ID A0A0B7MYI2_9FUNG Unreviewed; 353 AA.
AC A0A0B7MYI2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN Name=PARPA_04877.1 scaffold 15694 {ECO:0000313|EMBL:CEP11076.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP11076.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP11076.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP11076.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; LN725636; CEP11076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7MYI2; -.
DR STRING; 35722.A0A0B7MYI2; -.
DR OrthoDB; 1080at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR23063:SF2; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 4, ISOFORM D-RELATED; 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 Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 150..264
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 39975 MW; C443CDA177666968 CRC64;
MPPQDPSIPT SILLSSQNSS SESLDLMRSD YVQGTTKKSY QTEYTREQLL SFAKCFTSDV
VKASSRFLEM IGFLTAVPSI IIRYGILFPL RFFTLGASTI AFFMTLPIGV TLKSSEIVSF
CVKYYCKGIL FSLGVKANYI GEKPQLNEPH VFVANHTSYL DYILLGAHKF PHAVVMARHS
GVLGFLQNNG LNYLHSLCFD RANITERKDL SERLKKHVKS ANTWTNPMII FPEGTCVNNK
YAIRFQKGAF ELGVKVCPVG IKYDRSFGDP YWDTRKGFMF YAYYRMTRWI TPVDIVYCKP
EVPLKGETSV QYGERIKDKI ASSIGLKKVD FNGMAKRDLL EVLKEGNPAK KIL
//