ID E6ZRE5_SPORE Unreviewed; 883 AA.
AC E6ZRE5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 28-JUN-2023, entry version 46.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=sr15720 {ECO:0000313|EMBL:CBQ69802.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ69802.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ69802.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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DR EMBL; FQ311438; CBQ69802.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZRE5; -.
DR EnsemblFungi; CBQ69802; CBQ69802; sr15720.
DR VEuPathDB; FungiDB:sr15720; -.
DR eggNOG; ENOG502QY9M; Eukaryota.
DR HOGENOM; CLU_008597_0_0_1; -.
DR OrthoDB; 2728187at2759; -.
DR Proteomes; UP000008867; Chromosome 17.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd06661; GGCT_like; 1.
DR CDD; cd07992; LPLAT_AAK14816-like; 1.
DR Gene3D; 3.10.490.10; Gamma-glutamyl cyclotransferase-like; 1.
DR InterPro; IPR009288; AIG2-like_dom.
DR InterPro; IPR013024; GGCT-like.
DR InterPro; IPR036568; GGCT-like_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR31605; GLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 1; 1.
DR PANTHER; PTHR31605:SF0; GLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 1; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF06094; GGACT; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF110857; Gamma-glutamyl cyclotransferase-like; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 4: Predicted;
FT DOMAIN 70..199
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 883 AA; 96437 MW; C56859F357D3007D CRC64;
MTSITSAPAP SSKAARASAT AAGTKRTDST PTFGVMWTVM RSIGDVSLPF FFSSIHVASA
HAVPPPTTPL IVCSNHSNTI LDVAMLASHF PERRPLHFWA KAGFFRNRIT RFILTSSGNI
KVDRRNKNNQ ALFEGTFEAM KAGGAIALFP EGGSYTIPAL APLKMGAAWA ALEYSRCLQL
QREAGGDEVR ILPAAVVFDD KSVFRSRATL RFGKPLRLDG YIEEFLAAPE SESRAEKATA
TEAVKEDGTV PATPESMTRS NTASGAPPAE QYASPAHRAV ARLTADLQKA MQELTFNAPD
WQTFQAVRMA REIIFQSGHE EASEGIDEYV ELSRALMVLL TLDISTLTTQ PDVKRKSQQA
RRALFALSSL LHLADIDNAT LSRVARHSTT ARSALTTPLT SLLTRLPLYI PIFTPTLLPT
YVIPNYLAHH FAAREEESLS SVKTLFSFFL TSMLYSTLVV KTLQWTRWSP PGLLVGMAGV
WWLHDLNRTC VDRAWGLVKE ARLGWRVWRA GVGVDTVAPL RGQKQEARKG KSLFFYGTLV
HPKILARVIG NDGAHLEVQN GVLDGARLHH VKGEEYPGLV HVESAAGSIN AVKGTLVRGL
TPADLRCLDA FEGDEYERRP VTIIPDASSP AEPNSTRIAN AGTAPLHAIL SGLTKARIES
LCAAASEEAK VEAEVYTWTA GRDKLEERIW EFDVFAQTHA ANWVGEGEVE HEHEYQVVDR
VRSDQLTSTP TLTSSTDAPS TPADAEQEWI EAHASTLVEQ GPVHQAVVQV CKTLSTQPSI
QFYVDKAFKG GKVKRPRKGD ARLVRAVFRA RAAARAELEL LMRMVEAAQV EEVQQAVGLL
VGAKKRALAG VGARMTGEAG WPFNQEQVDE LGGGARVESR KMV
//