ID A0A1H8WUU4_9PROT Unreviewed; 533 AA.
AC A0A1H8WUU4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 ORFNames=SAMN02990966_04972 {ECO:0000313|EMBL:SEP31207.1};
OS Rhodospirillales bacterium URHD0017.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales.
OX NCBI_TaxID=1380357 {ECO:0000313|EMBL:SEP31207.1, ECO:0000313|Proteomes:UP000198826};
RN [1] {ECO:0000313|EMBL:SEP31207.1, ECO:0000313|Proteomes:UP000198826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URHD0017 {ECO:0000313|EMBL:SEP31207.1,
RC ECO:0000313|Proteomes:UP000198826};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FODP01000012; SEP31207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8WUU4; -.
DR STRING; 1380357.SAMN02990966_04972; -.
DR OrthoDB; 9803151at2; -.
DR Proteomes; UP000198826; Unassembled WGS sequence.
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; HUPs; 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 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 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}.
FT MOTIF 45..53
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT MOTIF 292..296
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ SEQUENCE 533 AA; 59442 MW; 58A0C36030F2E973 CRC64;
MSQFDRSLAE AARAWPFEEA RKLVARTGGK APAKGYVLFE TGYGPSGLPH IGTFGEVVRT
TMVRQAFRRL SDLPTRLFCF SDDMDGLRKV PDNVPNKEML AANLGKPLTS VPDPFSNEHP
SFGAANNARL RAFLDSFGFE YEFQSATDWY KSGRFDAMLL AMLQHYDEVQ AVMLPTLGEE
RRATYSIFLP ISPKTGRVLQ VPVIKTDAAA GTIVYRDEDG TLVETPVTGG NVKLQWKADW
AGRWFALGVD YEMYGKDLIP SAELSARIVK ILGGTPPEGF NFELFLDEEG KKISKSKGNG
LSVEEWLRYA PPESLALYMQ QQPRRAKRLY FDVIPRAVDD YLAAIEKLPA EEPAKALENA
AWHIHDGEAP TNSAAGVNFG MLLNLASVAH TDSKDVLWQY LRRYVPGATP ENAPYLDRLL
TGAVAYYQDF VKASKKFRLP AGKEREALQD LADTLGKLPE DSTAEFIQNE VYEAGKRHFA
QAELRQWFKT LYEVLLGSEQ GPRMGAFIKL YGRDNVVKLI ERALAGEDLS RAA
//
