ID L5M9Y8_MYODS Unreviewed; 896 AA.
AC L5M9Y8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Methionine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00018335};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN ORFNames=MDA_GLEAN10006655 {ECO:0000313|EMBL:ELK35085.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK35085.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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:0000256|ARBA:ARBA00001234};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
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DR EMBL; KB102780; ELK35085.1; -; Genomic_DNA.
DR RefSeq; XP_006757392.1; XM_006757329.2.
DR AlphaFoldDB; L5M9Y8; -.
DR GeneID; 102763573; -.
DR KEGG; myd:102763573; -.
DR CTD; 4141; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1247; Eukaryota.
DR OrthoDB; 1341752at2759; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:UniProt.
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; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd10307; GST_C_MetRS_N; 1.
DR CDD; cd00814; MetRS_core; 1.
DR CDD; cd00939; MetRS_RNA; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR45765; METHIONINE--TRNA LIGASE; 1.
DR PANTHER; PTHR45765:SF1; METHIONINE--TRNA LIGASE, CYTOPLASMIC; 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; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363039};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363039};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556}.
FT DOMAIN 74..210
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 837..893
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
SQ SEQUENCE 896 AA; 100903 MW; F62B64788742F556 CRC64;
MRLFVSEGAP GTLPVLAAAG RAQGRAQLLV STVGPEECVV PFLTRPKIPV LQLDSGNYLF
STNAICRYFF LLSGSEQDDL TNQWLEWEAT ELQPALSAAL YYLVVQGKKG EDVLGPIRRA
LTHIDHSLSR RSCPFLAGET ESVADIVLWG ALYPLLQDPA YLPEELGALH SWFQTLSSQE
PCQRAAETVL KKQGILALRP YLQKQLQPSF LEGRAVSNEP EEEELATLSE EEIAVAVTAW
EKGLGSLPPL RPKQKPVLPV AGERNVLITS ALPYVNNVPH LGNIIGCVLS ADVFARYSRL
RQWNTLYLCG TDEYGTATET KAMEEGLTPQ EICDKYHVIH ADIYRWFNIS FDIFGRTTTS
QQTEITQDIF QRLWNRGFVL QDTVEQLRCE RCARFLADRF VEGVCPFCGY EEARGDQCDK
CGKLINAVEL KKPQCKVCRS CPVVRSSRHL FLDLPKLEDR LEEWLGKTVP GSDWTPNARF
IIRSWLRDGL KPRCITRDLK WGTPVPLKGF EDKVFYVWFD ATFGYISITA NYTDQWEKWW
KNPEQVNLYQ FMAKDNVPFH GLVFPCSALG AEDNYTLVSH LIATEYLNYE DGKFSKSRGV
GVFVADIWRF YLLYIRPEGQ DSAFSWTDML LKNNSELLNN LGNFINRAGM FVSKFFGGYV
PEMVLTSDDQ RLLAHVSLEL QHYHQLLEKV RIRDALRSIL TISRYGNQYI QVNEPWKRIK
GSEADRQRAG TVTGLAVNIA ALLSTMLQPY MPTVSSMIAA QLQLPPPACS ILPTDFLCTL
PAGHQIGTVS PLFQKLENDQ IENLRQRFGG GQLEESLVLK AKVSPKPAVI ETAGPQQIQV
LMDEVTKQGN IVRELKAQKA DKNQVAAEVA KLLDLKKQLA LAEGKPLETP KGKKKK
//