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Database: UniProt
Entry: A0A328ALS9_9CAUL
LinkDB: A0A328ALS9_9CAUL
Original site: A0A328ALS9_9CAUL 
ID   A0A328ALS9_9CAUL        Unreviewed;       666 AA.
AC   A0A328ALS9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=DJ017_15950 {ECO:0000313|EMBL:RAK55892.1};
OS   Phenylobacterium soli.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=2170551 {ECO:0000313|EMBL:RAK55892.1, ECO:0000313|Proteomes:UP000249254};
RN   [1] {ECO:0000313|Proteomes:UP000249254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LX32 {ECO:0000313|Proteomes:UP000249254};
RA   Li X.;
RL   Submitted (MAY-2018) 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:RAK55892.1}.
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DR   EMBL; QFYQ01000001; RAK55892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A328ALS9; -.
DR   OrthoDB; 9810066at2; -.
DR   Proteomes; UP000249254; 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   GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd14728; Ere-like; 1.
DR   Gene3D; 3.40.1660.10; EreA-like (biosynthetic domain); 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00090; PIMT; 1.
DR   InterPro; IPR007815; Emycin_Estase.
DR   InterPro; IPR000682; PCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00080; pimt; 1.
DR   PANTHER; PTHR31299; ESTERASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05850)-RELATED; 1.
DR   PANTHER; PTHR31299:SF0; PRIBOSYLTRAN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05139; Erythro_esteras; 1.
DR   Pfam; PF01135; PCMT; 1.
DR   SUPFAM; SSF159501; EreA/ChaN-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01279; PCMT; 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:RAK55892.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249254};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00090};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00090, ECO:0000313|EMBL:RAK55892.1}.
FT   REGION          212..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        62
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00090"
SQ   SEQUENCE   666 AA;  74137 MW;  FA64F3ED68B7AD2D CRC64;
     MLDFAYARHR MVERQLAARG VGDRQVLDAM GEVPREAFVP DGMEEFAYED SPLPIESGQT
     ISQPYIVGLM IQAAGIRPGE RVLEVGAGSG YAAAVMSRIA QAVYAIERHE PLTRLAQSRI
     DRLGYDNIHL KTGDGTRGWA DAAPFDAILA AAGGPEVPAA LKAQLAIGGR LVMPVGEEPR
     LQRLKKLTRI SQAEFREEDL GEVTFVPLIG EQGWGEDEQR RPPEPRSFRA PSPAASIPKL
     IAHAAEPLPD LDDPAFGALF DRFAKAKVVL LGEASHGTSE FYRARAAITR RLIEHHGFKI
     VAVEADWPDA AHFDRYVRHL PPPKHDEPPF RRFPTWMWRN AEVEGFIEGL REWNLARAPD
     ARAGFYGLDL YNLSASIRAV LDYLDRVDPQ AGDIARQRYG CLTPWAKNPQ SYGRMALSAG
     YRACEEGVVR TLTELLGNRP EYVKADGTAF LDAMGNARLV KNAEAYYRAM YYGSAESWNL
     RDTHMFETLC SILDSQGPDA KAVVWAHNSH IGDASKTEMG TEREELNIGQ LCRERFGAEA
     ALIGFGTHAG TVACASDWDE PMEVKPVNAS LPDSYERLAH EAGVGRFLLD LREGAHDELR
     HRLLEPRLER FIGVIYRPET ERWSHYVACS LPQQFDAYVW FDETTAVKPL LTEARPGAEE
     TYPFGL
//
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