(data stored in ACNUC7421 zone)

SWISSPROT: C3MF02_SINFN

ID   C3MF02_SINFN            Unreviewed;       354 AA.
AC   C3MF02;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
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:ACP23839.1};
GN   OrderedLocusNames=NGR_c00350 {ECO:0000313|EMBL:ACP23839.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23839.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23839.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + L-tryptophan + tRNA(Trp) = AMP +
CC       diphosphate + L-tryptophyl-tRNA(Trp). {ECO:0000256|HAMAP-
CC       Rule:MF_00140, ECO:0000256|SAAS:SAAS00671774}.
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; CP001389; ACP23839.1; -; Genomic_DNA.
DR   RefSeq; WP_012706624.1; NC_012587.1.
DR   RefSeq; YP_002824592.1; NC_012587.1.
DR   ProteinModelPortal; C3MF02; -.
DR   STRING; 394.NGR_c00350; -.
DR   EnsemblBacteria; ACP23839; ACP23839; NGR_c00350.
DR   GeneID; 7790614; -.
DR   KEGG; rhi:NGR_c00350; -.
DR   PATRIC; fig|394.7.peg.2825; -.
DR   eggNOG; ENOG4105C31; Bacteria.
DR   eggNOG; COG0180; LUCA.
DR   HOGENOM; HOG000059940; -.
DR   KO; K01867; -.
DR   OMA; RKDDPGH; -.
DR   OrthoDB; POG091H00I9; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
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; C3MF02.
DR   SWISS-2DPAGE; C3MF02.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671783,
KW   ECO:0000313|EMBL:ACP23839.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00140,
KW   ECO:0000256|RuleBase:RU363036, ECO:0000256|SAAS:SAAS00671772};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
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:ACP23839.1};
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:UP000001054}.
FT   MOTIF        14     22       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   MOTIF       217    221       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00140}.
FT   BINDING     220    220       ATP. {ECO:0000256|HAMAP-Rule:MF_00140}.
SQ   SEQUENCE   354 AA;  39147 MW;  00595C56C325A556 CRC64;
     MNEFKPLVFS GVQPTGNLHL GNYLGAIRKF VALQENNDCI YCVVDLHSIT AQLVHEDLPG
     QIRSIAAAFV ASGIDPEKHI VFNQSAVPQH AELAWIFNCV ARIGWMNRMT QFKDKAGKDR
     ENASLGLLAY PSLMAADILV YRATHVPVGD DQKQHLELTR DIAQKFNIDF MEHIRARGCG
     VDIVVGEEPI HAYFPPVEPL IGGPAPRVMS LRDGTKKMSK SDPSDLSRIN LMDDAETIAK
     KIRKAKTDPD ALPSEVEGLQ GRPEAENLVG IYAALSDRTK QEVLAEFGGQ QFSVFKPALI
     DLAVDVLSPI TGEMRRLMDD TAHIDAILRS GGERARARAE KTMREVREII GFLQ
//

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