Summary for peptidase M12.144: atrolysin C

Summary Alignment Sequences Sequence features Distribution Structure Literature Substrates Inhibitors

 

Names
MEROPS Nameatrolysin C
Other namesCrotalus atrox metalloendopeptidase c
Domain architecture
MEROPS Classification
Classification Clan MA >> Subclan MA(M) >> Family M12 >> Subfamily B >> M12.144
Holotypeatrolysin C (Crotalus atrox), Uniprot accession P15167 (peptidase unit: 191-393), MERNUM MER0001126
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeMetallo
PeplistIncluded in the Peplist with identifier PL00185
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.24 (Metalloendopeptidases) >> Peptidase 3.4.24.42
EnzymologyBRENDA database
Proteolytic eventsCutDB database (10 cleavages)
PhysiologyLikely role in snake venom toxicity.
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/-/-Scissile bondlf/lvg/-/- (based on 60 cleavages)
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Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 4 3 7 7 0 8 8 4
Pro 2 4 2 4 0 0 1 0
Ala 3 6 8 14 3 2 11 5
Val 4 3 7 1 3 11 2 6
Leu 5 0 5 1 24 13 8 6
Ile 4 1 3 0 1 1 1 4
Met 1 0 0 1 2 0 0 0
Phe 0 1 0 1 10 6 4 1
Tyr 2 0 2 2 2 6 5 1
Trp 0 0 0 0 0 0 1 0
Ser 3 6 5 3 4 0 1 4
Thr 3 6 1 1 0 3 0 2
Cys 1 0 1 6 2 0 5 1
Asn 1 1 1 5 0 0 1 4
Gln 0 1 2 0 4 2 1 3
Asp 4 5 3 1 0 0 2 4
Glu 5 8 7 5 0 0 2 2
Lys 1 1 1 1 0 0 0 0
Arg 0 0 1 1 0 2 0 0
His 3 2 0 2 5 1 1 0