SYK_RICCN
ID SYK_RICCN Reviewed; 522 AA.
AC Q92IB5;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00177};
DE EC=6.1.1.6 {ECO:0000255|HAMAP-Rule:MF_00177};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00177};
DE Short=LysRS {ECO:0000255|HAMAP-Rule:MF_00177};
GN Name=lysS {ECO:0000255|HAMAP-Rule:MF_00177}; OrderedLocusNames=RC0505;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-
CC tRNA(Lys); Xref=Rhea:RHEA:20792, Rhea:RHEA-COMP:9696, Rhea:RHEA-
CC COMP:9697, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78529, ChEBI:CHEBI:456215; EC=6.1.1.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00177};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00177}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00177}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL03043.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006914; AAL03043.1; ALT_INIT; Genomic_DNA.
DR PIR; A97763; A97763.
DR RefSeq; WP_041471717.1; NC_003103.1.
DR AlphaFoldDB; Q92IB5; -.
DR SMR; Q92IB5; -.
DR PRIDE; Q92IB5; -.
DR EnsemblBacteria; AAL03043; AAL03043; RC0505.
DR KEGG; rco:RC0505; -.
DR PATRIC; fig|272944.4.peg.578; -.
DR HOGENOM; CLU_025562_2_0_5; -.
DR OMA; DWPMRWA; -.
DR Proteomes; UP000000816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR InterPro; IPR002904; Lys-tRNA-ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR37940; PTHR37940; 1.
DR Pfam; PF01921; tRNA-synt_1f; 1.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00467; lysS_arch; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..522
FT /note="Lysine--tRNA ligase"
FT /id="PRO_0000152742"
FT MOTIF 44..52
FT /note="'HIGH' region"
FT MOTIF 290..294
FT /note="'KMSKS' region"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00177"
SQ SEQUENCE 522 AA; 59998 MW; AE754C91EEF7825C CRC64;
MSEIWEDAIK SNAWPFVEAK KILDSLNGQI PEKGYVLFET GYGPSGLPHI GTFGENARMV
MVQKAFEQLS DIPTKLICFS DDMDGLRKVP SNIPNPEMVA QYMDMPLTSI PDTFGECESY
GHYMNAKLRS FLDKFGFEYE FYSSTNCYKA GMFDAMLIMV LEKYDEIMEL MLPTFREERK
ATYSPFMPIC PKTGKVLQVP IEKWDAKAGT VTYKDKAGNY IEVPVTGGHC KLQWKPDFGM
RWAALKVDYE MYGKDHLANA RLYSEICRIL GGKPPVQLCY ELFLDENGKK ISKSKGNSIS
IDDWLKYAPV ESMALFMYQN PTRAKRLFFD VIPKNVDEYI TFNQKYHLEE DRAKRFANPV
YHIHHGNVPK IETFGITYSL LLNLTSVCNP SDKSVLWGFI SKYEPKATPN TNPYLDHLAE
FAIRYYNDFI KAHKLYLSPS EKHKVILQDI LDMLSDIADQ TEAEAIQKAI YDIGMKAGYE
NLRDYFKDLY QILLGQNEGP RFGTFIKLYG VQEMKKLVEG QL