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Q7TV34 (SYW_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tryptophan--tRNA ligase

EC=6.1.1.2
Alternative name(s):
Tryptophanyl-tRNA synthetase
Short name=TrpRS
Gene names
Name:trpS
Ordered Locus Names:PMT_0422
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp). HAMAP-Rule MF_00140

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00140

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00140.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtryptophanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tryptophan-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Tryptophan--tRNA ligase HAMAP-Rule MF_00140
PRO_0000136660

Regions

Motif12 – 209"HIGH" region HAMAP-Rule MF_00140
Motif200 – 2045"KMSKS" region HAMAP-Rule MF_00140

Sites

Binding site2031ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7TV34 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 9489EC59E191CB9E

FASTA33737,323
        10         20         30         40         50         60 
MQRPRVLSGV QPTGALHLGN WLGAIRNWVD LQSSHDTYVC VVDLHAITVP HDPERLAEES 

        70         80         90        100        110        120 
LSTAALYLAC GMDPDLCSIF VQSQVSAHSE LCWLLNCVTP LNWLERMIQF KEKSVKQGDN 

       130        140        150        160        170        180 
VSVGLLDYPV LMAADILLYD ADLVPVGEDQ KQHLELARDI AQQRINARFG SEEKPVLKVP 

       190        200        210        220        230        240 
DPLIIKEGAR VMSLSDGRSK MSKSDPNEGS RITLLDPPEL ITKKIKRAKT DPQMGLQFGN 

       250        260        270        280        290        300 
PDRPEADNLL GIYAILSGRG RDAAAQECAE MGWGTFKPLL ADATVSALEP IQHRYQQLMG 

       310        320        330 
DRIELIRVLD QGRTRAEETA QATLQRVRQA LGFLIAS 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE20597.1.
RefSeqNP_894255.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7TV34.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74547.PMT0422.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE20597; CAE20597; PMT_0422.
GeneID1727667.
KEGGpmt:PMT0422.
PATRIC23008699. VBIProMar135351_0507.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0180.
KOK01867.
OMAGWGQFKP.
OrthoDBEOG686NJQ.
ProtClustDBPRK00927.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00140_B. Trp_tRNA_synth_B.
InterProIPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002306. Trp-tRNA-ligase.
IPR024109. Trp-tRNA-ligase_bac-type.
[Graphical view]
PANTHERPTHR10055. PTHR10055. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01039. TRNASYNTHTRP.
TIGRFAMsTIGR00233. trpS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYW_PROMM
AccessionPrimary (citable) accession number: Q7TV34
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries