SYL_PROMP
ID SYL_PROMP Reviewed; 858 AA.
AC Q7V1I2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=PMM0889;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
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:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; BX548174; CAE19348.1; -; Genomic_DNA.
DR RefSeq; WP_011132522.1; NC_005072.1.
DR AlphaFoldDB; Q7V1I2; -.
DR SMR; Q7V1I2; -.
DR STRING; 59919.PMM0889; -.
DR EnsemblBacteria; CAE19348; CAE19348; PMM0889.
DR KEGG; pmm:PMM0889; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_3; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001026; 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 Gene3D; 3.40.50.620; -; 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; 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; PTHR43740; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..858
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152065"
FT MOTIF 53..63
FT /note="'HIGH' region"
FT MOTIF 622..626
FT /note="'KMSKS' region"
FT BINDING 625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 858 AA; 99148 MW; 8CE816904876088F CRC64;
MITSENTDNR ATNLYKPSDI EGKWQKIWED DNLYNTDEQA SNKEKFYALS MFPYPSGNLH
MGHVRNYVIT DLIARFQRFQ GKVVLHPMGW DAFGLPAENA AIERGINPDK WTKQNIAHMK
SQLKLLGLSV DWDREFATCD ENYYVWTQFL FLELHKAGLV YQKESEVNWD PIDNTVLANE
QVDSEGKSWR SGAIVEKKLL TQWFLKITDY AEELLQDLEK LNEWPERVKI MQENWIGKSI
GTNINFKIKE FKKEKIQVFT TRPDTLFGVT YLAISVNHPL IKKISDNKIL SKLENLKIYL
QESKDKDQKK IGIPTNLIAI NPINSKEIPI LIASYVLDEY GTGAVMGVPA HDERDFEFAK
INSIDIKQVI IKEKDKITSQ LTNAFTDNGF LINSNNFDGL NNSDAKKHIS EHGERNGWAE
NKIQFRLRDW LISRQRYWGC PIPIIKCTNC GSVPVNKKDI PVRLPNEIKI SSNKINSLGS
NQSWINTTCP KCGNLASRET DTMDTFMCSS WYFLRYPSSK SLTKPFEKEK INKWLPVDQY
VGGVEHAILH LLYARFLTKA LRDNNLFDID EPFKRLLTQG MVQSAAYKNS ITGKYISPTD
IKDITNPKDP KDNSKLEVLF EKMSKSKYNG IDPESVIKKY GADTARMFIL FKAPPEKDLE
WGDSDVEGQY RFLCRIWKLF LDYSNNDITH EADKLKKENE SSLLKSINIA IKEISNDIKN
NQFNTAISEL MKFYNSISSN LNYVNKDLRR ESLMKFCILL APFAPHISDE IWHLIGNSKS
VHLEKWPVFD EDALKENSFE LVIQINGKVR DKINVEINIS DDEIKEKTLI RPNVKKWIDN
KTIRKIIIVK GRIINIVV