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Database: UniProt
Entry: A0A094D7U7_9PEZI
LinkDB: A0A094D7U7_9PEZI
Original site: A0A094D7U7_9PEZI 
ID   A0A094D7U7_9PEZI        Unreviewed;      2499 AA.
AC   A0A094D7U7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY55585.1};
GN   ORFNames=V497_06865 {ECO:0000313|EMBL:KFY55585.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY55585.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY55585.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
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:KFY55585.1}.
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DR   EMBL; JPJZ01001146; KFY55585.1; -; Genomic_DNA.
DR   STRING; 1420910.A0A094D7U7; -.
DR   HOGENOM; CLU_000022_6_0_1; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000029268; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 3.50.50.60; FAD/NAD(P)-binding domain; 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; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
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:SF15; POLYKETIDE SYNTHASE 16-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF01494; FAD_binding_3; 2.
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   PRINTS; PR00420; RNGMNOXGNASE.
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; SSF51905; FAD/NAD(P)-binding domain; 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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          364..796
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1664..1738
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1604..1649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1737..1780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1605..1649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1737..1776
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2499 AA;  270157 MW;  0D1E393200132C6A CRC64;
     MTGQVQFVVF GDQAVPYHTE LQKLIVKKES HTLAVFLAEA YHALKREISH LSPSQRTQFP
     TPSTLAELLV AHHSSSTPSC ALDSALVCLH QIASFVSYIS ETQNEYPQSS SSAVVGSCVG
     LLAATAVSCS QNVVDLLSLG PELVVLAFRL GLLVQTKTNS VASNSEKSTS YSSVVGGVDK
     DSAANLIDEY CLAKGLSALS RIYVSAVGHG SITVSGPPTH LRDFCSENSS FKSVNVPVSG
     LFHSPHLYAD INVEDLLRTL SPDLRKRVAR LDVLSNSDGQ NIPSKTCEGI LRIALLDILS
     KQLRWDLITE SASSKLTQLG ALDARILPFA SGSVQSLAAA IGQSGSRTVN IADTAVRLEQ
     ESKRSKIAII GFSGRYPEAE SNEEFWNLLV SGLDVHKEIP KDRFDPWLYY DPTGKGKNTS
     GVTKGNFLKN PGLFDARFFG LSPREAEQAD PAQRLAMMTA YESMEMAGFV PDATPSSQRD
     RVGVFYGTAS DDYRECNSSQ NIDTYFVPGG SRAFLPARIN YQWRFSGPSF DVDTACSSSL
     AAIHIACNSL WRQDCDTAIA GGTNVLTNPD NWAGLDRAHF LSHTGNCNTF DDGADGYCRA
     ESVATVLLKR LEDAEMDGDP IFGTILGAYT NHSAEAVSMT RPHSGAQRAI FSRIMTGAGV
     DSSDVSYVEM HGTGTQHGDA CEMDSVLSVF APEGTQRNQS LHLGSTKANI GHAESASGAS
     SLIKVLLMME KGWIPPHVGI KTRINRNFPT DLAQRNVHIA FKPTRWTRPL DKPQGRRAFV
     NNFGAAGGNS SVLLEDAPLP RPTVHDPRPL HMVAVSAKTP TSLKRNIRAL REYLDSNPDV
     SVSSLSFTTT ARRIHHGFRA IVSGTSTYDI RNALQIAEAK EGYTSTAAAN TTVGFCFTGQ
     GSQYLGMGQQ LLEIPQFRAI VMGLEDILRM QGFQSIIPII DGSCTTPLED LPPATLQLSI
     TCLQIALGKF WKSLDVTPQM VIGHSLGEYA ALNIAGVLSD SDTIHLVGTR AKLLEKHCTI
     GTHAMLAIKA SLEKVSSLIA PHQGLEIACV NGPEDTVVAG SNGDIEAFTN SLSRVSIKGT
     QLKVQFAFHS AQVEPMLEAF RHSCRSVTFK DPAIPMVSPL LGKVITTASE FGLPSVYLSR
     HCRETVKFCT ALQASCASGA VTEKMVWVEI GPHPICSNMI KNTVGPGVRA FPSLQRNESQ
     WKVFVSTLTS LYTCGLAVNW NEYHSGFKAA LRVLGLPAYQ WELKEYWIPY VHDWCLTKGN
     APAQIQQALP APAEEAPQPI FTASVQRIVE ENHSGNDTWI TARSDVKYPD LFAVLNGHRI
     NGQPLCPSSA YADMALTLFT RLLEKSSVAD KSDFGVSVCD MAVDKTLLLN GDPSQLIEMK
     VSANWSTRTA VFALCSITKE GKITTNHAKC TGTFTKKSEW TAEWKRRAFL VKSRIDHLQK
     SIHDDSESSA HLLKPGMFYK LFSSIVEYDD AFKGLREAII RSEDLECSAK VKFNTPVGES
     DKWVLSPYWI ESLGQITGFT LNGNDALDSE NQVFINHGWG TMKVLKKLSP EETYRTYIKM
     HTEDNTSYAG DLYILDSNEE IIGMYEGVVF NALNRKIFER VLPRPGASSS SSSKKNSVLP
     DIPVSSVPSR VSNVETQQQI TEQAPSSQPI PTVVPQLIKE DLGPDISVSI RAMISDEVGV
     PTNELKDEDD LVDLGVDSLL ALTMADRIRE EFDVTVPSTA FMGSLTVRDL IQLIAGDSAS
     SSGDDSSGPS TPPSTDGLTP ALATSTPPTE QPTPGIWDCN SKGKMLGHDL ASSTPLDFIK
     LAPLPLSSPR LEMAPATSVL LQGNPRTASK TLWLVPDGSG LATSYLPLPD IDDTVALYGL
     SSPFVKRTEG MSQCPFADLT AAYLTEIRRR QPHGPYFLGG WSAGGICAYD AAQYLIAAGE
     EVKRLILIDS PNPIGLQKLP DRLYDDFNRV GVFGSGGTSA KKPPAWLLPH FTGFVDILHS
     YEPRPWAGPK PLETWVIWAR DGVADDGSIE IRAGDPPNLK WLLRKRSLED LGPNGWDKLV
     GRENITIEVL EEANHFSMVK SPAAKGCSNY MSWRGQGKAA RPAPKSVHGA GPSGLALAAL
     LQAHSIHPTI YELRAKPTPA FFAAPCGMLD LHEDSGLKAV RAAGLWDAFQ ATLGDCSEEC
     RVLSPSGETL HTDQGELSER PEIARNALTK LLLGAVAPES VKWGSKVQSV RSAKTDAGAT
     EVTLDLGEEG SATYDFVVGA DGAWSRVRKM LTDVVPVYTG AQYMAATLRE ATAKFPQLVE
     VVGSGTMMAL GGGRGIMSHR GPQDSIRLYI AVKTPLENWA KEVGIAGKTA AEAKGVLLGE
     GGEYEKWAPQ LQELLATACD EEARDHPGEA MDILPLYMLP AGSRWDTQTG ATLVGDAAHL
     MTPWAGEGVN QALLDALELA GVLGGVGQAE GVVQWQEALE APLRKFEEAM IERTKGEAEK
     AARNGEMMLG EHGGQAIADI FKLFEDIAAK GGEFPEGLL
//
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