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Reviewed, UniProtKB/Swiss-Prot B4EV71 (SYQ_PROMH)

Last modified November 3, 2009. Version 9. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutaminyl-tRNA synthetase
    EC=6.1.1.18
Alternative name(s):
    Glutamine--tRNA ligase
      Short name=GlnRS
Gene names
Name: glnS
Ordered Locus Names: PMI0539
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). HAMAP MF_00126

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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 processglutaminyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

glutamyl-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

glutamine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 555555Glutaminyl-tRNA synthetase HAMAP MF_00126
PRO_1000095498

Regions

Motif34 – 4411"HIGH" region HAMAP MF_00126
Motif268 – 2725"KMSKS" region HAMAP MF_00126

Sites

Binding site2711ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B4EV71-1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: B27A127CA7A29829

FASTA55564,124
        10         20         30         40         50         60 
MNEADARPTN FIRQIIDEDL ATGKHNSVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYQG 

        70         80         90        100        110        120 
KCNLRFDDTN PVKEDVEYIN SIQKDVQWLG FQWDGNVHYS SDYFDQLYQY AIELINKGLA 

       130        140        150        160        170        180 
YVDELSAEEI REYRGTLKEP GKNSPYRSRS VEENLALFEK MRAGGFEEGK ACLRAKIDMA 

       190        200        210        220        230        240 
SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALENITHSLC TLEFQDNRRL 

       250        260        270        280        290        300 
YDWVLDNITI PCHPRQYEFS RLNLEYTVMS KRKLNQLVTE NIVDGWDDPR MPTISGLRRR 

       310        320        330        340        350        360 
GYTAESIREF CQRIGVTKQD NNVEMASLEA CIRDDLNENA PRAMAVIDPV RLVIENMPEG 

       370        380        390        400        410        420 
EEILTAPNHP NKPEMGTREV PFSREIYIDR ADFKEEANRQ YKRLVLGKEV RLRNAYVIKA 

       430        440        450        460        470        480 
ERVEKDEQGE ITTIYCTYDP QTLNKDPADG RKVKGVIHWV SIPHAIPAEI RLYDRLFSVP 

       490        500        510        520        530        540 
NPGAEEDFLS TINPESLVIR QGFVEASLKD AAIEKAYQFE REGYFCADKL STADKLVFNR 

       550 
TVGLRDTWAK ISKQG 

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed: 18375554] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM942759 Genomic DNA. Translation: CAR41300.1.
RefSeqYP_002150309.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6801487.
GenomeReviewsGene locus PMI0539 in contig AM942759_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMARMPTIAG.

Family and domain databases

HAMAPMF_00126.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth_Ic.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ic_codon-bd.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
[Graphical view]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
PANTHERPTHR10119:SF3. GlnS. 1 hit.
PTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
TIGRFAMsTIGR00440. glnS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYQ_PROMH
AccessionPrimary (citable) accession number: B4EV71
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: November 3, 2009
This is version 9 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

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