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P00799 (CARP_RHIMI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Mucorpepsin
EC=3.4.23.23
Alternative name(s):
Mucor rennin
OrganismRhizomucor miehei
Taxonomic identifier4839 [NCBI]
Taxonomic lineageEukaryota › Fungi › Fungi incertae sedis › Basal fungal lineages › Mucoromycotina › Mucorales › Mucoraceae › Rhizomucor

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme, capable of clotting milk is frequently used for cheese production.

Catalytic activity

Hydrolysis of proteins, favoring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen.

Sequence similarities

Belongs to the peptidase A1 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Propeptide23 – 6947Activation peptide
PRO_0000025893
Chain70 – 430361Mucorpepsin Ref.2
PRO_0000025894

Sites

Active site1071 By similarity
Active site3061 By similarity

Amino acid modifications

Glycosylation1481N-linked (GlcNAc...) Ref.2
Glycosylation2571N-linked (GlcNAc...) Ref.2
Disulfide bond120 ↔ 126 Ref.2
Disulfide bond341 ↔ 385 Ref.2

Natural variations

Natural variant2621G → S.

Experimental info

Sequence conflict1361A → T AA sequence Ref.3
Sequence conflict1571N → D AA sequence Ref.3
Sequence conflict163 – 1697Missing AA sequence Ref.3
Sequence conflict2521Missing AA sequence Ref.3
Sequence conflict3761Missing AA sequence Ref.3
Sequence conflict3921D → N AA sequence Ref.3
Sequence conflict3991V → Y AA sequence Ref.3
Sequence conflict4111Missing AA sequence Ref.3

Secondary structure

1 .......................................................................... 430
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00799 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 1431DB2435B71CEF

FASTA43046,168
        10         20         30         40         50         60 
MLFSQITSAI LLTAASLSLT TARPVSKQSE SKDKLLALPL TSVSRKFSQT KFGQQQLAEK 

        70         80         90        100        110        120 
LAGLKPFSEA AADGSVDTPG YYDFDLEEYA IPVSIGTPGQ DFLLLFDTGS SDTWVPHKGC 

       130        140        150        160        170        180 
TKSEGCVGSR FFDPSASSTF KATNYNLNIT YGTGGANGLY FEDSIAIGDI TVTKQILAYV 

       190        200        210        220        230        240 
DNVRGPTAEQ SPNADIFLDG LFGAAYPDNT AMEAEYGSTY NTVHVNLYKQ GLISSPLFSV 

       250        260        270        280        290        300 
YMNTNSGTGE VVFGGVNNTL LGGDIAYTDV MSRYGGYYFW DAPVTGITVD GSAAVRFSRP 

       310        320        330        340        350        360 
QAFTIDTGTN FFIMPSSAAS KIVKAALPDA TETQQGWVVP CASYQNSKST ISIVMQKSGS 

       370        380        390        400        410        420 
SSDTIEISVP VSKMLLPVDQ SNETCMFIIL PDGGNQYIVG NLFLRFFVNV YDFGNNRIGF 

       430 
APLASAYENE

« Hide

References

[1]"Primary structure of Mucor miehei aspartyl protease: evidence for a zymogen intermediate."
Gray G.L., Hayenga K., Cullen D., Wilson L.J., Norton S.
Gene 48:41-53(1986) [PubMed: 3549462] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Primary structure of a precursor to the aspartic proteinase from Rhizomucor miehei shows that the enzyme is synthesized as a zymogen."
Boel E., Bech A.-M., Randrup K., Draeger B., Fiil N.P., Foltmann B.
Proteins 1:363-369(1986) [PubMed: 3329734] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Partial primary structure of Mucor miehei protease."
Bech A.-M., Foltmann B.
Neth. Milk Dairy J. 35:275-280(1981)
Cited for: PROTEIN SEQUENCE OF 70-430.
[4]Foltmann B.
Submitted (NOV-1982) to the PIR data bank
Cited for: SEQUENCE REVISION.
[5]"Crystallization and preliminary X-ray structure solution of Rhizomucor miehei aspartic proteinase."
Jia Z., Vandonselaar M., Schneider P., Quail J.W.
Acta Crystallogr. D 51:243-244(1995) [PubMed: 15299327] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[6]"Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15-A resolution."
Yang J., Teplyakov A., Quail J.W.
J. Mol. Biol. 268:449-459(1997) [PubMed: 9159482] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M18411 mRNA. Translation: AAA33423.1.
M15267 Genomic DNA. Translation: AAA33421.1.
PIRCMUMF. A29039.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ASIX-ray2.15A70-430[»]
2RMPX-ray2.70A70-430[»]
ProteinModelPortalP00799.
SMRP00799. Positions 73-430.
ModBaseSearch...

Protein family/group databases

Allergome3880. Rhi m AP.
MEROPSA01.013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. Pept_Aspartic. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCARP_RHIMI
AccessionPrimary (citable) accession number: P00799
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: November 16, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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