UniProt: A0A1J6IKM9

Database: UniProt
Entry: A0A1J6IKM9_NICAT

LinkDB:  A0A1J6IKM9_NICAT 
Original site:  A0A1J6IKM9_NICAT

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (2)   
All databases (28)   

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ID   A0A1J6IKM9_NICAT        Unreviewed;       805 AA.
AC   A0A1J6IKM9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 31.
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   ORFNames=A4A49_38656 {ECO:0000313|EMBL:OIS99442.1};
OS   Nicotiana attenuata (Coyote tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=49451 {ECO:0000313|EMBL:OIS99442.1, ECO:0000313|Proteomes:UP000187609};
RN   [1] {ECO:0000313|EMBL:OIS99442.1, ECO:0000313|Proteomes:UP000187609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UT {ECO:0000313|Proteomes:UP000187609};
RC   TISSUE=Leaves {ECO:0000313|EMBL:OIS99442.1};
RA   Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA   Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA   Timmermann B., Baldwin I.T.;
RT   "The genome of Nicotiana attenuata.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OIS99442.1}.
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DR   EMBL; MJEQ01037190; OIS99442.1; -; Genomic_DNA.
DR   RefSeq; XP_019252161.1; XM_019396616.1.
DR   AlphaFoldDB; A0A1J6IKM9; -.
DR   STRING; 49451.A0A1J6IKM9; -.
DR   EnsemblPlants; OIS99442; OIS99442; A4A49_38656.
DR   GeneID; 109231072; -.
DR   Gramene; OIS99442; OIS99442; A4A49_38656.
DR   KEGG; nau:109231072; -.
DR   OMA; YMRMAGH; -.
DR   OrthoDB; 1341752at2759; -.
DR   Proteomes; UP000187609; Chromosome 8.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP 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-UniRule.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
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:UP000187609};
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          643..746
FT                   /note="TRNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50886"
FT   REGION          608..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..632
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   805 AA;  90602 MW;  21C25DB8CCB4AD2C CRC64;
     MGENCKTFPK LPIPGKRNIL ITSALPYVNN VPHLGNIIGC VLSADVFARY CRLRGYNAIY
     MCGTDEYGTA TETKALEENC TPKEICDEYH AIHKEVYKWF DISFDEFGRT STPQQTEVCQ
     AIFKKLFENN WLSENTMQQL YCDTCKKFLA DRLVEGNCPT PGCNYDSARG DQCEKCGKLL
     NPTELMEPKC KVCRNTPCIR DTDHLFLELP LLKDRLEAYV NNMSVAGGWS QNAIYTTHAW
     LREGLKPRCI TRDLKWGVPV PHEKYKDKVF YVWFDAPIGY VSITSCYTTE WEKWWKNPDD
     VELYQFMGKD NVPFHTVIFP STLLGTGENW TLMKTISVTE YLNYEAGKFS KSKGIGVFGN
     DAKDTNIPVE VWRYYLLTNR PEVSDTLFTW ADLQAKLNSE LLSNLGNFVN RVLSFIAKDS
     ASGYGSIIPD VEGAESHPLT KALGEKVGNY VEQYIEAMEK VKLKQGLKVA MSVSGEGNGY
     LQESQFWKLY KEDRRSCSIV MRTACGLVYL LACLLEPFMP SFSREVLKQL NLPPETQLSL
     ADEKGDVANS KRPWNIIPAG HKIGTPAPLF KELKDEEVEF YREKFAGSQA DRADRALKAE
     TDAKKMAEQL NKTKISDGNK KERAKKSSET KSKAPATVEG EISISRLDIR VGLITKAQKH
     PNADSLYVEE IDVGEALPRT VVSGLVNYIP LEEMQNRKVC VLCNLKPVSM RGIKSQAMVL
     AASNSDHTKV ELVEPPKDAA IGERVTFPGF DGKPDDVLNS KKKIWETVQL DLHTNKELVA
     CYKDLPFTTS SGICKVASIS EGSIR
//

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