(data stored in SCRATCH zone)

SWISSPROT: D3UY25_XENBS

ID   D3UY25_XENBS            Unreviewed;       344 AA.
AC   D3UY25;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 61.
DE   RecName: Full=Tryptophan--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00140};
DE            EC=6.1.1.2 {ECO:0000256|HAMAP-Rule:MF_00140};
DE   AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00140};
DE            Short=TrpRS {ECO:0000256|HAMAP-Rule:MF_00140};
GN   Name=trpS {ECO:0000256|HAMAP-Rule:MF_00140,
GN   ECO:0000313|EMBL:CBJ79203.1};
GN   OrderedLocusNames=XBJ1_0052 {ECO:0000313|EMBL:CBJ79203.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79203.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79203.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79203.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp).
CC       {ECO:0000256|HAMAP-Rule:MF_00140}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+)
CC         + L-tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-
CC         COMP:9671, Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57912,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78535, ChEBI:CHEBI:456215;
CC         EC=6.1.1.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00140,
CC         ECO:0000256|SAAS:SAAS01117870};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00140}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00140,
CC       ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671786}.
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DR   EMBL; FN667741; CBJ79203.1; -; Genomic_DNA.
DR   RefSeq; WP_012986676.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0052; -.
DR   EnsemblBacteria; CBJ79203; CBJ79203; XBJ1_0052.
DR   GeneID; 8829680; -.
DR   KEGG; xbo:XBJ1_0052; -.
DR   PATRIC; fig|406818.4.peg.45; -.
DR   eggNOG; ENOG4105C31; Bacteria.
DR   eggNOG; COG0180; LUCA.
DR   HOGENOM; HOG000059940; -.
DR   KO; K01867; -.
DR   OMA; GWGQFKP; -.
DR   BioCyc; XBOV406818:XBJ1_RS00240-MONOMER; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00806; TrpRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00140_B; Trp_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002306; Trp-tRNA-ligase.
DR   InterPro; IPR024109; Trp-tRNA-ligase_bac-type.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   TIGRFAMs; TIGR00233; trpS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UY25.
DR   SWISS-2DPAGE; D3UY25.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671783,
KW   ECO:0000313|EMBL:CBJ79203.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671772};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671773,
KW   ECO:0000313|EMBL:CBJ79203.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671767};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671771};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   NP_BIND      21     23       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   NP_BIND      29     30       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   NP_BIND     157    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   NP_BIND     205    209       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   MOTIF        22     30       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   MOTIF       205    209       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   BINDING     145    145       L-tryptophan. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   BINDING     196    196       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
SQ   SEQUENCE   344 AA;  38284 MW;  75CF4C77D7ACC765 CRC64;
     MNEPTVMKPN SQKPIVFSGA QPSGELTIGN YMGALRQWVK MQDEYDCIYC IVNQHAITVR
     QDPNELKKRT LDTLALYLAC GIDPKKSTIF VQSHVPQHSQ LSWVLNCYTY FGELGRMTQF
     KDKSARHAEN INAGLFSYPV LMAADILLYQ ANQIPVGIDQ KQHLELSRDL AQRFNAIYGD
     IFTVPEPFIP TGGAKVMSLQ DPAKKMSKSD DNCNNVIALL EDPKSVAKKI KRAVTDSEDP
     PRVRYDLENK PGVSNLLDIL SGVTGKTIAE LEAEFEGKMY GHLKGAVADA VSEMLTDLQE
     RYHHFRNDEA LLNQIMAEGA AKAQARAQAT LDKIYDAVGL LAHP
//

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