ID A0A135S6P8_9PEZI Unreviewed; 333 AA.
AC A0A135S6P8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Acyltransferase {ECO:0000313|EMBL:KXH31511.1};
GN ORFNames=CNYM01_06562 {ECO:0000313|EMBL:KXH31511.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH31511.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH31511.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH31511.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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:KXH31511.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JEMN01001617; KXH31511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135S6P8; -.
DR Proteomes; UP000070054; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR23063:SF1; LYSOPHOSPHATIDIC ACID:OLEOYL-COA ACYLTRANSFERASE 1; 1.
DR PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:KXH31511.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KXH31511.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 107..220
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 263..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 333 AA; 36638 MW; 4950718DBA7C0850 CRC64;
MEKFSQFRDK GSGISPFIPV KTALSPLSSI FHTFLFFIRL PLFLTYAATY FLFLQHLCPF
LPIAVRKVLL WGMMGIPGIW WVDLQLDGVR RGTLADQPPQ RFPHPGSVIA ANFTSPIDAV
YLAAIFDPIF TISYPNTRSV EQISLLRAVF YALSPVRFAP PPATRKLTDL AALVARYPDR
VVAVFPEGGT TNGKGVLPFT PSLLAVSPEV HIFPVSIRYT PADVTTPIPG RWAKFLWDLL
SRPTTCIRVR VAESILNSSA AQTNGVSSSA ASRENTAQRR IGAGGGDAPA LSIEEQRVLD
KVGEALARLC RNKRVGLTLR DKSAFIEAWN GRK
//
