(data stored in SCRATCH zone)

SWISSPROT: Q13EK0_RHOPS

ID   Q13EK0_RHOPS            Unreviewed;       369 AA.
AC   Q13EK0;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 88.
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=RPD_0249 {ECO:0000313|EMBL:ABE37489.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37489.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37489.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37489.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) 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; CP000283; ABE37489.1; -; Genomic_DNA.
DR   STRING; 316057.RPD_0249; -.
DR   EnsemblBacteria; ABE37489; ABE37489; RPD_0249.
DR   KEGG; rpd:RPD_0249; -.
DR   eggNOG; ENOG4105C31; Bacteria.
DR   eggNOG; COG0180; LUCA.
DR   HOGENOM; HOG000059940; -.
DR   KO; K01867; -.
DR   OMA; GWGQFKP; -.
DR   Proteomes; UP000001818; 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; Q13EK0.
DR   SWISS-2DPAGE; Q13EK0.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671783,
KW   ECO:0000313|EMBL:ABE37489.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671772};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
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:ABE37489.1};
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      32     34       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   NP_BIND      40     41       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   NP_BIND     172    174       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   NP_BIND     230    234       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
FT   MOTIF        33     41       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   MOTIF       230    234       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   BINDING     160    160       L-tryptophan. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   BINDING     221    221       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
SQ   SEQUENCE   369 AA;  40227 MW;  970C84297F2816BD CRC64;
     MDGAPNSAIG AAPFDHAQEL NMTTQRVFSG VQPTGNLHLG NYLGAIVNFV KLQETHNCIY
     CVVDLHAITV PVTVWGGPDE LRRNTREVTA AFIAAGIDPN KHIIFNQSQV AEHAELAWVF
     NCVARLGWLN RMTQFKEKAG KDRENASIGL YDYPVLMASD ILVYRATHVP VGEDQKQHLE
     LTRDIAQKFN NDFAESIAAQ GLGDSYFPMP EPVITGPATR VMSLRDGTKK MSKSDPSDYS
     RINLTDDADA IAQKIRKAKT DPEPLPSEEK GLETRPEADN LVGIYAALAG KPKTDVLAEF
     GGAQFSAFKS SLVDLAVEKL SPIAGEMKRL SADHGYVDSV LASGSDRARV IAAETMVGVK
     DIMGMVRKR
//

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