ID   A0A1V8SLH2_9PEZI        Unreviewed;       652 AA.
AC   A0A1V8SLH2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   28-JUN-2023, entry version 21.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=B0A48_14560 {ECO:0000313|EMBL:OQN99790.1};
OS   Rachicladosporium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQN99790.1, ECO:0000313|Proteomes:UP000192596};
RN   [1] {ECO:0000313|Proteomes:UP000192596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OQN99790.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NAJO01000038; OQN99790.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8SLH2; -.
DR   STRING; 1507870.A0A1V8SLH2; -.
DR   InParanoid; A0A1V8SLH2; -.
DR   OrthoDB; 2906776at2759; -.
DR   Proteomes; UP000192596; 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:UP000192596};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          128..250
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   652 AA;  71035 MW;  50838D7D6414AE6F CRC64;
     MATSSVKSDA GHAGGGLTLT KSGANNPNPI LHGSMGQAER AFSAGSTFLS GIMAISASQF
     IGAPLKLVDP KFYDSYMAWT KESFAVLMTT ITQWWAPTVV RVSGDESMKG QLYQMDDGTL
     KCNFPHRLVL MANHQLYTDW LYLWWVAYTN KMHGHIYIIL KESLKSIPIF GWSAQFYNFI
     FLSRKWETDK FRFKRALNGL KNPADKMWLL IFPEGTNLSA VTREKSAAWA KKTGTKDMKH
     QLLPRSTGLQ FCLQELKQTT NWLYDCTIAY EGVPKGMYGQ DVFTLKSSLF EGRPPKSVNM
     YWRRYRISEI PLETDEAFAR WLSNRWREKD YILEYFYKFG QFPADEPVAA LQAVKGKRPP
     NHRKAIATEV KGGGWDEFLS IYGPITSAAG ALSAIDMTEP LNFDMLLGQV AKAQHMNLAD
     LMRKAPTPPT SQEAIRQAIK AANKKKPLPK PVYDKLIADT PTTQKGMKRA LQKSGDPEIA
     KRVEFAPSVS ESLPSTTREN VTQAALRTQQ AISAGQGPKS PAATQLASKV KTKAGVANTQ
     AMVTRPLSTL AVQSAGGAIR KVAASRAQTK GPQSVPVVKK AGGIAPAAAS SNANGAAKNT
     TARQPATKLA PSKAGSVTGP PKLNGTAKAT PLTAANVAAV KSAPPKKKAI AS
//