ID M7WUX3_RHOT1 Unreviewed; 870 AA.
AC M7WUX3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Glyceronephosphate O-acyltransferase {ECO:0000313|EMBL:EMS24387.1};
GN ORFNames=RHTO_06391 {ECO:0000313|EMBL:EMS24387.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS24387.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS24387.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS24387.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
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DR EMBL; KB722645; EMS24387.1; -; Genomic_DNA.
DR RefSeq; XP_016275506.1; XM_016420052.1.
DR AlphaFoldDB; M7WUX3; -.
DR GeneID; 27370404; -.
DR eggNOG; KOG3730; Eukaryota.
DR HOGENOM; CLU_015023_0_0_1; -.
DR OrthoDB; 5478811at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:InterPro.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 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:EMS24387.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMS24387.1}.
FT DOMAIN 236..363
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 97395 MW; 97B666A7024D3CC5 CRC64;
MTAADKRKQR HSASLATLGP DDPEALLGVD FEPRTRPPTV VTTVEPGLVA LQPVLVQEEN
AVGVVKEEKK RVGNGEQRNL VENHQAHLRA DPIEFSKQLS LWASGTGWRS YTDYIGGRVF
YPGYSDDCMR GILSSKQVNK RIQEVTEKRL AGLQLPEGPE KEKKRRQIQD ELKKEARRLS
EGLVAKMDNV RFLRGFGALV NNILVRMYHQ GLEISIPEYA RFKEVAQMAA SKKQSLLILP
CHKSHIDYLT ISWLFFRLGL SLPHIIAGEN LNMPVVGPTL AKCGAVFIRR SFGDDPLYST
VVKEYIEQLL ENGKNIECFI EGTRSRTGKL LPPKLGILKY VLEALENGRT EDVWVCPISL
QYDKVIETES YVNELLGNPK EKETLTGLLL NTRVVQLQLG RIDVRFQKPF SLRGWLDEQK
KRRSTSTTSP LGGTGIKNDQ SVLLRALGYE VLAGINDCAV IMPAGLVGTV MLTIRGRGVG
KSELVSRVVW LKKAIEARGG RVADFGDMSP EEVVERALEF LKDLIGEQTD LIESTYYPIS
RFELSFWRNQ TIHLFVEEAM LCAVLYTRVK AGGAAPSQRM ERAEVLRELH FISRLLSNEF
VYPPDGLEAN SDKTIVALED DEVILTEGEL IGLNPKERAA GRNNFDFFCF LIWPFIETYW
LAAVSLFALA PTCPPPSADE PVAWYAEKAF QASAQLLAKT LFAQGDVSYL EAVNQGASSS
CRNRKRRELT PTLPAATLFN AFQRMVDVGV LLTRRSTSNA ANASIAKIGK DGKPKLPKKP
ASVPLMALHP DWVPRRQADG TIAPQGRLWE FVDRLSKFRR EGKNRRDNKT VSVRVFAHCS
TIAPQVIEYT AFQNDKPASD FWAEKRQAAL
//
