ID A0A1W6LLD8_9BACT Unreviewed; 853 AA.
AC A0A1W6LLD8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ECO:0000313|EMBL:ARN56563.1};
GN ORFNames=STSP1_00946 {ECO:0000313|EMBL:ARN56563.1};
OS Sedimentisphaera salicampi.
OC Bacteria; Planctomycetota; Phycisphaerae; Sedimentisphaerales;
OC Sedimentisphaeraceae; Sedimentisphaera.
OX NCBI_TaxID=1941349 {ECO:0000313|EMBL:ARN56563.1, ECO:0000313|Proteomes:UP000193334};
RN [1] {ECO:0000313|Proteomes:UP000193334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-PulAB-D4 {ECO:0000313|Proteomes:UP000193334};
RA Spring S., Bunk B., Sproer C.;
RT "Comparative genomics and description of representatives of a novel lineage
RT of planctomycetes thriving in anoxic sediments.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:RU363035}.
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; CP021023; ARN56563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6LLD8; -.
DR STRING; 1941349.STSP1_00946; -.
DR KEGG; pbp:STSP1_00946; -.
DR Proteomes; UP000193334; 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 CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.10.20.590; -; 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; IPR002300; aa-tRNA-synth_Ia.
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; 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; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 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:UP000193334}.
FT DOMAIN 15..148
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 260..447
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 459..649
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 705..817
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 623..627
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 853 AA; 97827 MW; 4771F4963ED34A60 CRC64;
MEKPGRYNFN QIEKKWQDFW DKNKTFKAEM KPEKPKYYVL DMFPYPSGQG LHVGHPEGYT
ASDIFSRYKR MNGFNVLHPM GWDAFGLPAE QYAVQTGTHP AETTKANVEN MRRQIKGLGF
SYDWDREVNT TDPNYYKWTQ WIFLKFYNSF FDRDQQKARP IEELEVPETV KEAGKDAVRE
YVDSRRLAYE HEAPVNWCPE LGTVLANEEV VNGVSERGGH PVIRKPMRQW MLRITEYAER
LLNGLEGLDW SHSIKKLQQD WIGKSIGAEV DFLLDGFDDV ISVFTTRPDT LFGATYMVLA
PEHPLVDKIT SKEHKKAVAE YKQQASKKSD LDRTDLAKEK TGQFTGAYAV NPVNGENIPV
WISDYVLLSY GTGAIMAVPA HDSRDFEFAK QFGIKIIQVV KPEDPELAAK AEAEEICFDG
EGIAVNSGQF NGKKTPQVKE EIIAWLEKQE QGKRAVNYKL RDWLFSRQRY WGEPFPILHA
EDGERIALDE SELPLMLPEV EDYKPTPDGA PPLGNAKDWI EVTLPDGRKA RRELNTMPQW
AGSCWYYLRY LDPKNSEEPV AKDKQKYWLP VDLYIGGAEH AVLHLLYSRF WHNLLYDLGY
LDYPEPFQKL VNQGMILGED GQKMSKSRGN VINPDAVVKD YGADSMRLYE MFMGPLEAAK
PWSMSGLEGV HRFLQKFWRV AVNESTGKLC ETVSDFKPDE QTERLMHQTI RKVSNDIDNF
AFNTAISQMM IFVNHLAKLK FKPLSAVKNA VILLYPFAPH MAEELWQICG GEGDTLAYHS
WPEYSEELAK EKEVEIAVQV KGKIKDRIMI NPEASEEEMK EAVLSSEKVS KAVEGKQIRK
VIAVKGRLVN IIT
//
