ID A0A1I7XJX3_HETBA Unreviewed; 673 AA.
AC A0A1I7XJX3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
OS Heterorhabditis bacteriophora (Entomopathogenic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heterorhabditidae;
OC Heterorhabditis.
OX NCBI_TaxID=37862 {ECO:0000313|Proteomes:UP000095283, ECO:0000313|WBParaSite:Hba_18015};
RN [1] {ECO:0000313|WBParaSite:Hba_18015}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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|RuleBase:RU363039}.
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DR AlphaFoldDB; A0A1I7XJX3; -.
DR WBParaSite; Hba_18015; Hba_18015; Hba_18015.
DR Proteomes; UP000095283; Unplaced.
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 Gene3D; 3.40.50.620; HUPs; 1.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
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; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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}.
FT DOMAIN 62..335
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 367..443
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
SQ SEQUENCE 673 AA; 76168 MW; FFCD79970961A41C CRC64;
MRGHQTLYIC GTDEYGTATE TKALYEGVTP REVCDKYHII HKEIYDWFNI EFDHFGRTTT
EQQTEFLADR FVTGVCPLCA YDDARGDQCD ACGKLINAID LIQPKCHVCK QEPKVRQSTH
IFLHLDRLQV SLLDDVRKYV ETQIERSDNR WSSNAIAIVK GWIKGGLDKR CITRDLKWGT
PVPLAEFSDK VFYVWYDAPI GYLSITKCLL GNNWVKWWKN PENVELYNFV GKDNVAFHGV
MFPSTQIGAG DNYTIVNNLC ATEYLNYENT KFSKSRGTGV FGDAAKETGI EADVWRFYLL
YMRPESQDTV FSWDDFALKV NSELLANLGN FVNRALSFLS NNFGGVIPEM HLTNIDVELL
CGIQDCEEWD SLLDGVKLKD AMRVVLAMSR RGNQYMQAMQ PWVLMKGTNQ DKERAGTVIG
VAANVSYQLS IVLHPFMPET GHKIGTPKPL FVKLDNAKIA EWKSKFGGAS NKVKKMTPVQ
AYPHLAKNQQ QIQQLLKVAS IKFEQARALF VKNKQIELEA CISKLDKEVR AVQKELVDAE
IAAGTIKVLF EDENIFYLVK QINVSLTDQA ASVPANRSSG SAPSTSVETL HKLDKNGGQP
KNECNKKCRE LNNGNRIRNS ILHYNFFKFQ VWETVSEHLK VSSEGFAAWK DAPLLVNGQT
RITAPTLRGV FVK
//