ID A0A368H8N8_ANCCA Unreviewed; 310 AA.
AC A0A368H8N8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Acyltransferase {ECO:0000313|EMBL:RCN52961.1};
GN ORFNames=ANCCAN_00956 {ECO:0000313|EMBL:RCN52961.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN52961.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN52961.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN52961.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-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:RCN52961.1}.
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DR EMBL; JOJR01000004; RCN52961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368H8N8; -.
DR STRING; 29170.A0A368H8N8; -.
DR Proteomes; UP000252519; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR10983:SF16; LYSOCARDIOLIPIN ACYLTRANSFERASE 1; 1.
DR Pfam; PF16076; Acyltransf_C; 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:RCN52961.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000252519};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RCN52961.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..204
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 310 AA; 35913 MW; 0CA54016F0D403A2 CRC64;
MFGRLNGVVF VLLVFLTSFL GSIFMLFPLL PFAYYGTKFW RICADRLVGY WLTFPASLVE
YVFGSNFHVT GDLILRDKPA LIIMNHRTRL DWLFLWNALY KMDPLLLTTE KISLKAPLKR
IPGAGWAMGC GAFLFLERNF ESDKCTIASS VEYYKESGNN YQLLLFPEGT DRGARAAAQS
DAFARENGLP LYDYVLHPRT TGFNYLLDVM RRSNYISYVY DVTVAYEDVI VDTEMRLLKE
GVFPKNVHFD VKKYDISDIP TDPEKSADWL KQLWHTKERR LKKFYEAESH KRRLDPSGEG
YMWPVGPCCL
//
