ID A0A1Q3QQF6_9BACT Unreviewed; 824 AA.
AC A0A1Q3QQF6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=BGO25_16850 {ECO:0000313|EMBL:OJV41388.1};
OS Acidobacteriales bacterium 59-55.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales.
OX NCBI_TaxID=1895690 {ECO:0000313|EMBL:OJV41388.1, ECO:0000313|Proteomes:UP000186822};
RN [1] {ECO:0000313|EMBL:OJV41388.1, ECO:0000313|Proteomes:UP000186822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=59-55 {ECO:0000313|EMBL:OJV41388.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJV41388.1}.
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DR EMBL; MKSV01000007; OJV41388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3QQF6; -.
DR STRING; 1895690.BGO25_16850; -.
DR Proteomes; UP000186822; 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: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; 2.170.220.10; -; 2.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR004495; Met-tRNA-synth_bsu_C.
DR InterPro; IPR023457; Met-tRNA_synth_2.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR033911; MetRS_core.
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; TIGR00399; metG_C_term; 1.
DR PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1.
DR Pfam; PF09334; tRNA-synt_1g; 3.
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; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 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 722..824
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT REGION 653..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 91950 MW; 23607ABF7981CE5A CRC64;
MSDTQKKFYL TTPIYYVNAR PHIGHAYTTI AADVIARRHR LLGEDTFFLT GTDEHGQKIE
RSATAAGIPP QQFADQVSAQ FESLWKRMGI TNDDYIRTTE ERHKKGVQKL WQLLRDRDKI
YLSTYTGQYS VGEEMFVEGP PGTIGPDGKP TETVTEENYF FRLSEYQRPL IDLIESGELA
IQPDVRKNEV LSFLRGNFSA EITEVYDREV RAGRETLAAG RDSWDPAEIA REEGKIDKST
AGHNYVPGSL KDLSISRSSF KWGIPVPRDP QTEKDHVVYV WLDALANYMT AIGYGSDDPA
DQAKFEKYWP ADLHLVGKEI IRFHCVYWPA FLLALNPATD SKKPEEVPFE VHRQWAKDWL
PKAITAHGWL LFEESKMSKS RGNIVRTETI LDAFGTLLPK AAEANSLVKG TASAVLQQTS
EGAALAAEVR LSSSEEWKHE QDLFASDVLR YFLLREIPFG QDGSFSFDSL VQRYNSDLAN
GYGNLVSRTL NLIHQNFAGI VPEDLEAQND PWSYFLTVVP LIAEQYKNGL LTLICANIMN
LVSVTDSAIT KNTPWKLAKS KHLEDQQKAR HTLRGAFEAI RIITALLHPI MPYATAKVWA
QLGLGDIELA ARNGELKDLK WGGLKPGTKL GPLAPIFPRA PKELIQTMTD MEQNNAPKPA
QPAGLPQVNN SVDKPAREHT EFREAPISSA SATPALNPIA ETTHPIADTA AAPDTPQIAI
DDFVKIDLRV ARIVLAERIP KADKLLRLEV DLGYEKRQIL SGIAQWYTPE ELIGRNIVVI
ANLAPRKMRG LESHGMLLAA SHGEDGKPIL ATFGEEIALG SRLK
//
