ID SYL1_SULAC Reviewed; 942 AA.
AC Q4JBP0;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Leucine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS 1 {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS1 {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=Saci_0373;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; CP000077; AAY79789.1; -; Genomic_DNA.
DR RefSeq; WP_011277291.1; NZ_CP046615.1.
DR AlphaFoldDB; Q4JBP0; -.
DR SMR; Q4JBP0; -.
DR STRING; 330779.Saci_0373; -.
DR GeneID; 78440723; -.
DR KEGG; sai:Saci_0373; -.
DR PATRIC; fig|330779.12.peg.371; -.
DR eggNOG; arCOG00809; Archaea.
DR HOGENOM; CLU_004174_0_0_2; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR Gene3D; 3.30.2320.20; Class I aminoacyl-tRNA synthetases (RS); 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.10.720; leucyl-tRNA synthetase; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_00049_A; Leu_tRNA_synth_A; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR020791; Leu-tRNA-lgase_arc.
DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR NCBIfam; TIGR00395; leuS_arch; 1.
DR PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..942
FT /note="Leucine--tRNA ligase 1"
FT /id="PRO_0000152142"
FT MOTIF 39..49
FT /note="'HIGH' region"
FT MOTIF 624..628
FT /note="'KMSKS' region"
FT BINDING 627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 942 AA; 108215 MW; C62D780A5A6C432F CRC64;
MDFLNEIASK WQKVWDSERV YEADVDRTKE KKFITVAFPY TNSPLHIGHG RTYITADIYA
RYLRMKGYNV LFPFAFQFTG TPILSIADAV KRGDEEIIST FTNVYQIPIG VISKFSDPSY
LSAYFKEDMR NTALTLGLSI DRRREFTTID PAFERFVQWQ YKRLQEIGYI KKEKAPVAYC
PVDEFPVGMH DTRGDIEPEI IDLDVIYFQG EKLLFLTATS RPETIFGAVA ILINPDSDYS
IVVDNKNGKR LVMSTEAFKK LSFQMSLTEE ERKKGGELIG LNVTNPVTLK KLTVLPSKYV
ESKQGTGVVM AVPAHEPLHY LALSELKESF EIVPVIKSED YGDFPAMEVL ETAQTTSAQE
LKDYIDTLYR IEFHKGSIRD EVVDLVPDYM KQFVGERIAG KSVREARSSV VELLRNLGVH
GNIYEIINGP VYCRCGAEVV VKVFDDQWFI DYSNSTWKSS VLKSLDKIEI LPQDAKREIS
KIIFNMKPRP FTRSRGLGVR LPWDDRQIID SLSDSTIYTV FYIVANKVKS YPTSILNERF
WDYVVLGRGD SSQLSRELGI PKEQLEELRM EVEYWYPVDS RHSGRDLVQN HIPYYLYHHV
GVLGEDKVPK RIVLNGFIRV GGKKMSKSFG NVYPLNKAIR EYGVDTVRLA LTSTSSLSDD
IEFSPNIAKS IGEQLKHIHD FIENLIKLQS VNEIRKVDLW ISSLISEYID LIDNCLSNLD
LRTAYKTIYY DIYEDLKDYL ELGNGKINSD IIKNVISVWI RLMAPFTPHL AEELWHKLDN
SLVVRQRFPS KGELQYDKRA LLEIEYLRYT IDLINSMKSK MSKEPETVII YVNEDNTQRD
LIRKAIESLK ERKSLPDFEK EVGDREMARL AYEIAGDLPD KIKNLAEIGI NESEILTSNA
QFLLNKLDVK EIYIYNSKDP STPDIKGKKS IALPYKPGII LT
//
