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B8D5E6 (B8D5E6_DESK1) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Proline--tRNA ligase HAMAP MF_01571
EC=6.1.1.15 HAMAP MF_01571
Alternative name(s):
Prolyl-tRNA synthetase HAMAP MF_01571
Gene names
Name:proS HAMAP MF_01571
Ordered Locus Names:DKAM_1001
OrganismDesulfurococcus kamchatkensis (strain 1221n / DSM 18924) [Complete proteome] [HAMAP]
Taxonomic identifier490899 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Desulfurococcus

Protein attributes

Sequence length479 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. HAMAP MF_01571

Ontologies

Keywords
   Biological processProtein biosynthesis HAMAP MF_01571
   Cellular componentCytoplasm HAMAP MF_01571
   LigandATP-binding HAMAP MF_01571
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase HAMAP MF_01571 EMBL ACL11327.1
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprolyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

proline-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
B8D5E6 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 938210F69EA2CAEB

FASTA47955,399
        10         20         30         40         50         60 
MSIRKSIGID KYENFPEWYQ AVLKEAGVID IRYPVKGMYV WMPYGLKALR LTQRIIVDLL 

        70         80         90        100        110        120 
EKTGHQEAYF PTMVPESVFS REKDFLQGFG GETFIVEGTM TRRFNERLFV RPTSETVMYY 

       130        140        150        160        170        180 
MWNMWIKGRK DLPLKMYQVV NVFRYETKMT HPILRVREIM GFIEAHTAHH SREEAEKQII 

       190        200        210        220        230        240 
EAIGIYKEFF NRLQLPYFIV KTPPWDTFAG AEYNYDFITV MPDGKGLELG SVINLGQKFA 

       250        260        270        280        290        300 
GAFEIKFMDT DGEEKYVYQT CYGVSERVLG AVIGIHGDEV GLFFPPEIAP IQVVIVPIMK 

       310        320        330        340        350        360 
PGEKEILEYA LKIGSMLESH GLRVFIDSDL EHTPGWKYYY WEMKGVPTRI EVGAREVETS 

       370        380        390        400        410        420 
TVTIARRDKR EKQVVRLEEV LETLRKIWSE INEYLRIKGL EHLKKKTIFL PDYLENKGFN 

       430        440        450        460        470 
GLIIAPWDGS KGCAEELEKE TGKNVLGEIV ESPIPLPSPT QYMACSNKAD RYALLGVTY

« Hide

References

[1]"Complete genome sequence of the anaerobic, protein-degrading hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis."
Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V., Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.
J. Bacteriol. 191:2371-2379(2009) [PubMed: 19114480] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001140 Genomic DNA. Translation: ACL11327.1.
RefSeqYP_002428694.1. NC_011766.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB8D5E6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7171620.
GenomeReviewsGene locus DKAM_1001 in contig CP001140_GR.
KEGGdka:DKAM_1001.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG334108.
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.
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 nameB8D5E6_DESK1
AccessionPrimary (citable) accession number: B8D5E6
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: January 25, 2012
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info