Skip Header

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

P43831 (SYQ_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine--tRNA ligase
EC=6.1.1.18
Alternative name(s):
Glutaminyl-tRNA synthetase
Short name=GlnRS
Gene names
Name:glnS
Ordered Locus Names:HI_1354
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus ›

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). HAMAP-Rule 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
Reference 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 – 557557Glutamine--tRNA ligase HAMAP-Rule MF_00126
PRO_0000195837

Regions

Motif42 – 5211"HIGH" region HAMAP-Rule MF_00126
Motif277 – 2815"KMSKS" region HAMAP-Rule MF_00126

Sites

Binding site2801ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P43831 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 4FF1452D57A29F72

FASTA55764,078
        10         20         30         40         50         60 
MMSHTETSLG AENTRTHNFI TQIIDEDLAS GKHKSVHTRF PPEPNGYLHI GHAKSICLNF 

        70         80         90        100        110        120 
GLAKEYQGLC NLRFDDTNPV KEDVEYVDSI KADVEWLGFK WEGEPRYASD YFDALYGYAV 

       130        140        150        160        170        180 
ELIKKGLAYV DELSPDEMRE YRGTLTEPGK NSPYRDRTIE ENLALFEKMK NGEFAEGKAS 

       190        200        210        220        230        240 
LRAKIDMASP FMVMREPVIY RIKFSSHHQT GDKWCIYPMY DFTHCISDAI ERITHSICTL 

       250        260        270        280        290        300 
EFQDNRRLYD WVLENISIER PLPHQYEFSR LNLEGTLTSK RKLLKLVNDE IVDGWNDPRM 

       310        320        330        340        350        360 
PTISGLRRRG YTPASLREFC RRIGVTKQDN VVEYSALEAC IREDLNENAP RAMAVIDPVR 

       370        380        390        400        410        420 
VVIENFESEA VLTAPNHPNR PELGERQLPF TKELYIDRAD FREEANKQYK RLVLGKEVRL 

       430        440        450        460        470        480 
RNAYVIKAER VEKDANGEIT TIFCTYDPET LGKNPADGRK VKGVIHWVSA VNNHPAEFRL 

       490        500        510        520        530        540 
YDRLFTVPNP GAEDDIESVL NPNSLVIKQG FVEQSLANAE AEKGYQFERE GYFCADSKDS 

       550 
RPEHLVFNLT VSLKEGF

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC23001.1.
PIRG64118.
RefSeqNP_439505.1. NC_000907.1.

3D structure databases

ProteinModelPortalP43831.
SMRP43831. Positions 18-555.
ModBaseSearch...

Protein-protein interaction databases

STRING71421.HI1354.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC23001; AAC23001; HI_1354.
GeneID950274.
KEGGhin:HI1354.
PATRIC20191393. VBIHaeInf48452_1407.

Phylogenomic databases

eggNOGCOG0008.
KOK01886.
OMARMPTIAG.
ProtClustDBPRK05347.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
2.40.240.10. 2 hits.
3.40.50.620. 2 hits.
HAMAPMF_00126. Gln_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth_Ib.
IPR022861. Gln_tRNA_ligase_bac.
IPR000924. Glu/Gln-tRNA-synth_Ib.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF50715. Ribosomal_L25rel. 1 hit.
TIGRFAMsTIGR00440. glnS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYQ_HAEIN
AccessionPrimary (citable) accession number: P43831
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents