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C3NET8 (SYP_SULIY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 20. 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:YG5714_1565
OrganismSulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1) [Complete proteome] [HAMAP]
Taxonomic identifier439386 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length481 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 – 481481Proline--tRNA ligase HAMAP MF_01571
PRO_1000215580

Sequences

Sequence LengthMass (Da)Tools
C3NET8 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: CD9522617108D6A4

FASTA48155,678
        10         20         30         40         50         60 
MQITRDKWSK NFSEWFDWVL REGEFYDYGR YPVKGMGVWM PYGFKLRQNI ISIIRNLLDS 

        70         80         90        100        110        120 
TGHEEVLFPL LIPEDLLRRE STHIKGFEEE VFWVTKGGSE DLDVKLALRP TSEVAITTME 

       130        140        150        160        170        180 
NLWLKSYKQL PKKYYQIVSV FRYETKATRP MIRLREITTF KEAHTVHETY DDAQRQVEEA 

       190        200        210        220        230        240 
IEIYKKIFNN LAIPYVLSER PEWDRFAGAL HTYAFDTIMP DGKVMQIGTV HHLGQNFSRA 

       250        260        270        280        290        300 
LDFKIQKKDG SLDYPHQTSY GISDRAIASV IAIHGDDHGP ILPPSVAPIK VVVVPIPAKN 

       310        320        330        340        350        360 
EEGTQQVMKY SIEICEMLNK NNITCVTDQD TEKTPGEKFY IWEIKGVPIR LEIGPRELAS 

       370        380        390        400        410        420 
STVFIKRRDN LKSYTVKKEE VVNKVKEVLN EIQEDLRKRA WESLKSRIEY ANDIEKAKNI 

       430        440        450        460        470        480 
LENNSGIVDV PWCGSKECGL KIEELTNARV LGYPIEDRKV NDKCVICKMN AKTVLRVAKT 


Y 

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References

[1]"Biogeography of the Sulfolobus islandicus pan-genome."
Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.
Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009) [PubMed: 19435847] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Y.G.57.14 / Yellowstone #1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001403 Genomic DNA. Translation: ACP45827.1.
RefSeqYP_002837749.1. NC_012622.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGC3NET8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7808049.
GenomeReviewsGene locus YG5714_1565 in contig CP001403_GR.
KEGGsiy:YG5714_1565.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAKFAEYEL.
ProtClustDBPRK08661.

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_SULIY
AccessionPrimary (citable) accession number: C3NET8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: January 25, 2012
This is version 20 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