Gene_Locus Report

Biblio print

Add to basket

Go to basket

Tree Display

AceDB Schema

XML Display

Feedback

Gene_locus Report for: aspnc-a2qr21

Aspergillus niger (strain CBS 513.88 / FGSC A1513) Endoprotease Endo-Pro-Aspergillus niger

Relationship
Family|Prolylcarboxypeptidase
Block| X
Position in NCBI Life Tree|Aspergillus niger
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Fungi: N E > Dikarya: N E > Ascomycota: N E > saccharomyceta: N E > Pezizomycotina: N E > leotiomyceta: N E > Eurotiomycetes: N E > Eurotiomycetidae: N E > Eurotiales: N E > Aspergillaceae: N E > Aspergillus: N E > Aspergillus niger: N E


Molecular evidence
Database
No mutation
1 structure:
7WAB: Crystal structure of the prolyl endoprotease, PEP, from Aspergillus niger
No kinetic





No Substrate
No inhibitor
1 Genbank : AM270168
1 UniProt : A2QR21
1 Structure : 7WAB
1 UniProt : A2QR21
1 Interpro : A2QR21
1 Prodom : A2QR21
1 Pfam : A2QR21
1 PIRSF : A2QR21
1 SUPERFAM : A2QR21
Sequence
Graphical view for this peptide sequence: aspnc-a2qr21
Colored MSA for Prolylcarboxypeptidase (raw)
MRSFSVVAAASLALSWASLAQAARPRLVPKPISRPASSKSAATTGEAYFE
QLLDHHNPEKGTFSQRYWWSTEYWGGPGSPVVLFNPGEVSADGYEGYLTN
DTLTGVYAQEIQGAVILIEHRYWGDSSPYEVLNAETLQYLTLDQSILDMT
YFAETVKLQFDNSSRSNAQNAPWVMVGGSYSGALTAWTESIAPGTFWAYH
ATSAPVEAIYDFWQYFYPIQQGMAQNCSKDVSLVAEYVDKIGKNGTAKEQ
QELKELFGLGAVEHYDDFAAVLPNGPYLWQDNDFVTGYSSFFQFCDAVEG
VEAGAAVTPGPEGVGLEKALANYANWFNSTILPNYCASYGYWTDEWSVAC
FDSYNASSPIFTDTSVGNPVDRQWEWFLCNEPFFWWQDGAPEGTSTIVPR
LVSASYWQRQCPLYFPEVNGYTYGSAKGKNSATVNSWTGGWDMTRNTTRL
IWTNGQYDPWRDSGVSSTFRPGGPLVSTANEPVQIIPGGFHCSDLYMEDY
YANEGVRKVVDNEVKQIKEWVEEYYA
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

MRSFSVVAAASLALSWASLAQAARPRLVPKPISRPASSKSAATTGEAYFE
QLLDHHNPEKGTFSQRYWWSTEYWGGPGSPVVLFNPGEVSADGYEGYLTN
DTLTGVYAQEIQGAVILIEHRYWGDSSPYEVLNAETLQYLTLDQSILDMT
YFAETVKLQFDNSSRSNAQNAPWVMVGGSYSGALTAWTESIAPGTFWAYH
ATSAPVEAIYDFWQYFYPIQQGMAQNCSKDVSLVAEYVDKIGKNGTAKEQ
QELKELFGLGAVEHYDDFAAVLPNGPYLWQDNDFVTGYSSFFQFCDAVEG
VEAGAAVTPGPEGVGLEKALANYANWFNSTILPNYCASYGYWTDEWSVAC
FDSYNASSPIFTDTSVGNPVDRQWEWFLCNEPFFWWQDGAPEGTSTIVPR
LVSASYWQRQCPLYFPEVNGYTYGSAKGKNSATVNSWTGGWDMTRNTTRL
IWTNGQYDPWRDSGVSSTFRPGGPLVSTANEPVQIIPGGFHCSDLYMEDY
YANEGVRKVVDNEVKQIKEWVEEYYA


References
    Title: Crystal structure and substrate recognition mechanism of the prolyl endoprotease PEP from Aspergillus niger
    Miyazono KI, Kubota K, Takahashi K, Tanokura M
    Ref: Biochemical & Biophysical Research Communications, 591:76, 2022 : PubMed

            

    Title: Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88
    Pel HJ, de Winde JH, Archer DB, Dyer PS, Hofmann G, Schaap PJ, Turner G, de Vries RP, Albang R and Stam H <59 more author(s)>
    Ref: Nat Biotechnol, 25:221, 2007 : 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.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer