ID A0A0F7ZVU4_9HYPO Unreviewed; 328 AA.
AC A0A0F7ZVU4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=HIM_03539 {ECO:0000313|EMBL:KJZ77218.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ77218.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ77218.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ77218.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; KQ030508; KJZ77218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7ZVU4; -.
DR OrthoDB; 5475670at2759; -.
DR Proteomes; UP000054481; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR23063:SF1; LYSOPHOSPHATIDIC ACID:OLEOYL-COA ACYLTRANSFERASE 1; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054481};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 105..217
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 328 AA; 36111 MW; E8027939EAE5D1ED CRC64;
MEKYSQFRDK STGIAPFLPV TTPLSAFSTL THSLLFLFRL PFFLTYAFSY FIVFHYLPLP
VVARKIALWG LMAIPGIWWV DLQLDGVRRG TLSEQPRERV PHPGSVIAAN FTSPIDAVYL
AAIFDPIFTV SYPGSRKLRK VGLLSAVIRA LGAVQTGPPE YADLVEIEDL LNEYPGRVIA
VFPECGTTNG KAILPFSPAL AECPPNAHIF PVSIRYAPSD VTTPVPGRWF RFLWDLLSQP
TTCIRVRIAE GRCKETTGSG SNGTVAATNG NGNLKQRKAA GSELTSDEQK LLDRIAEALA
RLSRVKRVGL TMNEKAAFVE ALNGKKTW
//
