(data stored in ACNUC7421 zone)

SWISSPROT: C7PYW7_CATAD

ID   C7PYW7_CATAD            Unreviewed;       605 AA.
AC   C7PYW7;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
DE   RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00098};
DE            EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_00098};
DE   AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00098};
DE            Short=MetRS {ECO:0000256|HAMAP-Rule:MF_00098};
GN   Name=metG {ECO:0000256|HAMAP-Rule:MF_00098};
GN   OrderedLocusNames=Caci_0586 {ECO:0000313|EMBL:ACU69523.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69523.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69523.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(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_00098}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP +
CC       diphosphate + L-methionyl-tRNA(Met). {ECO:0000256|HAMAP-
CC       Rule:MF_00098, ECO:0000256|SAAS:SAAS00337330}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00098};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00098};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00098}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00098,
CC       ECO:0000256|SAAS:SAAS00147475}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. MetG type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00098}.
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DR   EMBL; CP001700; ACU69523.1; -; Genomic_DNA.
DR   RefSeq; WP_012784818.1; NC_013131.1.
DR   ProteinModelPortal; C7PYW7; -.
DR   STRING; 479433.Caci_0586; -.
DR   EnsemblBacteria; ACU69523; ACU69523; Caci_0586.
DR   KEGG; cai:Caci_0586; -.
DR   eggNOG; ENOG4105CKH; Bacteria.
DR   eggNOG; COG0143; LUCA.
DR   HOGENOM; HOG000200402; -.
DR   KO; K01874; -.
DR   OMA; YMRMAGH; -.
DR   OrthoDB; POG091H0269; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 1.10.730.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00098; Met_tRNA_synth_type1; 1.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 2.
DR   SUPFAM; SSF57770; SSF57770; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7PYW7.
DR   SWISS-2DPAGE; C7PYW7.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00098,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00001319,
KW   ECO:0000313|EMBL:ACU69523.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00098,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00001334};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00098,
KW   ECO:0000256|SAAS:SAAS00415937};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00098,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00415959};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00098};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00098,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00001322};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00098,
KW   ECO:0000256|RuleBase:RU363039, ECO:0000256|SAAS:SAAS00001332};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00098}.
FT   DOMAIN        9    418       tRNA-synt_1g. {ECO:0000259|Pfam:PF09334}.
FT   DOMAIN      451    539       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   MOTIF        15     25       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00098}.
FT   MOTIF       355    359       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00098}.
FT   METAL       147    147       Zinc. {ECO:0000256|HAMAP-Rule:MF_00098}.
FT   METAL       150    150       Zinc. {ECO:0000256|HAMAP-Rule:MF_00098}.
FT   METAL       160    160       Zinc. {ECO:0000256|HAMAP-Rule:MF_00098}.
FT   METAL       163    163       Zinc. {ECO:0000256|HAMAP-Rule:MF_00098}.
FT   BINDING     358    358       ATP. {ECO:0000256|HAMAP-Rule:MF_00098}.
SQ   SEQUENCE   605 AA;  67198 MW;  2785E68000065A04 CRC64;
     MPSTQRTILT AVAWPYANGP RHIGHVSGFG VPSDVFSRYQ RMAGNRVLMV SGTDEHGTPI
     LVQADKEGVT ARELADRYNR VIAEDLQSLG LAYDLFTRTT TRNHYAVVQE IFKGLYDNGY
     IFPKTTMGAI SPSTGRTLPD RYIEGTCPIC GYDGARGDQC DNCGNQLDPD RLIDPRSRIN
     GETPKFIETE QFFLDLPAFA SVLGGWLQQQ KTWRPNVLKF SLNLLDDLQP RAISRDLDWG
     VPVPLEGWVD RPDKKLYVWF DAVVGYLSAS VEWARRTGDP DAWRAFWQTG PNGEAPDAYY
     FMGKDNIVFH SEIWPAMLLG YDGRGEKNGK PGSLGALNLP HEVVSSEFLT MEGRKFSSSR
     AVVIYVRDFL SRYDADALRY YITAAGPETQ DTDFTWSEFL RRNNDELVAG WGNLVNRAIS
     MAAKNLGQIP AAKDLTAEDE ALLATSRGAF AVVGDLLDRC RFKAALAEAM RLVAEANKYV
     SDHEPWKLAK TDPERMATVL HVTLQVVDDA KTLLTPFLPF SSEKVFHLLG GEGTWSAMPE
     LREVEDLDGG PGYPVLTGDY EQALARWEST PIEAGRPLAP PTPIFKKLDP SIVDEELARL
     GGEAA
//

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