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P00798

- PENP_PENJA

UniProt

P00798 - PENP_PENJA

Protein

Penicillopepsin

Gene
N/A
Organism
Penicillium janthinellum (Penicillium vitale)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei33 – 3311 PublicationPROSITE-ProRule annotation
    Active sitei213 – 21311 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Protein family/group databases

    MEROPSiA01.011.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Penicillopepsin (EC:3.4.23.20)
    Alternative name(s):
    Peptidase A
    OrganismiPenicillium janthinellum (Penicillium vitale)
    Taxonomic identifieri5079 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323PenicillopepsinPRO_0000199515Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi249 ↔ 283

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Helixi12 – 143
    Beta strandi17 – 237
    Beta strandi26 – 338
    Beta strandi39 – 413
    Helixi48 – 514
    Helixi59 – 624
    Beta strandi64 – 7411
    Beta strandi80 – 9213
    Beta strandi95 – 10814
    Helixi110 – 1134
    Beta strandi119 – 1235
    Helixi127 – 1293
    Beta strandi133 – 1353
    Helixi140 – 1445
    Helixi145 – 1473
    Beta strandi148 – 1569
    Beta strandi159 – 1613
    Beta strandi163 – 1697
    Helixi172 – 1743
    Beta strandi175 – 1773
    Beta strandi180 – 1834
    Beta strandi192 – 2009
    Beta strandi203 – 21210
    Beta strandi217 – 2215
    Helixi223 – 2308
    Beta strandi237 – 2393
    Turni240 – 2434
    Beta strandi244 – 2474
    Beta strandi256 – 2605
    Beta strandi263 – 2675
    Helixi269 – 2724
    Beta strandi273 – 2764
    Beta strandi278 – 2814
    Beta strandi283 – 2897
    Beta strandi294 – 2985
    Helixi300 – 3034
    Beta strandi306 – 3116
    Turni312 – 3154
    Beta strandi316 – 3227

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1APTX-ray1.80E1-323[»]
    1APUX-ray1.80E1-323[»]
    1APVX-ray1.80E1-323[»]
    1APWX-ray1.80E1-323[»]
    1BXOX-ray0.95A1-323[»]
    1BXQX-ray1.41A1-323[»]
    1PPKX-ray1.80E1-323[»]
    1PPLX-ray1.70E1-323[»]
    1PPMX-ray1.70E1-323[»]
    2WEAX-ray1.25A1-323[»]
    2WEBX-ray1.50A1-323[»]
    2WECX-ray1.50A1-323[»]
    2WEDX-ray1.50A1-323[»]
    3APPX-ray1.80A1-323[»]
    ProteinModelPortaliP00798.
    SMRiP00798. Positions 1-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00798.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PANTHERiPTHR13683. PTHR13683. 1 hit.
    PfamiPF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00798-1 [UniParc]FASTAAdd to Basket

    « Hide

    AASGVATNTP TANDEEYITP VTIGGTTLNL NFDTGSADLW VFSTELPASQ    50
    QSGHSVYNPS ATGKELSGYT WSISYGDGSS ASGNVFTDSV TVGGVTAHGQ 100
    AVQAAQQISA QFQQDTNNDG LLGLAFSSIN TVQPQSQTTF FDTVKSSLAQ 150
    PLFAVALKHQ QPGVYDFGFI DSSKYTGSLT YTGVDNSQGF WSFNVDSYTA 200
    GSQSGDGFSG IADTGTTLLL LDDSVVSQYY SQVSGAQQDS NAGGYVFDCS 250
    TNLPDFSVSI SGYTATVPGS LINYGPSGDG STCLGGIQSN SGIGFSIFGD 300
    IFLKSQYVVF DSDGPQLGFA PQA 323
    Length:323
    Mass (Da):33,461
    Last modified:July 15, 1998 - v2
    Checksum:iB4124268364CBA3B
    GO

    Sequence databases

    PIRiA00991. PEPLBJ.

    Cross-referencesi

    Sequence databases

    PIRi A00991. PEPLBJ.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1APT X-ray 1.80 E 1-323 [» ]
    1APU X-ray 1.80 E 1-323 [» ]
    1APV X-ray 1.80 E 1-323 [» ]
    1APW X-ray 1.80 E 1-323 [» ]
    1BXO X-ray 0.95 A 1-323 [» ]
    1BXQ X-ray 1.41 A 1-323 [» ]
    1PPK X-ray 1.80 E 1-323 [» ]
    1PPL X-ray 1.70 E 1-323 [» ]
    1PPM X-ray 1.70 E 1-323 [» ]
    2WEA X-ray 1.25 A 1-323 [» ]
    2WEB X-ray 1.50 A 1-323 [» ]
    2WEC X-ray 1.50 A 1-323 [» ]
    2WED X-ray 1.50 A 1-323 [» ]
    3APP X-ray 1.80 A 1-323 [» ]
    ProteinModelPortali P00798.
    SMRi P00798. Positions 1-323.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P00798.
    ChEMBLi CHEMBL4254.

    Protein family/group databases

    MEROPSi A01.011.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P00798.

    Family and domain databases

    Gene3Di 2.40.70.10. 2 hits.
    InterProi IPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    PANTHERi PTHR13683. PTHR13683. 1 hit.
    Pfami PF00026. Asp. 1 hit.
    [Graphical view ]
    PRINTSi PR00792. PEPSIN.
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and refinement of penicillopepsin at 1.8-A resolution."
      James M.N.G., Sielecki A.R.
      J. Mol. Biol. 163:299-361(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    2. "Amino acid sequence around the active site aspartic acid in penicillopepsin."
      Sodek J., Hofmann T.
      Can. J. Biochem. 48:1014-1016(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE.
    3. Ding J., Fraser M.E., Meyer J.H., Bartlett P.A., James M.N.G.
      Submitted (JUL-1997) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS).
    4. "Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes."
      Khan A.R., Parrish J.C., Fraser M.E., Smith W.W., Bartlett P.A., James M.N.G.
      Biochemistry 37:16839-16845(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS).

    Entry informationi

    Entry nameiPENP_PENJA
    AccessioniPrimary (citable) accession number: P00798
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 92 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

    The sequence shown is derived from the best amino acid sequence data as modified by the X-ray data.Curated

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3