ID K4A5Z4_SETIT Unreviewed; 807 AA.
AC K4A5Z4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=methionine--tRNA ligase {ECO:0000256|ARBA:ARBA00012838};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030904};
GN Name=101770288 {ECO:0000313|EnsemblPlants:KQK91949};
GN ORFNames=SETIT_9G490200v2 {ECO:0000313|EMBL:RCV45893.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV45893.1};
RN [1] {ECO:0000313|EMBL:RCV45893.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK91949,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV45893.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV45893.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV45893.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK91949}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK91949};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363039}.
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DR EMBL; AGNK02006085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003536; RCV45893.1; -; Genomic_DNA.
DR RefSeq; XP_004985187.1; XM_004985130.2.
DR AlphaFoldDB; K4A5Z4; -.
DR STRING; 4555.K4A5Z4; -.
DR EnsemblPlants; KQK91949; KQK91949; SETIT_034298mg.
DR GeneID; 101770288; -.
DR Gramene; KQK91949; KQK91949; SETIT_034298mg.
DR KEGG; sita:101770288; -.
DR eggNOG; KOG1247; Eukaryota.
DR eggNOG; KOG2241; Eukaryota.
DR HOGENOM; CLU_009710_1_0_1; -.
DR InParanoid; K4A5Z4; -.
DR OMA; HLNTTEY; -.
DR OrthoDB; 1341752at2759; -.
DR Proteomes; UP000004995; Chromosome IX.
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-UniRule.
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 CDD; cd02799; tRNA_bind_EMAP-II_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; 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 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|RuleBase:RU363039};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363039};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363039};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039};
KW Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00209};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00209}.
FT DOMAIN 645..748
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT REGION 613..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 89747 MW; 2DD639A934906956 CRC64;
MASSSSSPPP PPPPPKLPIP GRRNILITSA LPYVNNVPHL GNIIGCVLSA DVFARYCRLR
GYNAIYICGT DEYGTATETK AMEEKCTPKE ICDKYHAIHD EVYKWFNIKF DKFGRTSSPE
QTEVCHAIFH KLMENNWLTE NTMQQLYCDT CQRFLADRLV EGTCPNKVCN ASARGDQCES
CSTLLNPTEL IDPKCKVCKN TPRIRDTDHL FLELPLLKDK LVNYINETSV AGLWSQNAIQ
ATNAWLKEGL KPRCITRDLK WGVPVPHEKY KDKVFYVWFD APIGYVSITA SYTPDWEKWW
KDPDNVELFQ FMGKDNVPFH TIMFPSTLLG TGEKWTMMKT ISVTEYLNYE AGKFSKSKGI
GVFGNDARDT NLPPEVWRYY LLMNRPEASD TLFTWADLQA KLNSELLNNL GNFINRVLSF
VAKPAGAGYD SIVPDAPNAE SHPLTKALAE KTSKWVEQYL DAMEKVKLKQ GLKSAMAISS
DGNAYLQESQ FWKLYKEDSA ACAIVMKTSV GLVYLLACLL EPFMPSFSEE VLRQLNLSPE
ENLSFSEEKG EIAKAKSPWD FVPAGHTIGK PAPLFKELRD EDVALHREKY AGSQAERSSK
AAADAEANKV ANQLKGTKLS GGGPKKEQKK QSGGSKSKTA EADITVAKLD IRVGLIRKAE
KHPDADSLYV EEIDVGEDAP RTVVSGLVKF IPLEEMQNRK VCVLCNLKPV AMRGIKSHAM
VLAASNEDHT KVELVEPPES AAVGERVTFA GYSGEPEASL SGKSKTWEKL AAELHSNGEL
VACYKDVPFT TSAGICKVKT IANGEIR
//
