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Database: UniProt/TrEMBL
Entry: F4GY48_CELFA
LinkDB: F4GY48_CELFA
Original site: F4GY48_CELFA 
ID   F4GY48_CELFA            Unreviewed;       511 AA.
AC   F4GY48;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   26-NOV-2014, entry version 24.
DE   RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
DE            EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
DE   AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252};
GN   Name=lysS {ECO:0000256|HAMAP-Rule:MF_00252};
GN   OrderedLocusNames=Celf_0576 {ECO:0000313|EMBL:AEE44716.1};
OS   Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513
OS   / NCIMB 8980 / NCTC 7547).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Cellulomonadaceae; Cellulomonas.
OX   NCBI_TaxID=590998 {ECO:0000313|EMBL:AEE44716.1, ECO:0000313|Proteomes:UP000008460};
RN   [1] {ECO:0000313|EMBL:AEE44716.1, ECO:0000313|Proteomes:UP000008460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 /
RC   NCTC 7547 {ECO:0000313|Proteomes:UP000008460};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I.,
RA   Mead D., Brumm P., Woyke T.;
RT   "Complete sequence of Cellulomonas fimi ATCC 484.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate
CC       + L-lysyl-tRNA(Lys). {ECO:0000256|HAMAP-Rule:MF_00252,
CC       ECO:0000256|RuleBase:RU000336, ECO:0000256|SAAS:SAAS00032979}.
CC   -!- COFACTOR:
CC       Note=Binds 3 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00252, ECO:0000256|RuleBase:RU000336};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00252,
CC       ECO:0000256|RuleBase:RU003746}.
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DR   EMBL; CP002666; AEE44716.1; -; Genomic_DNA.
DR   RefSeq; YP_004452103.1; NC_015514.1.
DR   EnsemblBacteria; AEE44716; AEE44716; Celf_0576.
DR   GeneID; 10591340; -.
DR   KEGG; cfi:Celf_0576; -.
DR   PATRIC; 54612016; VBICelFim18861_0573.
DR   KO; K04567; -.
DR   OMA; NEDADRS; -.
DR   BioCyc; CFIM590998:GJFK-580-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00252; Lys_tRNA_synth_class2; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR002313; Lys-tRNA-ligase_II.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   PANTHER; PTHR22594; PTHR22594; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00499; lysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00032854};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00032774};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008460};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00252};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00032825};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|RuleBase:RU000336};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|RuleBase:RU000336};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00033004};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00252,
KW   ECO:0000256|SAAS:SAAS00032795};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008460}.
FT   METAL       422    422       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
FT   METAL       429    429       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
FT   METAL       429    429       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00252}.
SQ   SEQUENCE   511 AA;  56709 MW;  C352FFBA2FE78409 CRC64;
     MTAAPDETIA PAPSAPADDT PEQIQVRRAK RERLLAEGTD AYPVGLPRTH TIAQVRAEHP
     DLEPGTETQD EVGVAGRVVF LRNTGKLCFA MLQDGEGNRL QAMLSLREVG EERLAAFKTD
     VDLGDHVFVH GRVVASRTGE LSVFADAWAM AAKAIRPLPN VYEGAELSEE ARVRQRYVDL
     IVNQRSRDMV RTRAAVLRSV RDNLHRRGFL EVETPMLQVR PEGAAARQFE THMNAFDIPL
     FLRIAPELFL KRAAVGGVER VFEINRNFRN EGVDATHSPE FAMLEAYEAY GDYDTIAELT
     QDLVQTAARD AFGSTTVTLA DGSEYDLGGE WERLPMYDSL SAALGEEITH DTTDEVLLAL
     LDKAGVELAP GQRNHGKMVE ELWEHHVGHH LTAPTFVRDF PVETSPLVRD HRHKAGLVEK
     WDLYVRGMEL ATGYSELVDP VIQRQRFEAQ ALLAARGDDD AMRIDEDFLT AMEFAMPPSG
     GMGMGIDRLL IALTGLGIRE TILFPLVKPQ A
//
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