ID   A0A090L5L1_STRRB        Unreviewed;       697 AA.
AC   A0A090L5L1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Lysocardiolipin acyltransferase 1 {ECO:0000313|EMBL:CEF63402.1, ECO:0000313|WBParaSite:SRAE_1000166400.1};
GN   ORFNames=SRAE_1000166400 {ECO:0000313|EMBL:CEF63402.1,
GN   ECO:0000313|WBParaSite:SRAE_1000166400.1,
GN   ECO:0000313|WormBase:SRAE_1000166400};
OS   Strongyloides ratti (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF63402.1};
RN   [1] {ECO:0000313|EMBL:CEF63402.1, ECO:0000313|Proteomes:UP000035682}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC   ECO:0000313|WBParaSite:SRAE_1000166400.1}, and ED321 Heterogonic
RC   {ECO:0000313|EMBL:CEF63402.1};
RA   Martin A.A.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SRAE_1000166400.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (DEC-2020) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR   EMBL; LN609528; CEF63402.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090L5L1; -.
DR   STRING; 34506.A0A090L5L1; -.
DR   EnsemblMetazoa; SRAE_1000166400.1; SRAE_1000166400.1; WBGene00258272.
DR   WBParaSite; SRAE_1000166400.1; SRAE_1000166400.1; WBGene00258272.
DR   WormBase; SRAE_1000166400; SRP10648; WBGene00258272; -.
DR   OMA; GNWIGFI; -.
DR   OrthoDB; 2906776at2759; -.
DR   Proteomes; UP000035682; Chromosome X.
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; 2.
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; 2.
DR   SMART; SM00563; PlsC; 2.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:CEF63402.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CEF63402.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        322..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        362..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        629..648
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        654..678
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          60..184
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   DOMAIN          394..518
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   697 AA;  82062 MW;  6E707EDC0D918CE1 CRC64;
     MIIKRIKTFL FVTLLFFSTF YGSIFVLFPF VFCIKLSPNI WRFIADRAVA FWLTLPAALS
     IIIMNHRTRL DWMFLWNALY KINPWLLVTE KISLKEPLKN YIGIGWAMQC AGYLFLHRDF
     KTDQKNMELA IEYYSKSGNN YQILLFPEGT DKGKSATDKS NEFARKKGLP QYDNVLHPRT
     TGFEHMISTM KKYNYISSIY DVTVGYDEIT QSEIDLIISG KIPKFIHFDV KRYNIKDFVI
     DEKKQIFSSK DSCIIKSSPG DYLKKLWADK EQKLEKFYQQ KNISKRCFLA DSLDDIIHDN
     KYIMGEPETV TTSPFYFKLC GIFIAFLLFL STLFGSIFML WPFTFLIVIY PSLWRRFADI
     LVGLWFLFPA GLLELCYGIK FTATGDLISH KTPAIIIMNH RTRLDWLFFW NVLYRMDPIL
     LTTEKIILKF FLKLIPGAGY SMCCNAFIFL KRTFLKDQAS IDTILTYYRD TQNPYQILLF
     PEGTDKDDLG VARSNAYAEK FGLEKYEYVL HPRTTGFIHI VKKLRELNYI DFIYDVTVGY
     ADKIVQGEDD IVKLGVFPKN IHFNVQKISI EDIGESDEEI EKWLKVKWEE KEKKLKEFYS
     NDDPNLRTFH KNDKTTNHFI LTNHAKREMV MTIVFWILMV CSIFYLMITY IPFVIFFCSG
     FLFFTFCQIF AGGIEFIMPK FVKSIDNYNT ERKNLKT
//