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Protein

Penicillopepsin

Gene
N/A
Organism
Penicillium janthinellum (Penicillium vitale)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 – 331PROSITE-ProRule annotation1 Publication
Active sitei213 – 2131PROSITE-ProRule annotation1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.23.20. 4621.

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
AASGVATNTP TANDEEYITP VTIGGTTLNL NFDTGSADLW VFSTELPASQ
60 70 80 90 100
QSGHSVYNPS ATGKELSGYT WSISYGDGSS ASGNVFTDSV TVGGVTAHGQ
110 120 130 140 150
AVQAAQQISA QFQQDTNNDG LLGLAFSSIN TVQPQSQTTF FDTVKSSLAQ
160 170 180 190 200
PLFAVALKHQ QPGVYDFGFI DSSKYTGSLT YTGVDNSQGF WSFNVDSYTA
210 220 230 240 250
GSQSGDGFSG IADTGTTLLL LDDSVVSQYY SQVSGAQQDS NAGGYVFDCS
260 270 280 290 300
TNLPDFSVSI SGYTATVPGS LINYGPSGDG STCLGGIQSN SGIGFSIFGD
310 320
IFLKSQYVVF DSDGPQLGFA PQA
Length:323
Mass (Da):33,461
Last modified:July 15, 1998 - v2
Checksum:iB4124268364CBA3B
GO

Sequence databases

PIRiA00991. PEPLBJ.

Cross-referencesi

Sequence databases

PIRiA00991. PEPLBJ.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Chemistry

BindingDBiP00798.
ChEMBLiCHEMBL4254.

Protein family/group databases

MEROPSiA01.011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.23.20. 4621.

Miscellaneous databases

EvolutionaryTraceiP00798.

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]
ProtoNetiSearch...

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: April 1, 2015
This is version 94 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.