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	PROSITE documentation PDOC00122 [for PROSITE entry PS00560]

Serine carboxypeptidases, active sites

All known carboxypeptidases are either metallo carboxypeptidases or serine carboxypeptidases (EC 3.4.16.5 and EC 3.4.16.6). The catalytic activity of the serine carboxypeptidases, like that of the trypsin family serine proteases, is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a histidine, which is itself hydrogen-bonded to a serine [1]. Proteins known to be serine carboxypeptidases are:

• Barley and wheat serine carboxypeptidases I, II, and III [2].
• Yeast carboxypeptidase Y (YSCY) (gene PRC1), a vacuolar protease involved in degrading small peptides.
• Yeast KEX1 protease, involved in killer toxin and α-factor precursor processing.
• Fission yeast sxa2, a probable carboxypeptidase involved in degrading or processing mating pheromones [3].
• Penicillium janthinellum carboxypeptidase S1 [4].
• Aspergullus niger carboxypeptidase pepF.
• Aspergullus satoi carboxypeptidase cpdS.
• Vertebrate protective protein / cathepsin A [5], a lysosomal protein which is not only a carboxypeptidase but also essential for the activity of both β-galactosidase and neuraminidase.
• Mosquito vitellogenic carboxypeptidase (VCP) [6].
• Naegleria fowleri virulence-related protein Nf314 [7].
• Yeast hypothetical protein YBR139w.
• Caenorhabditis elegans hypothetical proteins C08H9.1, F13D12.6, F32A5.3, F41C3.5 and K10B2.2.

This family also includes:

• Sorghum (s)-hydroxymandelonitrile lyase (EC 4.1.2.11) (hydroxynitrile lyase) (HNL) [8], an enzyme involved in plant cyanogenesis.

The sequences surrounding the active site serine and histidine residues are highly conserved in all these serine carboxypeptidases.

Note:

These proteins belong to family S10 in the classification of peptidases [9,E1].

Last update:

February 2003 / Patterns and text revised.

PROSITE methods (with tools and information) covered by this documentation:

CARBOXYPEPT_SER_HIS, PS00560; Serine carboxypeptidases, histidine active site  (PATTERN)

• Consensus pattern:
  [LIVF]-x(2)-[LIVSTA]-x-[IVPST]-x-[GSDNQL]-[SAGV]-[SG]-H-x-[IVAQ]-P-x(3)-[PSA]
  H is the active site residue
• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 212
  • detected by PS00560: 82 (true positives)
  • undetected by PS00560: 130 (129 false negatives and 1 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS00560:
  NONE.
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00560
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00560
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS00560
• View ligand binding statistics of PS00560
• Matching PDB structures: 1AC5 1BCR 1BCS 1CPY ... [ALL]

CARBOXYPEPT_SER_SER, PS00131; Serine carboxypeptidases, serine active site  (PATTERN)

• Consensus pattern:
  [LIVM]-x-[GSTA]-E-S-Y-[AG]-[GS]
  S is the active site residue
• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 220
  • detected by PS00131: 162 (true positives)
  • undetected by PS00131: 58 (56 false negatives and 2 'partials')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS00131:
  6 false positives.
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00131
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00131
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS00131
• View ligand binding statistics of PS00131
• Matching PDB structures: 1AC5 1BCR 1BCS 1IVY ... [ALL]

1	Authors	Liao D.I., Remington S.J.
	Title	Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase.
	Source	J. Biol. Chem. 265:6528-6531(1990).
	PubMed ID	2324088

2	Authors	Sorensen S.B., Svendsen I., Breddam K.
	Title	Primary structure of carboxypeptidase III from malted barley.
	Source	Carlsberg Res. Commun. 54:193-202(1989).
	PubMed ID	2639682

3	Authors	Imai Y., Yamamoto M.
	Title	Schizosaccharomyces pombe sxa1+ and sxa2+ encode putative proteases involved in the mating response.
	Source	Mol. Cell. Biol. 12:1827-1834(1992).
	PubMed ID	1549128

4	Authors	Svendsen I., Hofmann T., Endrizzi J., Remington S.J., Breddam K.
	Title	The primary structure of carboxypeptidase S1 from Penicillium janthinellum.
	Source	FEBS Lett. 333:39-43(1993).
	PubMed ID	8224168

5	Authors	Galjart N.J., Morreau H., Willemsen R., Gillemans N., Bonten E.J., d'Azzo A.
	Title	Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function.
	Source	J. Biol. Chem. 266:14754-14762(1991).
	PubMed ID	1907282

6	Authors	Cho W.L., Deitsch K.W., Raikhel A.S.
	Title	An extraovarian protein accumulated in mosquito oocytes is a carboxypeptidase activated in embryos.
	Source	Proc. Natl. Acad. Sci. U.S.A. 88:10821-10824(1991).
	PubMed ID	1961751

7	Authors	Hu W.N., Kopachik W., Band R.N.
	Title	Cloning and characterization of transcripts showing virulence-related gene expression in Naegleria fowleri.
	Source	Infect. Immun. 60:2418-2424(1992).
	PubMed ID	1587609

8	Authors	Wajant H., Mundry K.W., Pfizenmaier K.
	Title	Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.). Homologies to serine carboxypeptidases.
	Source	Plant Mol. Biol. 26:735-746(1994).
	PubMed ID	7948927

9	Authors	Rawlings N.D., Barrett A.J.
	Title	Families of serine peptidases.
	Source	Methods Enzymol. 244:19-61(1994).
	PubMed ID	7845208

E1	Title	https://www.uniprot.org/docs/peptidas
	Source	?

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