ALAXM_METMA
ID ALAXM_METMA Reviewed; 251 AA.
AC Q8Q0A4;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Alanyl-tRNA editing protein AlaX-M;
DE Short=AlaX-M;
DE Short=AlaXp;
DE AltName: Full=Alanyl-tRNA deacylase AlaX-M;
GN Name=alaXM; Synonyms=alaX; OrderedLocusNames=MM_0233;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP FUNCTION IN EDITING DEFECTIVE E.COLI, AND MUTAGENESIS OF LYS-232 AND
RP LYS-234.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=18723508; DOI=10.1074/jbc.m805943200;
RA Chong Y.E., Yang X.L., Schimmel P.;
RT "Natural homolog of tRNA synthetase editing domain rescues conditional
RT lethality caused by mistranslation.";
RL J. Biol. Chem. 283:30073-30078(2008).
RN [3]
RP FUNCTION AS TRNA(ALA) EDITING PROTEIN, AND MUTAGENESIS OF 232-LYS--LYS-234.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=18172502; DOI=10.1038/nature06454;
RA Beebe K., Mock M., Merriman E., Schimmel P.;
RT "Distinct domains of tRNA synthetase recognize the same base pair.";
RL Nature 451:90-93(2008).
CC -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC mischarged Ser-tRNA(Ala). Recognition depends, at least in part, on the
CC acceptor stem of tRNA(Ala). {ECO:0000269|PubMed:18172502,
CC ECO:0000269|PubMed:18723508}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Editing domain AlaX-M subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM29929.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008384; AAM29929.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048037132.1; NC_003901.1.
DR AlphaFoldDB; Q8Q0A4; -.
DR SMR; Q8Q0A4; -.
DR STRING; 192952.MM_0233; -.
DR EnsemblBacteria; AAM29929; AAM29929; MM_0233.
DR GeneID; 44086586; -.
DR GeneID; 66135038; -.
DR KEGG; mma:MM_0233; -.
DR PATRIC; fig|192952.21.peg.284; -.
DR eggNOG; arCOG01254; Archaea.
DR HOGENOM; CLU_004485_3_2_2; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..251
FT /note="Alanyl-tRNA editing protein AlaX-M"
FT /id="PRO_0000391647"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MUTAGEN 232..234
FT /note="KGK->AGA: No removal of mischarged Ser from Ser-
FT tRNA(Ala)."
FT /evidence="ECO:0000269|PubMed:18172502"
FT MUTAGEN 232
FT /note="K->A: Severe reduction in removal of mischarged Ser
FT from Ser-tRNA(Ala)."
FT /evidence="ECO:0000269|PubMed:18723508"
FT MUTAGEN 234
FT /note="K->A: Modest reduction in removal of mischarged Ser
FT from Ser-tRNA(Ala)."
FT /evidence="ECO:0000269|PubMed:18723508"
SQ SEQUENCE 251 AA; 28203 MW; 2691B9677C106139 CRC64;
MTEALYFLDC YLKEFEATVE KVTEGKYIVL DRTAFYPESG GQPSDTGKLV RERDGAEFKV
VYAGKFNGDI SHEISPEGET GAEGLKVGDK VKGIIDWDRR YRHMRMHTAT HVIANVIEKE
AGAQITGNQL GLDQSRVDFS LEAFDREKFA EYEKIANEII AENHSVNLYL VSRKEAEERL
SRLTTLAKGF SEEITEVRLV EIEGVTIEAC GGSHLKNTGE IKGIKIEKLQ NKGKSNRRMY
FSLLDQASGL K
