(data stored in ACNUC7421 zone)

SWISSPROT: C8W2R3_DESAS

ID   C8W2R3_DESAS            Unreviewed;       533 AA.
AC   C8W2R3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 85.
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=Dtox_0106 {ECO:0000313|EMBL:ACV61069.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61069.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61069.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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}.
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: Monomer. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228}.
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; CP001720; ACV61069.1; -; Genomic_DNA.
DR   RefSeq; WP_012813521.1; NC_013216.1.
DR   STRING; 485916.Dtox_0106; -.
DR   EnsemblBacteria; ACV61069; ACV61069; Dtox_0106.
DR   KEGG; dae:Dtox_0106; -.
DR   eggNOG; ENOG4105CKH; Bacteria.
DR   eggNOG; COG0143; LUCA.
DR   HOGENOM; HOG000200401; -.
DR   KO; K01874; -.
DR   OMA; TYVWFDA; -.
DR   OrthoDB; 761140at2; -.
DR   BioCyc; DACE485916:G1GFV-113-MONOMER; -.
DR   Proteomes; UP000002217; 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:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; 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; IPR014729; Rossmann-like_a/b/a_fold.
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   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W2R3.
DR   SWISS-2DPAGE; C8W2R3.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159323,
KW   ECO:0000313|EMBL:ACV61069.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159304};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01228};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01228,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS01159317};
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:UP000002217};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   DOMAIN        3    136       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      150    361       tRNA-synt_1g. {ECO:0000259|Pfam:PF09334}.
FT   DOMAIN      398    499       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF        13     23       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_01228}.
FT   MOTIF       298    302       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_01228}.
FT   METAL       128    128       Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   METAL       131    131       Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   METAL       146    146       Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}.
FT   METAL       149    149       Zinc. {ECO:0000256|HAMAP-Rule:MF_01228}.
SQ   SEQUENCE   533 AA;  61081 MW;  21BCD7AAE4ADDD28 CRC64;
     MSKPTFYIST PIYYPSDKLH IGHAYTTVAA DSFARYKRMK GYDVWFLTGS DEHGQKIERT
     AKEKGQSPLE YVDQIVAGFK SLWKKLDVSY DDFIRTTQER HKKVVQDIFQ KLYDQGDIYK
     AQYEGHYCTP CETFWTEYQL DADGNCPDCG RPVEILQEES YFFKMSKYAD EILKYIEDNA
     EFIQPNSRRN EMVSFIKSGL ADLCVSRTTF DWGIQVPFDP KHVIYVWVDA LTNYISALGY
     GTGDDSLFRK YWPADMHLVG KDIVRFHTII WPIMLMAAGI ELPKQVLGHG WLLLDSGKMS
     KSKGNVVDPL ELCDKYGVDA IRYYLLRELP LGSDGYYSEE ALVNRINIDL ANDLGNLISR
     STSMIVKFSK GVLEEPETPR EPVLLEQYLG SEEAPAEDRD LISLALKTKY EVDDLMERRD
     ISGALAAVWR LVGRANKYVE ETSPWSLAKD PELRGRLATV LYNLAETIRF VTVMVTPFMP
     NFPSMVWQQL AIGNQPELHV WEALEWGNLP AGTRVVKGDA IFPRIDLKTL EKE
//

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