ID E4UU88_ARTGP Unreviewed; 418 AA.
AC E4UU88;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=MGYG_09034 {ECO:0000313|EMBL:EFR00855.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; DS989824; EFR00855.1; -; Genomic_DNA.
DR RefSeq; XP_003173685.1; XM_003173637.1.
DR AlphaFoldDB; E4UU88; -.
DR STRING; 535722.E4UU88; -.
DR GeneID; 10028968; -.
DR VEuPathDB; FungiDB:MGYG_09034; -.
DR eggNOG; KOG1505; Eukaryota.
DR HOGENOM; CLU_041844_3_2_1; -.
DR InParanoid; E4UU88; -.
DR OMA; RMVMIAN; -.
DR OrthoDB; 2906776at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
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; 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:UP000002669};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 132..264
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 418 AA; 48340 MW; B8A9E22F6F2FD7AD CRC64;
MPRARHRKTA SQARIGSKPE LMKSSRHMYE REPANYGLFV QLVRSFLIVA WFCCCCTCII
VAQVVGLPLY VIKKEYFNAW IALTKESFGL AITALTEWSA PTPVRISGDR SVLGQVTLTS
NGGIKTNFPD RLVLIANHQV YTDWLYLWWV TYTNKMHGHI YIILKESLKY IPLVGQGMTL
YGFIFMARKW MADKPRLQHR LSKLSVKRAE SSSGNPLFDP MWLLIFPEGT NLSLHTKDVS
DAYGKKKGIP PLKHELHPRS TGLFFCLQQL RGTVGHVYDC TMAYEGPPKG SFPDSYFTIR
STYLKCRPPR VVNFYWRRFA FEDIPLENQE EFEAWLFERW AEKDQLLDTF IETGKFPPFE
DADLVEMDPN NPDIQTTSGK NHGYVEGEVR LNYWAEICRV FAVPALIAFL IHVYRRYC
//