ID PLMP_GRIFR STANDARD; PRT; 167 AA. AC P81054; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Peptidyl-Lys metalloendopeptidase (EC 3.4.24.20) (MEP) (GFMEP). OS Grifola frondosa (Maitake). OC Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes; OC Agaricales; Schizophyllaceae; Grifola. OX NCBI_TaxID=5627; RN [1] RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY. RX MEDLINE=98043693; PubMed=9374478; DOI=10.1074/jbc.272.48.30032; RA Nonaka T., Dohmae N., Hashimoto Y., Takio K.; RT "Amino acid sequences of metalloendopeptidases specific for acyl- RT lysine bonds from Grifola frondosa and Pleurotus ostreatus fruiting RT bodies."; RL J. Biol. Chem. 272:30032-30039(1997). CC -!- CATALYTIC ACTIVITY: Preferential cleavage in proteins: Xaa-|-Lys CC (in which Xaa may be Pro). CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- MASS SPECTROMETRY: MW=18028; METHOD=MALDI; RANGE=1-167; CC NOTE=Ref.1. CC -!- SIMILARITY: Belongs to the peptidase M35 family. DR PDB; 1G12; X-ray; A=1-167. DR PDB; 1GE5; X-ray; A=1-167. DR PDB; 1GE6; X-ray; A=1-167. DR PDB; 1GE7; X-ray; A/B=1-167. DR MEROPS; M35.004; -. DR InterPro; IPR006025; Pept_M_Zn_BS. DR PROSITE; PS00142; ZINC_PROTEASE; FALSE_NEG. KW 3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; KW Metalloprotease; Zinc. FT DISULFID 5 75 FT DISULFID 77 97 FT METAL 117 117 Zinc (catalytic) (By similarity). FT ACT_SITE 118 118 By similarity. FT METAL 121 121 Zinc (catalytic) (By similarity). FT CARBOHYD 42 42 O-linked (Man); partial. FT STRAND 2 3 FT HELIX 7 33 FT HELIX 39 45 FT HELIX 50 64 FT TURN 65 65 FT HELIX 68 70 FT STRAND 72 74 FT STRAND 84 85 FT TURN 88 89 FT TURN 91 92 FT STRAND 93 96 FT HELIX 98 102 FT TURN 108 109 FT HELIX 111 121 FT HELIX 123 125 FT TURN 126 126 FT STRAND 129 129 FT HELIX 134 144 FT HELIX 146 149 FT TURN 150 151 FT STRAND 152 152 FT HELIX 153 161 SQ SEQUENCE 167 AA; 18044 MW; A372825B68EA55BB CRC64; TYNGCSSSEQ SALAAAASAA QSYVAESLSY LQTHTAATPR YTTWFGSYIS SRHSTVLQHY TDMNSNDFSS YSFDCTCTAA GTFAYVYPNR FGTVYLCGAF WKAPTTGTDS QAGTLVHESS HFTRNGGTKD YAYGQAAAKS LATMDPDKAV MNADNHEYFS ENNPAQS //