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P15369

- PRTB_SCYLI

UniProt

P15369 - PRTB_SCYLI

Protein

Scytalidopepsin B

Gene
N/A
Organism
Scytalidium lignicola (Hyphomycete)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 2 (26 Sep 2003)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei107 – 1071Transition state stabilizer
    Active sitei190 – 1901Proton acceptor1 Publication

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Protein family/group databases

    MEROPSiG01.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Scytalidopepsin B (EC:3.4.23.32)
    Short name:
    SLB
    Alternative name(s):
    Acid protease B
    OrganismiScytalidium lignicola (Hyphomycete)
    Taxonomic identifieri5539 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesmitosporic LeotiomycetesScytalidium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 54341 PublicationPRO_0000028493Add
    BLAST
    Chaini55 – 260206Scytalidopepsin BPRO_0000028494Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi101 ↔ 1811 Publication
    Disulfide bondi195 ↔ 2191 Publication
    Disulfide bondi248 ↔ 2571 Publication

    Keywords - PTMi

    Disulfide bond, Zymogen

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    260
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi56 – 583
    Beta strandi60 – 667
    Beta strandi70 – 789
    Beta strandi81 – 9616
    Beta strandi98 – 1003
    Beta strandi105 – 11410
    Beta strandi118 – 12710
    Beta strandi129 – 1313
    Beta strandi142 – 15110
    Beta strandi154 – 1618
    Turni162 – 1654
    Beta strandi166 – 1727
    Beta strandi184 – 1907
    Beta strandi193 – 1953
    Turni197 – 2004
    Beta strandi202 – 2043
    Beta strandi209 – 2124
    Beta strandi214 – 22310
    Beta strandi226 – 2283
    Helixi230 – 2323
    Beta strandi234 – 2363
    Beta strandi246 – 2516
    Beta strandi254 – 2596

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S2BX-ray2.10A55-260[»]
    1S2KX-ray2.00A55-260[»]
    2IFRX-ray1.95A55-260[»]
    2IFWX-ray2.30A/B55-260[»]
    ProteinModelPortaliP15369.
    SMRiP15369. Positions 55-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15369.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase G1 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR000250. Peptidase_G1.
    [Graphical view]
    PfamiPF01828. Peptidase_A4. 1 hit.
    [Graphical view]
    PRINTSiPR00977. SCYTLDPTASE.
    SUPFAMiSSF49899. SSF49899. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15369-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFTTAAVLS ALVSAEIAFA APGGNGFARR QARRQARAAG LKASPFRQVN    50
    AKEATVESNW GGAILIGSDF DTVSATANVP SASGGSSAAG TAWVGIDGDT 100
    CQTAILQTGF DWYGDGTYDA WYEWYPEVSD DFSGITISEG DSIQMSVTAT 150
    SDTSGSATLE NLTTGQKVSK SFSNESSGSL CRTNAEFIIE DFEECNSNGS 200
    DCEFVPFASF SPAVEFTDCS VTSDGESVSL DDAQITQVII NNQDVTDCSV 250
    SGTTVSCSYV 260
    Length:260
    Mass (Da):27,165
    Last modified:September 26, 2003 - v2
    Checksum:iD73852833694C6E0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 919SGGSSAAGT → TGASGGSSA AA sequence (PubMed:6370989)Curated
    Sequence conflicti179 – 1791Missing AA sequence (PubMed:6370989)Curated
    Sequence conflicti198 – 1981N → D AA sequence (PubMed:6370989)Curated
    Sequence conflicti202 – 2021Missing AA sequence (PubMed:6370989)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB038553 mRNA. Translation: BAA92164.1.
    D83963 Genomic DNA. Translation: BAA12157.1.
    PIRiA28864.
    JC4883.
    JE0300.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB038553 mRNA. Translation: BAA92164.1 .
    D83963 Genomic DNA. Translation: BAA12157.1 .
    PIRi A28864.
    JC4883.
    JE0300.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S2B X-ray 2.10 A 55-260 [» ]
    1S2K X-ray 2.00 A 55-260 [» ]
    2IFR X-ray 1.95 A 55-260 [» ]
    2IFW X-ray 2.30 A/B 55-260 [» ]
    ProteinModelPortali P15369.
    SMRi P15369. Positions 55-260.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi G01.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P15369.

    Family and domain databases

    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR000250. Peptidase_G1.
    [Graphical view ]
    Pfami PF01828. Peptidase_A4. 1 hit.
    [Graphical view ]
    PRINTSi PR00977. SCYTLDPTASE.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiPRTB_SCYLI
    AccessioniPrimary (citable) accession number: P15369
    Secondary accession number(s): Q92333, Q9P962
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: September 26, 2003
    Last modified: October 1, 2014
    This is version 86 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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