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Q9Y9G0 (SYP_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. 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:APE_2328
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length485 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 – 485485Proline--tRNA ligase HAMAP MF_01571
PRO_0000249155

Sequences

Sequence LengthMass (Da)Tools
Q9Y9G0 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 8A451465E1C26CC5

FASTA48556,185
        10         20         30         40         50         60 
MLGPPSREKW SSDFPRWFDW VIETAEVYDY GRYPVKGMGV WMPYGFQIRR RVLEVVRGLL 

        70         80         90        100        110        120 
DSTGHEEVLF PLLIPEHLLR RESEHIRGFE GEVYWVTHGG REELDVKLAL RPTSETSITY 

       130        140        150        160        170        180 
METFWIKSYR QLPKKYYQVV SIFRYETKAT RPMIRLREVT TFKEAHTVHE SFEDAERQVL 

       190        200        210        220        230        240 
EAIEVYKAIF DRLLIPYVIS KRPEWDKFAG ALYTIAFDTI MPDGRALQIG TVHHLGQSFT 

       250        260        270        280        290        300 
RAFDFRIQMR DERLDHPWQT SYGVSDRVVA SLIAVHGDDR GLVIPPSVAP IQVVVIPITP 

       310        320        330        340        350        360 
GDEEKRGKVL TYTAKAAEAL EKAGLRVHVD DREWERPGAK FYYWEAKGVP IRVEIGLREA 

       370        380        390        400        410        420 
EQDTLTIARR DTLEKTEVPL GEAGNRIREL MAQIESSMRE RAKSFFGERL LRTESLEEAR 

       430        440        450        460        470        480 
DWVEGRRGIA EIPWCGRESC GLEMEERVNG KVLGTPWPEE PVEEGKRCPL CGRPAVAWIR 


LAKTY 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA81340.1.
PIRD72460.
RefSeqNP_148542.1. NC_000854.2.

3D structure databases

HSSPHSSP built from PDB template 1NJ2 based on UniProtKB O26708.
ProteinModelPortalQ9Y9G0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1445351.
GenomeReviewsGene locus APE_2328 in contig BA000002_GR.
KEGGape:APE_2328.
NMPDRfig|272557.1.peg.1650.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG334108.
OMAKFAEYEL.
PhylomeDBQ9Y9G0.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycAPER272557:APE2328-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_AERPE
AccessionPrimary (citable) accession number: Q9Y9G0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 73 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