ID   A0A0C2D0Z0_9BILA        Unreviewed;       393 AA.
AC   A0A0C2D0Z0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Acyltransferase {ECO:0000313|EMBL:KIH55702.1};
GN   ORFNames=ANCDUO_14135 {ECO:0000313|EMBL:KIH55702.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH55702.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH55702.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH55702.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR   EMBL; KN736901; KIH55702.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2D0Z0; -.
DR   Proteomes; UP000054047; 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:SF76; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE EPSILON; 1.
DR   PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 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; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:KIH55702.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KIH55702.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        24..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        372..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          90..262
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   393 AA;  44751 MW;  B087C4E51144AD16 CRC64;
     MIISVLAAAD QIRAAVPCSL LSFSMVPFAT ISLGIGAVSW VVPRKTTQFL DNTLYRAYMR
     LCLFVFENLS GVQLKLYGDV EQLRQKPESA LVLANHQSDV DWAVIVMLAQ RQGAEGNDAG
     FRVMVKHVIH YVPLFGWYIF QDGFQLITLL MFVLNCLYYS LGLSQHGYIY VRRFGEFLSA
     PVLKQLAWLD TIDEKFWLLV FPEGTRYSLK RKENILVSQE FCRRKGIPEF KNVLSPRAGG
     AFMALENLES LDAVYDVTIA YGQTRLPNRR GLAPNMFEFC CGSPAAKTLS VHVKRYPAEQ
     LHKNSRKELQ DWIIQAYYEK DRLLDEFHKT GEFPDPVSVN EPAVSLFRTL PPTLFFAAAL
     VAPFYSPTVR SAYFYTMASF PLLILWLEVK KCA
//