ID A0A1H1SUW5_9FLAO Unreviewed; 686 AA.
AC A0A1H1SUW5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00098};
DE EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_00098};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00098};
DE Short=MetRS {ECO:0000256|HAMAP-Rule:MF_00098};
GN Name=metG {ECO:0000256|HAMAP-Rule:MF_00098};
GN ORFNames=SAMN04489797_1771 {ECO:0000313|EMBL:SDS51724.1};
OS Winogradskyella sediminis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=1382466 {ECO:0000313|EMBL:SDS51724.1, ECO:0000313|Proteomes:UP000198963};
RN [1] {ECO:0000313|EMBL:SDS51724.1, ECO:0000313|Proteomes:UP000198963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA_55 {ECO:0000313|EMBL:SDS51724.1,
RC ECO:0000313|Proteomes:UP000198963};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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_00098}.
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_00098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00098};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00098};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00098}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00098}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 1 subfamily. {ECO:0000256|ARBA:ARBA00008258,
CC ECO:0000256|HAMAP-Rule:MF_00098}.
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DR EMBL; LT629774; SDS51724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1SUW5; -.
DR STRING; 1249933.SAMN04489797_1771; -.
DR Proteomes; UP000198963; Chromosome I.
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; 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 HAMAP; MF_00098; Met_tRNA_synth_type1; 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 NCBIfam; TIGR00399; metG_C_term; 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|HAMAP-Rule:MF_00098};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00098};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00098};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00098};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00098};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00098};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00098}; Zinc {ECO:0000256|HAMAP-Rule:MF_00098}.
FT DOMAIN 584..686
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT MOTIF 12..22
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT MOTIF 333..337
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
FT BINDING 336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098"
SQ SEQUENCE 686 AA; 77349 MW; 3F2D4D94593FB5DB CRC64;
MSKRYTITAA LPYTNGPIHI GHLAGVYVPA DIYARYLRLT GNDVAFICGS DEHGVPITIK
AKKEGVTPQD IVDKYHAIIK QSFVDFGISL DNYSRTTAKI HHDTAQEFFK TLYDKNEFVE
EVTEQLYDEE ANQFLADRFV TGTCPKCGNE EAYGDQCESC GTSLNATDLI NPKSAITGNV
PTLKETKHWF LPLNKHEEFL REWILKGHKK DWKPNVYGQV KSWIDDGLRP RAVTRDLDWG
IPVPVEGGEG KVLYVWFDAP IGYISATKEW AEREGKNWED YWKDEDTKLV HFIGKDNIVF
HCIIFPSMLK AEGSYILPEN VPANEFLNLE GQKLSTSKNW AVWLPDYLID FPNQQDVLRY
ALTANAPETK DNDFTWKDFQ ARNNNELVAI FGNFINRVVV LTNKYYNGII PEPSDYSAID
QEILAAVKAY PAVISSSIER YRFREASQEL MNLARLGNKY LADEEPWKTV KTDEARTKTV
MFVALQIASA LAVLSEPFLP FTSNKLKSIL CHSALDAEST WDDISSKELL LPANHKIGKA
DLLFSKIEDA QIEAQLEKLI ASKKANEAAN KAVEPQKEEI TFEDFTKLDL RVGTIIEAEK
MPKTKKLLVL KVDTGLDTRT IVSGIAESFK PEEVIGKRVT VLVNLAPRKL RGVESQGMIL
MTEDEGGNLV FVNPDKDNVS NGLQIS
//
