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Q5G935 (Q5G935_9ARCH) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 28. 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 names
EC=3.1.1.1 EMBL AAW62260.1
Organismuncultured archaeon EMBL AAW62260.1
Taxonomic identifier115547 [NCBI]
Taxonomic lineageArchaeaenvironmental samples

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Ontologies

Keywords
   Molecular functionHydrolase EMBL AAW62260.1
   Technical term3D-structure PDB 2C7B
Gene Ontology (GO)
   Molecular_functioncarboxylic ester hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q5G935 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: B0F5BC9FA756C15D

FASTA31133,785
        10         20         30         40         50         60 
MPLDPQIKPI LERIRALSIA ASPQELRRQV EEQSRLLTAA VQEPIAETRD VHIPVSGGSI 

        70         80         90        100        110        120 
RARVYFPKKA AGLPAVLYYH GGGFVFGSIE THDHICRRLS RLSDSVVVSV DYRLAPEYKF 

       130        140        150        160        170        180 
PTAVEDAYAA LKWVADRADE LGVDPDRIAV AGDSAGGNLA AVVSILDRNS GEKLVKKQVL 

       190        200        210        220        230        240 
IYPVVNMTGV PTASLVEFGV AETTSLPIEL MVWFGRQYLK RPEEAYDFKA SPLLADLGGL 

       250        260        270        280        290        300 
PPALVVTAEY DPLRDEGELY AYKMKASGSR AVAVRFAGMV HGFVSFYPFV DAGREALDLA 

       310 
AASIRSGLQP S 

« Hide

References

[1]Rhee J.-K., Ahn D.-G., Kim Y.-G., Oh J.-W.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[2]"New thermophilic and thermostable esterase with sequence similarity to the hormone-sensitive lipase family, cloned from a metagenomic library."
Rhee J.K., Ahn D.G., Kim Y.G., Oh J.W.
Appl. Environ. Microbiol. 71:817-825(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties."
Byun J.S., Rhee J.K., Kim N.D., Yoon J., Kim D.U., Koh E., Oh J.W., Cho H.S.
BMC Struct. Biol. 7:47-47(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY726780 Genomic DNA. Translation: AAW62260.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C7BX-ray2.30A/B1-311[»]
ProteinModelPortalQ5G935.
SMRQ5G935. Positions 17-310.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR002168. Lipase_GDXG_AS.
[Graphical view]
PfamPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5G935.

Entry information

Entry nameQ5G935_9ARCH
AccessionPrimary (citable) accession number: Q5G935
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2005
Last sequence update: March 1, 2005
Last modified: June 11, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)