SYMC_CAEEL
ID SYMC_CAEEL Reviewed; 917 AA.
AC Q20970;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Methionine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=mars-1 {ECO:0000312|WormBase:F58B3.5a};
GN Synonyms=mrs-1 {ECO:0000312|WormBase:F58B3.5a};
GN ORFNames=F58B3.5 {ECO:0000312|WormBase:F58B3.5a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; Z73427; CAA97803.1; -; Genomic_DNA.
DR PIR; T22898; T22898.
DR RefSeq; NP_001255570.1; NM_001268641.1.
DR AlphaFoldDB; Q20970; -.
DR SMR; Q20970; -.
DR BioGRID; 43186; 35.
DR STRING; 6239.F58B3.5a; -.
DR iPTMnet; Q20970; -.
DR EPD; Q20970; -.
DR PaxDb; Q20970; -.
DR PeptideAtlas; Q20970; -.
DR EnsemblMetazoa; F58B3.5a.1; F58B3.5a.1; WBGene00003415.
DR GeneID; 178089; -.
DR KEGG; cel:CELE_F58B3.5; -.
DR UCSC; F58B3.5; c. elegans.
DR CTD; 178089; -.
DR WormBase; F58B3.5a; CE06007; WBGene00003415; mars-1.
DR eggNOG; KOG1247; Eukaryota.
DR eggNOG; KOG2241; Eukaryota.
DR GeneTree; ENSGT00550000075017; -.
DR HOGENOM; CLU_009710_1_0_1; -.
DR InParanoid; Q20970; -.
DR OMA; MTTQLYC; -.
DR OrthoDB; 333013at2759; -.
DR PhylomeDB; Q20970; -.
DR PRO; PR:Q20970; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003415; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q20970; baseline and differential.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 2.20.28.20; -; 1.
DR Gene3D; 2.40.50.140; -; 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; 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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002547; tRNA-bd_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR45765; PTHR45765; 1.
DR Pfam; PF19303; Anticodon_3; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF57770; SSF57770; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..917
FT /note="Methionine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000139265"
FT DOMAIN 756..857
FT /note="tRNA-binding"
FT REGION 591..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT MOTIF 367..371
FT /note="'KMSKS' region"
FT COMPBIAS 604..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 917 AA; 101714 MW; 3B42AABA314FBDF0 CRC64;
MGHDLADIKK SFEASLPGYV EKKDPKSILP QPGKRNILIT AALPYVNNVP HLGNIIGCVL
SADVFARYCN LRGHQTFYVG GTDEYGTATE TKALQEGCTP RELCDKYHAI HKGIYEWFGI
DFSHFGRTTT DHQTEICQDM FLKLHKNGYT SSQSVDQLYC NQCEKFLADR FVTGTCPMCA
YDDARGDQCD GCGKLINAVD LKDAKCHMCK ATPEVKQSTH IFLSLDKLQQ KTTEHLDREL
AKEDNRWSSN AVGITKAWMK LGLDPRCITR DLKWGTAVPL DGFEKKVFYV WFDAPIGYLS
ITKCVLGDNW TKWWKNPENV ELFNFVGKDN VAFHAVMFPC SQLGANDNYT VVNNLCATEY
LNYEDTKFSK SRGTGIFGDA AQGTEIPADI WRFYLLYMRP ESQDTAFSWD DFVLKVNSEL
LNNLGNFINR ALSFVANSFG GVVPEMNLTN DDAEVLSEIH NECMQWDKQF DGVHLKDAVK
TILNVSRLGN QYMQAQTPWV LMKKDEEGKK RAGTIIGVAA NIAYHVSVLL YPIMPTISAT
IREQCGLPAL PLFTPFPICY LKAGHKIGQP SPLFQKLDPA QIAEFKAKFG GSQDAQSSAP
KTAEKPKQQK KQAPTKDKKG DKKMASTAAF VELEQGAKVI SQLIAQNLKK FDQAKALFTR
NQLQRLDGEN KQLTIDVKTL QHQLIELETA AGIKQVPKPV VSCTPTPTST PASGIITEAP
KKEAPSTPAP SEPKKAKEQK KGKGGAAAAP VDDTIDVGRL DMRVGRIIKC EKHPDADALY
VEQIDVGESA PRTVVSGLVR HVPLDQMQNR LVVVLCNLKP AKMRGVESRA MVMCASSPDK
VEIMEVPADS KPGTPVVCPP YTHRPDEQLN PKKKIWETVA EDLKVSAEGF AEWKGQPLLI
GSESKMTAPT LRGVHVK
