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Database: UniProt
Entry: A0A1G8U9F8_9EURY
LinkDB: A0A1G8U9F8_9EURY
Original site: A0A1G8U9F8_9EURY 
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
//
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