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Q3IS99 (SYP_NATPD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:NP1796A
OrganismNatronomonas pharaonis (strain DSM 2160 / ATCC 35678) [Complete proteome] [HAMAP]
Taxonomic identifier348780 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeNatronomonas

Protein attributes

Sequence length482 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 – 482482Proline--tRNA ligase HAMAP MF_01571
PRO_0000249166

Sequences

Sequence LengthMass (Da)Tools
Q3IS99 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 615F741B85F9EF52

FASTA48254,269
        10         20         30         40         50         60 
MTDQELGITE SKEHNPGEWY AEVVQKAGLA DYAPMGGFIV TRPRGYALWE RLQDHLDGWF 

        70         80         90        100        110        120 
KETGVQNTYF PMFIPESYLE REKDIVDGFD PEVAWVTHGG HDELEERLAV RPTSESIITP 

       130        140        150        160        170        180 
FIAEWVRSYR DLPLRVNQWC SVVRWEATET KPFFRTKEFL WQEGHTAHAT EESAWDETMT 

       190        200        210        220        230        240 
RLEQYERLYE EVMAIPGMTG RKPEHDKFPG ADTTTTIEAL MPDGKSVQAG TSHYLGTSFA 

       250        260        270        280        290        300 
EAFDIEYTDE DETKQTAHTT SWGLSWRALG ALIMTHSDDQ GLVIPPALAP TQVVVVPIWQ 

       310        320        330        340        350        360 
ADTEEAVKEY AADLAAELDE QFRVELDDRD ERNPGFKFNE HELQGVPLRI EIGPNEVEDE 

       370        380        390        400        410        420 
AATLVHRPDG ESDVAERESI TDAVDEALET VYAKLYASAE ATLEENIRKA HGRGEILGTL 

       430        440        450        460        470        480 
GQHGGYVKTG WCGDEACEAE IKDEIAAEIV MLPLDEDEPP VYDTCGVCGD EATETAYFAK 


SY 

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References

[1]"Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis."
Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., Oesterhelt D.
Genome Res. 15:1336-1343(2005) [PubMed: 16169924] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2160 / ATCC 35678.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR936257 Genomic DNA. Translation: CAI48989.1.
RefSeqYP_326554.1. NC_007426.1.

3D structure databases

ProteinModelPortalQ3IS99.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3IS99.

Proteomic databases

PRIDEQ3IS99.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3703057.
GenomeReviewsGene locus NP1796A in contig CR936257_GR.
KEGGnph:NP1796A.
NMPDRfig|348780.3.peg.1093.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04466.
HOGENOMHBG334108.
OMAKFAEYEL.
PhylomeDBQ3IS99.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycNPHA348780:NP1796A-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. 1 hit.
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_NATPD
AccessionPrimary (citable) accession number: Q3IS99
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: November 8, 2005
Last modified: January 25, 2012
This is version 47 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