SYMC_XENLA
ID SYMC_XENLA Reviewed; 905 AA.
AC Q6PF21;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Methionine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.10 {ECO:0000250|UniProtKB:P56192};
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=mars1; Synonyms=mars;
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=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the specific attachment of an amino acid to its
CC cognate tRNA in a 2 step reaction: the amino acid (AA) is first
CC activated by ATP to form AA-AMP and then transferred to the acceptor
CC end of the tRNA. Plays a role in the synthesis of ribosomal RNA in the
CC nucleolus. {ECO:0000250|UniProtKB:P56192}.
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 Evidence={ECO:0000250|UniProtKB:P56192};
CC -!- SUBUNIT: Monomer. Part of a multisubunit complex that groups tRNA
CC ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu
CC (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu and
CC Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and
CC EEF1E1/p18. {ECO:0000250|UniProtKB:P56192}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P56192}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P56192}. Note=Localizes to the nucleolus in
CC proliferative cells but disappears in quiescent cells.
CC {ECO:0000250|UniProtKB:P56192}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; BC057757; AAH57757.1; -; mRNA.
DR RefSeq; NP_001079984.1; NM_001086515.1.
DR AlphaFoldDB; Q6PF21; -.
DR SMR; Q6PF21; -.
DR IntAct; Q6PF21; 1.
DR DNASU; 379675; -.
DR GeneID; 379675; -.
DR KEGG; xla:379675; -.
DR CTD; 379675; -.
DR Xenbase; XB-GENE-17340220; mars1.S.
DR OrthoDB; 333013at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 379675; Expressed in zone of skin and 20 other tissues.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; ISS:UniProtKB.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 2.20.28.20; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR041598; MARS_N.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR029038; MetRS_Zn.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR PANTHER; PTHR45765; PTHR45765; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF18485; GST_N_5; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF57770; SSF57770; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 2: Evidence at transcript level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Nucleus; Protein biosynthesis; Reference proteome;
KW RNA-binding; tRNA-binding.
FT CHAIN 1..905
FT /note="Methionine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000139264"
FT DOMAIN 1..75
FT /note="GST N-terminal"
FT DOMAIN 72..199
FT /note="GST C-terminal"
FT DOMAIN 844..900
FT /note="WHEP-TRS"
FT REGION 813..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 271..281
FT /note="'HIGH' region"
FT MOTIF 591..595
FT /note="'KMSKS' region"
FT COMPBIAS 821..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 905 AA; 102359 MW; C79BFA3254468964 CRC64;
MKLFVGEGNP QGVKVLAAAA LWAQHVQIDR LQQEEKIVPF MSQPRLPVLD LENGNYLFLS
NAICRYFYLS SGHDMCDLSN QWLEWEAAEL QPALSAALYA HVVQGKKKED VMATISASLK
HLDQSLAGKS SPYLIKDALT VVDIVVWGSI YPLIVDASNL PEEMASLKRW FQNVSQLEQC
QKAASSLLKD KGSSVFKPFL QKQPAPITPP GKSVCKEQEG EDMPSLSEED IQAAAEAWAK
GLTGASKPKQ RPHPILPVEG EKNVLITSAL PYVNNVPHLG NIIGSVLSAD VFARYCRLRN
WNTLYICGTD EYGTATETKA MEEGLTPQQI CDKYNAIHTA IYQWFNISFD YFGRTTTQHQ
TTISQDIFHR LLEREFLLTD TVEQLRCEKC QRFLADRFVE GICPFCNYEE ARGDQCDKCG
KLINAVELKK PQCKICKQSP VIKSSKHLFL DLPKLEKRLE QWLEQSFSTG DWTSNARFIT
RSWIRDGLKP RCITRDLKWG TPVPLDGFRD KVFYVWFDAP IGYISITANY TDQWEKWWKS
PQQVQLYNFM AKDNVPFHSV VFPSCLLGAE DNYTLVNHLV ATEYLNYEDG KFSKSRGVGV
FGDMAKDTGI PADIWRFYLL YVRPEGQDSA FSWSDLMLKN NSELLNNLGN FVNRAGMFVQ
KFFNGCVPEM ELLSEDKRLL AQVAAELQQY NLLLEKVRIR DALRCILNIS RHGNQYIQVN
EPWKCIKGNQ QEQKRAGTVT GVAVNMAALL SIMLHPYMPT ISSVIQEQLL MPQESKVLTT
DFCCCLQSGH QIGNVSPLFQ KLENDQIESL RKRFGGGQVK TESKVSPSQE APEQQAPKAS
GPERVKELMQ ELEKQGNHVR ELKGKKAEKS VIDPEVQKLL ALKKELALAE GKSPDPPTQK
GKKKK
