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Database: UniProt
Entry: B9LSC4_HALLT
LinkDB: B9LSC4_HALLT
Original site: B9LSC4_HALLT 
ID   B9LSC4_HALLT            Unreviewed;       906 AA.
AC   B9LSC4;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN   OrderedLocusNames=Hlac_0366 {ECO:0000313|EMBL:ACM55969.1};
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS   34).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=416348 {ECO:0000313|EMBL:ACM55969.1, ECO:0000313|Proteomes:UP000000740};
RN   [1] {ECO:0000313|EMBL:ACM55969.1, ECO:0000313|Proteomes:UP000000740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34
RC   {ECO:0000313|Proteomes:UP000000740};
RX   PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA   Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA   Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA   Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA   Woese C.R., Kyrpides N.C.;
RT   "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT   strain ACAM 34.";
RL   Stand. Genomic Sci. 11:70-70(2016).
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, ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; CP001365; ACM55969.1; -; Genomic_DNA.
DR   RefSeq; WP_012659610.1; NC_012029.1.
DR   AlphaFoldDB; B9LSC4; -.
DR   GeneID; 7399759; -.
DR   KEGG; hla:Hlac_0366; -.
DR   eggNOG; arCOG00809; Archaea.
DR   HOGENOM; CLU_004427_0_0_2; -.
DR   Proteomes; UP000000740; Chromosome 1.
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:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.30.2320.20; Class I aminoacyl-tRNA synthetases (RS); 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.10.720; leucyl-tRNA synthetase; 1.
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; 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|RuleBase:RU363035};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000740}.
FT   DOMAIN          40..174
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          223..421
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          432..628
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          670..790
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   906 AA;  101814 MW;  05303293B93F10D8 CRC64;
     MSQESYDHTA VEKRWQEAWD DASVYRTPDE VDDPTYVLGM YPYPSGKLHM GHVRNYTITD
     AYARYRRMRG DDVLHPMGWD AFGLPAENAA KERDTNPRDW TFDCIDTMKG QMQSMGFGYD
     WDREVTTCTP DYYQWNQWLF RRFHEAGLVE RRDAEVNWCP SCETVLADEQ VEGDDELCWR
     CDTPVETRDL DQWFLEITEY ADELLEAIDG LAGWPDSVRQ MQRNWIGRQH GTTLDFEVSE
     ARSASNGRGE GTDPREYGPV EAFTTRVDTI HGATFFALAP DHPISEELAE SDADVRHFIE
     EEADPEGDEP NGVATGLTAT NPVTSEEIPV FVADFVLSDV GTGALMAVPG HDDRDHAFAE
     KMGVEIKPVI APKPEDWDGE TIPDAPDVSE GAFTDDGVVI DSGEYSGLDS ETARERLTED
     IESAETTTQY RLRDWGISRQ RYWGTPIPVV HCDDCGSVLV PEADLPVELP EFINTTGNPL
     DAAEEWKETT CPECGEPATR ETDTMDTFVD SSWYFLRYVS PGAEDVPFDL DRANDWMPVD
     QYVGGIEHAV MHLLYSRFVT KVLADEEGLA HREPFTNLLA QGMVQLEGEK MSKSKGNTVS
     PQRIVDEYGA DTARLFIMQA AQPERDFDWA EEGVKSTHRF LARLTDLVEE YAAGEAETAS
     SDADRDTIDD YVADEVDAAV AIAGAEYDDL TFNVALREAQ DLVGTLRSYR GHADPHPETY
     ERGLDVAVRL LAPVVPHLAE ELWETLDREG FVVEAEWPTA TVDRETVERR RRLVANTRED
     VRDIVEVAGI EDPERIDVVV APDWKYDALS IAIDSDADNL ISELMGEPHI REQGDDAASY
     GQDLQANREA LQETLSGDDE YDALRAASWL IEREFDAPVR VERAADADES VVRKAEPGRP
     AIDIVE
//
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