The serine carboxypeptidase like gene family of rice (Oryza sativa L. ssp. japonica).

Abstract

Serine carboxypeptidases (SCPs) comprise a large family of protein hydrolyzing enzymes and have roles ranging from protein turnover and C-terminal processing to wound responses and xenobiotic metabolism. The proteins can be classified into three groups, namely carboxypeptidase I, II and III, based on their coding protein sequences and the fact that each family is characterized by a central catalytic domain of unique topology designated as the "alpha/beta hydrolase fold". The available SCP protein sequences have been utilized as datasets to build a HMM (hidden Markov model) profile, which is used to search the rice (Oryza sativa L. ssp. japonica) proteome. A total of 71 SCP and serine carboxypeptidase-like (SCPL) protein-coding genes exist in rice. The intron-exon structure, chromosome localization, expression and characteristics of encoded protein sequences of the 71 putative genes are reviewed.

• Authors: Ying Feng, Qingzhong Xue
• Journal: Functional & integrative genomics (Funct Integr Genomics) Vol. 6 Issue 1 Pg. 14-24 (Jan 2006) ISSN: 1438-793X [Print] Germany
• PMID: 15809843 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Proteome
• Carboxypeptidases
• serine carboxypeptidase

Topics

• Amino Acid Sequence
• Carboxypeptidases (genetics)
• Chromosomes, Plant
• Databases, Genetic
• Genome, Plant
• Molecular Sequence Data
• Multigene Family
• Oryza (enzymology, genetics)
• Proteome
• Sequence Homology, Amino Acid