SYMC_DICDI
ID SYMC_DICDI Reviewed; 736 AA.
AC Q54X95;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable methionine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=metS; ORFNames=DDB_G0279113;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000027; EAL67895.1; -; Genomic_DNA.
DR RefSeq; XP_641872.1; XM_636780.1.
DR AlphaFoldDB; Q54X95; -.
DR SMR; Q54X95; -.
DR STRING; 44689.DDB0231297; -.
DR PaxDb; Q54X95; -.
DR EnsemblProtists; EAL67895; EAL67895; DDB_G0279113.
DR GeneID; 8621878; -.
DR KEGG; ddi:DDB_G0279113; -.
DR dictyBase; DDB_G0279113; metS.
DR eggNOG; KOG1247; Eukaryota.
DR eggNOG; KOG2241; Eukaryota.
DR HOGENOM; CLU_009710_1_0_1; -.
DR InParanoid; Q54X95; -.
DR OMA; YMRMAGH; -.
DR PhylomeDB; Q54X95; -.
DR PRO; PR:Q54X95; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0017102; C:methionyl glutamyl tRNA synthetase complex; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; ISS:dictyBase.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; ISS:dictyBase.
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 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..736
FT /note="Probable methionine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000328567"
FT DOMAIN 573..680
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT MOTIF 25..35
FT /note="'HIGH' region"
FT /evidence="ECO:0000250"
FT MOTIF 346..350
FT /note="'KMSKS' region"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 736 AA; 83132 MW; 058DFE76A1857801 CRC64;
MSKPSNTPPL PKDGERNILI TSALPYVNNV PHLGNIIGCV LSADVYARYC RLKNYNCIYI
CGTDEYGTAT ETKALSEGCT PKEICDKYHE IHKEIYEWFN ISFDKFGRTS TNSQTEIAQD
IFNKIKDNGY TLTQEIEQLY CEQTCKMFLA DRFVEGTCPH CKFEDARGDQ CDGCSKLLNP
TELINPRCKV CSKPPVIKST KHIFIDLPQL QQQVDQFVET NSKGGNWSEN SIAITNTWVK
GELKPRCITR DLKWGTPVPM EEFKDKVFYV WFDAPIGYIS ITAEYTNEWE KWWKNPENVK
LVQFMGKDNV PFHTVIFPAS LIGSKDNYTL LNNLSTTEFL NYETGKFSKS RNTGVFGDGA
KATGIPSEVW RFYLLNNRPE SSDSIFSWDD FNFKNNELLN NFGNLVNRVL KMLNTNAAFN
GVVPKIGELN EVDKKLVQEV DEHLVQYFQK LEEISLKEGL KIAMSISKLG NTYMQDNKPW
DLSGKDNERC GQVLAILINL IKLLSTLLEP YIPSLTDKVH QQLNVEPTKY STHFDINAIP
AGHEISKEIL PLVKKIEADD LKKWRTKFSG IGPEFPIDMK IATVLEVNDH PSAENLYVIK
LSLGGDQTKT AVSGIKANFE KSQLIGKKLA VVLNLKPSKF KGVLSEAMIL VADDGQATKE
SLSFLVPSNP QSIEAGSKIA GKGMSIKPKP TIDYQKEFLH YDLTCIDKII SYNKSQLFIN
QNEPLVSEKI GNGKVR