GenomeNet

Database: UniProt
Entry: A0A3R9ZL06_9RICK
LinkDB: A0A3R9ZL06_9RICK
Original site: A0A3R9ZL06_9RICK 
ID   A0A3R9ZL06_9RICK        Unreviewed;       518 AA.
AC   A0A3R9ZL06;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=EIC27_03845 {ECO:0000313|EMBL:RST66114.1};
OS   Candidatus Aquarickettsia rohweri.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Candidatus Midichloriaceae; Aquarickettsia.
OX   NCBI_TaxID=2602574 {ECO:0000313|EMBL:RST66114.1, ECO:0000313|Proteomes:UP000279470};
RN   [1] {ECO:0000313|Proteomes:UP000279470}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=a_cerv_44 {ECO:0000313|Proteomes:UP000279470};
RA   Klinges J.G., Rosales S.M., Mcminds R., Shaver E.C., Shantz A.,
RA   Peters E.C., Burkepile D.E., Silliman B.R., Vega Thurber R.L.;
RT   "Phylogenetic, genomic, and biogeographic characterization of a novel and
RT   ubiquitous marine invertebrate-associated Rickettsiales parasite,
RT   Candidatus Marinoinvertebrata rohwerii, gen. nov., sp. nov.";
RL   Submitted (NOV-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RST66114.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; RXFM01000046; RST66114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R9ZL06; -.
DR   OrthoDB; 9803151at2; -.
DR   Proteomes; UP000279470; 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; IPR045462; aa-tRNA-synth_I_cd-bd.
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; 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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000279470}.
FT   DOMAIN          430..508
FT                   /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19269"
FT   MOTIF           40..48
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT   MOTIF           286..290
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
FT   BINDING         289
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00177"
SQ   SEQUENCE   518 AA;  60354 MW;  73558D1C38E30A1D CRC64;
     MLDLNNINSW AFKEANLLLK KINNQPPKKG YVLFETGYGP SGLPHIGTFG EIVRTSMVRK
     AFQYISDIPT KLFCMSDDMD GLRKVPDNIP NKENYYQYID LPLTNIPDPF RKNQSYGDYM
     NSKLIEFLDH FNFDYEFISA TKCYKSGKFN DYLTKVLEKY DNIIDILIPT LGKERRESYS
     PFLPICEKTG KVLQAKVINK NIESKTITYL DNTGHKVETS ILNGKCKLQW KPDFAMRWAA
     LDVDYEIYGK DIQANAEIYD KICTVLGKSP PQQMSYELFL DENGQKISKS KGNGLSIDDW
     LKYANQESLN LFMYQSPKKA KKLYFSIIPK TFDEYLNHLS KFNQLTDEKE KISNPIFYIH
     TDKIPNINLD KITFSLLLNL VNACNTDNKD VLWGYIKDFI DHDNINKETH EYIDSMLGYA
     INYFQDFIKP KKKYKIPNEQ EIKLLKLLLE NLKTVNNTAE DIQNTVYKIS KDNNIPLKEW
     FQSLYEILLG TKEGPRIGTF IKLYGVKKIE KLIYEKIC
//
DBGET integrated database retrieval system