ID A0A099B9J4_9HELI Unreviewed; 710 AA.
AC A0A099B9J4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 59.
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 ECO:0000313|EMBL:TLD95886.1};
GN ORFNames=DCO61_00650 {ECO:0000313|EMBL:MWV68577.1}, LS64_000530
GN {ECO:0000313|EMBL:TLD95886.1};
OS Helicobacter saguini.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1548018 {ECO:0000313|EMBL:TLD95886.1, ECO:0000313|Proteomes:UP000029714};
RN [1] {ECO:0000313|EMBL:TLD95886.1, ECO:0000313|Proteomes:UP000029714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 97-6194 {ECO:0000313|EMBL:TLD95886.1,
RC ECO:0000313|Proteomes:UP000029714};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(2014).
RN [2] {ECO:0000313|EMBL:TLD95886.1, ECO:0000313|Proteomes:UP000029714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 97-6194 {ECO:0000313|EMBL:TLD95886.1,
RC ECO:0000313|Proteomes:UP000029714};
RX PubMed=27245408; DOI=.1128/IAI.00235-16;
RA Shen Z., Mannion A., Whary M.T., Muthupalani S., Sheh A., Feng Y., Gong G.,
RA Vandamme P., Holcombe H.R., Paster B.J., Fox J.G.;
RT "Helicobacter saguini, a Novel Helicobacter Isolated from Cotton-Top
RT Tamarins with Ulcerative Colitis, Has Proinflammatory Properties and
RT Induces Typhlocolitis and Dysplasia in Gnotobiotic IL-10-/- Mice.";
RL Infect. Immun. 84:2307-2316(2016).
RN [3] {ECO:0000313|EMBL:TLD95886.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MIT 97-6194 {ECO:0000313|EMBL:TLD95886.1};
RA Sheh A., Shen Z., Mannion A.J., Fox J.G.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:MWV68577.1, ECO:0000313|Proteomes:UP000477070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-048 {ECO:0000313|EMBL:MWV68577.1}, and 16-048 (F4)
RC {ECO:0000313|Proteomes:UP000477070};
RA Mannion A., Shen Z., Fox J.G.;
RT "Multi-Generational Helicobacter saguini Isolates.";
RL Submitted (DEC-2019) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001234, ECO:0000256|HAMAP-
CC Rule:MF_01228};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01228};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01228};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC 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 MetG type 2A subfamily. {ECO:0000256|HAMAP-Rule:MF_01228}.
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:TLD95886.1}.
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DR EMBL; QBIU01000001; MWV68577.1; -; Genomic_DNA.
DR EMBL; JRMP02000001; TLD95886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099B9J4; -.
DR STRING; 1548018.LS64_03495; -.
DR OrthoDB; 9810191at2; -.
DR Proteomes; UP000029714; Unassembled WGS sequence.
DR Proteomes; UP000477070; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00814; MetRS_core; 1.
DR CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR InterPro; IPR004495; Met-tRNA-synth_bsu_C.
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; 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 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; 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; 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|HAMAP-Rule:MF_01228};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01228};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01228};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01228};
KW Metal-binding {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:UP000029714};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01228};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_01228}; Zinc {ECO:0000256|HAMAP-Rule:MF_01228}.
FT DOMAIN 609..710
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT REGION 539..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 10..20
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT MOTIF 314..318
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT COMPBIAS 539..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ SEQUENCE 710 AA; 80884 MW; CBACAF5B218B1F6A CRC64;
MKRLLTTPIY YVNDVPHIGH AYSTIIADVI KKYWTLQGDD VFLLTGTDEH GQKIEEAARK
KGIKTIEYAN TIANKFRDVW DKFHIDYNKF IRTTYLEHIL SVQKAFEIMF DKGDIYKGEY
EGQYCVSCES FFTQTQVLDG IYCPDCGKET RLVKEESYFF RLSKYQNKLL EWYKNNPACI
LPLHKKNEVI KFVDNSLQDL SITRTSFEWG IKVPLKLKDD KHIVYVWLDA LMNYPSALGY
GLDYNNAREL LQHKAEQNPA LESKMEYFKH TSHVVGKDIL RFHAIYWPAF LMSLELPLPE
HIFVHGWWTI DGVKMSKSIG NVINPLDILE AYPLDIFRYF LLKEVPFGQD GDFSERALIN
RNNGELSNDL GNLVNRLIGM SEKYFEYDLS DSFSIDRFQL EREKVDELSH EALGFMNNMQ
PNKYLESIWE MLHLANAMIT KFAPWEMMKR GEVQECKELL NLIANILLKV SLLLYPIMPT
TCLKIAACLG VKIDSVGFRG FIVEFEYKRD FKITKIDALF PKIDSPRMKK DSNVIASESE
AIESKGNSPT LAGNATSLPP HLAGDTTLSS PPLAGGARGG VKSHAPDSKD SQKSNIESKN
IESKITLSDF QKIHLKVGTI LSAEKLEKSE KLLKLKVDLG EENPRQIIAG ISQFYNPESL
VNSQVIVLAN LKPAKLMGEL SEGMLLACKD SNGLSLLRPE NPRHPGTPIS
//
