ID Q9HST1_HALSA Unreviewed; 245 AA.
AC Q9HST1;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=protein-L-isoaspartate(D-aspartate) O-methyltransferase {ECO:0000256|ARBA:ARBA00011890};
DE EC=2.1.1.77 {ECO:0000256|ARBA:ARBA00011890};
GN Name=pimT1 {ECO:0000313|EMBL:AAG18721.1};
GN OrderedLocusNames=VNG_0089G {ECO:0000313|EMBL:AAG18721.1};
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX NCBI_TaxID=64091 {ECO:0000313|EMBL:AAG18721.1, ECO:0000313|Proteomes:UP000000554};
RN [1] {ECO:0000313|EMBL:AAG18721.1, ECO:0000313|Proteomes:UP000000554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1
RC {ECO:0000313|Proteomes:UP000000554}, and NRC-1
RC {ECO:0000313|EMBL:AAG18721.1};
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.W., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2] {ECO:0000313|EMBL:DAC77406.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC77406.1};
RX PubMed=18313895; DOI=.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [3] {ECO:0000313|EMBL:DAC77406.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC77406.1};
RX PubMed=26042526;
RA Pfeiffer F., Oesterhelt D.;
RT "A manual curation strategy to improve genome annotation: application to a
RT set of haloarchael genomes.";
RL Life 5:1427-1444(2015).
RN [4] {ECO:0000313|EMBL:DAC77406.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC77406.1};
RA Pfeiffer F., Marchfelder A., Habermann B.H., Dyall-Smith M.;
RT "The genome of the Halobacterium salinarum type strain is closely related
RT to that of the laboratory strains NRC-1 and R1.";
RL Microbiol. Resour. Announc. 0:0-0(2019).
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.
CC {ECO:0000256|ARBA:ARBA00025330}.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00029295};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005369}.
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DR EMBL; AE004437; AAG18721.1; -; Genomic_DNA.
DR EMBL; BK010829; DAC77406.1; -; Genomic_DNA.
DR PIR; E84169; E84169.
DR RefSeq; WP_010902016.1; NC_002607.1.
DR AlphaFoldDB; Q9HST1; -.
DR STRING; 64091.VNG_0089G; -.
DR PaxDb; 64091-VNG_0089G; -.
DR GeneID; 68693070; -.
DR KEGG; hal:VNG_0089G; -.
DR PATRIC; fig|64091.14.peg.57; -.
DR HOGENOM; CLU_055432_2_0_2; -.
DR OrthoDB; 194891at2157; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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 Methyltransferase {ECO:0000313|EMBL:AAG18721.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000554};
KW Transferase {ECO:0000313|EMBL:DAC77406.1}.
SQ SEQUENCE 245 AA; 26216 MW; A26FBBBCFAA5DB78 CRC64;
MEFGALREEM VDSLLDAGTA LADARPADAA MRAVPRHEFV DAGHRAYTDQ AFEHRGTRVL
APSTVARLVG ALEPRAGDDV LVVGAGVGYT VAVVAEIAGP THVHAVDIDR QVVYDARGNL
ADAGYEDVLV DCRDGAEGLA EYAPFDRVLV EAGAASVPDA LARQLAADGR LVFPEGVGDQ
RLVSVRDGET VGVHGPVSFA PLLVAGEQAS AVERNRTVRE DRERVREAAQ SRPGWEREWI
DWEDA
//
