ID G0QIJ8_NANS0 Unreviewed; 442 AA.
AC G0QIJ8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Lysine--tRNA ligase {ECO:0000256|ARBA:ARBA00015745};
DE EC=6.1.1.6 {ECO:0000256|ARBA:ARBA00013166};
DE AltName: Full=Lysyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030563};
GN ORFNames=J07AB43_10670 {ECO:0000313|EMBL:EGQ43078.1};
OS Nanosalina sp. (strain J07AB43).
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Nanohaloarchaea;
OC Nanosalina.
OX NCBI_TaxID=889948 {ECO:0000313|EMBL:EGQ43078.1, ECO:0000313|Proteomes:UP000009379};
RN [1] {ECO:0000313|EMBL:EGQ43078.1, ECO:0000313|Proteomes:UP000009379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07AB43 {ECO:0000313|Proteomes:UP000009379};
RA Narasingarao P., Podell S., Ugalde J.A., Brochier-Armanet C., Emerson J.B.,
RA Brocks J.J., Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "De novo metagenomic assembly reveals abundant novel major lineage of
RT Archaea in hypersaline microbial communities.";
RL ISME J. 0:0-0(2011).
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; GL982576; EGQ43078.1; -; Genomic_DNA.
DR AlphaFoldDB; G0QIJ8; -.
DR HOGENOM; CLU_025562_1_0_2; -.
DR Proteomes; UP000009379; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 1.10.10.770; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 6.10.20.10; Lysine tRNA ligase, stem contact fold domain; 1.
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; IPR042078; Lys-tRNA-ligase_SC_fold.
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; 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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:EGQ43078.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000009379}.
FT REGION 401..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 51988 MW; A37EAF9D4A9C8E4E CRC64;
MQYLVLRGSK SMDERPVFWS DQLAFGTRKK FEDEEEYVCA SGVSPSGVVH AGNFREIITT
DFVVKSLKHQ GEDVKFIYSW DDYDRFRKVP EGVPESFEKH IGKPLVEVPD PQGCHESYAK
HYEEKLENQL EDMHVDINFI RQAENFRNGE YADLIKKGLE KRSEIKQILD KYRKEPLEEP
YYPVHVYCTE CGKDFTEVKS WDGSYMLEYH CNECGEQREI NFKQEGNVKP PWRIDWPMRW
KYEQVNFEPA GKEHSAAGGS RDTGNELSEK IYDKEPPVHQ MYEFVTKDGS KISSSQGEGV
FTLSELKDIY SPEIIRFLFS ETKPNKAFEI PFESEEVIQI YDRFDRYEED YFEDSEDDKD
TRHRERVYEQ AAVEVPENQP VRIPFKHAAF VAQTVPEEEW KTNGVKSLKR TGHAPDSLDR
DDKNRVVSRL ERAKEWARKL RT
//
