ID A0A0W0VL86_9GAMM Unreviewed; 404 AA.
AC A0A0W0VL86;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=tryptophan--tRNA ligase {ECO:0000256|ARBA:ARBA00013161};
DE EC=6.1.1.2 {ECO:0000256|ARBA:ARBA00013161};
GN ORFNames=Lisr_1634 {ECO:0000313|EMBL:KTD20844.1};
OS Legionella israelensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=454 {ECO:0000313|EMBL:KTD20844.1, ECO:0000313|Proteomes:UP000054761};
RN [1] {ECO:0000313|EMBL:KTD20844.1, ECO:0000313|Proteomes:UP000054761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bercovier 4 {ECO:0000313|EMBL:KTD20844.1,
RC ECO:0000313|Proteomes:UP000054761};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363036}.
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:KTD20844.1}.
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DR EMBL; LNYH01000095; KTD20844.1; -; Genomic_DNA.
DR RefSeq; WP_058501976.1; NZ_UGOE01000001.1.
DR AlphaFoldDB; A0A0W0VL86; -.
DR STRING; 454.Lisr_1634; -.
DR PATRIC; fig|454.4.peg.1776; -.
DR OrthoDB; 9801042at2; -.
DR Proteomes; UP000054761; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002306; Trp-tRNA-ligase.
DR NCBIfam; TIGR00233; trpS; 1.
DR PANTHER; PTHR43766; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43766:SF1; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR Pfam; PF00579; tRNA-synt_1b; 2.
DR PRINTS; PR01039; TRNASYNTHTRP.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363036};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363036};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363036};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363036};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363036};
KW Reference proteome {ECO:0000313|Proteomes:UP000054761}.
SQ SEQUENCE 404 AA; 46021 MW; 5EE52C1F690E6D83 CRC64;
MSALFTANKR VVSGMRVSGR LHLGHYHGVL KNWVKLQHQY DCFFFAADWH GLTTGYDNPG
FMEEHLWDMV VDWLACGVNP GLSKIFIQSW VPEHAELHLL LSMITPLGWL ERVPSFKDQQ
EKLKEKDLST YGFLGYPLLQ SADVLIYQAD LVPVGEDQVP HIELTREVAR RFNYIYGREH
NFEQLVQEAI KKMGKKNGKI YTELRRQFQQ DGCQESLNTA QALLMNQHNL SMGDKERLLG
FLDGSGKIIL SEPHPLLTEC AKMPGIDGQK MSKSYGNTIM LREPPEQVEK KILTMPTDPA
RVKRTDPGEP EKCPVWDLHK IYSDEETKQW VQIGCRTAGI GCIDCKRPVI EAINEELKPI
QSAIKEYESD ISSVKRIVTE GSDAARDEAQ KTLSTVREVM GLDY
//