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Q18JG3 (SYP_HALWD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:
Proline--tRNA ligase

EC=6.1.1.15
Alternative name(s):
Prolyl-tRNA synthetase
Short name=ProRS
Gene names
Name:proS
Ordered Locus Names:HQ1715A
OrganismHaloquadratum walsbyi (strain DSM 16790) [Complete proteome] [HAMAP]
Taxonomic identifier362976 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloquadratum

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro) By similarity. HAMAP MF_01571

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01571

Subunit structure

Homodimer By similarity. HAMAP MF_01571

Subcellular location

Cytoplasm By similarity HAMAP MF_01571.

Domain

Consists of three domains: the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension By similarity. HAMAP MF_01571

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

proline-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 512512Proline--tRNA ligase HAMAP MF_01571
PRO_0000288418

Sequences

Sequence LengthMass (Da)Tools
Q18JG3 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 6987029E985A1681

FASTA51257,527
        10         20         30         40         50         60 
MSEDQDLGIT QSKIHNTGEW YAEVVQKAEL ANYGPEGMSG FIVTRPRAYG LWERVQSYLD 

        70         80         90        100        110        120 
TRFKQTGVQN AYFPLFIPEG YLEREKEIVE GFDPEVAWVE QAGRNELEER LAVRPTSESI 

       130        140        150        160        170        180 
IAPYLSQWIR SYRDLPLRVN QWTSVVRWEA TETKPFFRTK EFLWQEGHTA HATRADAWAE 

       190        200        210        220        230        240 
TMLRLNQYES TYEDLLAIPV LQGAKPEHDK FPGADTTTTV EALMPDGKSV QGATSHYLGT 

       250        260        270        280        290        300 
EFADAFDITY TDTDETSRVA HTTSWGLSWR ALGALIMTHS DNQGLVLPPT VAPEQVVIVP 

       310        320        330        340        350        360 
IWQTETKERV LEYAEDVANN LDDAGIRVEL DDRDDQNPGF KFNEWELKGV PLRAEIGPDE 

       370        380        390        400        410        420 
ATEGTVTLIH RPDGESITAE RSEIVETVQE QFDAVYAKLY AAAEETLNSN IRIAETRSEL 

       430        440        450        460        470        480 
LGTIGQHGGY VKTPWCGDEG CETAIKDEIA AEIVMVPISS DEDDEQDTTD ENMGVNNDTT 

       490        500        510 
VESNEKSLDL TDSTCVVCDN PAFKTAYFAK SY 

« Hide

References

[1]"The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity."
Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D.
BMC Genomics 7:169-169(2006) [PubMed: 16820047] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 16790.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM180088 Genomic DNA. Translation: CAJ51843.1.
RefSeqYP_657483.1. NC_008212.1.

3D structure databases

ProteinModelPortalQ18JG3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ18JG3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4194509.
GenomeReviewsGene locus HQ1715A in contig AM180088_GR.
KEGGhwa:HQ1715A.
NMPDRfig|362976.6.peg.722.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04466.
HOGENOMHBG334108.
OMAYSKWIRG.
PhylomeDBQ18JG3.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycHWAL362976:HQ1715A-MONOMER.

Family and domain databases

HAMAPMF_01571. Pro_tRNA_synth_type3.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002316. Pro-tRNA-synth_IIa.
IPR004499. Pro-tRNA-synth_IIa_arc-type.
IPR017449. Pro-tRNA_synth_II.
IPR016061. Pro-tRNA_synth_II_C.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:3.30.110.30. Pro-tRNA-synth_II_C_arc/euk. 2 hits.
KOK01881.
PANTHERPTHR11451:SF6. ProS_fam_I. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF09180. ProRS-C_1. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
SMARTSM00946. ProRS-C_1. 1 hit.
[Graphical view]
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF64586. Pro-tRNA_synth_II_C. 1 hit.
TIGRFAMsTIGR00408. ProS_fam_I. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_HALWD
AccessionPrimary (citable) accession number: Q18JG3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: July 25, 2006
Last modified: January 25, 2012
This is version 44 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

SIMILARITY comments

Index of protein domains and families