ID A0A158QY53_NIPBR Unreviewed; 522 AA.
AC A0A158QY53;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=PlsC domain-containing protein {ECO:0000313|WBParaSite:NBR_0000789201-mRNA-1};
GN ORFNames=NBR_LOCUS7893 {ECO:0000313|EMBL:VDL71482.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0000789201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0000789201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL71482.1, ECO:0000313|Proteomes:UP000271162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; UYSL01019938; VDL71482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158QY53; -.
DR STRING; 27835.A0A158QY53; -.
DR WBParaSite; NBR_0000789201-mRNA-1; NBR_0000789201-mRNA-1; NBR_0000789201.
DR OMA; YMRILVK; -.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PHOSPHOLIPID ACYLTRANSFERASE; 1.
DR PANTHER; PTHR23063:SF53; PLSC DOMAIN-CONTAINING PROTEIN; 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000271162};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..522
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033250503"
FT TRANSMEM 6..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 243..354
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 522 AA; 59658 MW; 278A1CAA51539B67 CRC64;
MAAWVVLMLF PPMTLAVLVV VIVATFGGTL GVREMFVEGL TRIFEWGSKT SHGYEYLETE
VEPSSTESAP RLKKRHSSGD LGIIHREKSE LIDSKLHSTD APPCRQTTVS VVVDDSIDFI
TAGIEAIIED QVTSRFRAEQ LPSWNLLTRT RYSFQYINWR LSLLWAAGFL FRYLFLVPIR
IFLFMLGLST MCGVCYIVGH IPNPKVKKFL NRHVMLMSMR IFSRSFSSII RFHDQENRAK
KGGICVANHT SPIDVMVLSC DNCYAMIGQK QGGLLGFIQD SLSRSEHHIW FERSEAADRK
KVTQRLKEHV EDENKLPIII FPEGTCINNT SVMMFKKGSF EIGSTIYPIA MKYDSRLTDA
FWNSSEQSYG EYLWRMMTSW AIICDVWYLP PMTKEPGEDA IAFARRVKRA IAKKGGLVDL
EWDGALKRER VSSKLIQLQQ KLYYDRLTRT TTINNLTEED MQTDVLDIMQ SISEEDRNSL
MKQLDETDDD DAIIRKVSAY GHELRKVSDS MGAVLEPEVK NA
//
