ID SYL2_SULTO Reviewed; 944 AA.
AC Q970Z6; F9VNE0;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 24-JAN-2024, entry version 112.
DE RecName: Full=Leucine--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS 2 {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS2 {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=STK_14550;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAK54586.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000023; BAK54586.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q970Z6; -.
DR SMR; Q970Z6; -.
DR STRING; 273063.STK_14550; -.
DR KEGG; sto:STK_14550; -.
DR PATRIC; fig|273063.9.peg.1660; -.
DR eggNOG; arCOG00809; Archaea.
DR Proteomes; UP000001015; 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; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..944
FT /note="Leucine--tRNA ligase 2"
FT /id="PRO_0000152147"
FT MOTIF 36..46
FT /note="'HIGH' region"
FT MOTIF 621..625
FT /note="'KMSKS' region"
FT BINDING 624
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 944 AA; 109427 MW; CAC4A1005C676676 CRC64;
MTSIAEKWQK EWEKAKIFEA NPDRTRNKFF TTVAFPYPNS PFHLGHGRTY VTCDIYARYM
RMKGYNVLFP MGFHYTGTPI IAMADDVAKG DKELIDIFKN IYEIPDNVIS KLADPLFMAN
YFRDEIKKAM KEIGLSIDWR REFTTIDPEF SSFIVWQFNK LQEKGYIVRD THPVGWCPVH
HIPVGMHDTK GDMEPEIGEF VLIYFNSDLG ILPAATLRPE TVFGAIGIWV NPDVTYSIIE
LDGKKMIVSE RAAFKLTFQF DNIKNLGSIK GSELTKYKAV NPITGKEIPI MAADFVDPNV
ATGIVMSVPA HAPFDYYYLK KNKQQDMQIV SVIQVEGQGD TLAKDLVEKT NPKNKDDLQK
LTEQVYRIEY NKGKMKDVSS LVKPEFVNYF KSFIGLSVPE ARQKVTEFLI EKGLGRKIYE
IMNRPVYCRC GNEVVVKILK DQWFLDYGNP QWKALAKKLI SNMKFIPPEI RKDFEFVTDW
LQKRACARTR GLGTPLPWDK KWIIESLSDS TIYMAYYTIS HKIRQYQLKP SQLTYDFWNY
IMLGIGDIDK ISSETGISKE IIREMRNEFL YWYPLDIRHS GKDLIPNHLS FFIFNHAAIF
PEELWPKAIA VNGFVLYEGK KMSKSLRNII PLRKALRIYS PDVVRIALTS TADMGSDVNF
SDSYAKSVGE ILRRYYEFIK ELPKYDGEGS EFANNWLKAQ VSSIVLSSTK NMDNIDFRST
INDILYSFDS YLREYIDMCK ADGKEPNGKL LREVIETWIK LLAPFAPHFA EEIWHELGHT
TFISLEKWPT AEESSEDLYY ILIHEYHKRI IEDSQKIINY YYKGKPSIVK IYVAEQELMK
VLREAVQILS NGGTLKQLME KERPSDKKLA NIIRKIYELA VELDDNMKKL ILGYNINERE
ILELGTKYMS YKLGIPVEVY DVSKLDKSKY NKEALPLKPA IIVE
//
