ID F0NIB9_SULIR Unreviewed; 944 AA.
AC F0NIB9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN OrderedLocusNames=SiRe_1417 {ECO:0000313|EMBL:ADX85483.1};
OS Sulfolobus islandicus (strain REY15A).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=930945 {ECO:0000313|EMBL:ADX85483.1, ECO:0000313|Proteomes:UP000002664};
RN [1] {ECO:0000313|EMBL:ADX85483.1, ECO:0000313|Proteomes:UP000002664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=REY15A {ECO:0000313|EMBL:ADX85483.1,
RC ECO:0000313|Proteomes:UP000002664};
RX PubMed=21278296; DOI=10.1128/JB.01487-10;
RA Guo L., Brugger K., Liu C., Shah S.A., Zheng H., Zhu Y., Wang S.,
RA Lillestol R.K., Chen L., Frank J., Prangishvili D., Paulin L., She Q.,
RA Huang L., Garrett R.A.;
RT "Genome analyses of icelandic strains of Sulfolobus islandicus, model
RT organisms for genetic and virus-host interaction studies.";
RL J. Bacteriol. 193:1672-1680(2011).
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|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_00049}.
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DR EMBL; CP002425; ADX85483.1; -; Genomic_DNA.
DR RefSeq; WP_014512711.1; NC_017276.1.
DR AlphaFoldDB; F0NIB9; -.
DR STRING; 930945.SiRe_1417; -.
DR GeneID; 78428857; -.
DR KEGG; sir:SiRe_1417; -.
DR eggNOG; arCOG00809; Archaea.
DR HOGENOM; CLU_004174_0_0_2; -.
DR Proteomes; UP000002664; 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 CDD; cd00812; LeuRS_core; 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; 1.
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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}.
FT DOMAIN 7..663
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 696..829
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT COILED 905..932
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 36..46
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 623..627
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 944 AA; 109335 MW; 458B25424C37F167 CRC64;
MNNVAHKWQT KWEEAKVYES NPNSNRSKFF TTVAFPYPNS PWHIGHGRTY VTGDILARYK
RMRGYNVLFP MAFHYTGTPI MAMADAIAKG DKELIETFKD IYEISPDVIP RMSDPLFMAN
YFKEDIKTSM REIGLGIDWR REFTTIDPEF SSFVTWQFHK LQSKGYVVKD THPVGWCPVH
HIPVGMHDTK GDVEPEIGEF VLIYFNSEKG IFPAATLRPE TIFGATGLWI NPNEMYVIAN
ILDKKMILSE KSATKLSFQI DNIEIEDKIK GSKLVGLKVE NPITGKYIVV MGADFVDASL
GTGVVMSVPA HAPFDYYYSK KMLKNNNIGI IPVITVEGLG NELAKDVVEK NNPKNDEDLK
KLTEYVYRTE YNKGILRSDL ENLIKEEYRN ELKNLGGLPV PKGRELITNF LISKGLGRKI
FEIMNKPVYC RCGTEIVVKI LKDQWFLDYS NEEWKELARK SLSKMQIIPE ESRKDFEFTI
EWLEKRACAR TRGLGTPLPW DKKWIIESLS DSTIYMAFYT ISHKIKQYKI SPSKLTQEFW
DYVMLGIGNL EDVSKNTGIP SNIIKELREE FLYWYPLDIR HSGKDLIPNH LTFFIFNHAA
IFQENLWPKA IAVNGLVLYE GKKMSKSLRN IIPLRKGLKM YGVDVMRIAV SSTADMGSDV
NFSESLVKTV GETLRRMYEL FKSLDNYTED TFGFPEKWLS SRIYEITTNT TKHMEALELR
DAANELLFVF SSDLDEYFGM VNAEGRRANN KLLREVLTIW LKLITPFAPH LAEEIWHEIL
KQTTFIVNEK WPEIEGSKID ELTLLKHEYM KRIVEDIRSI LNVFKGTPKL IKIYALNDSR
YVELLRDAIE ANGQMKKFMD AHKPKSKEDA RVLQKIFNES LEIDDKMKKL IMNYNINEVD
VLNELSKYIR RKLNVEIQVE AYNEEVKKAY NKEAMPLRPA IIIE
//
