ID V7IXI2_MYCAV Unreviewed; 294 AA.
AC V7IXI2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:ETA90825.1};
GN ORFNames=O984_19935 {ECO:0000313|EMBL:ETA90825.1};
OS Mycobacterium avium 05-4293.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1392002 {ECO:0000313|EMBL:ETA90825.1, ECO:0000313|Proteomes:UP000018553};
RN [1] {ECO:0000313|EMBL:ETA90825.1, ECO:0000313|Proteomes:UP000018553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05-4293 {ECO:0000313|EMBL:ETA90825.1};
RX PubMed=24482526;
RA Bannantine J.P., Bayles D.O., Robbe-Austerman S., Burrell A.M.,
RA Stabel J.R.;
RT "Draft Genome Sequence of a Mycobacterium avium Complex Isolate from a
RT Broadbill Bird.";
RL Genome Announc. 2:e01263-13(2014).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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:ETA90825.1}.
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DR EMBL; AYLW01000094; ETA90825.1; -; Genomic_DNA.
DR AlphaFoldDB; V7IXI2; -.
DR PATRIC; fig|1392002.3.peg.4061; -.
DR Proteomes; UP000018553; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003333; CMAS.
DR InterPro; IPR047672; CMAS_actinobact.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; NF040660; mycolic_MTase; 1.
DR PANTHER; PTHR43667; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR PANTHER; PTHR43667:SF1; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR Pfam; PF02353; CMAS; 1.
DR PIRSF; PIRSF003085; CMAS; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Methyltransferase {ECO:0000313|EMBL:ETA90825.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ETA90825.1}.
FT ACT_SITE 275
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-1"
FT BINDING 39..40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 74..82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 100..105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 129..130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
SQ SEQUENCE 294 AA; 33488 MW; F9D89849C6D9AD27 CRC64;
MSENTGDAVN LQPHFDDVQA HYDLSDEFFA LFLDPTRTYS CAYFERDDMT LEEAQIAKVD
LSLGKLGLQP GMTLLDIGCG WGTTIVRALE RYDVNVVGLT LSRNQQAHVQ RPLDNHPSPR
SKRVLLQGWE QFDEKVDRIV SIGAFEHFGR DRYDDFFKMA YAALPDDGVM MLHTIIKPSD
EEFAERGLPI TMTKLRFMKF IMDEIFPGGD LPQAKGVIEH AQRAGFGVQR VQALRPHYAR
TLDTWAAALR ARRDEAIAIQ SEEVYDRYMK YLTGCADLFR EGYTDVAQFT LTKG
//
