LMCPB_LEIME
ID LMCPB_LEIME Reviewed; 443 AA.
AC P36400;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cysteine proteinase B;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=LMCPB; Synonyms=LMCPB2.8;
OS Leishmania mexicana.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5665;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=MNYC/BZ/62/M379;
RX PubMed=1397299; DOI=10.1016/0014-5793(92)81382-v;
RA Souza A.E., Waugh S., Coombs G.H., Mottram J.C.;
RT "Characterization of a multi-copy gene for a major stage-specific cysteine
RT proteinase of Leishmania mexicana.";
RL FEBS Lett. 311:124-127(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MNYC/BZ/62/M379;
RX PubMed=9162063; DOI=10.1074/jbc.272.22.14285;
RA Mottram J.C., Frame M.J., Brooks D.R., Tetley L., Hutchison J.E.,
RA Souza A.E., Coombs G.H.;
RT "The multiple cpb cysteine proteinase genes of Leishmania mexicana encode
RT isoenzymes that differ in their stage regulation and substrate
RT preferences.";
RL J. Biol. Chem. 272:14285-14293(1997).
CC -!- DEVELOPMENTAL STAGE: Primarily expressed in amastigotes.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR EMBL; Z14061; CAA78443.1; -; mRNA.
DR EMBL; Z49962; CAA90236.1; -; Genomic_DNA.
DR PIR; S29245; S29245.
DR PDB; 6P4E; X-ray; 1.35 A; A/B=125-341.
DR PDBsum; 6P4E; -.
DR AlphaFoldDB; P36400; -.
DR SMR; P36400; -.
DR BindingDB; P36400; -.
DR ChEMBL; CHEMBL3821; -.
DR MEROPS; C01.074; -.
DR VEuPathDB; TriTrypDB:LmxM.08.1030a; -.
DR BRENDA; 3.4.22.B5; 2951.
DR SABIO-RK; P36400; -.
DR PHI-base; PHI:6330; -.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR021981; DUF3586.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF12131; DUF3586; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Protease; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..125
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000026382"
FT CHAIN 126..443
FT /note="Cysteine proteinase B"
FT /id="PRO_0000026383"
FT ACT_SITE 150
FT /evidence="ECO:0000250"
FT ACT_SITE 288
FT /evidence="ECO:0000250"
FT ACT_SITE 308
FT /evidence="ECO:0000250"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 147..188
FT /evidence="ECO:0000250"
FT DISULFID 181..226
FT /evidence="ECO:0000250"
FT DISULFID 281..329
FT /evidence="ECO:0000250"
FT CONFLICT 185..186
FT /note="ND -> DN (in Ref. 1; CAA78443)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="D -> S (in Ref. 1; CAA78443)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="M -> V (in Ref. 1; CAA78443)"
FT /evidence="ECO:0000305"
FT CONFLICT 373..374
FT /note="TQ -> RR (in Ref. 1; CAA78443)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="P -> H (in Ref. 1; CAA78443)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="A -> S (in Ref. 1; CAA78443)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="L -> F (in Ref. 1; CAA78443)"
FT /evidence="ECO:0000305"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:6P4E"
FT TURN 132..136
FT /evidence="ECO:0007829|PDB:6P4E"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:6P4E"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:6P4E"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6P4E"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:6P4E"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:6P4E"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6P4E"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:6P4E"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:6P4E"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:6P4E"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:6P4E"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:6P4E"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:6P4E"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:6P4E"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:6P4E"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:6P4E"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:6P4E"
FT STRAND 319..326
FT /evidence="ECO:0007829|PDB:6P4E"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:6P4E"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:6P4E"
SQ SEQUENCE 443 AA; 47728 MW; CF9122C5792B8834 CRC64;
MATSRAALCA VAVVCVVLAA ACAPARAIHV GTPAAALFEE FKRTYGRAYE TLAEEQQRLA
NFERNLELMR EHQARNPHAQ FGITKFFDLS EAEFAARYLN GAAYFAAAKR HAAQHYRKAR
ADLSAVPDAV DWREKGAVTP VKDQGACGSC WAFSAVGNIE GQWYLAGHEL VSLSEQQLVS
CDDMNDGCDG GLMLQAFDWL LQNTNGHLHT EDSYPYVSGN GYVPECSNSS ELVVGAQIDG
HVLIGSSEKA MAAWLAKNGP IAIALDASSF MSYKSGVLTA CIGKQLNHGV LLVGYDMTGE
VPYWVIKNSW GGDWGEQGYV RVVMGVNACL LSEYPVSAHV RESAAPGTST SSETPAPRPV
MVEQVICFDK NCTQGCRKTL IKANECHKNG GGGASMIKCS PQKVTMCTYS NEFCVGGGLC
FETPDGKCAP YFLGSIMNTC HYT
