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Database: UniProt
Entry: A0A1M3HNR6_9SPHI
LinkDB: A0A1M3HNR6_9SPHI
Original site: A0A1M3HNR6_9SPHI 
ID   A0A1M3HNR6_9SPHI        Unreviewed;       218 AA.
AC   A0A1M3HNR6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE            EC=2.1.1.77 {ECO:0000256|HAMAP-Rule:MF_00090};
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE   AltName: Full=Protein L-isoaspartyl methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE   AltName: Full=Protein-beta-aspartate methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090};
DE            Short=PIMT {ECO:0000256|HAMAP-Rule:MF_00090};
GN   Name=pcm {ECO:0000256|HAMAP-Rule:MF_00090};
GN   ORFNames=BGO55_17130 {ECO:0000313|EMBL:OJW60191.1};
OS   Sphingobacteriales bacterium 50-39.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW60191.1, ECO:0000313|Proteomes:UP000184242};
RN   [1] {ECO:0000313|EMBL:OJW60191.1, ECO:0000313|Proteomes:UP000184242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=50-39 {ECO:0000313|EMBL:OJW60191.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl residues
CC       in peptides and proteins that result from spontaneous decomposition of
CC       normal L-aspartyl and L-asparaginyl residues. It plays a role in the
CC       repair and/or degradation of damaged proteins. {ECO:0000256|HAMAP-
CC       Rule:MF_00090}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-L-isoaspartate + S-adenosyl-L-methionine =
CC         [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:12705, Rhea:RHEA-COMP:12143, Rhea:RHEA-
CC         COMP:12144, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90596,
CC         ChEBI:CHEBI:90598; EC=2.1.1.77; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00090};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00090}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC       isoaspartyl/D-aspartyl protein methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005369, ECO:0000256|HAMAP-Rule:MF_00090}.
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:OJW60191.1}.
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DR   EMBL; MKTZ01000002; OJW60191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3HNR6; -.
DR   STRING; 1895841.BGO55_17130; -.
DR   Proteomes; UP000184242; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0036211; P:protein modification process; IEA:UniProtKB-UniRule.
DR   GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00090; PIMT; 1.
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.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00090};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090,
KW   ECO:0000313|EMBL:OJW60191.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:OJW60191.1}.
FT   ACT_SITE        67
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00090"
SQ   SEQUENCE   218 AA;  24908 MW;  2472C0BD83EA0191 CRC64;
     MRTFEDTYRH KGLRRQLVDS IRQKGITDER VLDAIQQIPR HFFMDSALDK TAYEDRAFPI
     GEGQTISQPY TVAYQTQLLE VKPFEKVLEI GTGSAYQASV LSEMGALVYS IERQKKLFET
     NKTFPYLKKY RNLKLFYGDG FEGLPTYGPF DKVIVTAAAP FIPPRLVEQL KPGGKMVIPV
     GEGQVQRMLR LTRQEDGGVT EELFDNFSFV PMLEGKNH
//
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