ALAXM_METBF
ID ALAXM_METBF Reviewed; 243 AA.
AC Q46AR9;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Alanyl-tRNA editing protein AlaX-M;
DE Short=AlaX-M;
DE AltName: Full=Alanyl-tRNA deacylase AlaX-M;
GN Name=alaXM; OrderedLocusNames=Mbar_A2092;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [2]
RP FUNCTION AS TRNA(ALA) EDITING PROTEIN.
RX PubMed=14663147; DOI=10.1073/pnas.2136934100;
RA Ahel I., Korencic D., Ibba M., Soll D.;
RT "Trans-editing of mischarged tRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15422-15427(2003).
CC -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC incorrectly charged Ser-tRNA(Ala) or Gly-tRNA(Ala). Has no activity on
CC incorrectly charged Ser-tRNA(Thr), nor on correctly charged Ala-
CC tRNA(Ala) or Ser-tRNA(Ser). {ECO:0000269|PubMed:14663147}.
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}.
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DR EMBL; CP000099; AAZ71023.1; -; Genomic_DNA.
DR RefSeq; WP_011307069.1; NC_007355.1.
DR AlphaFoldDB; Q46AR9; -.
DR SMR; Q46AR9; -.
DR STRING; 269797.Mbar_A2092; -.
DR EnsemblBacteria; AAZ71023; AAZ71023; Mbar_A2092.
DR GeneID; 3625707; -.
DR KEGG; mba:Mbar_A2092; -.
DR eggNOG; arCOG01254; Archaea.
DR HOGENOM; CLU_004485_3_2_2; -.
DR OMA; LMRLHTA; -.
DR OrthoDB; 60779at2157; -.
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; IDA: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; Zinc.
FT CHAIN 1..243
FT /note="Alanyl-tRNA editing protein AlaX-M"
FT /id="PRO_0000391646"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 243 AA; 27600 MW; 9BD49E10BC3F5360 CRC64;
MTEALYFLDC YMKEFEATVE KVTDDKFVVL DRTVFYPESG GQPSDTGKLV RESDGAEFNV
LYVRKFNGDI SHEIDGENVS NGLKAGDKVK GFIDWDRRYR HMRMHTATHV IANVIEKEAG
AQITGNQLGL DQSRVDFSLE VFDRDKFAEY EKIANDLIAQ KSPVNLYLVS RKEAEEKLSR
LTTLAKGFSD EIKEVRIVEI EGVTIEACGG THVKNTEEIK GVKIIKLQNK GKSNRRMYFT
LVD