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Database: UniProt
Entry: A0A1R0H821_9FUNG
LinkDB: A0A1R0H821_9FUNG
Original site: A0A1R0H821_9FUNG 
ID   A0A1R0H821_9FUNG        Unreviewed;       256 AA.
AC   A0A1R0H821;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:OLY85297.1};
GN   ORFNames=AYI68_g504 {ECO:0000313|EMBL:OLY85297.1};
OS   Smittium mucronatum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX   NCBI_TaxID=133383 {ECO:0000313|EMBL:OLY85297.1, ECO:0000313|Proteomes:UP000187455};
RN   [1] {ECO:0000313|EMBL:OLY85297.1, ECO:0000313|Proteomes:UP000187455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY85297.1,
RC   ECO:0000313|Proteomes:UP000187455};
RX   PubMed=27343289; DOI=10.1093/molbev/msw126;
RA   Wang Y., White M.M., Kvist S., Moncalvo J.M.;
RT   "Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First
RT   Horizontally Transferred Ubiquitin Gene from a Mosquito Host.";
RL   Mol. Biol. Evol. 33:2544-2554(2016).
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:OLY85297.1}.
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DR   EMBL; LSSL01000161; OLY85297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R0H821; -.
DR   STRING; 133383.A0A1R0H821; -.
DR   Proteomes; UP000187455; 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   ECO:0000313|EMBL:OLY85297.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187455};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OLY85297.1}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..256
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012344806"
FT   DOMAIN          1..123
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   256 AA;  29973 MW;  B25B65554DF9A386 CRC64;
     MMSNHQAYID WILLWSLLRL QNLEGSIKIV LKDSLKNIPI IGWGMQYFDF IFLKRNWNKD
     KETLESHMAK INKSKYPTTL LLFPEGTTFT QNTLTKSLAY AAKTLPELHH PIHVILPRAT
     GIRCCLQSLS SQKTKYLYDV TVAYSGVSSD EFAEDIYTMK NVFYNEGYPR KVHINIRRFL
     ISEIPLEDES VFSTWLIDRF MEKDSMLDYY YKNGNFHAQD KIPYLTDPLT KVQAILGMRS
     LFLAFVSICF FIKLLY
//
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