ID A0A0B2V9I5_TOXCA Unreviewed; 386 AA.
AC A0A0B2V9I5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE SubName: Full=Lysocardiolipin acyltransferase 1 {ECO:0000313|EMBL:KHN78132.1};
GN Name=LCLAT1 {ECO:0000313|EMBL:KHN78132.1};
GN ORFNames=Tcan_06207 {ECO:0000313|EMBL:KHN78132.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN78132.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN78132.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN78132.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-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:KHN78132.1}.
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DR EMBL; JPKZ01002158; KHN78132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2V9I5; -.
DR STRING; 6265.A0A0B2V9I5; -.
DR OMA; ESSAWLM; -.
DR Proteomes; UP000031036; 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:KHN78132.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KHN78132.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..215
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 386 AA; 44512 MW; A0B943E67A9908B7 CRC64;
MAEPKRIQHT DVWDKVRGSV LCVFTLLSAL LGSMYILTPL LPLLFISHQK WRKIIDRLVG
YWLMLPSALI EFAFGTKIRV TGTMIDHSEP ALIIMNHRTR LDWLFFWNLL IRMDPWLLTS
EKISLKGILK YLPGAGWAMG CNAFIFLDRS FEKDSVRLAK MIDYYANSGF NYQLLLFPEG
TDKCERATER SRIYAEKKGL VHYAHVLHPK TTGFTFIMKK MREAGYIKHV YDVTVAYADS
IVQSEVDLLK LGACPRSVHF DVRKVDAASL PEDDEELAKW LVELWRKKED RLEQFYAQES
IWDRTLDMEP DAAVFNVTTH SRAIQCLVAA FWIFLTMAWM HIFITYSLQF SLAVLTFSLF
IGAQVIYGGI EWLAVNVAAN RGTLKS
//
