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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
 
 
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