(data stored in ACNUC1104 zone)

SWISSPROT: D3VG54_XENNA

ID   D3VG54_XENNA            Unreviewed;       345 AA.
AC   D3VG54;
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:CBJ88144.1};
GN   OrderedLocusNames=XNC1_0056 {ECO:0000313|EMBL:CBJ88144.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88144.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88144.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
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; FN667742; CBJ88144.1; -; Genomic_DNA.
DR   RefSeq; WP_013183055.1; NC_014228.1.
DR   STRING; 406817.XNC1_0056; -.
DR   EnsemblBacteria; CBJ88144; CBJ88144; XNC1_0056.
DR   KEGG; xne:XNC1_0056; -.
DR   eggNOG; ENOG4105C31; Bacteria.
DR   eggNOG; COG0180; LUCA.
DR   HOGENOM; HOG000059940; -.
DR   KO; K01867; -.
DR   OMA; GWGQFKP; -.
DR   Proteomes; UP000008075; 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; D3VG54.
DR   SWISS-2DPAGE; D3VG54.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671783,
KW   ECO:0000313|EMBL:CBJ88144.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671772};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
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:CBJ88144.1};
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:UP000008075}.
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     206    210       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   MOTIF        22     30       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   MOTIF       206    210       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   BINDING     145    145       L-tryptophan. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   BINDING     197    197       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
SQ   SEQUENCE   345 AA;  38464 MW;  710A6C4349BECF61 CRC64;
     MNEPTEMKLN SQKPIVFSGA QPSGELTIGN YMGALRQWVN MQDDYDCIYC IVNQHAITVR
     QDPSELKKRT LDTLALYLAC GIDPKKSTIF VQSHVPQHSQ LSWVLNCYAY FGELSRMTQF
     KDKSARHAEN INAGLFDYPV LMAADILLYQ ANQIPVGGDQ KQHLELSRDL ALRFNALYGD
     IFTVPEPFIP QGGSARVMSL QDPTKKMSKS DDNRNNVIAL LEDPKSVAKK IKRAVTDSEE
     PPRVHYDLEN KPGVSNLLDI LAGVTGKTVP ELEAEFEGKM YGHLKGAVAD AVSEMLTDLQ
     ERYHHFRNDE ALLNQIMTEG AAKAQARAQA TLDKVYDAVG LLAHP
//

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