ID H0EUP6_GLAL7 Unreviewed; 1353 AA.
AC H0EUP6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Putative Phthiocerol synthesis polyketide synthase type I PpsC {ECO:0000313|EMBL:EHK97750.1};
GN ORFNames=M7I_6483 {ECO:0000313|EMBL:EHK97750.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK97750.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHK97750.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(2012).
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:EHK97750.1}.
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DR EMBL; AGUE01000179; EHK97750.1; -; Genomic_DNA.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; H0EUP6; -.
DR Proteomes; UP000005446; 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF49; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF21089; PKS_DH_N; 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 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 PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005446};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1243..1327
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1353 AA; 148490 MW; 835E3D919AD514AF CRC64;
MDTPNLDQLF KHQQYIETNP ENQDIDLMNN TLSKLDHPPS WNIKEELLKH ESVALVNLLR
QFGVKPAAVV GHSSANEAII IAYYRGQVTK GFSRRGGMAA VGLGREDVMS FLNPGVSIAC
ENSSSSVTLS GDEDALNATC EIIKTALPDV FLRPLKVEMA YHSPQDHLFL EIGPHSALAG
PIRQILKANS RKNDTKYPNH EILGSRTVEG NELQPEWRNV LHLDNVPWLR DHQIINDVVF
PCAGYLSMAC EAIRQISASE DFTFRNIVIQ TALVMSDSKS VEMITSLRPL FIVSTCEGTL
RNINKLCVPT SIDQLYICGG KSTSGIKAEA CGAQTSTGTI SGDVVAISGD AIILSLIGGQ
FSPIEEDSSD EDLDTVAGAR LDWKPDLDFV QIDNLIRPRQ QSTAATKTLE KFTLLSMIDI
GRRISGLVTK SEYLEKFRSW INAQVERASE DRYNLVEDAQ ALTVLNAGER QMLIAELSKE
ISNSEVATSG ELISRVVKNC EDIMSGTPNG LHRFLYSGWA FETKLTGPGN RVWNRRHLSC
HARKLLAEDG RLFLQELSPQ VQFANLIMGV LPGWWLGEAD GRANEPYISP ERWAVELRKA
GFSGCDATVY DAEQPYQFNA NIISRPAKVD RIARRITLLY EPNLNIQQIK FSLENKGYSV
DLCTIQEEPP AGQDIVSLLE LETPMFEKIS AQIESYDPRF GMVLGLARTL RSELSLSIAT
LEIDTVDEVA YNAITNVFDK LKNSSSVSDM NPDYEFGLLQ TLRWVPDLQN KVGHDQVIVE
PRCAGLNFKD VLVSMGIVSG DGLGLEGSGT VVGVGSEVTD FQVGDRVLYI DQNCFSTRTA
IPALRCAKIP STLSWEEAAT MPCVYATVIH SLLNLGRIQK GQSVLIHSAC GGIGLAAIQI
CQNIVGAQIY VTVGNEEKVH YLMDTFGISR DHIFNSRDTS FLPAIKAATN GRGVDVVLNS
LSGELLHASW ECVAEYGSMV EIGKRDFIGK AQLNMDLFES NRSFFGVDLA KFDAARCQLL
LVQMMEFYEK GLIKPIAPMK VFEGAKVEDS FRYMQKGSHI GKIVVTIPEQ NTDLPLASIV
PKLKLNPDAG YLLVGGLGGL GRAVSTWMVE RGARHLIFLS RSAGKSDQDQ SFFPTSSLSG
SFGNAGQANY AAANTFLDAF VQYRHSLGLP ASVVDIGVMG DIGYVSRNAA IQESLRGAGT
YFLQEQDFLD SLNWAVAKSA VKPSLPGQNQ LLIGVRSSKS LSDPSNHQLK SFMSSVETDS
SILNVPASLD LVTNEIGTLA ALGVDSLVTI EIRNWMKRSF GGLEFSTLEI LNAGTIEALG
LLTIEGLKRK YEMKDGEAKF SEREDTYLLM KAP
//
