CPBP family intramembrane metalloprotease [Chloroflexi bacterium]
CPBP family intramembrane glutamic endopeptidase( domain architecture ID 11441430)
CPBP (CAAX proteases and bacteriocin-processing enzymes) family intramembrane protease similar to Saccharomyces cerevisiae Rce1, a type II CAAX prenyl protease that processes all farnesylated and geranylgeranylated CAAX proteins. It is an integral membrane endoprotease that belongs to the glutamate IMPs, sharing a conserved sequence motif EExxxR
List of domain hits
Name | Accession | Description | Interval | E-value | |||
YdiL | COG1266 | Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ... |
154-254 | 1.17e-10 | |||
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, chaperones]; : Pssm-ID: 440877 [Multi-domain] Cd Length: 97 Bit Score: 57.49 E-value: 1.17e-10
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Name | Accession | Description | Interval | E-value | |||
YdiL | COG1266 | Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ... |
154-254 | 1.17e-10 | |||
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440877 [Multi-domain] Cd Length: 97 Bit Score: 57.49 E-value: 1.17e-10
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Rce1-like | pfam02517 | Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ... |
156-248 | 1.92e-09 | |||
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive infection) family) contains putative IMPs and has homologs in all three domains of life, including Rce1 from S. cerevisiae. Rce1 is a type II CAAX prenyl protease that processes all farnesylated and geranylgeranylated CAAX proteins. It is an integral membrane endoprotease localized to the endoplasmic reticulum that mediates the cleavage of the carboxyl-terminal three amino acids from CaaX proteins. It is involved in processing the Ras family of small GTPases, the gamma-subunit of heterotrimeric GTPases, nuclear lamins, and protein kinases and phosphatases. Three residues of S. cerevisiae Rce1 -E156, H194 and H248- are critical for catalysis. The structure of Rce1 from the archaea Methanococcus (MmRce1) suggests that this group of proteins represents a novel IMP (intramembrane protease) family, the glutamate IMPs. There is a conserved sequence motif EExxxR. Pssm-ID: 460578 [Multi-domain] Cd Length: 92 Bit Score: 53.71 E-value: 1.92e-09
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Name | Accession | Description | Interval | E-value | |||
YdiL | COG1266 | Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ... |
154-254 | 1.17e-10 | |||
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440877 [Multi-domain] Cd Length: 97 Bit Score: 57.49 E-value: 1.17e-10
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Rce1-like | pfam02517 | Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ... |
156-248 | 1.92e-09 | |||
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive infection) family) contains putative IMPs and has homologs in all three domains of life, including Rce1 from S. cerevisiae. Rce1 is a type II CAAX prenyl protease that processes all farnesylated and geranylgeranylated CAAX proteins. It is an integral membrane endoprotease localized to the endoplasmic reticulum that mediates the cleavage of the carboxyl-terminal three amino acids from CaaX proteins. It is involved in processing the Ras family of small GTPases, the gamma-subunit of heterotrimeric GTPases, nuclear lamins, and protein kinases and phosphatases. Three residues of S. cerevisiae Rce1 -E156, H194 and H248- are critical for catalysis. The structure of Rce1 from the archaea Methanococcus (MmRce1) suggests that this group of proteins represents a novel IMP (intramembrane protease) family, the glutamate IMPs. There is a conserved sequence motif EExxxR. Pssm-ID: 460578 [Multi-domain] Cd Length: 92 Bit Score: 53.71 E-value: 1.92e-09
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Blast search parameters | ||||
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