ID A0A061SVZ9_9RHOB Unreviewed; 848 AA.
AC A0A061SVZ9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=PM02_07560 {ECO:0000313|EMBL:KAJ03670.1};
OS Sulfitobacter mediterraneus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=83219 {ECO:0000313|EMBL:KAJ03670.1, ECO:0000313|Proteomes:UP000027337};
RN [1] {ECO:0000313|EMBL:KAJ03670.1, ECO:0000313|Proteomes:UP000027337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1FIGIMAR09 {ECO:0000313|EMBL:KAJ03670.1,
RC ECO:0000313|Proteomes:UP000027337};
RX PubMed=24855294;
RA Mas-Llado M., Pina-Villalonga J.M., Brunet-Galmes I., Nogales B., Bosch R.;
RT "Draft Genome Sequences of Two Isolates of the Roseobacter Group,
RT Sulfitobacter sp. Strains 3SOLIMAR09 and 1FIGIMAR09, from Harbors of
RT Mallorca Island (Mediterranean Sea).";
RL Genome Announc. 2:e00350-14(2014).
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: 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:KAJ03670.1}.
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DR EMBL; JEMU01000005; KAJ03670.1; -; Genomic_DNA.
DR RefSeq; WP_037906889.1; NZ_JEMU01000005.1.
DR AlphaFoldDB; A0A061SVZ9; -.
DR STRING; 83219.PM02_07560; -.
DR eggNOG; COG0495; Bacteria.
DR Proteomes; UP000027337; 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; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 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; PF00133; tRNA-synt_1; 2.
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:UP000027337}.
FT DOMAIN 36..171
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..403
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 424..582
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 619..658
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 693..813
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 619..623
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 848 AA; 94948 MW; F04E6AA0EF382E95 CRC64;
MPRYTPAEIE ARWQQAWEKD EVFKAVRAAD KPKYYVLEMF PYPSGRIHMG HVRNYTMGDV
IARYKIATGH NVLHPMGWDA FGMPAENAAM AIGGHPKDWT YGNIDDMRGQ MKPLGLSIDW
SREFATCDPE YYGQQQALFL DFLDEGLVYR KNAVVNWDPV DMTVLANEQV EAGRGWRSGA
LVERRELTQW FFKISDHSEE LLAALDTLDN WPAKVKLMQA NWIGKSRGLQ FAFSTIDAPE
GHDRIEVYTT RPDTLMGTSF VGISPDHPLA KMLERENEDV AAFCAECRKG GTTEEAIETA
EKLGFDTGIR VRHPFDTAHE LPVYIANFIL MDYGTGAIFG CPAHDQRDFE FATKYELPII
STYLPSEDAN EVLEEAYVPA KSDKVFYNRG FAGDAWQTGE EAINAAVDFC EQNGVGQGVT
KYRLRDWGLS RQRYWGCPIP VVHCDACGVV PEKKENLPIE LPYDVDFGTP GNPLDRHPTW
RDCACPSCGA PAKRETDTMD TFVDSSWYFA RFTAPRAETP TNMEDAKYWM NVDQYIGGIE
HAILHLLYSR FFARAMQITG HLPESAIEPF DALFTQGMVT HEIYQTRDAK DRPVYHLPED
VTDGKLADGT EVEIIPSAKM SKSKKNVVDP LHIISNYGAD TARWFVLSDS PPERDVEWTA
SGADAAFKHL TRVWNICDRI GEMDKDAKGQ GDDDLLRAMH KTIHDVTMGV ESFGFNAAIA
KLYAFTATLQ KSKAGYAAQR EAIITLAQLM SPMTPHLAED IWAHQGGTGL IVTAPWPKAD
EAMLVDDTVT LPIQVNGKRR AEIQVPADMP KEEVEKIALA HEAVVRSLDG AAPKKVIVVP
GRIVNVVA
//
