Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7V286 (SYW_PROMP) 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:PMM0598
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length338 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 – 338338Tryptophan--tRNA ligase HAMAP-Rule MF_00140
PRO_0000136661

Regions

Motif13 – 219"HIGH" region HAMAP-Rule MF_00140
Motif200 – 2045"KMSKS" region HAMAP-Rule MF_00140

Sites

Binding site2031ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V286 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 03AE06A283DD2A9A

FASTA33838,463
        10         20         30         40         50         60 
MTNKKRILSG VQPTGDLHIG NWLGAINNWV ELQEKHETFL CVVDLHAITT EYDTKQLSKN 

        70         80         90        100        110        120 
TLSTAALYIA CGINPKICSI FVQSQISAHS ELCWILNCMT PINWMERMIQ FKEKSIQQGN 

       130        140        150        160        170        180 
NVSIGLFDYP ILMAADILLY DADYVPVGED QKQHLELAKD IAQQRINAKF GKEENILKIP 

       190        200        210        220        230        240 
QPIIMKKGSK IMSLNDGSKK MSKSDINEGS RINLLDTPEI ITKKIKRAKS DSYMGMEFNN 

       250        260        270        280        290        300 
PERPESRNLL MIYSLLSGKE VSELENDLSQ TGWGTFKKIF TEQIIESLKP IQERYQVLIN 

       310        320        330 
DPHELNKILI QGKEKAEVVA NKTLSRVKSE LGFFEIEK 

« 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: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548174 Genomic DNA. Translation: CAE19057.1.
RefSeqNP_892716.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7V286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59919.PMM0598.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE19057; CAE19057; PMM0598.
GeneID1726704.
KEGGpmm:PMM0598.
PATRIC23031968. VBIProMar68066_0653.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0180.
HOGENOMHOG000059940.
KOK01867.
OMAGWGQFKP.
OrthoDBEOG686NJQ.
ProtClustDBPRK00927.

Enzyme and pathway databases

BioCycPMAR59919:GJMQ-619-MONOMER.

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_PROMP
AccessionPrimary (citable) accession number: Q7V286
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