SYMC_BOVIN
ID SYMC_BOVIN Reviewed; 898 AA.
AC Q2T9L8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) 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. Forms a linear complex that contains MARS1, EEF1E1, EPRS1
CC and AIMP2 that is at the core of the multisubunit complex.
CC {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; BC111362; AAI11363.1; -; mRNA.
DR RefSeq; NP_001033180.1; NM_001038091.2.
DR AlphaFoldDB; Q2T9L8; -.
DR SMR; Q2T9L8; -.
DR STRING; 9913.ENSBTAP00000024487; -.
DR PaxDb; Q2T9L8; -.
DR PeptideAtlas; Q2T9L8; -.
DR PRIDE; Q2T9L8; -.
DR GeneID; 512531; -.
DR KEGG; bta:512531; -.
DR CTD; 4141; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1247; Eukaryota.
DR InParanoid; Q2T9L8; -.
DR OrthoDB; 333013at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; PF00043; GST_C; 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; 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; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..898
FT /note="Methionine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000246786"
FT DOMAIN 74..198
FT /note="GST C-terminal"
FT DOMAIN 839..895
FT /note="WHEP-TRS"
FT MOTIF 273..283
FT /note="'HIGH' region"
FT MOTIF 593..597
FT /note="'KMSKS' region"
FT BINDING 596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FL6"
FT MOD_RES 833
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68FL6"
SQ SEQUENCE 898 AA; 100634 MW; 174EFB5712AE15CD CRC64;
MRLFVSEGAP GSLPVLAAAG RAQGRAELLI STVGPEECVV PFLTRPKVPV LQLDSGNYLF
STSAICRYFF LLSGWEQDDL TNQWLEWEAT ELQPALSAAL YYLVVQGKKG EDVLGPVRRA
LTHIDHSLSR RSCPFLAGET ESLADIVLWG ALYPLLQDPS YLPEELGALH SWFQTLSSQE
PCQRAAETVL KQQGVLALRP YLQKQPQPSS LEGRLVSNEP EEEELATLSE EEIAVAVAAW
EKGLESLPPL RPQQNPVLPV AGERNVLITS ALPYVNNVPH LGNIIGCVLS ADVFARYSRL
RQWNTLYLCG TDEYGTATET KAMEEGLTPQ EICDKYHVIH ADIYRWFNIS FDFFGRTTTP
QQTKITQDIF QRLLARGFVL QDTVEQLRCE HCARFLADRF VEGVCPFCGY EEARGDQCDK
CGKLINAIEL KKPQCKVCRS CPVVKSSQHL FLDLPKLAAR VEEWLEKTLP GSDWTANARF
IIRSWLRDGL KPRCITRDLK WGTPVPLEGF EDKVFYVWFD ATIGYLSITA NYTDQWEKWW
KNPEQVNLYQ FMAKDNVPFH GIVFPSSALG AEDNYTLVSH LIATEYLNYE DGKFSKSRGV
GVFGDMAQDT GIPADIWRFY LLYNRPEGQD SAFSWTDMLF KNNSELLNNL GNFINRAGMF
VSKFFGGFVP EMVLTSDDQR LLTHITLELQ HYHQLLEKVR IRDALRSILT ISRHGNQYIQ
VNEPWKRIKG GEADRQRAGT VTGLAVNIAA LLSVMLQPYM PTVSATIQAQ LQLPPPACSI
LPTNFLCTLP AGHQIGTVSP LFQKLENDQI ESLKQRFSGG QAKASPKTAA GLTTAGPQQI
QALTEEVTKQ GNIVRELKAQ KADKNQIAAE VAKLLDLKKQ LALAEGKPLE TSKGKKKK
