SYMM_XENLA
ID SYMM_XENLA Reviewed; 562 AA.
AC Q7T0Z0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Methionine--tRNA ligase, mitochondrial;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase 2;
DE AltName: Full=Mitochondrial methionyl-tRNA synthetase;
DE Short=MtMetRS;
DE Flags: Precursor;
GN Name=mars2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC ChEBI:CHEBI:456215; EC=6.1.1.10;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BC055977; AAH55977.1; -; mRNA.
DR RefSeq; NP_001079838.1; NM_001086369.1.
DR AlphaFoldDB; Q7T0Z0; -.
DR SMR; Q7T0Z0; -.
DR MaxQB; Q7T0Z0; -.
DR DNASU; 379528; -.
DR GeneID; 379528; -.
DR KEGG; xla:379528; -.
DR CTD; 379528; -.
DR Xenbase; XB-GENE-5862169; mars2.L.
DR OrthoDB; 788159at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 379528; Expressed in oocyte and 19 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR023457; Met-tRNA_synth_2.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR43326; PTHR43326; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..10
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 11..562
FT /note="Methionine--tRNA ligase, mitochondrial"
FT /id="PRO_0000045496"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 332..336
FT /note="'KMSKS' region"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 562 AA; 63461 MW; A6C04967DEC299F4 CRC64;
MLRSLALRTF ANILGLSSRS GSTAAMSRNA VASRPHLYTT PIFYVNAAPH LGHVYSALLA
DVQHRYSAMC GIESKLSTGT DEHGMKVQQA ASALGLDPQT FCSTVSLQFR TIFDALDISY
TDFVRTTEPR HIEAVSRFWM TLEEQGYIYK GTYEGWYCTS DEAFLSEGQT AEHTDFEGNK
IRVSLESGHQ VHWVSEENYM FRLSSLRPAL LNWLQTEPVH PAPFLKLVHH WLEEELPDLS
VSRQRSRLSW GIPVPSDSSH VIYVWLDALV NYLTAAGYPN PQLAPWGPST HLLGKDILRF
HAIYWPAFLI AAGLPPPQKL LVHSHWTSEG TKMSKSLKNV VDPSDCIRRY TTDGLRYYLL
RHGAPERDCD FTHRTARMLL NSELADALGG LLNRCTAPAI NPMQHFPKFQ YENFPVASRD
QVHDLLGALQ ELPVEVDQWI KKFQVHKALE CIDACVRRSN AFFQSQAPWK LQRGVEKEAA
LRDSVIYLTL EALRLYATLL HPAVPGLATV VLDRLGVPHK MRTLKKNTFL AATRGEICYF
QAQTLGPDKG LLFPRLEKSE AF