ID F3ZR40_9BACE Unreviewed; 943 AA.
AC F3ZR40;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=Bcop_0415 {ECO:0000313|EMBL:EGJ70633.1};
OS Bacteroides coprosuis DSM 18011.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=679937 {ECO:0000313|EMBL:EGJ70633.1, ECO:0000313|Proteomes:UP000018439};
RN [1] {ECO:0000313|EMBL:EGJ70633.1, ECO:0000313|Proteomes:UP000018439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18011 {ECO:0000313|EMBL:EGJ70633.1,
RC ECO:0000313|Proteomes:UP000018439};
RX PubMed=21677860; DOI=10.4056/sigs.1784330;
RA Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Non-contiguous finished genome sequence of Bacteroides coprosuis type
RT strain (PC139).";
RL Stand. Genomic Sci. 4:233-243(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|ARBA:ARBA00001372, ECO:0000256|HAMAP-
CC 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|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC ECO:0000256|RuleBase:RU363039}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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DR EMBL; CM001167; EGJ70633.1; -; Genomic_DNA.
DR RefSeq; WP_006743787.1; NZ_CM001167.1.
DR AlphaFoldDB; F3ZR40; -.
DR STRING; 679937.Bcop_0415; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_10; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000018439; 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; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR Gene3D; 3.40.50.620; HUPs; 3.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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}; Reference proteome {ECO:0000313|Proteomes:UP000018439}.
FT DOMAIN 37..120
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 276..442
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 794..905
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 717..721
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 720
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 943 AA; 108888 MW; 8837552C01224562 CRC64;
MEYNFRDIEK KWQKMWVENN TYKVVEDKSK EKLYILNMFP YPSGAGLHVG HPLGYIASDI
YARYKRLCGY NVLNPMGYDA YGLPAEQYAI QTGQHPAVTT EQNIKRYREQ LDKIGFSFDW
SREVRTCDPN YYHWTQWAFI QMFKSYFDTK VNKAMPIENL VSYFEKNGSK DIPASGSEEL
DFTAEEWKAM DESKQQDVLM NYRIAYLGDM MVNWCPELGT VLANDEVIDG LSERGGYPVI
QKVMRQWCLR VSAYSQRLLD GLNTIEWTDS LKETQRNWIG RSDGAEMQFK VKDSDVEMTI
FTTRADTVFG VTFMVLAPES ELVDTLTTPE QKAEVDAYLE RSKKRTERER IADRKVTGVF
TGSYAINPLT KEAIPVWVSD YVLAGYGTGA IMAVPAHDSR DYAFAKHFGL EIRPLIEGCD
ISEESFDAKE GIMTNSPIEG MNTDLVLNGL TVTEAIAKTK QFIEETKLGH IKTNYRLRDA
TFSRQRYWGE PFPVYYKNGH PYMIEEEYLP IELPDVEKFL PTETGEPPLG RAKVWAWDTV
NKKVVSNDLI DNKTVFHLEL NTMPGFAGSS AYFLRYMDPQ NSEALVSKGV CEYWQNVDLY
VGGTEHATGH LIYSRFWNMF LYDVDVAVRQ EPFQKLVNQG MIQGRSNFVY RINGTNKFVS
LDKKDEYETT AIHVDVNIVE NDFLDLEAFK AWRPEFSSAE FILNEDGQYL CGWAVEKMSK
SMFNVVNPDM IVDRYGADTL RMYEMFLGPL EQSKPWDTNG IDGVYRFIHR FWGLFFDRQG
NSLIEDKPAT KEELKALHKL IKKSTEDIEN FSFNTTVSAS MICVNELNSL KCHKKEILEQ
LTIVLSPFIP HVCEELWDVL GHENSICIAD WPKYNEEFMK EAVKNYNISF NGKSRFNMDF
AADASREEIQ KKVLEDERTS RWLEGKEPKK IIVVPGKIVN LVF
//
