ID A0A395MWK4_9HYPO Unreviewed; 420 AA.
AC A0A395MWK4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:RFN52274.1};
GN ORFNames=FIE12Z_3460 {ECO:0000313|EMBL:RFN52274.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN52274.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN52274.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN52274.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFN52274.1}.
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DR EMBL; PXXK01000073; RFN52274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395MWK4; -.
DR STRING; 2594813.A0A395MWK4; -.
DR OrthoDB; 2906776at2759; -.
DR Proteomes; UP000265631; 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: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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RFN52274.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 59..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 143..276
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 420 AA; 48607 MW; B24E6262C9509696 CRC64;
MAGTTNADPP ETALPVPEVL AGITEEDLAK ERKTLPKEEH PSGKESYGTF MQIIRGSCFA
LYFNSCLLVI FITQLIGSPL YFVNRDWYYA WMAMTKRSFG LTITLMTQIW GPTTIRVSGD
ESVAGQIKLR SDGGVQFEFP ERLILIANHQ IYTDWLYLWW ISYANSPSMH GHIYIILKES
LKRIPLVGLG MQFYSFIFMS RKMASDQPRM AYRLNKLKQR KVDPNGRSYM DPMWLLLFPE
GTNLSNNGRR KSAGWAAKND LKDPEHVLLP RSTGMFFCLN ELKGSIDYVY DCTVAYEGIP
RGGFGEEYFG LVSTYFQGRP PKSVNFHWRR FRVSDIPLED PKAFDLWLRE EWYKKDTLME
EYMTTGRFPR MAGSKVDYIE TEVKTRQPWE ILQIFTVVGT AALVWHNIKK TFTTMTTVFR
//
