SYM_NANEQ
ID SYM_NANEQ Reviewed; 776 AA.
AC Q74MZ1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Methionine--tRNA ligase;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=metG; OrderedLocusNames=NEQ457;
OS Nanoarchaeum equitans (strain Kin4-M).
OC Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC Nanoarchaeaceae; Nanoarchaeum.
OX NCBI_TaxID=228908;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kin4-M;
RX PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA Stetter K.O., Short J.M., Noorderwier M.;
RT "The genome of Nanoarchaeum equitans: insights into early archaeal
RT evolution and derived parasitism.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 1 subfamily. {ECO:0000305}.
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DR EMBL; AE017199; AAR39300.1; -; Genomic_DNA.
DR PDB; 5H34; X-ray; 1.75 A; A/B=663-776.
DR PDBsum; 5H34; -.
DR AlphaFoldDB; Q74MZ1; -.
DR SMR; Q74MZ1; -.
DR STRING; 228908.NEQ457; -.
DR EnsemblBacteria; AAR39300; AAR39300; NEQ457.
DR KEGG; neq:NEQ457; -.
DR PATRIC; fig|228908.8.peg.470; -.
DR HOGENOM; CLU_009710_1_2_2; -.
DR OMA; YMRMAGH; -.
DR BRENDA; 6.1.1.10; 8261.
DR Proteomes; UP000000578; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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-KW.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR Gene3D; 2.20.28.20; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR041872; Anticodon_Met.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
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 PANTHER; PTHR45765; PTHR45765; 2.
DR Pfam; PF09334; tRNA-synt_1g; 2.
DR Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF57770; SSF57770; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..776
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139192"
FT DOMAIN 676..776
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT MOTIF 10..20
FT /note="'HIGH' region"
FT MOTIF 375..379
FT /note="'KMSKS' region"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 674..678
FT /evidence="ECO:0007829|PDB:5H34"
FT STRAND 682..692
FT /evidence="ECO:0007829|PDB:5H34"
FT STRAND 700..705
FT /evidence="ECO:0007829|PDB:5H34"
FT STRAND 710..716
FT /evidence="ECO:0007829|PDB:5H34"
FT TURN 718..720
FT /evidence="ECO:0007829|PDB:5H34"
FT HELIX 723..726
FT /evidence="ECO:0007829|PDB:5H34"
FT STRAND 730..737
FT /evidence="ECO:0007829|PDB:5H34"
FT STRAND 740..742
FT /evidence="ECO:0007829|PDB:5H34"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:5H34"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:5H34"
FT STRAND 760..767
FT /evidence="ECO:0007829|PDB:5H34"
FT STRAND 774..776
FT /evidence="ECO:0007829|PDB:5H34"
SQ SEQUENCE 776 AA; 90600 MW; E467863337FC1CCD CRC64;
MRILVTAALP YSNGPIHLGH IAGAYLPADI FYRFVKLKGY NALYICGSDQ YGSPIELNAI
KLNIDPKDYA SFYRKIQEEI FKKFNIKFDI YSGTAESNIH PIIVKEFFLS LFSAGLLIEK
EQELPYDPKI KRFLPDRFVV GQCPYCGYEK AYGDQCEKCG RLLEPKELIN PKSAITGEKV
IFKKTRHLFF NIPKLKDKLK QYIESKKDVW NDFTYSWSLA LLDNFKERAI TRDNKWGVKV
PAKEMLEILK KALKEGKTPK DFGLLIDSTN EKDLENHIKE YENKVLYVWF DAPIGYISFT
FETSPEYRYY WDEKEKPYIV HFIGKDNIPF HTIFWPALII GRNLGYKNIN HILDFDIALP
YQVFGNPYLN YYGKKFSKSK RWGVFLDNID KIDIDIDYFR FYLAYIHTVS KDMSFEWDQF
KEVINKELVD NIGNFIHRVL TFIYNRFNGI PPKIEHLDDK DKELLDKIKQ LPEKVFNFIW
KGEIGNALRE IVNTSNLANK YFQEKEPWKT NDPNTIAIAF EAVKTFIILL YPFIPEKAKL
LASIANIDIK WDFNQKVEKI NKPFIVFHKL SDNQIEMAKQ ILTNPKEYDL GKKKVIGVLR
YEDELYKIEL ECDDNPWVCL KRELDKRKIK YIYDTVKGDV PPHIIDGNTY IYLLPALEKP
NLEKAEEEYG LVSYLDFAKL DMRVGKIIDV QDHPNADKLY IIKVSLGNKQ KTLVGGLKQY
YKKEELIGKY VVLINNLKPK QLRGITSEGM LLAADDGKEV ALLMPDKPIS LGSKVR
