ID   SYM_ORYSJ               Reviewed;         801 AA.
AC   Q9ZTS1; Q5Z9M1;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Probable methionine--tRNA ligase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   OrderedLocusNames=Os06g0508700, LOC_Os06g31210; ORFNames=P0561B08.33;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11118226; DOI=10.1093/emboj/19.24.6908;
RA   Kaminska M., Deniziak M., Kerjan P., Barciszewski J., Mirande M.;
RT   "A recurrent general RNA binding domain appended to plant methionyl-tRNA
RT   synthetase acts as a cis-acting cofactor for aminoacylation.";
RL   EMBO J. 19:6908-6917(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF040700; AAC99620.1; -; mRNA.
DR   EMBL; AP003618; BAD61657.1; -; Genomic_DNA.
DR   EMBL; AP014962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015643979.1; XM_015788493.1.
DR   AlphaFoldDB; Q9ZTS1; -.
DR   SMR; Q9ZTS1; -.
DR   STRING; 4530.OS06T0508700-01; -.
DR   PaxDb; Q9ZTS1; -.
DR   PRIDE; Q9ZTS1; -.
DR   GeneID; 4341140; -.
DR   KEGG; osa:4341140; -.
DR   eggNOG; KOG2241; Eukaryota.
DR   InParanoid; Q9ZTS1; -.
DR   OrthoDB; 333013at2759; -.
DR   BRENDA; 6.1.1.10; 4460.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR   GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 2.20.28.20; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.620; -; 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; 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   PANTHER; PTHR45765; PTHR45765; 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; SSF47323; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF57770; SSF57770; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..801
FT                   /note="Probable methionine--tRNA ligase"
FT                   /id="PRO_0000139267"
FT   DOMAIN          639..742
FT                   /note="tRNA-binding"
FT   REGION          606..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           25..35
FT                   /note="'HIGH' region"
FT   MOTIF           347..351
FT                   /note="'KMSKS' region"
FT   COMPBIAS        606..630
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         350
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        8
FT                   /note="P -> PPPP (in Ref. 1; AAC99620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443
FT                   /note="V -> A (in Ref. 1; AAC99620)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   801 AA;  89453 MW;  5760F2E3E0DA33C3 CRC64;
     MASPPPPPKL PVPGRRNILV TSALPYVNNV PHLGNIIGCV LSADVFARYC RLRGYNVIYI
     CGTDEYGTAT ETKAMEEKCS PKEICDKYHA VHSEVYKWFD IKFDKFGRTS SPQQTEVCQA
     IFQKLMENNW LTENTMQQLY CDTCQRFLAD RLVEGKCPTE GCNYEAARGD QCENCSKLLN
     PTELIDPKCK VCKNTPRVRD TDHLFLELPL LSDKLVNYIN ETSVAGMWSQ NAIQATNAWL
     KEGLKPRCIT RDLKWGVPVP HEKYKDKVFY VWFDAPIGYV SITASYTPDW EKWWKDPDNV
     ELFQFMGKDN VPFHTVMFPS TLLGTGEKWT MMKTISVTEY LNYEAGKFSK SHGIGVFGND
     AKDTNIPPEV WRYYLLTNRP EVSDTLFTWA DLQAKLNSEL LNNLGNFINR VLSFVAKPAG
     AGYDSIVPDA PNAESHPLTK ALVEKTNKWV EQYLEAMEKV KLKQGLKSAM GISSDGNAYL
     QESQFWKLYK EDPAACAVVM KTSVGVVYLL ACLLEPFMPS FSNEVLLQLN MTPEESLSFC
     DDKGEIAKAK RPWDFVSAGH KIGKPSPLFK ELKDEEVESF RNKFAGSQAE RSSKAQADAE
     AKKVADKLKG TKLSDGGQKK EQKKQSGGSK SKNAEVDVTV AKLDIRVGLI RKAQKHPDAD
     SLYVEEIDVG EEAPRTVVSG LVKFIPLEEM QNRKVCVLCN LKPVAMRGIK SHAMVLAASN
     EDHTKVELVE PPESAAVGER VTFAGYSGEP EASLNAKSKT WEKLSADLHS NGELVACYKD
     VPFTTSAGVC KVKSIASGEI R