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Q9UY33 (ENDA_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
tRNA-splicing endonuclease

EC=4.6.1.16
Alternative name(s):
tRNA-intron endonuclease
Gene names
Name:endA
Ordered Locus Names:PYRAB16750
ORF Names:PAB1099
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length170 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a stem of 4 bp By similarity. HAMAP-Rule MF_01833

Catalytic activity

PretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus. HAMAP-Rule MF_01833

Subunit structure

Homotetramer; although the tetramer contains four active sites, only two participate in the cleavage. Therefore, it should be considered as a dimer of dimers By similarity.

Sequence similarities

Belongs to the tRNA-intron endonuclease family. Archaeal short subfamily.

Ontologies

Keywords
   Biological processtRNA processing
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtRNA splicing, via endonucleolytic cleavage and ligation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionlyase activity

Inferred from electronic annotation. Source: UniProtKB-KW

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

tRNA-intron endonuclease activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 170170tRNA-splicing endonuclease HAMAP-Rule MF_01833
PRO_0000109475

Sites

Active site1101 By similarity
Active site1161 By similarity
Active site1471 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UY33 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 8D31F2957EBC3442

FASTA17020,360
        10         20         30         40         50         60 
MKKVIEFYLS GDRVYSTREK AINQLYNNRG YGELKGNKLF LSLIEAAYLV ERGWIKVLDE 

        70         80         90        100        110        120 
DRELTFEEIF KLGKRKDEDF DIKYLVYKDL RDRGYIVKSA LKFGSHFRVY RKNAEHSDWL 

       130        140        150        160        170 
IWVLRESEKL SPNDMTARVR VAHGVRKNMV MAIVDEDNDV VYYKIEWIKF 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248288 Genomic DNA. Translation: CAB50579.1.
HE613800 Genomic DNA. Translation: CCE71143.1.
PIRE75017.
RefSeqNP_127349.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9UY33.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB1099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB50579; CAB50579; PAB1099.
GeneID1495972.
KEGGpab:PAB1099.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1676.
HOGENOMHOG000107823.
KOK01170.
OMAALKFGSH.

Family and domain databases

Gene3D3.40.1350.10. 1 hit.
HAMAPMF_01833. EndA_short.
InterProIPR011856. tRNA_endonuc-like_dom.
IPR006677. tRNA_intron_Endonuc_cat-like.
IPR006678. tRNA_intron_Endonuc_N.
IPR006676. tRNA_splic.
IPR016442. tRNA_splic_arch_short.
[Graphical view]
PfamPF01974. tRNA_int_endo. 1 hit.
PF02778. tRNA_int_endo_N. 1 hit.
[Graphical view]
PIRSFPIRSF005285. tRNA_splic_archaea. 1 hit.
SUPFAMSSF53032. SSF53032. 1 hit.
SSF55267. SSF55267. 1 hit.
TIGRFAMsTIGR00324. endA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameENDA_PYRAB
AccessionPrimary (citable) accession number: Q9UY33
Secondary accession number(s): G8ZK36
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families