ID A0A1G8U9F8_9EURY Unreviewed; 704 AA.
AC A0A1G8U9F8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
GN ORFNames=SAMN05216226_104123 {ECO:0000313|EMBL:SDJ50371.1};
OS Halovenus aranensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halovenus.
OX NCBI_TaxID=890420 {ECO:0000313|EMBL:SDJ50371.1, ECO:0000313|Proteomes:UP000198856};
RN [1] {ECO:0000313|EMBL:SDJ50371.1, ECO:0000313|Proteomes:UP000198856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M10015 {ECO:0000313|EMBL:SDJ50371.1,
RC ECO:0000313|Proteomes:UP000198856};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363039}.
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DR EMBL; FNFC01000004; SDJ50371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8U9F8; -.
DR STRING; 890420.SAMN05216226_104123; -.
DR OrthoDB; 371856at2157; -.
DR Proteomes; UP000198856; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.20.28.20; Methionyl-tRNA synthetase, Zn-domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR004495; Met-tRNA-synth_bsu_C.
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 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 Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF57770; Methionyl-tRNA synthetase (MetRS), Zn-domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50886; TRBD; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000198856};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00209};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00209}.
FT DOMAIN 606..704
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT COILED 559..586
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 704 AA; 79305 MW; D2ACB77C26709B66 CRC64;
MSQEDFPTDQ PAVVTVGLPY ANGDLHVGHL LGYITGDTYA RGLRRLGQQT AFVCGSDMHG
TPVAVNAAKQ DREPEALAMD HHEQYEQRFP SFNVEFDNYG HTHDETNTEL TQEFVETWIE
QDHVVEKEIE VAFDTETDDP LPDRYVEGTC PYCGEKARGD ECDEGCQRHL EPGEIEDPVS
VTTGNPAEYR KQPHKFLRLS DFQEYLQEFI DRLEGTEKAR NQPREWIEGE LQDLCITRDM
DWGVDYPGED REDLVLYVWV DAPIEYVAST KQYSEQVGTD EFDWEAAWKL DGQTRPDTSW
TDDWSQDNGE IIHVIGTDII QHHCVYWPAM LRGAGFNEPR AVIATGFVGI DGKSLSTSRN
RAVWATEYLD AGFDPDLLRY YLTTGSGVES DIDFSWDRFA ERVNGELVGN LGNFCYRALL
FAERNYDGTP DADPSEEVRE RIEQATETFE QAVREYDVRT VGEVALDLAD FGNEYIQRNE
PWNLIGDDPE AAAVVIRDCV QLAKACAVFM QPVMPGKAAD LWAQLGEDGD VADAELSAAL
EPPAADFDEP TELFTQVEDE TIEDLNEQLR ERVETAQEET DDQDDSETAT MTDIDPIEDE
RIGFEQFQDI DMRVGEIVTA DPIEDSDDLV RLEVDIGVET RQVVAGIKQL HDADDLPETR
VVLLANMEKA ELFGVESNGM VLAAGEEADL LTTHEDAPLG TRVR
//