ID   SYL2_SULAC              Reviewed;         942 AA.
AC   Q4J8J7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 93.
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=Saci_1572;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY80885.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; CP000077; AAY80885.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q4J8J7; -.
DR   SMR; Q4J8J7; -.
DR   STRING; 330779.Saci_1572; -.
DR   EnsemblBacteria; AAY80885; AAY80885; Saci_1572.
DR   KEGG; sai:Saci_1572; -.
DR   PATRIC; fig|330779.12.peg.1512; -.
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   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.90.740.10; -; 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   PANTHER; PTHR45794; PTHR45794; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00395; leuS_arch; 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 2"
FT                   /id="PRO_0000152143"
FT   MOTIF           35..45
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   942 AA;  109179 MW;  4DD802C8C8C861C4 CRC64;
     MKISEKWQKE WENKRVFDAT PDPNKKKFFT TIAFPYPNSP FHLGHGRTYV TGDIYARYMR
     MRGYNVLFPM AFHYTGTPII AMADDVAKGD KELIDIFKSI YEIPDDVISK LVDPLFMANY
     FKEEIKQAMK EIGLSIDWRR EFTTIDPEFS SFIIWQFRKL QEKGFIVRDT HPVGWCPVHH
     IPVGMHDTKG DMEPEIGEFV LIYFDSDMGI LPVATLRPET VFGAIAVWVN PHESYSIVEI
     DGKKYVMSEK ASSKLSFQID NLKVITVVKG SELVKHSAVN PITGKEVPII GANFVDPLTG
     TGVVMSVPAH APFDYFYLKK TKSELSIISV IRVEGMGETL AKDLVEKSNP QNDNDLKKLT
     EQVYRIEYNK GVMIDITKLV KPEYVEELKP LVNLPVPAAR QKITEFITQK GLGRKIYEIM
     NRPVYCRCGN EVVVKILKDQ WFLDYGNQEW KDLARKSIES IRFIPPEIKK DFEFVVDWLQ
     KRACARTRGL GTPLPWDKKW IIESLSDSTI YMAFYTIAHR LKEHKLKPSQ LTYEFWEYIM
     LGNGNPDEIS KISGIPVEVI KAMRDEFLYW YPLDVRHSGK DLVPNHLSFF IFNHAAIFPH
     QLWPKGIAVN GFVLYDGKKM SKSLRNIVPL RKAIRMYSPD VIRIALTTNA DIGSDVNFSD
     SYAKSIIDTL KNYYDLLEKL KEFKGEDEGF PEKWLKSKFY QMVINVTQYM DSLDLRSSSN
     EILYNFSSYI NEYFELVRSE GREPNGKLLS QILQIWIKLL SPFAPHFAEE LWHKIGKNTL
     VSLESWPIID QSNVDLFIDL THTYHRKLLN DIQAILSVYK DTPKSIKIFV ANKEFLNVLR
     DAINIVQKGG QLRQLMEIHK PKGKQDARLY QKIYEEAREI DDDMKKLVTN FDFDEKDLLD
     KGLKYLSYKL GIKEIRILDA SEMDRTKYNK DALPLRPAII IE