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Database: UniProt
Entry: A0A094EEY0_9PEZI
LinkDB: A0A094EEY0_9PEZI
Original site: A0A094EEY0_9PEZI 
ID   A0A094EEY0_9PEZI        Unreviewed;      2248 AA.
AC   A0A094EEY0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V499_05002 {ECO:0000313|EMBL:KFY74983.1};
OS   Pseudogymnoascus sp. VKM F-103.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY74983.1, ECO:0000313|Proteomes:UP000029295};
RN   [1] {ECO:0000313|EMBL:KFY74983.1, ECO:0000313|Proteomes:UP000029295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY74983.1,
RC   ECO:0000313|Proteomes:UP000029295};
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:KFY74983.1}.
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DR   EMBL; JPKB01000765; KFY74983.1; -; Genomic_DNA.
DR   HOGENOM; CLU_000022_6_0_1; -.
DR   Proteomes; UP000029295; 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; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
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; 2.
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; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          381..813
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1661..1735
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1789..1870
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1743..1790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1746..1781
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2248 AA;  244373 MW;  726372E7E5154B38 CRC64;
     MAEKISFLLF GEQSLDTQGF LADFCRNGNP SILSHAFLNR VASTLQNEIE RLPSLERRHI
     PSFTTIQELS QRYHTRDVTH PAIDSALLVT TQLAHYIDRA EKVPEDATRP QETWTVGLCT
     GLIAAVAVSI APSLSALVNI GAEFVLLAFR TGRHVSALAE HIHESGDAAK SWTYVVPGLN
     EPAGRSLLAD FNESKGYTTT SQAYISAITS TSIAFSGPPP TLKALVDEHE FKDGPLPLPI
     YGPYHASHLY SAAEIEAVLR LNDSNLSEVL KNASRRFPVI SCSTGQWLAE KDPKKLITAV
     IRDILLEPLN FQRVLASCVT QANNYRSSSC LVIPFGPTQA ASSLVQQLKN ETGLEVHLRR
     APHSKKDRMA PHTGDHGSSK RCKLAIVGMA GRFPDAATHE KLWELLEKGL ALHREVPADR
     FDMKTHCDPS GKVMNTSHTS YGAWIENPGL FDPRFFNMSP REAHQTDPMQ RMAITTAYEA
     LEMSGYVPNR TRSTKLDRVG TFYGQTSDDW REINAAQEVD TYFITGGVRA FGPGRINYHF
     GFSGPSFSID TACSSSMAAM QLACTSLWAK DCDTAVVGGL SCMTNSDIFA GLSRGQFLSK
     NGPCATFDND ADGYCRADAC ATVIVKRLED AIADKDNVLG VILGTATNHS ADAVSITHPH
     AGTQEILYRN ILNMAGVDPL DVDYVEMHGT GTQAGDATEM KSVTNVFAPA DQKRSAEQSL
     YLGSVKANVG HGEAASGVTA LIKVLMMLQK NTVPPHVGIK KTINRTFPKD LAERNVHIAY
     HSTPLLKKAG QPRRVFVNNF SAAGGNSGLL LEDGPATKTL LTDNRSAHMV SITAKSKSAV
     IKNAERLMYY IEQHPEASLA DISYTTTARR IQHNWRISVT GFNITQVREF IKHKLTEDIT
     PIPLTTQEIV FVFTGQGSHY AALGKELFES SSLFKETMLE FNNIAAMYCL PSFLPLIDGS
     AAAVEDLSPV VVQLGLLCFE MAMARLWASW GINPSVVIGH SLGEYAALNV AGIISASDAI
     YLIGKRAQLL MEKCTVSSHG LLAVKASVLS IRESVDEASI NIACINGPEE TVLSGDTALI
     YVISERLTAA GFKCMQLKVP FAFHSAQVDP ILDKFEKLAA SVQFHAPTAP IVSTLLGRQL
     REGETVNASY LRRHAREPVN FLDGINSIRS AGLVNEKTLF LEVGPHPVCI GMVKSTLGKE
     TVAVSSLRRT ESAYKTLSDS LSTLHTAGFN IDWNEYHRDH LECVQLLDLP TYAFDEKNYW
     IQYTGDWCLT KGRASDSQVA SCQDSKPKIS TTTVHKVVED LVDGDVATVS TESDLARADL
     RSAVMGHLVN GAGLCPSSIY ADMAMTVCEY GYKLVRPDVE NIGINVASME VIKPLIARPD
     GASQILKLTA YIDASRSSAK LIFSSGSDKA RVDHAHCVVS FGDCAAWLSE WERVAYLIQH
     RVDWLKNAEK NGKASKIGRG LAYKLFSALV DYDAKYRGME EVILCSENME ATSHISFQTK
     PTDGTFVCSP YWIDSVAHIS GFIVNGSDAV DSGNQVYVSH GWDSLRIAEP FSAEKTYRSY
     VKMQPAGGKM LAGDVYVFDG SRIVAVVGGL KFQCILRTVL NTLLPPVGVT APPAQAPVAE
     PSPAVAIPTT STLHKTTTTT TKIKTAQDST TSLEPASKKF VTICSQTMDI VAKEVGVGMD
     ELVDNITFAD LGVDSLMSLT IGGTVREKLE IELPSSIFLE CPTIGQFKSF LARFERADSE
     ISEDTEDSIL YTNTDDSTPN TDDSTPNSDS STPNFGEMSP LSTPADDSDL ELSKDDQLCE
     IIQNTIAVEV GVTTQEVAHA LDLALLGVDS LMALLILGKL REKTDLSLPA DLFVTCASIK
     DIERKLGIGQ PPKPVRIPAR SFPKLLPRPI STETVSPKET GHQVTNITPE RFATSVLLQG
     KIRTATSHLW MVPDGSGSAT SYADIPEISP GLAMWGLNSP YMKTSEEFTC GVPGIAAKYI
     QEVKRRQPVG PYLLAGWSAG GVIAFEMLNQ LVKAGDRVSH LIMIDAPCPL IIEALPTSLH
     RWFASIGLLG DGDPNKLPSW LLPHFAASVA ALSTYDAVSI PKDKAPSVTA IWCEDGVCKN
     ESDPRPDPYP EGHALFLLDN RSDFGPNLWD SLLPAEKIRC VPMKDALLKR ASKVLLITMY
     DHYLDSRFDY VTQSKLSHPS VTILARDALP VLETHGQKRA LSDIINDLNT KKSYGRSGLS
     QAASAQLHVE DVAALSDSAI GRRTGTEP
//
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