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P15369 (PRTB_SCYLI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Scytalidopepsin B

Short name=SLB
EC=3.4.23.32
Alternative name(s):
Acid protease B
OrganismScytalidium lignicola (Hyphomycete)
Taxonomic identifier5539 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesmitosporic LeotiomycetesScytalidium

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: 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 – 2020 Potential
Propeptide21 – 5434
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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 55-260, ACTIVE SITE, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

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

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S2BX-ray2.10A55-260[»]
1S2KX-ray2.00A55-260[»]
2IFRX-ray1.95A55-260[»]
2IFWX-ray2.30A/B55-260[»]
ProteinModelPortalP15369.
SMRP15369. Positions 55-260.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSG01.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR008985. ConA-like_lec_gl_sf.
IPR000250. Peptidase_G1.
[Graphical view]
PfamPF01828. Peptidase_A4. 1 hit.
[Graphical view]
PRINTSPR00977. SCYTLDPTASE.
SUPFAMSSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP15369.

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: October 16, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references