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Database: UniProt
Entry: A0A1C0VEL0_9CYAN
LinkDB: A0A1C0VEL0_9CYAN
Original site: A0A1C0VEL0_9CYAN 
ID   A0A1C0VEL0_9CYAN        Unreviewed;       537 AA.
AC   A0A1C0VEL0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01228};
DE            EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_01228};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228};
DE            Short=MetRS {ECO:0000256|HAMAP-Rule:MF_01228};
GN   Name=metG {ECO:0000256|HAMAP-Rule:MF_01228};
GN   ORFNames=BCR12_14310 {ECO:0000313|EMBL:OCQ96242.1};
OS   Limnothrix sp. P13C2.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC   Pseudanabaenaceae; Limnothrix.
OX   NCBI_TaxID=1880902 {ECO:0000313|EMBL:OCQ96242.1, ECO:0000313|Proteomes:UP000093334};
RN   [1] {ECO:0000313|EMBL:OCQ96242.1, ECO:0000313|Proteomes:UP000093334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P13C2 {ECO:0000313|EMBL:OCQ96242.1};
RA   Tan B., Te S.H., Gin K., Thompson J.;
RT   "Draft genome of Limnothrix sp. P13C2.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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       ECO:0000256|HAMAP-Rule:MF_01228}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01228};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363039}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01228}.
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:OCQ96242.1}.
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DR   EMBL; MBRF01000009; OCQ96242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C0VEL0; -.
DR   STRING; 1880902.BCR12_14310; -.
DR   Proteomes; UP000093334; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 2.170.220.10; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
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; 2.
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|HAMAP-Rule:MF_01228};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01228}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01228};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01228};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_01228}; Reference proteome {ECO:0000313|Proteomes:UP000093334}.
FT   DOMAIN          20..153
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          156..379
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          414..533
FT                   /note="Methionyl-tRNA synthetase anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19303"
FT   MOTIF           26..36
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   MOTIF           315..319
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ   SEQUENCE   537 AA;  61235 MW;  42DD5D3B42188CC9 CRC64;
     MVVTEDLTSS PPPPQPSPFT ITTPLYYVNA LPHIGSAYTT MAVDAVGRFY RLQGHPVLMI
     TGTDEHGQKI ERTAQERNKN PQEHCDEIVQ GFADLWQKLN IRYDRFIRTT DERHRAIVVE
     FFERVWAAGD IYSGKQQGWY CVSCEEFKEE RELTEDHHCL VHPNKQAEWR DEENYFFRLS
     KYQTALQQFY GDHPEFIQPE SRRNEVLAFV ERGLQDFSIS RVNIDWGFAL PNDPKHTLYV
     WFDALLGYVT ALLEPGEAPT LENALRHWWP ISTHVIGKDI LRFHAIYWPA MLMSAGLPIP
     QRLFGHGFLT KDGQKMGKTL GNTIDPVALI DRYGSDAVRY YFLKEIEFGR DGDFNETRFI
     NIVNADLAND LGNLLNRTLK MAHKYCEGRV PSVTVAETDP LRQLGTTLGD RAGRAYRAMA
     LHEACQSVLM LAQTGNKYLD EQAPWTKFKQ GDRAAVEAIL YAVLESVRLA AYWLSPIVPQ
     LSSRIYGQLG FAVDFDRVDA DPSLREQLGG HGHWGGLPTG QGLAEPQPVF QKLEMPQ
//
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