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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)DescriptionActionsGraphical viewLength
Active sitei33PROSITE-ProRule annotation1 Publication1
Active sitei213PROSITE-ProRule annotation1 Publication1

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4254.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001995151 – 323PenicillopepsinAdd BLAST323

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi249 ↔ 283

Keywords - PTMi

Disulfide bond

Interactioni

Chemistry databases

BindingDBiP00798.

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi12 – 14Combined sources3
Beta strandi17 – 23Combined sources7
Beta strandi26 – 33Combined sources8
Beta strandi39 – 41Combined sources3
Helixi48 – 51Combined sources4
Helixi59 – 62Combined sources4
Beta strandi64 – 74Combined sources11
Beta strandi80 – 92Combined sources13
Beta strandi95 – 108Combined sources14
Helixi110 – 113Combined sources4
Beta strandi119 – 123Combined sources5
Helixi127 – 129Combined sources3
Beta strandi133 – 135Combined sources3
Helixi140 – 144Combined sources5
Helixi145 – 147Combined sources3
Beta strandi148 – 156Combined sources9
Beta strandi159 – 161Combined sources3
Beta strandi163 – 169Combined sources7
Helixi172 – 174Combined sources3
Beta strandi175 – 177Combined sources3
Beta strandi180 – 183Combined sources4
Beta strandi192 – 200Combined sources9
Beta strandi203 – 212Combined sources10
Beta strandi217 – 221Combined sources5
Helixi223 – 230Combined sources8
Beta strandi237 – 239Combined sources3
Turni240 – 243Combined sources4
Beta strandi244 – 247Combined sources4
Beta strandi256 – 260Combined sources5
Beta strandi263 – 267Combined sources5
Helixi269 – 272Combined sources4
Beta strandi273 – 276Combined sources4
Beta strandi278 – 281Combined sources4
Beta strandi283 – 289Combined sources7
Beta strandi294 – 298Combined sources5
Helixi300 – 303Combined sources4
Beta strandi306 – 311Combined sources6
Turni312 – 315Combined sources4
Beta strandi316 – 322Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00798.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 320Peptidase A1PROSITE-ProRule annotationAdd BLAST304

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
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.
PS51767. PEPTIDASE_A1. 1 hit.
[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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

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_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
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.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 101 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

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 one 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.