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Reviewed, UniProtKB/Swiss-Prot P15369 (PRTB_SCYLI)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Scytalidopepsin B
      Short name=SLB
    EC=3.4.23.32
Alternative name(s):
    Acid protease B
OrganismScytalidium lignicolum
Taxonomic identifier5539 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotamitosporic AscomycotaScytalidium

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Hydrolysis of proteins with broad specificity, cleaving 24-Phe-|-Phe-25, but not 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 in the B chain of insulin.

Subunit structure

Monomer.

Sequence similarities

Belongs to the peptidase G1 family.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   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 – 2020 Potential
Propeptide21 – 5434 Ref.3
PRO_0000028493
Chain55 – 260206Scytalidopepsin B
PRO_0000028494

Sites

Active site1901Proton acceptor Ref.4
Site1071Transition state stabilizer

Amino acid modifications

Disulfide bond101 ↔ 181 Ref.4
Disulfide bond195 ↔ 219 Ref.4
Disulfide bond248 ↔ 257 Ref.4

Experimental info

Sequence conflict83 – 919SGGSSAAGT → TGASGGSSA AA sequence Ref.3
Sequence conflict1791Missing AA sequence Ref.3
Sequence conflict1981N → D AA sequence Ref.3
Sequence conflict2021Missing AA sequence Ref.3

Secondary structure

........................................... 260
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15369-1 [UniParc].

Last modified September 26, 2003. Version 2.
Checksum: D73852833694C6E0

FASTA26027,165
        10         20         30         40         50         60 
MKFTTAAVLS ALVSAEIAFA APGGNGFARR QARRQARAAG LKASPFRQVN AKEATVESNW 

        70         80         90        100        110        120 
GGAILIGSDF DTVSATANVP SASGGSSAAG TAWVGIDGDT CQTAILQTGF DWYGDGTYDA 

       130        140        150        160        170        180 
WYEWYPEVSD DFSGITISEG DSIQMSVTAT SDTSGSATLE NLTTGQKVSK SFSNESSGSL 

       190        200        210        220        230        240 
CRTNAEFIIE DFEECNSNGS DCEFVPFASF SPAVEFTDCS VTSDGESVSL DDAQITQVII 

       250        260 
NNQDVTDCSV SGTTVSCSYV 

« Hide

References

[1]"Nucleotide sequence of the gene encoding the precursor protein of pepstatin insensitive acid protease B, scytalidopepsin B, from Scytalidium lignicolum."
Oda N., Gotoh Y., Oyama H., Murao S., Oda K., Tsuru D.
Biosci. Biotechnol. Biochem. 62:1637-1639(1998) [PubMed: 9757573] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence of the gene encoding pepstatin-insensitive acid protease B, Scytalidopepsin B, of Scytalidium lignicolum."
Kakimori T., Yoshimoto T., Oyama H., Oda N., Gotoh Y., Oda K., Murao S., Tsuru D.
Biosci. Biotechnol. Biochem. 60:1210-1211(1996) [PubMed: 8782420] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-260.
[3]"Complete amino acid sequence of Scytalidium lignicolum acid protease B."
Maita T., Nagata S., Matsuda G., Maruta S., Oda K., Murao S., Tsuru D.
J. Biochem. 95:465-475(1984) [PubMed: 6370989] [Abstract]
Cited for: PROTEIN SEQUENCE OF 55-260.
[4]"The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum."
Fujinaga M., Cherney M.M., Oyama H., Oda K., James M.N.
Proc. Natl. Acad. Sci. U.S.A. 101:3364-3369(2004) [PubMed: 14993599] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 55-260, ACTIVE SITE, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB038553 mRNA. Translation: BAA92164.1.
D83963 Genomic DNA. Translation: BAA12157.1.
PIRA28864.
JC4883.
JE0300.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1S2BX-ray2.10A55-260[»]
1S2KX-ray2.00A55-260[»]
2IFRX-ray1.95A55-260[»]
2IFWX-ray2.30A/B55-260[»]
ModBaseSearch...

Protein family/group databases

MEROPSG01.001.

Enzyme and pathway databases

BRENDA3.4.23.32. 279702.

Family and domain databases

InterProIPR000250. Peptidase_G1.
[Graphical view]
PfamPF01828. Peptidase_A4. 1 hit.
[Graphical view]
PRINTSPR00977. SCYTLDPTASE.
ProDomPD018627. Peptidase_A4. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry namePRTB_SCYLI
AccessionPrimary (citable) accession number: P15369
Secondary accession number(s): Q92333, Q9P962
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: September 26, 2003
Last modified: June 16, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents