ID   A0A1X2IC74_9FUNG        Unreviewed;       313 AA.
AC   A0A1X2IC74;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   SubName: Full=Acyltransferase-domain-containing protein {ECO:0000313|EMBL:ORZ13707.1};
GN   ORFNames=BCR42DRAFT_378063 {ECO:0000313|EMBL:ORZ13707.1};
OS   Absidia repens.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ13707.1, ECO:0000313|Proteomes:UP000193560};
RN   [1] {ECO:0000313|EMBL:ORZ13707.1, ECO:0000313|Proteomes:UP000193560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ13707.1,
RC   ECO:0000313|Proteomes:UP000193560};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORZ13707.1}.
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DR   EMBL; MCGE01000016; ORZ13707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2IC74; -.
DR   STRING; 90262.A0A1X2IC74; -.
DR   OrthoDB; 1289at2759; -.
DR   Proteomes; UP000193560; 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:SF24; 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 3, ISOFORM E-RELATED; 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:ORZ13707.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193560};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ORZ13707.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          87..209
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   313 AA;  36605 MW;  1441F3391B77A59B CRC64;
     MNIQPIATIS KATNAVFYGV GLFGMTGLLQ TFQIPSMIIG PFSPRLLVKI NSYLIGTVWR
     VLQTVFEKRK KGHITFSGDI VPANESALVI SNHRSWTDFY MIHSVAIRRN MLPNCKYFVK
     DSIKWLPFFG WGMWLAGFMF VRRNWLQDQT KINKTFASMK TMKTPAWIIN YVEGSRFTPE
     KSQQCQALCR ERGYTTTENV LLPRTRGFTT CVKEFQNSHI EYIYDFTLAY RHHSKNAEFN
     EAPDMVRVHT SALSPEYEFH VNVKRYAIAD LPTDDEGIAQ WLRQRYVEKD RFLAQLRDRW
     TDGLDIPVRE EKW
//