(data stored in SCRATCH zone)

SWISSPROT: A0LEK4_SYNFM

ID   A0LEK4_SYNFM            Unreviewed;       636 AA.
AC   A0LEK4;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 101.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01228};
DE            EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_01228};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228};
DE            Short=MetRS {ECO:0000256|HAMAP-Rule:MF_01228};
GN   Name=metG {ECO:0000256|HAMAP-Rule:MF_01228};
GN   OrderedLocusNames=Sfum_0154 {ECO:0000313|EMBL:ABK15856.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15856.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15856.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Is required not only for elongation of protein synthesis
CC       but also for the initiation of all mRNA translation through
CC       initiator tRNA(fMet) aminoacylation. {ECO:0000256|HAMAP-
CC       Rule:MF_01228, ECO:0000256|SAAS:SAAS00621504}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01228, ECO:0000256|SAAS:SAAS01159305};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01228};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01228};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01228,
CC       ECO:0000256|SAAS:SAAS00621513}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228,
CC       ECO:0000256|SAAS:SAAS00578164}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. MetG type 2A subfamily. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01228}.
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DR   EMBL; CP000478; ABK15856.1; -; Genomic_DNA.
DR   RefSeq; WP_011697029.1; NC_008554.1.
DR   STRING; 335543.Sfum_0154; -.
DR   EnsemblBacteria; ABK15856; ABK15856; Sfum_0154.
DR   KEGG; sfu:Sfum_0154; -.
DR   eggNOG; ENOG4105CKH; Bacteria.
DR   eggNOG; COG0073; LUCA.
DR   eggNOG; COG0143; LUCA.
DR   HOGENOM; HOG000200401; -.
DR   KO; K01874; -.
DR   OMA; TYVWFDA; -.
DR   OrthoDB; 761140at2; -.
DR   BioCyc; SFUM335543:G1G7I-158-MONOMER; -.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR004495; Met-tRNA-synth_bsu_C.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
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   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 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   TIGRFAMs; TIGR00398; metG; 1.
DR   TIGRFAMs; TIGR00399; metG_C_term; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LEK4.
DR   SWISS-2DPAGE; A0LEK4.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159323,
KW   ECO:0000313|EMBL:ABK15856.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159304};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|SAAS:SAAS00104184};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159317,
KW   ECO:0000313|EMBL:ABK15856.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01228};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159262};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159279};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01228, ECO:0000256|PROSITE-
KW   ProRule:PRU00209, ECO:0000256|SAAS:SAAS00104020};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01228, ECO:0000256|PROSITE-
KW   ProRule:PRU00209, ECO:0000256|SAAS:SAAS00469761};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   DOMAIN      537    636       TRNA-binding. {ECO:0000259|PROSITE:
FT                                PS50886}.
FT   MOTIF        11     21       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_01228}.
FT   MOTIF       295    299       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_01228}.
FT   METAL       126    126       Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   METAL       129    129       Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   METAL       143    143       Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   METAL       146    146       Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}.
SQ   SEQUENCE   636 AA;  72716 MW;  0C344D2D0119DD81 CRC64;
     MNRFYITTPI YYVNAEPHIG HAYTTIVADV MNRFHKLMGF GTFFLTGTDE HGDKIVQAAA
     DAGTAPKEYA DRISGMFKEA WSKLNISNDH FIRTTDPEHI RVVQHILQQV YDSGDITFST
     YRGLYCVGCE RFYTERELVD GKCPDHDKEP IEREEANYFF RMSKYQNWLI EHIESNPDFI
     RPERYRNEVL AFLREPLEDL CISRPKERLA WGITLPFDER YVTYVWFDAL INYVSALGYP
     DGPLFGEFWP VVQHTIAKDI LKPHGIYWPT IIKAAGFPVY RHLNVHGYWK INEGKMSKSR
     GTVVRPLDMI PLYGLDAFRY FLLREMVFGL DANFSEDALV QRLNSDLAND LGNLFSRTLA
     MTLKYFDGKV PPFGSEPDDM DRDLISRVER TVAEFREELP VFCFHKALMS IWECLNAANK
     YIDTVGPWGL AKDPSRHGRL ETVIRILLEL NKTMAVLISP FMPSTSEKML ERLGVVKRSI
     DLRLAEDGRW GTLVEGTPVS KGDALFPRID IKEERKPAVP RQPEKRQPSL PLLDLEAFKQ
     VDLRTGVVKH AERVPKSEKL LRLLVDIGEE RQVVAGIAQS YSPEELTGKQ VVVVANLKPA
     KLMGIESHGM VLAVRDGDAL RLLTTEKPVP AGLRVS
//

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