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Database: UniProt
Entry: F7W2S3_SORMK
LinkDB: F7W2S3_SORMK
Original site: F7W2S3_SORMK 
ID   F7W2S3_SORMK            Unreviewed;       428 AA.
AC   F7W2S3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   03-MAY-2023, entry version 43.
DE   SubName: Full=WGS project CABT00000000 data, contig 2.22 {ECO:0000313|EMBL:CCC11924.1};
GN   ORFNames=SMAC_05137 {ECO:0000313|EMBL:CCC11924.1};
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC11924.1, ECO:0000313|Proteomes:UP000001881};
RN   [1] {ECO:0000313|EMBL:CCC11924.1, ECO:0000313|Proteomes:UP000001881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC   {ECO:0000313|Proteomes:UP000001881};
RC   TISSUE=Mycelium {ECO:0000313|EMBL:CCC11924.1};
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA   Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC11924.1}.
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DR   EMBL; CABT02000022; CCC11924.1; -; Genomic_DNA.
DR   RefSeq; XP_003346877.1; XM_003346829.1.
DR   AlphaFoldDB; F7W2S3; -.
DR   STRING; 771870.F7W2S3; -.
DR   GeneID; 10804275; -.
DR   KEGG; smp:SMAC_05137; -.
DR   VEuPathDB; FungiDB:SMAC_05137; -.
DR   eggNOG; KOG1505; Eukaryota.
DR   HOGENOM; CLU_041844_3_2_1; -.
DR   InParanoid; F7W2S3; -.
DR   OMA; RMVMIAN; -.
DR   OrthoDB; 2906776at2759; -.
DR   Proteomes; UP000001881; 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:UP000001881};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        61..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          148..280
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   428 AA;  49197 MW;  120A0637C91CC227 CRC64;
     MGDLRQRASY PDITSSDAST NPNPNEAGLL VQRNDNSQKT IQNAHPSGKE KHNRLIQILR
     GVSLAIFFTA CSVGIVATQF LGAPLYWINR DLYYTYMALT KQSFGLTITT MTQWWGPTTI
     RISGDGSVAG QIKKTPDGRV EFNFPERMVM IANHQIYTDW LYLWWVGYAN APRMHGYLYI
     ILKESLKYLP IVGQGMMFYG FIFMSRKMNV DQPRLAYRLG KLKTKHTHNG RQYLNPMWLL
     LFPEGTNCTQ NGRNKSKKWA DKIGIKDTEH VLLPRSTGIY FCLKELKGTV EYVYDCTVAY
     EGVPRGMYGD QFFTLSSTYL RGQPPKSVNF YWRRFAVDDI PLENQDEFDV WLRERWYEKD
     ALMEQYLTTG RFPPSPPTKE GGHEGHLETE VRARHPLEFL QIFSVLGAAG VLTTTAARTW
     GRVAQWLS
//
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