(data stored in SCRATCH zone)

SWISSPROT: D3F4Z3_CONWI

ID   D3F4Z3_CONWI            Unreviewed;       206 AA.
AC   D3F4Z3;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   07-JUN-2017, entry version 47.
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   OrderedLocusNames=Cwoe_0135 {ECO:0000313|EMBL:ADB48571.1};
OS   Conexibacter woesei (strain DSM 14684 / JCM 11494 / NBRC 100937 /
OS   ID131577).
OC   Bacteria; Actinobacteria; Thermoleophilia; Solirubrobacterales;
OC   Conexibacteraceae; Conexibacter.
OX   NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB48571.1, ECO:0000313|Proteomes:UP000008229};
RN   [1] {ECO:0000313|Proteomes:UP000008229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14684 / JCM 11494 / NBRC 100937 / ID131577
RC   {ECO:0000313|Proteomes:UP000008229};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA   Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Conexibacter woesei DSM 14684.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl
CC       residues in peptides and proteins that result from spontaneous
CC       decomposition of normal L-aspartyl and L-asparaginyl residues. It
CC       plays a role in the repair and/or degradation of damaged proteins.
CC       {ECO:0000256|HAMAP-Rule:MF_00090}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-
CC       isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate
CC       alpha-methyl ester. {ECO:0000256|HAMAP-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|HAMAP-Rule:MF_00090}.
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DR   EMBL; CP001854; ADB48571.1; -; Genomic_DNA.
DR   RefSeq; WP_012931624.1; NC_013739.1.
DR   ProteinModelPortal; D3F4Z3; -.
DR   STRING; 469383.Cwoe_0135; -.
DR   EnsemblBacteria; ADB48571; ADB48571; Cwoe_0135.
DR   KEGG; cwo:Cwoe_0135; -.
DR   eggNOG; ENOG4105E26; Bacteria.
DR   eggNOG; COG2518; LUCA.
DR   HOGENOM; HOG000257189; -.
DR   KO; K00573; -.
DR   OMA; PYTVAFQ; -.
DR   OrthoDB; POG091H06AY; -.
DR   Proteomes; UP000008229; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030091; P:protein repair; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00090; PIMT; 1.
DR   InterPro; IPR000682; PCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR11579; PTHR11579; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00080; pimt; 1.
DR   PROSITE; PS01279; PCMT; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3F4Z3.
DR   SWISS-2DPAGE; D3F4Z3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008229};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00090};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00090,
KW   ECO:0000313|EMBL:ADB48571.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008229};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00090,
KW   ECO:0000313|EMBL:ADB48571.1}.
FT   ACT_SITE     56     56       {ECO:0000256|HAMAP-Rule:MF_00090}.
SQ   SEQUENCE   206 AA;  21806 MW;  64FEE1CFBBCBB19B CRC64;
     MDPAAELARS LRSVVADARV LAAIAAVPRE LFVPEALRER AYDNVALPIG QGQTISQPLV
     VARMLEVLDL GPDDDVLDVG TGSGYHAALL ARLVRHVWTI ERHRRLSAAA EGNLRAAGVE
     NVTVLVGDGS RGLDEQAPFD AINVAAAAWP QVPAALERQL ARGGRLVAPV GASGQQLVLV
     ERGADGELRR TALEAVRFVP LIEGEP
//

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