ID D3SSK0_NATMM Unreviewed; 971 AA.
AC D3SSK0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 94.
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 Name=leuS2 {ECO:0000313|EMBL:ADD06845.1};
GN Synonyms=leuS {ECO:0000313|EMBL:ELY28227.1};
GN OrderedLocusNames=Nmag_3295 {ECO:0000313|EMBL:ADD06845.1};
GN ORFNames=C500_13756 {ECO:0000313|EMBL:ELY28227.1};
OS Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS magadii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=547559 {ECO:0000313|EMBL:ADD06845.1, ECO:0000313|Proteomes:UP000001879};
RN [1] {ECO:0000313|Proteomes:UP000001879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC 8861 / NBRC 102185 / NCIMB 2190 / MS3
RC {ECO:0000313|Proteomes:UP000001879};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E.,
RA Maupin-Furlow J.A., Woyke T.;
RT "Complete sequence of chromosome of Natrialba magadii ATCC 43099.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADD06845.1, ECO:0000313|Proteomes:UP000001879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD06845.1}, and ATCC 43099 / DSM
RC 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861 / NBRC 102185 /
RC NCIMB 2190 / MS3 {ECO:0000313|Proteomes:UP000001879};
RX PubMed=22559199; DOI=10.1186/1471-2164-13-165;
RA Siddaramappa S., Challacombe J.F., Decastro R.E., Pfeiffer F., Sastre D.E.,
RA Gimenez M.I., Paggi R.A., Detter J.C., Davenport K.W., Goodwin L.A.,
RA Kyrpides N., Tapia R., Pitluck S., Lucas S., Woyke T., Maupin-Furlow J.A.;
RT "A comparative genomics perspective on the genetic content of the
RT alkaliphilic haloarchaeon Natrialba magadii ATCC 43099T.";
RL BMC Genomics 13:165-165(2012).
RN [3] {ECO:0000313|EMBL:ELY28227.1, ECO:0000313|Proteomes:UP000011543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM
RC 8861 / NBRC 102185 / NCIMB 2190 / MS3
RC {ECO:0000313|Proteomes:UP000011543}, and MS-3
RC {ECO:0000313|EMBL:ELY28227.1};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4] {ECO:0000313|EMBL:ADD06845.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 43099 {ECO:0000313|EMBL:ADD06845.1};
RA Pfeiffer F.;
RL Submitted (SEP-2016) 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};
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; CP001932; ADD06845.1; -; Genomic_DNA.
DR EMBL; AOHS01000043; ELY28227.1; -; Genomic_DNA.
DR RefSeq; WP_004215935.1; NZ_AOHS01000043.1.
DR AlphaFoldDB; D3SSK0; -.
DR STRING; 547559.Nmag_3295; -.
DR PaxDb; 547559-Nmag_3295; -.
DR GeneID; 8826159; -.
DR KEGG; nmg:Nmag_3295; -.
DR PATRIC; fig|547559.17.peg.2722; -.
DR eggNOG; arCOG00807; Archaea.
DR eggNOG; arCOG00808; Archaea.
DR HOGENOM; CLU_004427_0_0_2; -.
DR OrthoDB; 23906at2157; -.
DR Proteomes; UP000001879; Chromosome.
DR Proteomes; UP000011543; Unassembled WGS sequence.
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; 3.
DR Gene3D; 1.10.10.720; leucyl-tRNA synthetase; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 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 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:UP000001879}.
FT DOMAIN 260..455
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 470..662
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 704..823
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 182..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 971 AA; 107500 MW; DB1B220A3B1898D1 CRC64;
MTNQYDHAQV QEFWQYVWER DGVAELPDGA VDPTYVLGMF PYTSGTLHMG HVRNYAITDA
YARYRRLRGD DVLHPMGWDA FGLPAENAAY ERASDPESWT RACIRRMREE LETLGFGYDW
SREITTCEPS YYRWNQWLFK RFHEAGLVEF TGATVNWCPD CETVLADAQV AVDEGGQAVT
ATADEAGDNG DSAGGAHDES NGNAHVHEHS TARVCWRCGT PVEQRELDQW FFTITDYADE
LVDGLDDLDQ WPEGVREIQR NWIGRQEGAR LTFDVSTAAD ESDTAVDVFS TRSETVFGAT
FVAISPEHDL ASELANADED VATFVDQART SAPDTGHAAR DDFSTAGVKT DATAENPHTG
EELPVYVAEY VLADVGTGAV MGVPGHNERD HEFAREHDLP VETVVVPHGH NGTGSDGGVA
TDAPMTGEGT LVLESPADRA SEYDGQPSED VREHLVDDHE AIDPDVTYRL RDWLISRQRY
WGTPIPVVHC EDCGHVLVPD EELPVELPEF VQTTGNPLDA AEEWKETSCP DCGGPAERET
DTMDTFVDSS WYFLRFLSPD LADAPFDTEL ANEWLPVDVY VGGDEHAILH LLYIRFVTRA
LADLGFLDQR EPVERLVSQG TVLYEGEKMS SSSGNVVTPD EYGAETTRLF VLSAAHPEQD
FEWTANDVRG AYDLQQALYS MATEFVDEGE TRVERVSHDE FVDREIDRTI VAARTEFERF
RFHRVVTEVQ ELAGLLRQYR GYDRIHGEVY RRGLLTIAAL ISPLAPHLGE ELWNKLRGDG
LVVEADWPAL ESDPATIESD YQLERRLVET TRADVRDILD VASIDAPDQI DLVVAEPWKY
EVATRLAVSA GELDGDSATG TVDTAGADTI DVGALADEVA VETDVLAEFV ADQRRTDAQH
SSSEGLTASR EQTLLEQAAW LLADEFDVTV SVRSATAVGT EDETADAAAD DVPDADVASR
ARPGKPAIRI Q
//
