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Database: UniProt
Entry: A0A0G1QGC1_9BACT
LinkDB: A0A0G1QGC1_9BACT
Original site: A0A0G1QGC1_9BACT 
ID   A0A0G1QGC1_9BACT        Unreviewed;       499 AA.
AC   A0A0G1QGC1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00018753};
DE            EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN   ORFNames=UX61_C0006G0004 {ECO:0000313|EMBL:KKU44036.1};
OS   Parcubacteria group bacterium GW2011_GWA2_46_7.
OC   Bacteria.
OX   NCBI_TaxID=1618837 {ECO:0000313|EMBL:KKU44036.1, ECO:0000313|Proteomes:UP000034469};
RN   [1] {ECO:0000313|EMBL:KKU44036.1, ECO:0000313|Proteomes:UP000034469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- FUNCTION: Is required not only for elongation of protein synthesis but
CC       also for the initiation of all mRNA translation through initiator
CC       tRNA(fMet) aminoacylation. {ECO:0000256|ARBA:ARBA00003314}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KKU44036.1}.
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DR   EMBL; LCMW01000006; KKU44036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1QGC1; -.
DR   PATRIC; fig|1618837.3.peg.125; -.
DR   Proteomes; UP000034469; 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:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
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; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 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.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 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}.
FT   DOMAIN          131..363
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          379..475
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
SQ   SEQUENCE   499 AA;  56645 MW;  3ADA85D8F7D3829A CRC64;
     MPQKFYITTA IPYASGDPHI GHFLEFIQAD VLARYHRLQG EEVFFLTGTD EHGIKIAEYA
     VKAGKTPDRF VSEIAEKFQN IADALRISYS YFIRTTNQQK HWPNVRKIWE LLADNGDIYK
     GHYKGKYCVG CEKYVTESDL ENGLCPFHQK PPEELDEDNY FFRLSRYQDQ LRQLIISDEV
     KILPGFRKQE VLSFIDRGIQ DVSFSRPKEK LNWGIPVPGD ESQVIYVWAD ALTNYLSGVD
     FAEAGVTFQR WWPPDVQIVG KDIWRFHALY WPAMLLSAHL PLPKVLFVHG FVTVGGEKIS
     KSLGNGIDPI AIMQKFSVDA DAVRYFFLRE MSPVEDGDYT DEKFITRYNG DLANGIGNFL
     ARVNQLGVLG RGTIALNTNT FQDAIVAAYN DYAKAMQEFR FNEALVFASQ LVKIGDGYIN
     EQKPWELLKS GTDEAHEKFN QHISSLTLLL GNIAQLLTPF MPATAEKILI AIGLAGQVPD
     AWQGKTVTFQ SLSPLFPRK
//
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