ID A0A0R0M2H9_9MICR Unreviewed; 546 AA.
AC A0A0R0M2H9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Putative phosphate acyltransferase {ECO:0000313|EMBL:KRH93233.1};
GN ORFNames=M153_12580001917 {ECO:0000313|EMBL:KRH93233.1};
OS Pseudoloma neurophilia.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pseudoloma.
OX NCBI_TaxID=146866 {ECO:0000313|EMBL:KRH93233.1, ECO:0000313|Proteomes:UP000051530};
RN [1] {ECO:0000313|EMBL:KRH93233.1, ECO:0000313|Proteomes:UP000051530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MK1 {ECO:0000313|EMBL:KRH93233.1,
RC ECO:0000313|Proteomes:UP000051530};
RA Ndikumana S., Pelin A., Sanders J., Corradi N.;
RT "The genome of Pseudoloma neurophilia, a relevant intracellular parasite of
RT the zebrafish.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:KRH93233.1}.
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DR EMBL; LGUB01000425; KRH93233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0M2H9; -.
DR VEuPathDB; MicrosporidiaDB:M153_12580001917; -.
DR Proteomes; UP000051530; 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:SF2; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 4, ISOFORM D-RELATED; 1.
DR PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 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:KRH93233.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000051530};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRH93233.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 79..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 191..302
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 546 AA; 63798 MW; 3CF0E0ABE738FDB2 CRC64;
MFNSKSKNNH PYTSPFSHKM RRFFLNDAVD LVGLGTRSIN SDSFTKCFEP ISQLEMDNSG
ILYIFSFMIR YFILLPLRIV FFIIGTLIFF GLFFLGCTIS YFQKRKIFSF RNFSIKNTIS
NLFRRKSIQN KINMIKSAQS SKNITNPQVK TSSLGNLLIE KSFLFYCKIF CMSFGAIITH
HGKKPSLNVP HIFIANHTSF LDFIVLSSYK YCHAIVAENH GGLFGFFLNK LLSKNGSLHF
KRSEKNDKKL VLRKIEKHIN LLQTPMLLFP EGTCVNNKYT VMFQKGVFQL NIVICPVIIK
YKRKLFDPYW NRRKHTFTEH IFYLMSRWMI EVDVYWMDPI SRKTNANQAS KFNTVQNIAQ
DVAQDGKEKL AKEESVNEFI DRTKALISEK GGLINTNWNG YMKNQIIIKD IDILRQAYKE
TYLKHIVKEN DTLKYGAEKK GATNKSSALK DDSIEISNKN RKDDKIESNA EKKYELRVSD
SLEVQYFDSL EYSEFIDNLL QKYSILKFKN KSEPIDTFFI KEMRVKCNCK PKTSRTSTCR
EEMRKS
//
