ID A0A163L7X0_DIDRA Unreviewed; 597 AA.
AC A0A163L7X0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Trans-aconitate 2-methyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ST47_g1152 {ECO:0000313|EMBL:KZM27569.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM27569.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM27569.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM27569.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
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:KZM27569.1}.
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DR EMBL; JYNV01000060; KZM27569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163L7X0; -.
DR STRING; 5454.A0A163L7X0; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0030798; F:trans-aconitate 2-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd08589; PI-PLCc_SaPLC1_like; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR Gene3D; 1.10.150.290; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR032075; PI-PLC-C1.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR023149; Trans_acon_MeTrfase_C.
DR PANTHER; PTHR43861:SF1; TRANS-ACONITATE 2-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43861; TRANS-ACONITATE 2-METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR Pfam; PF16670; PI-PLC-C1; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..597
FT /note="Trans-aconitate 2-methyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007843857"
SQ SEQUENCE 597 AA; 64826 MW; 7478EEEB94A13998 CRC64;
MRAILVAGMS AFVAVVSAPS AGAETTTNQV RSFSETTSVG VHNSYEKATF PYFADALDSG
ASLLELDLWT NGGGPDWRVS HMNPVVSDSN CVGAQDASGL RSGLRDQGFR GCLADMRAWH
EANPEHPPVM IKLEIKDGFT AGYGRGPADL DALILGTLGD AVFTPADLMG ESYSTPDAAV
TERGWPSTSE MTGKFLFELI PGTIEEGNPL DTEWTDRQYA THLRDLSSAG LVELGAAFPA
VHRASPGDPR LDRYTDPGIR PWFVIFDGDA LDYTAGVVDP SWYHDRGYLL VMTDAHKVAP
QIDGTHATET EASERLDLLA GQHASYITAD WSRLPNDGFM RTVTWNPEVY GRYSGERSRP
FVDLVSRVAT EDPTRVADLG CGSGTLTAML GERWPDASVS GFDSSPEMVA QAPTDLPGNV
TVELGDIMSF DATGYDVVVS NAALQWVPSH RELIDQWADT LESGSWLAWQ VPGNFDAPSH
ALMRDLAESA EWSERLGGVL RGPEGVDSPV QYAQRLQEHG FDVDAWETTY VHVLAGADPV
LGWVRGTGLR PVLDVLGEAD APEFERQYSD LLREAYPATA AGTLFPFRRV FCVGRKR
//
