ID A9A261_NITMS Unreviewed; 529 AA.
AC A9A261;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00177};
DE EC=6.1.1.6 {ECO:0000256|HAMAP-Rule:MF_00177};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00177};
DE Short=LysRS {ECO:0000256|HAMAP-Rule:MF_00177};
GN Name=lysS {ECO:0000256|HAMAP-Rule:MF_00177};
GN OrderedLocusNames=Nmar_0578 {ECO:0000313|EMBL:ABX12474.1};
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=436308 {ECO:0000313|EMBL:ABX12474.1, ECO:0000313|Proteomes:UP000000792};
RN [1] {ECO:0000313|EMBL:ABX12474.1, ECO:0000313|Proteomes:UP000000792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1 {ECO:0000313|EMBL:ABX12474.1,
RC ECO:0000313|Proteomes:UP000000792};
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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:0000256|ARBA:ARBA00000204, ECO:0000256|HAMAP-
CC Rule:MF_00177};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00177}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00177}.
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DR EMBL; CP000866; ABX12474.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A261; -.
DR STRING; 436308.Nmar_0578; -.
DR EnsemblBacteria; ABX12474; ABX12474; Nmar_0578.
DR KEGG; nmr:Nmar_0578; -.
DR eggNOG; arCOG00485; Archaea.
DR HOGENOM; CLU_025562_1_0_2; -.
DR InParanoid; A9A261; -.
DR OrthoDB; 6838at2157; -.
DR PhylomeDB; A9A261; -.
DR Proteomes; UP000000792; 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; 1.10.10.770; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00177; Lys_tRNA_synth_class1; 1.
DR InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
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 NCBIfam; TIGR00467; lysS_arch; 1.
DR PANTHER; PTHR37940; LYSINE--TRNA LIGASE; 1.
DR PANTHER; PTHR37940:SF1; LYSINE--TRNA LIGASE; 1.
DR Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF01921; tRNA-synt_1f; 1.
DR SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00177};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00177};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00177};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00177};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00177};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00177}; Reference proteome {ECO:0000313|Proteomes:UP000000792}.
FT DOMAIN 436..525
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
FT MOTIF 42..50
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 298..302
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT BINDING 301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 529 AA; 59977 MW; BEBEDA5167C743A9 CRC64;
MSEQEIIGKG TWIDKLAYEL LEREKALGRN TDVLRVESGL GASGIPHIGS LGDAVRAYGV
KLALENLGYK SELIAYSDDL DGLRKIPEGM KDFGLEEHIA KPVSLIPDPY GEHDSYGMHM
SSILLEGLDE VGIKYEFRRA KDTYKQGLLK DQIHTILQNS TKIGDKIAEL VGQEKYQKYL
PYFPVCANCN RLYTAEAIEY IADEKKVKYR CHDAEIGGKM VKGCGYEGEA DITKDLGKLA
WKVEFAARWS AFDIRFEAYG KDIMDSVKVN DWVADEILQF PHPHHVKYEM FLDKGGKKIS
KSLGNVLTAQ RWMEFGSPKS ILLLLYKRIT GARELGLEDI PSLMSEYNEL EDIFFGRIKV
DNPAKLTKSK GLYEYVNLLN PPKQASTHVN YRLLIELAKI FKENRNERVM KKLLDYGVIK
NPEPEIEKLI DLAGNYSDEF DEQEKTQIDL DETSKKALKI LSEALGADEE PEDIQNTIYQ
IAKSNDVQPK DFFKILYQII LGTSRGPKIG PFISDIGRKQ VAKTISEYT
//
