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 08-NOV-2023, entry version 110. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:0070007; F:glutamic-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd13425; Peptidase_G1_like; 1. DR Gene3D; 2.60.120.700; Peptidase G1; 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:SF1; ASPERGILLOPEPSIN, PUTAITVE (AFU_ORTHOLOGUE AFUA_7G01200); 1. DR PANTHER; PTHR37536; PUTATIVE (AFU_ORTHOLOGUE AFUA_3G02970)-RELATED; 1. DR Pfam; PF01828; Peptidase_A4; 1. DR PRINTS; PR00977; SCYTLDPTASE. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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 //