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
//