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C5A5P1 (C5A5P1_THEGJ) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Proline--tRNA ligase HAMAP-Rule MF_01571

EC=6.1.1.15 HAMAP-Rule MF_01571
Alternative name(s):
Prolyl-tRNA synthetase HAMAP-Rule MF_01571
Gene names
Name:proS HAMAP-Rule MF_01571 EMBL ACS33553.1
Ordered Locus Names:TGAM_1051 EMBL ACS33553.1
OrganismThermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3) [Complete proteome] [HAMAP] EMBL ACS33553.1
Taxonomic identifier593117 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length483 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-Rule MF_01571

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01571

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01571.

Domain

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

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 3 subfamily. HAMAP-Rule MF_01571

Ontologies

Keywords
   Biological processProtein biosynthesis HAMAP-Rule MF_01571
   Cellular componentCytoplasm HAMAP-Rule MF_01571
   LigandATP-binding HAMAP-Rule MF_01571
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase HAMAP-Rule MF_01571 EMBL ACS33553.1
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: UniProtKB-EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
C5A5P1 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 89A3DA57FD926675

FASTA48356,181
        10         20         30         40         50         60 
MAKVKREKWS NEFSEWYNEL LETAGIIDKR YPVKGMNVWL PYGLKIMRNI EKFIHSEMAR 

        70         80         90        100        110        120 
TGHEEVLFPA LIPETEFQKE AEHIKGFEDE VYWVTHAGLD PLDVRLILRP TSETAMYSMF 

       130        140        150        160        170        180 
SLWIRSHADL PFKVYQIVNV YRYETKHTRP LIRVREISRF FEAHTAHVDF EDAERQIKED 

       190        200        210        220        230        240 
LEIFDRLAKF LALPYVISRR PDWDKFPGAF YSLGAEIMMP DGRTLQIGTM HNYKQNFAKA 

       250        260        270        280        290        300 
YNIQYETETG DHEYVHQTTF GMSERLLAAV IAVHGDDSGM VLPPTIAPIQ VVIVPIPKKD 

       310        320        330        340        350        360 
ANVDVFAYAR EIAEELGKAG FRVHVDERDI RPGRKYYDWE LKGVPLRIEV GPRDVEGRKA 

       370        380        390        400        410        420 
VLARRDTFEK VTVERDAIVE EVKKTLDAIH ENLYQRAKEF LESHIKRVDT IEEAKAVFED 

       430        440        450        460        470        480 
RRGIVEIPWC GDEECGLKME EELDAKMLGT PYPEEKAREG IEGKKCPVCG REAKFIARFA 


RTY 

« Hide

References

[1]"Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea."
Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M., Anthouard V., Forterre P., Wincker P., Confalonieri F.
Genome Biol. 10:R70.1-R70.23(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15229 / JCM 11827 / EJ3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001398 Genomic DNA. Translation: ACS33553.1.
RefSeqYP_002959417.1. NC_012804.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING593117.TGAM_1051.

Proteomic databases

PaxDbC5A5P1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS33553; ACS33553; TGAM_1051.
GeneID7986925.
KEGGtga:TGAM_1051.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0442.
HOGENOMHOG000167538.
KOK01881.
OMAPIQVDIL.
ProtClustDBPRK08661.

Enzyme and pathway databases

BioCycTGAM593117:GHFT-1074-MONOMER.

Family and domain databases

Gene3D3.30.110.30. 1 hit.
3.40.50.800. 1 hit.
HAMAPMF_01571. Pro_tRNA_synth_type3.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002316. Pro-tRNA-ligase_IIa.
IPR004499. Pro-tRNA-ligase_IIa_arc-type.
IPR016061. Pro-tRNA_ligase_II_C.
IPR017449. Pro-tRNA_synth_II.
[Graphical view]
PANTHERPTHR11451:SF6. PTHR11451:SF6. 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. SSF52954. 1 hit.
SSF64586. SSF64586. 1 hit.
TIGRFAMsTIGR00408. proS_fam_I. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC5A5P1_THEGJ
AccessionPrimary (citable) accession number: C5A5P1
Entry history
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)