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P15369

- PRTB_SCYLI

UniProt

P15369 - PRTB_SCYLI

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Protein

Scytalidopepsin B

Gene
N/A
Organism
Scytalidium lignicola (Hyphomycete)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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 – 2020 Reviewed predictionAdd
BLAST
Propeptidei21 – 5434PRO_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.

Miscellaneous databases

EvolutionaryTraceiP15369.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase G1 family.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 919SGGSSAAGT → TGASGGSSA AA sequence 1 Publication
Sequence conflicti179 – 1791Missing AA sequence 1 Publication
Sequence conflicti198 – 1981N → D AA sequence 1 Publication
Sequence conflicti202 – 2021Missing AA sequence 1 Publication

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: September 3, 2014
This is version 85 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

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