SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00798

- PENP_PENJA

UniProt

P00798 - PENP_PENJA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Penicillopepsin
Gene
N/A
Organism
Penicillium janthinellum (Penicillium vitale)
Status
Reviewed - 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 – 3311 Publication
Active sitei213 – 21311 Publication

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB-KW
Complete GO annotation...

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 – 323323Penicillopepsin
PRO_0000199515Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Interactioni

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP00798.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.

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: May 14, 2014
This is version 91 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.

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