ID S5R327_CARRU Unreviewed; 512 AA.
AC S5R327;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
GN Name=leuS {ECO:0000313|EMBL:AGS06609.1};
GN ORFNames=CRDC_00620 {ECO:0000313|EMBL:AGS06609.1};
OS Candidatus Carsonella ruddii DC.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Zymobacter group; Candidatus Carsonella.
OX NCBI_TaxID=667013 {ECO:0000313|EMBL:AGS06609.1, ECO:0000313|Proteomes:UP000015332};
RN [1] {ECO:0000313|EMBL:AGS06609.1, ECO:0000313|Proteomes:UP000015332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC {ECO:0000313|EMBL:AGS06609.1,
RC ECO:0000313|Proteomes:UP000015332};
RX PubMed=23850282; DOI=10.1016/j.cub.2013.06.027;
RA Nakabachi A., Ueoka R., Oshima K., Teta R., Mangoni A., Gurgui M.,
RA Oldham N.J., van Echten-Deckert G., Okamura K., Yamamoto K., Inoue H.,
RA Ohkuma M., Hongoh Y., Miyagishima S.Y., Hattori M., Piel J., Fukatsu T.;
RT "Defensive bacteriome symbiont with a drastically reduced genome.";
RL Curr. Biol. 23:1478-1484(2013).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR EMBL; CP003467; AGS06609.1; -; Genomic_DNA.
DR AlphaFoldDB; S5R327; -.
DR KEGG; cri:CRDC_00620; -.
DR PATRIC; fig|667013.4.peg.110; -.
DR HOGENOM; CLU_432575_0_0_6; -.
DR Proteomes; UP000015332; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR PRINTS; PR00985; TRNASYNTHLEU.
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|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035}.
FT DOMAIN 16..214
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 333..484
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
SQ SEQUENCE 512 AA; 62451 MW; 9C350FE3422214D3 CRC64;
MKYFKNPIFI EKKIIKKIKQ IKKQKFFSMP MFPYPSGKLH LGHVRNYVLT DIIAKIKQLE
NYNVIHPLGW DSFGLPAENA SKKYNINSLK WTISNIKLMR HQLKLVNIDY YKKTEFLTCD
FNFYKWEFWI FIQFLKNNLL YKNYENVYWD KIENCILSNE QVINNICWRS GIKAETRRIK
TWFINIKKYT KRLIFNLKKI NWSKKVKNIQ KKWINITIFF IKKNHFYSNY NNIYININFL
RIKNKNLLHL IILKNFSNFI FKKKIFVFDK KLKIKKKIIL NNFKIINFLI NKKKLNLLIF
KKNIFYIKLT NIKNWSFERN RLWGSFFFYK KVKNKNFKSK STIDTFFQSS WYYINYLKTK
NLTNLNKLKW FPINIYVGGI EHANLHLIYL RIINNIFYDL NILKNKEIIF NLINQGFINN
KVFYKFKNYK KIFCRKTKNC IYSGIEKMSK SKKNGVNPIP IIIKYGSDLL RLSIITNKPI
YKNIVWENVN FEFLKKFIIK LNNLIILKKK KL
//
