ID D3SNK8_THEAH Unreviewed; 604 AA.
AC D3SNK8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
GN OrderedLocusNames=Thal_0108 {ECO:0000313|EMBL:ADC88745.1};
OS Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX NCBI_TaxID=638303 {ECO:0000313|EMBL:ADC88745.1, ECO:0000313|Proteomes:UP000002043};
RN [1] {ECO:0000313|Proteomes:UP000002043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14484 / JCM 11386 / HI 11/12
RC {ECO:0000313|Proteomes:UP000002043};
RX DOI=10.4056/sigs.761490;
RA Wirth R., Sikorski J., Brambilla E., Misra M., Lapidus A., Copeland A.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Tapia R., Bruce D., Goodwin L., Pitluck S., Pati A., Anderson I.,
RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA Bilek Y., Hader T., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Tindall B.J., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Thermocrinis albus type strain (HI 11/12T).";
RL Stand. Genomic Sci. 2:194-202(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001372};
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; CP001931; ADC88745.1; -; Genomic_DNA.
DR RefSeq; WP_012991152.1; NC_013894.1.
DR AlphaFoldDB; D3SNK8; -.
DR STRING; 638303.Thal_0108; -.
DR KEGG; tal:Thal_0108; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_1_0; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000002043; Chromosome.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
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 CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002043}.
FT DOMAIN 34..178
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 219..399
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 400..568
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
SQ SEQUENCE 604 AA; 69986 MW; 2C0555041180EA8F CRC64;
MEIYDPHSIE EKWQKIWEEK GVFKTEEKGE KVYVLEMFPY PSGRIHMGHV RNYTIGDAIA
RFLRMRGKAV LHPMGWDAFG LPAENAAIKH GVHPAQWTKS NISYMRDQLR RLGFSYDWDR
EIATCDPEYY RWNQWIFLKF LEKGLAYRKE AEVNYCPNDE TVLANEQVIE GRCWRCGTPI
VRKKVPSWYL RITQYAERLL EDLEKLEGKW PERVIAQQKN WIGKSTGAIV KFPVGDSYVE
IFTTRPDTIF GATFLVLAPE HPMTLTLAQM GGREKEVQKF LRKMESMSTR ERSTSEEKEG
VFLGVWAKNP ATGEEIPVWT ANYVLYEYGT GAIMAVPAHD QRDYEFAIKY NLPVKVVVVP
EDGVKVEGRA YEEAGILVNS GPFDGMPSQE AKKAIVEWLA QKGLARWHTT YRLRDWNISR
QRYWGTPIPV VHCPVCGIVP VPEDQLPVLL PTHVKVTGHG NPLQQVDEFV NTVCPKCKGP
AKRETDTMDT FFDSSWYFLR FCDPHNDKKP FDEEKVKRWM PVDLYIGGIE HAVLHLLYAR
FFQKFLKDLG MVDHDEPFLR LVTQGMVLKR WVSVERLLKF LGLSEDDPLD KLVEAVRRLA
TVEK
//
