(data stored in SCRATCH zone)

SWISSPROT: B4STA4_STRM5

ID   B4STA4_STRM5            Unreviewed;       430 AA.
AC   B4STA4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 78.
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   OrderedLocusNames=Smal_0242 {ECO:0000313|EMBL:ACF49947.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49947.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49947.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49947.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF49947.1; -; Genomic_DNA.
DR   RefSeq; WP_004137142.1; NC_011071.1.
DR   STRING; 391008.Smal_0242; -.
DR   EnsemblBacteria; ACF49947; ACF49947; Smal_0242.
DR   KEGG; smt:Smal_0242; -.
DR   eggNOG; ENOG4105C31; Bacteria.
DR   eggNOG; COG0180; LUCA.
DR   HOGENOM; HOG000059939; -.
DR   KO; K01867; -.
DR   OMA; GWGQFKP; -.
DR   OrthoDB; 951354at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01230-MONOMER; -.
DR   Proteomes; UP000001867; 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   InterPro; IPR036913; YegP-like_sf.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   SUPFAM; SSF160113; SSF160113; 1.
DR   TIGRFAMs; TIGR00233; trpS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4STA4.
DR   SWISS-2DPAGE; B4STA4.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671783,
KW   ECO:0000313|EMBL:ACF49947.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671772};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
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:ACF49947.1};
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}.
FT   NP_BIND      10     12       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   NP_BIND      18     19       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   NP_BIND     155    157       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   NP_BIND     202    206       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   MOTIF        11     19       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   MOTIF       202    206       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   BINDING     143    143       L-tryptophan. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   BINDING     195    195       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
SQ   SEQUENCE   430 AA;  47657 MW;  3F130490F9F8439F CRC64;
     MTTRVLTGIT PSGTPHLGNY VGAIRPAIAA SRAPGIESFF FLADLHSLIK SQDPQRTQRA
     TLEIAASWLA CGLDPEHVWF YRQSDIRETT ELMWFLTAIA SKGILNRAHA YKAAVDKNRE
     EGVDEDAGVS AGLFMYPVLM AADILIFKAN QVPVGRDQIQ HIEMARDFAQ RFNHVYGKEY
     FPLPDVVIDE QVATLAGLDG RKMSKSYHNT IPLFVPREEL KKLVFSILTD SRAPGEPKDT
     EGSALFQMYQ AFATPEQTAE FAKAFAAGIS WGDAKQQLFE RIDSELSPLR ERYNALMAEP
     EKIEALLKRR GQQLREQLAA PLLDELRHAV GLRDLSSAGD IASEDAGVAR VAPPLFKQYR
     EKDGRFYFKL TAGDGTLLIQ SEGFDSPRDA GQLIAVLKQA EQGDQLQSDL FKLDAEVDAV
     LAALAMLREA
//

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