ID   SYL2_SACS2              Reviewed;         944 AA.
AC   O33768; Q9UWZ3;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   27-MAR-2024, entry version 144.
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}; Synonyms=leuS;
GN   OrderedLocusNames=SSO0589; ORFNames=C21_009;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=10701121; DOI=10.1139/g99-108;
RA   Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA   Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA   Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA   Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA   Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT   "Gene content and organization of a 281-kbp contig from the genome of the
RT   extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL   Genome 43:116-136(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 762-944.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=9209067; DOI=10.1128/jb.179.13.4429-4432.1997;
RA   Charlebois R.L., Sensen C.W., Doolittle W.F., Brown J.R.;
RT   "Evolutionary analysis of the hisCGABdFDEHI gene cluster from the archaeon
RT   Sulfolobus solfataricus P2.";
RL   J. Bacteriol. 179:4429-4432(1997).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y18930; CAB57710.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40902.1; -; Genomic_DNA.
DR   EMBL; U82227; AAB63016.1; -; Genomic_DNA.
DR   PIR; G90205; G90205.
DR   RefSeq; WP_009991108.1; NC_002754.1.
DR   AlphaFoldDB; O33768; -.
DR   SMR; O33768; -.
DR   STRING; 273057.SSO0589; -.
DR   PaxDb; 273057-SSO0589; -.
DR   EnsemblBacteria; AAK40902; AAK40902; SSO0589.
DR   GeneID; 72912416; -.
DR   KEGG; sso:SSO0589; -.
DR   PATRIC; fig|273057.12.peg.598; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   InParanoid; O33768; -.
DR   PhylomeDB; O33768; -.
DR   Proteomes; UP000001974; 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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
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_0000152145"
FT   MOTIF           36..46
FT                   /note="'HIGH' region"
FT   MOTIF           623..627
FT                   /note="'KMSKS' region"
FT   BINDING         626
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   944 AA;  109104 MW;  9ACAFCFBF04160DC CRC64;
     MNNIAYKWQT RWEEDKIYES NPNPSKPKFF TTVAFPYPNS PWHIGHGRTY VTGDILARYK
     RMRGYNVLFP MAFHYTGTPI MAMADAIAKG DKELIETFKD IYEISPDVIP RMSDPLFMAN
     YFKEDIKASM REIGLGIDWR REFTTIDPEF SSFVTWQFHK LQSKGYIVKD THPVGWCPVH
     HIPVGMHDTK GDVEPEIGEF VLIYFNSEKG IFPAATLRPE TIFGATALWI NPSEMYVVAS
     MLGKKMILSE KAAAKLSFQI DDIEIEEKIK GSKLVGLKVE NPITGKHIAV LGADFVDVSL
     GTGVVMSVPA HAPFDYYYSK KTFKNNNIEI IPVITVEGLG NALAKDVVEK NNPKSDEDLK
     KLTEYVYRTE YNKGVLRSDL GNLIREEYRN ELKSLGGLPV PKGRELITNF LISKGLGRKI
     FEVMNKPVYC RCGTEIVVKI LKDQWFLDYS NKEWKELARK SLSKINVIPE ESRKDFEFTI
     EWLEKRACAR TRGLGTPLPW DKKWIIESLS DSTIYMAYYT ISHKIKQYKL SPSKLTQEFW
     DYVMLGIGNL EEISEKTGIP SNIIKEFREE FLYWYPLDIR HSGKDLIPNH LTFFIFNHAA
     IFQENLWPKA IAVNGLVLYE GKKMSKSLRN IIPLRKGLKM YGVDVMRIAV SSTADMGSDV
     NFSESLVKTV GETLRKMYEL FKSLDNYTGD ILGFPEKWLL SRIYEITSST TRHMEALELR
     DAVNELLFVF SSDLDEYFGM VSAEGREANN KVLREVLTIW LKLITPFAPH LAEEIWHEIL
     KQKTYIVNEG WPEVEGSKMD ELTLLEHEYM KRIVEDIRSI LNIFKGTPKL IKIYALNDSR
     YMELLRDAIV ANGQMKKFMD IHKPKSREDA RILQKIFNES LEIDDKMKKL VTNYNINEVD
     VLNKLSKYIR RKLNVDILIE PYDEEVKKTY NKEAMPLRPA IIIE
//