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Conserved domains on  [gi|6323930|ref|NP_014001|]
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CAAX prenyl protease [Saccharomyces cerevisiae S288C]

Protein Classification

CPBP family intramembrane glutamic endopeptidase( domain architecture ID 10494850)

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:0004222|GO:0016020|GO:0070007|GO:0071586
MEROPS:  G5
PubMed:  24291792

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 143-254 2.70e-08

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: 50.63  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323930    143 IWSFRNFIFAPITEEIFYTSMLLTTYLNLiphsqLSYQQLFWQPSLFFGLAHAHHAYeqlqegsmttvsillttcFQILY 222
Cdd:pfam02517   5 LLLLLLALLAPIGEELLFRGYLLPRLRRR-----LWPVLAILISSLLFGLAHLPNGP------------------QLFLL 61

                          90       100       110
                  ....*....|....*....|....*....|..
gi 6323930    223 TTLFGGLTKFVFVRTGgNLWCCIILHALCNIM 254
Cdd:pfam02517  62 AFLLGLILGYLYLRTG-SLWAAILLHALNNLL 92
 
Name Accession Description Interval E-value
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 143-254 2.70e-08

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: 50.63  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323930    143 IWSFRNFIFAPITEEIFYTSMLLTTYLNLiphsqLSYQQLFWQPSLFFGLAHAHHAYeqlqegsmttvsillttcFQILY 222
Cdd:pfam02517   5 LLLLLLALLAPIGEELLFRGYLLPRLRRR-----LWPVLAILISSLLFGLAHLPNGP------------------QLFLL 61

                          90       100       110
                  ....*....|....*....|....*....|..
gi 6323930    223 TTLFGGLTKFVFVRTGgNLWCCIILHALCNIM 254
Cdd:pfam02517  62 AFLLGLILGYLYLRTG-SLWAAILLHALNNLL 92
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 148-256 1.44e-03

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 37.46  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323930  148 NFIFAPITEEIFYTSMLLT---TYLNLIPHSQLSyqqlfwqpSLFFGLAHAHHAYeqlqegsmttvsillttcfQILYTT 224
Cdd:COG1266  11 VVILAPIAEELLFRGYLLGrlrRRFGPWLAILLS--------SLLFGLLHLPNLL-------------------GFLPAF 63

                        90       100       110
                ....*....|....*....|....*....|..
gi 6323930  225 LFGGLTKFVFVRTGgNLWCCIILHALCNIMGF 256
Cdd:COG1266  64 LLGLVLGLLYLRTG-SLWVPILLHALNNLLAL 94
 
Name Accession Description Interval E-value
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 143-254 2.70e-08

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: 50.63  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323930    143 IWSFRNFIFAPITEEIFYTSMLLTTYLNLiphsqLSYQQLFWQPSLFFGLAHAHHAYeqlqegsmttvsillttcFQILY 222
Cdd:pfam02517   5 LLLLLLALLAPIGEELLFRGYLLPRLRRR-----LWPVLAILISSLLFGLAHLPNGP------------------QLFLL 61

                          90       100       110
                  ....*....|....*....|....*....|..
gi 6323930    223 TTLFGGLTKFVFVRTGgNLWCCIILHALCNIM 254
Cdd:pfam02517  62 AFLLGLILGYLYLRTG-SLWAAILLHALNNLL 92
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 148-256 1.44e-03

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 37.46  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323930  148 NFIFAPITEEIFYTSMLLT---TYLNLIPHSQLSyqqlfwqpSLFFGLAHAHHAYeqlqegsmttvsillttcfQILYTT 224
Cdd:COG1266  11 VVILAPIAEELLFRGYLLGrlrRRFGPWLAILLS--------SLLFGLLHLPNLL-------------------GFLPAF 63

                        90       100       110
                ....*....|....*....|....*....|..
gi 6323930  225 LFGGLTKFVFVRTGgNLWCCIILHALCNIMGF 256
Cdd:COG1266  64 LLGLVLGLLYLRTG-SLWVPILLHALNNLLAL 94
 
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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