Reviewed, UniProtKB/Swiss-Prot P15369 (PRTB_SCYLI)

Names and origin

Protein names	Recommended name:     Scytalidopepsin B       Short name=SLB     EC=3.4.23.32 Alternative name(s):     Acid protease B
Organism	Scytalidium lignicolum
Taxonomic identifier	5539 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › mitosporic Ascomycota › Scytalidium

Protein attributes

Sequence length	260 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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
Domain	Signal
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Propeptide

21 – 54

34

Ref.3

PRO_0000028493

Chain

55 – 260

206

Scytalidopepsin B

PRO_0000028494

Sites

Active site

190

1

Proton acceptor Ref.4

Site

107

1

Transition state stabilizer

Amino acid modifications

Disulfide bond

101 ↔ 181

Ref.4

Disulfide bond

195 ↔ 219

Ref.4

Disulfide bond

248 ↔ 257

Ref.4

Experimental info

Sequence conflict

83 – 91

9

SGGSSAAGT → TGASGGSSA AA sequence Ref.3

Sequence conflict

179

1

Missing AA sequence Ref.3

Sequence conflict

198

1

N → D AA sequence Ref.3

Sequence conflict

202

1

Missing AA sequence Ref.3

Secondary structure

1

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260

Helix Strand Turn

Details...

Beta strand

47 – 49

3

Beta strand

51 – 54

4

Beta strand

56 – 58

3

Beta strand

60 – 66

7

Beta strand

70 – 78

9

Beta strand

81 – 96

16

Beta strand

98 – 101

4

Beta strand

106 – 114

9

Beta strand

118 – 123

6

Beta strand

142 – 151

10

Beta strand

154 – 160

7

Beta strand

162 – 164

3

Beta strand

167 – 172

6

Beta strand

184 – 190

7

Beta strand

193 – 195

3

Beta strand

200 – 204

5

Beta strand

209 – 212

4

Beta strand

214 – 223

10

Beta strand

234 – 236

3

Beta strand

246 – 251

6

Beta strand

254 – 259

6

Sequences

	Sequence		Length	Mass (Da)
	P15369-1 [UniParc]. Last modified September 26, 2003. Version 2. Checksum: D73852833694C6E0	FASTA	260	27,165
	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

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

EMBLGenBankDDBJ

AB038553 mRNA. Translation: BAA92164.1.
D83963 Genomic DNA. Translation: BAA12157.1.

PIR

A28864.
JC4883.
JE0300.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein family/group databases

MEROPS

G01.001.

Enzyme and pathway databases

BRENDA

3.4.23.32. 279702.

Family and domain databases

InterPro

IPR000250. Peptidase_G1.
[Graphical view]

Pfam

PF01828. Peptidase_A4. 1 hit.
[Graphical view]

PRINTS

PR00977. SCYTLDPTASE.

ProDom

PD018627. Peptidase_A4. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

Entry information

Entry name

PRTB_SCYLI

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)