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};
GN   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
//