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Q5G935

- Q5G935_9ARCH

UniProt

Q5G935 - Q5G935_9ARCH

Protein
Submitted name:

Carboxylesterase

Gene
N/A
Organism
uncultured archaeon
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 29 (01 Oct 2014)
      Sequence version 1 (01 Mar 2005)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. carboxylic ester hydrolase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    HydrolaseImported

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    CarboxylesteraseImported (EC:3.1.1.1Imported)
    Organismiuncultured archaeonImported
    Taxonomic identifieri115547 [NCBI]
    Taxonomic lineageiArchaeaenvironmental samples

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C7BX-ray2.30A/B1-311[»]
    ProteinModelPortaliQ5G935.
    SMRiQ5G935. Positions 17-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5G935.

    Family & Domainsi

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR002168. Lipase_GDXG_AS.
    [Graphical view]
    PfamiPF07859. Abhydrolase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS01174. LIPASE_GDXG_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5G935-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLDPQIKPI LERIRALSIA ASPQELRRQV EEQSRLLTAA VQEPIAETRD    50
    VHIPVSGGSI RARVYFPKKA AGLPAVLYYH GGGFVFGSIE THDHICRRLS 100
    RLSDSVVVSV DYRLAPEYKF PTAVEDAYAA LKWVADRADE LGVDPDRIAV 150
    AGDSAGGNLA AVVSILDRNS GEKLVKKQVL IYPVVNMTGV PTASLVEFGV 200
    AETTSLPIEL MVWFGRQYLK RPEEAYDFKA SPLLADLGGL PPALVVTAEY 250
    DPLRDEGELY AYKMKASGSR AVAVRFAGMV HGFVSFYPFV DAGREALDLA 300
    AASIRSGLQP S 311
    Length:311
    Mass (Da):33,785
    Last modified:March 1, 2005 - v1
    Checksum:iB0F5BC9FA756C15D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY726780 Genomic DNA. Translation: AAW62260.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY726780 Genomic DNA. Translation: AAW62260.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C7B X-ray 2.30 A/B 1-311 [» ]
    ProteinModelPortali Q5G935.
    SMRi Q5G935. Positions 17-310.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q5G935.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR002168. Lipase_GDXG_AS.
    [Graphical view ]
    Pfami PF07859. Abhydrolase_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS01174. LIPASE_GDXG_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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).

    Entry informationi

    Entry nameiQ5G935_9ARCH
    AccessioniPrimary (citable) accession number: Q5G935
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 1, 2005
    Last sequence update: March 1, 2005
    Last modified: October 1, 2014
    This is version 29 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported

    External Data

    Dasty 3