ID   SYL2_METS5              Reviewed;         950 AA.
AC   A4YI28;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Msed_1940;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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}.
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DR   EMBL; CP000682; ABP96080.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4YI28; -.
DR   SMR; A4YI28; -.
DR   STRING; 399549.Msed_1940; -.
DR   PRIDE; A4YI28; -.
DR   EnsemblBacteria; ABP96080; ABP96080; Msed_1940.
DR   KEGG; mse:Msed_1940; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004174_0_0_2; -.
DR   OMA; AWNMAFQ; -.
DR   Proteomes; UP000000242; 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..950
FT                   /note="Leucine--tRNA ligase 2"
FT                   /id="PRO_0000334842"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           631..635
FT                   /note="'KMSKS' region"
FT   BINDING         634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   950 AA;  109016 MW;  3C6D2635D180537E CRC64;
     MITIPSHEFT DLLNEISKKW QEEWSKNRIF EADPKDQKKF FTTVAFPYPN SPFHLGHGRT
     YVTGDVYARF MRMKGYNVLF PMGFHFTGTP IITMADDVAK GDKDLLDIFQ NIYEIPADVI
     PKLSDPLFMA NYFKEDIKAA MREIGLSIDW RREFTTIDPQ FSAFIVWQFS KLQKKGYVVK
     DTHPVGWCPV HNLPVGMHDT KGDMEPEIGE YVVIFFESKM GALAAATLRP ETIFGAVAVW
     VNPKATYTVA EIWGKKVIVS EKAAEKLKFQ TDVKVLEKVS GSDLLKIVAI NPITGKEIPI
     LPADFVDPTT ATGVVMSVPA HAPFDYFYLK KAKVGIEPIP VVAVEGQGDA PAKDLVESSH
     PKNDADLKKL TEQLYRLEFN KGLMRSDILR LVKDELRAEL SVVAGKQVPE ARKMVTDILI
     QRKAGTKMLE IMNKPVYCRC GNEVVVKILQ DQWFLDYGNP EWKAKAKKLL DSMRVIPEET
     RKDFEYALDW LQKRACARTR GLGTPLPWDK KWIIESLSDS TIYMAYYTLS HKIKEFGLHP
     SQLTEETWDY IMLGEGDVKA ISERNKIGVD ALQELRRHFT YWYPLDLRHS GPDLIPNHLS
     FFIFNHAGIF PENLWPRGVA VNGFILYEGK KMSKSLRNIV PLRKAIRTYG ADVIRIALSS
     LVDMSSDANF TEAGARAIAD NLKRFYELMQ MQDGSTIDGT PEKWLRSKLH RLVRDVTPLM
     ESMRFREVIN ELLFNLSSYI NEYLEMVRSE SREYNRDVIR EVVETWTKLM APFAPHLTEE
     MWHQLGHNTF LSLESWPTPD NSKINDQIEL EHEYHKLLIE DIRAILNVYK GKPSSVLLYV
     HDGSLNQVVK SALDVLNSGG TMKDFMQKNT PKSKEEARVL QRIMQYVTEM PETVKKLIYS
     NVNEMEVTRK GVPLLRYKLN LEIEVLAYTQ EVKQKLNKDA LPYRPAILVK