ID C4YC03_CLAL4 Unreviewed; 411 AA.
AC C4YC03;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 03-MAY-2023, entry version 48.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=CLUG_05731 {ECO:0000313|EMBL:EEQ41603.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ41603.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ41603.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ41603.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; CH408083; EEQ41603.1; -; Genomic_DNA.
DR RefSeq; XP_002614245.1; XM_002614199.1.
DR AlphaFoldDB; C4YC03; -.
DR STRING; 306902.C4YC03; -.
DR GeneID; 8494836; -.
DR KEGG; clu:CLUG_05731; -.
DR VEuPathDB; FungiDB:CLUG_05731; -.
DR HOGENOM; CLU_041844_3_2_1; -.
DR InParanoid; C4YC03; -.
DR OMA; RMVMIAN; -.
DR OrthoDB; 2906776at2759; -.
DR Proteomes; UP000007703; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProt.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007703};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..257
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 411 AA; 46232 MW; F51AF6811B03EB17 CRC64;
MISRHSWPVV VLRTAFVIFA FIFGTLGIRL LQELGGVVFS RHPAHFHACV ALTKSHFLAL
LTFLTALVNP TAVSVTWDAR QMSSSRFEVR AGHLHSTLAA NAVWISNHQI YTDWLFWWFL
AYTGGHAGAA YIVLKENLAK IPVLGPGMRR FRFMFLSRKW ATDKLRLTSQ LLELDANARG
MGPVAGVTCA ASESSRLPGV RQWPPGHGSV AANYHLIVYP EGTVMSPHTR ERSDKFCASI
NRPPLRHVLL PRARGLFLML RSLRGSVDVV YDLTTGYTGL GPEQYGEEVF TLKAYYLFGY
GPRKINFAVR TWNLADIPLG PDDGNIDVDD VDPQVMRQFE EWLYDAWYAK DELMSRFFAT
GSFEGEETKT VEAPFQLRSP LEALAPFVPS LTLVLMLYLS VRLISFAWSL L
//
