ID U2Z519_9RHOB Unreviewed; 939 AA.
AC U2Z519;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
GN ORFNames=MBELCI_2572 {ECO:0000313|EMBL:GAD56520.1};
OS Limimaricola cinnabarinus LL-001.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1337093 {ECO:0000313|EMBL:GAD56520.1, ECO:0000313|Proteomes:UP000016566};
RN [1] {ECO:0000313|EMBL:GAD56520.1, ECO:0000313|Proteomes:UP000016566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL-001 {ECO:0000313|EMBL:GAD56520.1,
RC ECO:0000313|Proteomes:UP000016566};
RA Nishi S., Tsubouchi T., Takaki Y., Koyanagi R., Satoh N., Maruyama T.,
RA Hatada Y.;
RT "Draft Genome Sequence of Loktanella cinnabarina LL-001T, Isolated from
RT Deep-Sea Floor Sediment.";
RL Genome Announc. 1:e00927-13(2013).
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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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:GAD56520.1}.
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DR EMBL; BATB01000039; GAD56520.1; -; Genomic_DNA.
DR AlphaFoldDB; U2Z519; -.
DR STRING; 1337093.MBELCI_2572; -.
DR eggNOG; COG0495; Bacteria.
DR Proteomes; UP000016566; Unassembled WGS sequence.
DR GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IEA:InterPro.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
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 Gene3D; 3.30.160.150; Lipoprotein like domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR007485; LPS_assembly_LptE.
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; PF04390; LptE; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:GAD56520.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 150..300
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 358..514
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 553..592
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 625..745
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 939 AA; 103413 MW; 99C82C05B675E41B CRC64;
MLHPMGWDAF GMPAENAAMA SGGHPKEWTY NNIADMRAQM KPLGLSIDWS REFATCDPEY
YGQQQALFID MLEKGLVYRK NAVVNWDPVD MTVLANEQVI DGKGWRSGAD VERRELTQWF
FKISEYSDEL LSALDGLDDW PAKVKLMQAN WIGRSRGLEM AFGLTETTHG HDRIEVYTTR
PDTLLGASFV GISPDHPLAR ALEAEREDVA AFCAEARRGG TTEEALETGE KLGFDTGLTV
RHPFDEGRAL PVWIANFVLM DYGTGAIFGC PGHDQRDLDF ARKYDLPVIS TFAPAKDDGQ
ALAEDGGPAY VPPKSEPVIY IRGFAGETEQ SGETAIDAAI AFCEEHGVGR GVTRFRLRDW
GLSRQRYWGT PIPIVHCADC GAVPEKKENL PVRLPDDVSF DVPGNPLDRH PTWRDAPCPR
CGKAARRETD TMDTFVDSSW YFARFTSPRA ETPTDMAEAE YWMNVDQYIG GIEHAILHLL
YSRFFARAMH ATGHLPEKAI EPFNALFTQG MVTHEIYQTR NANGRPVYHL PESVENGALK
DSGEKVEIIP SAKMSKSKKN VVDPDAILAQ YGADTARWFV LSDSPPERDV EWTASGAEAA
HKHLARVWRI ADEVAEATDG DTDADEDLLR QLHRTIRDVT LGLESFGFNA AIAKLYAFTS
VLSKSSASAG TRRVAARTLA QLMSPMTPHL AEEIWTRLGG EGFVASAPWP VAEERFLVED
SVTLPIQING KRRSEITVPK AMPKDEIEAL VLGDEAVSKA LGGAPRKSSS WCRAGSSMWS
SDPSRRRWLL GALALGGCGF TPAFGPGGDA ARLHGKVRVE APATFLGYLL RARLLDRLGP
AEAPRYVLTL ETSEEVEQAA VSAEGAVLRY RLLGRAEYEL RPLDDDPALA RGTVEDFAGY
SATLGTVASE AAERDARERL ARLLTVQITT RLLAVPAPE
//
