ID F9CUQ6_9ARCH Unreviewed; 959 AA.
AC F9CUQ6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN ORFNames=MY1_0331 {ECO:0000313|EMBL:EGP93102.1};
OS Nitrosarchaeum koreense MY1.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosarchaeum.
OX NCBI_TaxID=1001994 {ECO:0000313|EMBL:EGP93102.1, ECO:0000313|Proteomes:UP000004440};
RN [1] {ECO:0000313|EMBL:EGP93102.1, ECO:0000313|Proteomes:UP000004440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY1 {ECO:0000313|EMBL:EGP93102.1,
RC ECO:0000313|Proteomes:UP000004440};
RX PubMed=21914867; DOI=10.1128/JB.05717-11;
RA Kim B.K., Jung M.Y., Yu D.S., Park S.J., Oh T.K., Rhee S.K., Kim J.F.;
RT "Genome Sequence of an Ammonia-Oxidizing Soil Archaeon, "Candidatus
RT Nitrosoarchaeum koreensis" MY1.";
RL J. Bacteriol. 193:5539-5540(2011).
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:0000256|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGP93102.1}.
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DR EMBL; AFPU01000001; EGP93102.1; -; Genomic_DNA.
DR RefSeq; WP_007549762.1; NZ_AFPU01000001.1.
DR AlphaFoldDB; F9CUQ6; -.
DR STRING; 1001994.MY1_0331; -.
DR PATRIC; fig|1001994.6.peg.316; -.
DR OrthoDB; 23906at2157; -.
DR Proteomes; UP000004440; Unassembled WGS sequence.
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 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}.
FT DOMAIN 12..664
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 699..832
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 39..49
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 626..630
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 629
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 959 AA; 109950 MW; B4C8428920E97534 CRC64;
MEIRWNEIES KWRKRWNDSK NFETDPSEKE KKFITVAYPY PNSPQHIGHG RTYTLADVHA
RFYRMNGFNV LFPMAFHYTG TPILGMAKRV EANDREIIEN LKNLYGVPEE SIKTFVEPVK
IADYFHKEIK TGMIEIGYSI DWRREFTTID PVYSKFIEWQ IKTLREKKLI IQGSHPVGWC
PKDQNPVSQH DTLGDVEPDF TEYILIKFKY EDYIIPTATL RPETIFGVVN LWVNPEIIYK
KITVDNEKWI VSKECAYKLE FLDKKITHDG EIKGAELIGK LVTVPHRNES ILMLPASFVE
SGTGTGMVMS VPAHAPFDYQ ALEDLKKAKI EPELASKVAK IIPISIIQTE GFGENPAKEA
VEKFGVVNQS DPKLEEATKE VYGKEFYGGK LKQNTEQFAG IKVAYAKDTI KEWLIKNKHA
DILLELTNTP VRCRCGAECV VKVLNNQWFL NYGNKDWKEL ATKCFDEMNI LPQEIRSEFN
YVIGWLRERA CARQHGLGTK LPWDKDWIVE SLSDSVIYMA YYTISKFVND GTLKAEKLSP
EFFDYIFLGK GDANKVSSIT ELTVDVINQI KKEFDYFYPV DSRHSGRDLV PNHLTFFVLN
HVAIFPENNW PKEIVVNGSV LMNGSKMSKS MGNIIPLRKA IQDYGADPIR LAIIISAELL
QDADFNMESV SGIQNKLESL YNECSRLKAE KIENLEAEDK WILSKTQSMI SQVTTSIEKM
RLREALHDIL FSFESDLSWY TKRVNAKNRT NISGILHQIN SVRVAMLSPF APHIAEEMWE
KLGHSDLAST SQWPKYSEEN INASAIQSEE LLKLLIDDIG NILKVTKITP KKITIYTADL
FKSKVYHSIL EKVMSGQTNM GIVMKELIAN SETADVKKTP DFVQKTIKDI LSEPTEIRQM
KLESKEFDEK KFLTNELTDI GKKEFGVDID VFSESDDGIY DPKAKARHAR PFKPAILIE
//
