Gene_Locus Report

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Gene_locus Report for: deira-DR0165

Deinococcus radiodurans acyl-peptide hydrolase, putative

Relationship
Family|ACPH_Peptidase_S9
Block| X
Position in NCBI Life Tree|Deinococcus radiodurans
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Bacteria: N E > Terrabacteria group: N E > Deinococcus-Thermus: N E > Deinococci: N E > Deinococcales: N E > Deinococcaceae: N E > Deinococcus: N E > Deinococcus radiodurans: N E
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data


Molecular evidence
Database
No mutation
7 structures (e.g. : 5YZM, 5YZN, 5YZO... more)
No kinetic





1 substrate:
Met-Ala-Ala
No inhibitor
1 Genbank : AE001879
>3 Structure links 4 more: 5YZN, 5YZM, 5YZO
1 UniProt : Q9RXY9
1 Interpro : Q9RXY9
1 Prodom : Q9RXY9
1 Pfam : Q9RXY9
1 PIRSF : Q9RXY9
1 SUPERFAM : Q9RXY9
Sequence
Graphical view for this peptide sequence: deira-DR0165
Colored MSA for ACPH_Peptidase_S9 (raw)
MNNSETPAPGPDSLLALAFPSDPQVSPDGKQVAFVLAQISEEDPAKPDKD
FARPRYRSGLWLSEGGAARPLTHAETGRGDSAPRWSPDGQNLAFVRSAGE
VKAALMLLPLKGGEARRVTHFKNGVSGPQWSPDGRFIAFTTTADTEDKRD
ERGEARVLTRPVYRANGADWLPERPAALWLYDVEADKLREWYAPEIGIGA
LSWWPDSRGVLIVQSEDEWQASQWRQDVYDLPLPTADAPAAPQKLLDWNS
AAHGLAPHPDGQRFALIGRPAGKGNTEHAHLYLIENGQHRRLDTGHDHPV
GDAVGGDCHVGAFPEGPRWLDGDTLLFSSTVRGSVGLFTAHIGGGVKAYD
HDPQGVISAFTANEHGVALIRESATRFPEVELNGQRVTDLHARFPFPVRE
PQRVTFETELGEGEGWVLLPEGEQKVPALLNIHGGPHTDYGHGFTHEFQL
MAARGYGVCYSNPRGSVGYGQAWVDAIYGRWGTVDADDLLNFFDRCLEAV
PRLDAAKTAVMGGSYGGFMTNWITGHTTRFQAAITDRCISNLISFGGTSD
IGLRFWDDELGLDFSRRADALKLWDLSPLQYVENVKTPTLIVHSVLDHRC
PVEQAEQWYAALHKHQVPVRFVRFPEENHELSRSGRPDRRLTRLNEYFAW
LERWL
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MNNSETPAPGPDSLLALAFPSDPQVSPDGKQVAFVLAQISEEDPAKPDKD
FARPRYRSGLWLSEGGAARPLTHAETGRGDSAPRWSPDGQNLAFVRSAGE
VKAALMLLPLKGGEARRVTHFKNGVSGPQWSPDGRFIAFTTTADTEDKRD
ERGEARVLTRPVYRANGADWLPERPAALWLYDVEADKLREWYAPEIGIGA
LSWWPDSRGVLIVQSEDEWQASQWRQDVYDLPLPTADAPAAPQKLLDWNS
AAHGLAPHPDGQRFALIGRPAGKGNTEHAHLYLIENGQHRRLDTGHDHPV
GDAVGGDCHVGAFPEGPRWLDGDTLLFSSTVRGSVGLFTAHIGGGVKAYD
HDPQGVISAFTANEHGVALIRESATRFPEVELNGQRVTDLHARFPFPVRE
PQRVTFETELGEGEGWVLLPEGEQKVPALLNIHGGPHTDYGHGFTHEFQL
MAARGYGVCYSNPRGSVGYGQAWVDAIYGRWGTVDADDLLNFFDRCLEAV
PRLDAAKTAVMGGSYGGFMTNWITGHTTRFQAAITDRCISNLISFGGTSD
IGLRFWDDELGLDFSRRADALKLWDLSPLQYVENVKTPTLIVHSVLDHRC
PVEQAEQWYAALHKHQVPVRFVRFPEENHELSRSGRPDRRLTRLNEYFAW
LERWL


References
    Title: Carboxypeptidase in prolyl oligopeptidase family: Unique enzyme activation and substrate-screening mechanisms
    Yadav P, Goyal VD, Gaur NK, Kumar A, Gokhale SM, Jamdar SN, Makde RD
    Ref: Journal of Biological Chemistry, 294:89, 2019 : PubMed

            

    Title: Expression, purification, crystallization and preliminary X-ray diffraction analysis of acylpeptide hydrolase from Deinococcus radiodurans
    Are VN, Ghosh B, Kumar A, Yadav P, Bhatnagar D, Jamdar SN, Makde RD
    Ref: Acta Crystallographica F Struct Biol Commun, 70:1292, 2014 : PubMed

            

    Title: Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1
    White O, Eisen JA, Heidelberg JF, Hickey EK, Peterson JD, Dodson RJ, Haft DH, Gwinn ML, Nelson WC and Fraser CM <22 more author(s)>
    Ref: Science, 286:1571, 1999 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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