ID A0A1A6GH80_NEOLE Unreviewed; 255 AA.
AC A0A1A6GH80;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|RuleBase:RU003802};
DE EC=2.1.1.77 {ECO:0000256|RuleBase:RU003802};
DE Flags: Fragment;
GN ORFNames=A6R68_06826 {ECO:0000313|EMBL:OBS64642.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS64642.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS64642.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS64642.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS64642.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:ARBA00035815};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12706;
CC Evidence={ECO:0000256|ARBA:ARBA00035815};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005369, ECO:0000256|RuleBase:RU003802}.
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:OBS64642.1}.
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DR EMBL; LZPO01097158; OBS64642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A6GH80; -.
DR STRING; 56216.A0A1A6GH80; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; 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: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 NCBIfam; TIGR00080; pimt; 1.
DR PANTHER; PTHR11579; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11579:SF7; 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.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|RuleBase:RU003802};
KW Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU003802};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU003802}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..255
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008345594"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OBS64642.1"
SQ SEQUENCE 255 AA; 27661 MW; C1617EE339F68383 CRC64;
SRVTVACIVA DSLVLPASVC TLQCHQNDSE IHLMSHLLKI AVSFISENGI IKTDKVFEVM
LATDRSHYAK SNPYMDSPQS IGFQATISAP HMHAYALELL FDQLHEGAKA LDVGSGSGIL
TACFARMVGQ SGKVIGIDHI KELVDDSINN VRKDDPMLLT SGRVRLVVGD GRMGYAEEAP
YDAIHVGAAA PVVPQALIDQ LKPGGRLILP VGPAGGNQML EQYDKLQDGS VKMKPLMGVI
YVPLTDKEKQ WSRWK
//
