PRTB_SCYLI
ID PRTB_SCYLI Reviewed; 260 AA.
AC P15369; Q92333; Q9P962;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Scytalidopepsin B;
DE Short=SLB;
DE EC=3.4.23.32;
DE AltName: Full=Acid protease B;
DE Flags: Precursor;
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9757573; DOI=10.1271/bbb.62.1637;
RA Oda N., Gotoh Y., Oyama H., Murao S., Oda K., Tsuru D.;
RT "Nucleotide sequence of the gene encoding the precursor protein of
RT pepstatin insensitive acid protease B, scytalidopepsin B, from Scytalidium
RT lignicolum.";
RL Biosci. Biotechnol. Biochem. 62:1637-1639(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-260.
RX PubMed=8782420; DOI=10.1271/bbb.60.1210;
RA Kakimori T., Yoshimoto T., Oyama H., Oda N., Gotoh Y., Oda K., Murao S.,
RA Tsuru D.;
RT "Nucleotide sequence of the gene encoding pepstatin-insensitive acid
RT protease B, Scytalidopepsin B, of Scytalidium lignicolum.";
RL Biosci. Biotechnol. Biochem. 60:1210-1211(1996).
RN [3]
RP PROTEIN SEQUENCE OF 55-260.
RX PubMed=6370989; DOI=10.1093/oxfordjournals.jbchem.a134628;
RA Maita T., Nagata S., Matsuda G., Maruta S., Oda K., Murao S., Tsuru D.;
RT "Complete amino acid sequence of Scytalidium lignicolum acid protease B.";
RL J. Biochem. 95:465-475(1984).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 55-260, ACTIVE SITE, AND DISULFIDE
RP BONDS.
RX PubMed=14993599; DOI=10.1073/pnas.0400246101;
RA Fujinaga M., Cherney M.M., Oyama H., Oda K., James M.N.;
RT "The molecular structure and catalytic mechanism of a novel carboxyl
RT peptidase from Scytalidium lignicolum.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3364-3369(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity, cleaving 24-
CC Phe-|-Phe-25, but not 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 in the B
CC chain of insulin.; EC=3.4.23.32;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the peptidase G1 family. {ECO:0000305}.
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DR EMBL; AB038553; BAA92164.1; -; mRNA.
DR EMBL; D83963; BAA12157.1; -; Genomic_DNA.
DR PIR; A28864; A28864.
DR PIR; JC4883; JC4883.
DR PIR; JE0300; JE0300.
DR PDB; 1S2B; X-ray; 2.10 A; A=55-260.
DR PDB; 1S2K; X-ray; 2.00 A; A=55-260.
DR PDB; 2IFR; X-ray; 1.95 A; A=55-260.
DR PDB; 2IFW; X-ray; 2.30 A; A/B=55-260.
DR PDBsum; 1S2B; -.
DR PDBsum; 1S2K; -.
DR PDBsum; 2IFR; -.
DR PDBsum; 2IFW; -.
DR AlphaFoldDB; P15369; -.
DR SMR; P15369; -.
DR MEROPS; G01.001; -.
DR KEGG; ag:BAA92164; -.
DR BRENDA; 3.4.23.32; 5643.
DR EvolutionaryTrace; P15369; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd13425; Peptidase_G1_like; 1.
DR Gene3D; 2.60.120.700; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000250; Peptidase_G1.
DR InterPro; IPR038656; Peptidase_G1_sf.
DR InterPro; IPR033863; Scytalidoglutamic_peptidase.
DR PANTHER; PTHR37536; PTHR37536; 1.
DR Pfam; PF01828; Peptidase_A4; 1.
DR PRINTS; PR00977; SCYTLDPTASE.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..54
FT /evidence="ECO:0000269|PubMed:6370989"
FT /id="PRO_0000028493"
FT CHAIN 55..260
FT /note="Scytalidopepsin B"
FT /id="PRO_0000028494"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:14993599"
FT SITE 107
FT /note="Transition state stabilizer"
FT DISULFID 101..181
FT /evidence="ECO:0000269|PubMed:14993599"
FT DISULFID 195..219
FT /evidence="ECO:0000269|PubMed:14993599"
FT DISULFID 248..257
FT /evidence="ECO:0000269|PubMed:14993599"
FT CONFLICT 83..91
FT /note="SGGSSAAGT -> TGASGGSSA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 81..96
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:2IFR"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2IFR"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:1S2K"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2IFR"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:2IFW"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:2IFR"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:2IFR"
SQ SEQUENCE 260 AA; 27165 MW; D73852833694C6E0 CRC64;
MKFTTAAVLS ALVSAEIAFA APGGNGFARR QARRQARAAG LKASPFRQVN AKEATVESNW
GGAILIGSDF DTVSATANVP SASGGSSAAG TAWVGIDGDT CQTAILQTGF DWYGDGTYDA
WYEWYPEVSD DFSGITISEG DSIQMSVTAT SDTSGSATLE NLTTGQKVSK SFSNESSGSL
CRTNAEFIIE DFEECNSNGS DCEFVPFASF SPAVEFTDCS VTSDGESVSL DDAQITQVII
NNQDVTDCSV SGTTVSCSYV
