEMK
     VSANWSTRTA TFTLCSITEG GKITTNHAKC TGTFTRKSEW TAEWKRRTFL VKSRIDHLQK
     SIHDDSESSA HLLKPGMFYK LFSSIVEYDD AFKGLREAII RSEDLECTAK VKFNTLVGEG
     DKWVLSPYWI ESLGQITGFT LNGNDALDSA NQVFINHGWG TMKILKALSP EETYRTYIKM
     HTEDNSSYAG DLYILDSNEE LIGMYEGVTF NALNRKVFER VLPRPGASSS LKKDSVSRGT
     HASSSTSSHA SSVETQEQIT RRAQPSLPMP PAVVQLKKDN LGPDIAASIR AMISDEVGVP
     TNELKDEDDL VDLGVDSLLA LTMADRIREE FDVTVDSTAF MGSLTVRDLI QLIARDSASS
     SGDDSSGPST PPSTDGLTPA VAVLTPLSGL PTPGIWDCNS NRKMLGHDLA GSTPPDSIKT
     PPLPLSAPIL KMVSATSVLL QGNPPMASKT LWLVPDGSGL ATSYLPLPDI DATVAVYGLS
     SPFIKRTEGM SQYPFSDLTA TYLTEIRRRQ PHGPYYLGGW SAGGICAYDA AQNLVAVGEE
     VKRLILIDSP NPIGLQKLPP RLYDDFDRIG IFGSSGTSAK KPPAWLLPHF TGFVDILHSY
     EPQPWVGQKP LETWVVWARD GVADDGSIEI RAGDPPNLKW LLRKRSAEDL GPNGWDKLVG
     RENITIEVLE EANHFSMVKS PAANGVSDFI AKAMA
//
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