ID A0A0D1W511_9EURO Unreviewed; 797 AA.
AC A0A0D1W511;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN ORFNames=PV11_05770 {ECO:0000313|EMBL:KIV83775.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV83775.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV83775.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV83775.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; KN846952; KIV83775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1W511; -.
DR STRING; 1016849.A0A0D1W511; -.
DR HOGENOM; CLU_016735_0_0_1; -.
DR OrthoDB; 2906776at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 122..244
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 86902 MW; 38E705C860C5FC68 CRC64;
MTALEPAAGF SLESPADRPD GVPLKKGEYS IASRALALST YFLSGALAIN LSQFMGAPLA
LVNQDWYNAW IAFTKQSFGL LTMTLTQTFA PTKVIVSGDE SVRGQLFKST DGDLVLDFPD
RLILIANHQI YTDWLYLWWI AYCNGMHGRL YIILKESLKK IPVLGWGMQF NQFIFLKRNW
EQDRPNMASA LQRLNKPADP MWLLLFPEGT NLAPSTRAKS TAWANKQGIP DTRHVLLPRS
TGLHFCLEEL KNTVDYVYDC TVAYEGVPRG QFAQDIFTLK SGYLEGRPPK SVSMHWRRFA
VKDIPLHNDK AFELWLLARW REKDVLIEKW YQTGRFPADN GATKYRSGKV LRGCGHMEVP
IRASHWYEFL QIFAPMGILA MVLYIFYGDL PQKFWKSINK QALKTGSEDI KRTAVEAGQG
AKSVGTSLSG LTLDSFFDAD QQKDTFKAGA MAVQKLLMSP SAQTLLNRAD FMQQFLSDPQ
KMVTEGITSK QQTFMQQLAE EEGRRQQGRL AAAPTNSARP MTNGAVAKKG TFWSSLEAEE
KNRQGSVAPG RGTFWQDLKA AEEKKNGPPV KVNFWDAMKA EENSRYGTVV TLSSNASTAV
ASTRSTSTKG SAPKLPGKPS TSTIKPVQKA ATAKKPAAIG PAKTQTTTAP GSKPTPTKKP
TTSARPAAAK PVKPTTTTPS KPPPKQIPST NGAPRPIAAK KPASASAKQP ATGGPPKLNR
TTSASTTSTT ASKKLPPQNK SAGTATPAKK PASQTPSTNK TQTVASTPST TTKAPPKLSD
SSKPPAKTTA GPPKLET
//
