Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q55522 (SYV_SYNY3)

Last modified June 16, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Valyl-tRNA synthetase
    EC=6.1.1.9
Alternative name(s):
    Valine--tRNA ligase
      Short name=ValRS
Gene names
Name: valS
Ordered Locus Names: slr0557
OrganismSynechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP]
Taxonomic identifier1148 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechocystis

Protein attributes

Sequence length910 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a "posttransfer" editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner By similarity.

Catalytic activity

ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). HAMAP MF_02004

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site By similarity.

The C-terminal coiled-coil domain is crucial for aminoacylation activity By similarity.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

protein binding

Inferred from physical interaction. Source: IntAct

valine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

trxAP522311EBI-862103,EBI-862916

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 910910Valyl-tRNA synthetase HAMAP MF_02004
PRO_0000106237

Regions

Coiled coil845 – 90965 Potential
Motif46 – 5611"HIGH" region HAMAP MF_02004
Motif539 – 5435"KMSKS" region HAMAP MF_02004

Sites

Binding site5421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q55522-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4D909BCD889BF42E

FASTA910102,737
        10         20         30         40         50         60 
MTTSLPPQYE PTVTEAKWQT AWEESHAFKA DPDRPGEPYC VVIPPPNVTG SLHMGHAFES 

        70         80         90        100        110        120 
SLIDTLVRYH RMRGDNTLWL PGTDHASIAV QTILERQLKA EGKTRDDLGR EKFLERAWQW 

       130        140        150        160        170        180 
KAESGSTIVN QLRRLGVSVD WTRERFTMDE GLSQAVKTAF IKLYEEGLIY RGNYLVNWCP 

       190        200        210        220        230        240 
ASQSAVSDLE VENQEVDGHL WYFRYPLTDG SGELVVATTR PETMLGDTGV AVNPHDERYA 

       250        260        270        280        290        300 
AMVGKTITLP LVNREIPIVA DELVDPEFGT GCVKVTPAHD PNDFVMGQRH NLPFINLLNK 

       310        320        330        340        350        360 
DGSLNENGGD FAGQDRFEAR KNVVQALEAQ GFLVKIEPYR HSVPYGDRGK VPVEPLLSTQ 

       370        380        390        400        410        420 
WFVKIESLAQ NALACLDEDN SPNFVPERWG KVYRDWLVKL KDWCISRQLW WGHQIPAWYV 

       430        440        450        460        470        480 
ISETNGAITD HTPFIVAYDE AEALAKAKAE YGPTVQLQQD PDVLDTWFSS GLWPFSTMGW 

       490        500        510        520        530        540 
PEQTDDLAKY YPTSTLVTGF DIIFFWVARM TMMAGHFTGQ IPFKDVYIHG LVRDENGKKM 

       550        560        570        580        590        600 
SKSANNGIDP LLLINKYGTD ALRYTLIREV AGAGQDISLQ YDRQKDESES VEASRNFANK 

       610        620        630        640        650        660 
LWNAARFVMM NLDGQTPQQL GLAPGEDLEL ADRWILSRLN QVIQQTREQI EDYGLGEAAK 

       670        680        690        700        710        720 
GLYEFIWGDF CDWYIELAKP RLWNKEGGDV GTQRQLVARQ VLAHTLDSII KLLHPFMPHI 

       730        740        750        760        770        780 
TEELWQTLHQ AEGQFLALQA YPTVNQSLVD PALETQFALL IETLRTIRNL RAEAGIKPGA 

       790        800        810        820        830        840 
MVTVILQSEN DQERQTLQLG ETYIRDIGKV ENLQVVSQLP PEQTQAIAGV VDTIQVLIPL 

       850        860        870        880        890        900 
SGLVDLDILR NKIQKTLDKV TKEYESIEKR LSNPGFVNKA PEEVIAGAKE SLNAAAVQRQ 

       910 
MLQERLKMLG 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
DNA Res. 2:153-166(1995) [PubMed: 8590279] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

BA000022 Genomic DNA. Translation: BAA10881.1.
PIRS76034.
RefSeqNP_442810.1.

3D structure databases

HSSPHSSP built from PDB template 1IVS based on UniProtKB P96142.
ModBaseSearch...

Protein-protein interaction databases

IntActQ55522. 2 interactions.

Genome annotation databases

GeneID952772.
GenomeReviewsGene locus slr0557 in contig BA000022_GR.
KEGGsyn:slr0557.
NMPDRfig|1148.1.peg.2911.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ55522.
OMAQ55522. TDQWYVS.

Enzyme and pathway databases

BioCycSSP1148:SLR0557-MON.

Family and domain databases

HAMAPMF_02004.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR014729. Rossmann-like_a/b/a_fold.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR002303. Val-tRNA_synth_Ia.
IPR011321. Val-tRNA_synth_Ia_C.
IPR019754. Val-tRNA_synth_Ia_N.
IPR019499. Val-tRNA_synth_Ia_tRNA-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.287.380. Val-tRNA_synth_Ia_C. 1 hit.
PANTHERPTHR11946:SF5. tRNA-synt_val. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF10458. Val_tRNA-synt_C. 1 hit.
[Graphical view]
PRINTSPR00986. TRNASYNTHVAL.
TIGRFAMsTIGR00422. valS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYV_SYNY3
AccessionPrimary (citable) accession number: Q55522
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents