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Conserved domains on  [gi|488219396|ref|WP_002290604|]
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MULTISPECIES: CPBP family glutamic-type intramembrane protease [Enterococcus]

Protein Classification

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.

EC:  3.4.-.-
Gene Ontology:  GO:0016020|GO:0070007|GO:0071586
PubMed:  24291792

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 118-211 3.32e-16

Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 70.98  E-value: 3.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219396 118 IMEAPAFILATTIAGPIMEEFVFRRSILGIISRYSNFWVGAVISSLLFAFAHNDG--HLLIYFFLGFFFSLEYKATGRIW 195
Cdd:COG1266    1 LLWLLLFLLVVVILAPIAEELLFRGYLLGRLRRRFGPWLAILLSSLLFGLLHLPNllGFLPAFLLGLVLGLLYLRTGSLW 80

                         90
                 ....*....|....*.
gi 488219396 196 TSMITHVGMNTLVVLV 211
Cdd:COG1266   81 VPILLHALNNLLALLL 96
 
Name Accession Description Interval E-value
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 118-211 3.32e-16

Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 70.98  E-value: 3.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219396 118 IMEAPAFILATTIAGPIMEEFVFRRSILGIISRYSNFWVGAVISSLLFAFAHNDG--HLLIYFFLGFFFSLEYKATGRIW 195
Cdd:COG1266    1 LLWLLLFLLVVVILAPIAEELLFRGYLLGRLRRRFGPWLAILLSSLLFGLLHLPNllGFLPAFLLGLVLGLLYLRTGSLW 80

                         90
                 ....*....|....*.
gi 488219396 196 TSMITHVGMNTLVVLV 211
Cdd:COG1266   81 VPILLHALNNLLALLL 96
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 123-207 6.04e-12

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: 59.49  E-value: 6.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219396  123 AFILATTIAGPIMEEFVFRRSILGIISRYSNFWVGAVISSLLFAFAH---NDGHLLIYFFLGFFFSLEYKATGRIWTSMI 199
Cdd:pfam02517   5 LLLLLLALLAPIGEELLFRGYLLPRLRRRLWPVLAILISSLLFGLAHlpnGPQLFLLAFLLGLILGYLYLRTGSLWAAIL 84


                  ....*...
gi 488219396  200 THVGMNTL 207
Cdd:pfam02517  85 LHALNNLL 92
 
Name Accession Description Interval E-value
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 118-211 3.32e-16

Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 70.98  E-value: 3.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219396 118 IMEAPAFILATTIAGPIMEEFVFRRSILGIISRYSNFWVGAVISSLLFAFAHNDG--HLLIYFFLGFFFSLEYKATGRIW 195
Cdd:COG1266    1 LLWLLLFLLVVVILAPIAEELLFRGYLLGRLRRRFGPWLAILLSSLLFGLLHLPNllGFLPAFLLGLVLGLLYLRTGSLW 80

                         90
                 ....*....|....*.
gi 488219396 196 TSMITHVGMNTLVVLV 211
Cdd:COG1266   81 VPILLHALNNLLALLL 96
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 123-207 6.04e-12

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: 59.49  E-value: 6.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219396  123 AFILATTIAGPIMEEFVFRRSILGIISRYSNFWVGAVISSLLFAFAH---NDGHLLIYFFLGFFFSLEYKATGRIWTSMI 199
Cdd:pfam02517   5 LLLLLLALLAPIGEELLFRGYLLPRLRRRLWPVLAILISSLLFGLAHlpnGPQLFLLAFLLGLILGYLYLRTGSLWAAIL 84


                  ....*...
gi 488219396  200 THVGMNTL 207
Cdd:pfam02517  85 LHALNNLL 92
COG4449 COG4449
Predicted protease, Abi (CAAX) family [General function prediction only];
123-214 6.79e-03

Predicted protease, Abi (CAAX) family [General function prediction only];


Pssm-ID: 443548  Cd Length: 176  Bit Score: 36.15  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488219396 123 AFILATTIAGPIMEEFVFRRSILGIISRYSNF---WVGAVISSLLFAFAH----------------NDGHLLIYFFLGFF 183
Cdd:COG4449   61 AVILILLLFPAIGEELLFRGLLLPHPVELASGlnwWLWILLSLVLFVLYHplnaltfypagrptflNPRFLLLAGLLGLA 140

                         90       100       110
                 ....*....|....*....|....*....|.
gi 488219396 184 FSLEYKATGRIWTSMITHvgmnTLVVLVQLA 214
Cdd:COG4449  141 CTIAYLLTGSLWPAVIIH----WLVVVVWLL 167
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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