ID A0A101V8P9_9FIRM Unreviewed; 208 AA.
AC A0A101V8P9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|ARBA:ARBA00013346};
DE EC=2.1.1.77 {ECO:0000256|ARBA:ARBA00011890};
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase {ECO:0000256|ARBA:ARBA00031350};
DE AltName: Full=Protein L-isoaspartyl methyltransferase {ECO:0000256|ARBA:ARBA00030757};
DE AltName: Full=Protein-beta-aspartate methyltransferase {ECO:0000256|ARBA:ARBA00031323};
GN ORFNames=APF76_06650 {ECO:0000313|EMBL:KUO50137.1};
OS Desulfitibacter sp. BRH_c19.
OC Bacteria; Bacillota; Clostridia; Moorellales; Desulfitibacteraceae;
OC Desulfitibacter.
OX NCBI_TaxID=1734395 {ECO:0000313|EMBL:KUO50137.1, ECO:0000313|Proteomes:UP000053015};
RN [1] {ECO:0000313|EMBL:KUO50137.1, ECO:0000313|Proteomes:UP000053015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c19 {ECO:0000313|EMBL:KUO50137.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005369}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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:KUO50137.1}.
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DR EMBL; LOER01000034; KUO50137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101V8P9; -.
DR STRING; 1734395.APF76_06650; -.
DR Proteomes; UP000053015; Unassembled WGS sequence.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00080; pimt; 1.
DR PANTHER; PTHR11579; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11579:SF0; PROTEIN-L-ISOASPARTATE(D-ASPARTATE) O-METHYLTRANSFERASE; 1.
DR Pfam; PF01135; PCMT; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01279; PCMT; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01023};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT DOMAIN 1..208
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT BINDING 106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 208 AA; 23296 MW; 8365E1D85C504B23 CRC64;
MESLEELVQK LENRGVLKTS SIKEALLKVD RINFIIPEYK EYVYQDRPLP LKEGQTISQP
LTVIFMLELL QPKNGHHVLD VGSGSGWTTA LLSELVGEDG NVYAIERINS LKKFGEENLS
KLGYENVLFM EGNGAKGWPE NAPFDRILVN ASAKTIPPAL TEQLKTGGKM VIPLDNAYGH
LKLLNKITSR SYEEEVYPGF AFVPFINE
//
