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Conserved domains on  [gi|2558417448|ref|WP_304517388|]
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CPBP family intramembrane glutamic endopeptidase [Cecembia rubra]

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:0004222|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, ...
 137-232 5.08e-18

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


:

Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 77.52  E-value: 5.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558417448 137 MAILFALFILVSVGEEVLIRGYVLKNFMLSFNKYFALIVSSLLFSIMHGFNphfdFIAFVNLFLAGLVLGISYIYSKNLW 216
Cdd:COG1266     5 LLFLLVVVILAPIAEELLFRGYLLGRLRRRFGPWLAILLSSLLFGLLHLPN----LLGFLPAFLLGLVLGLLYLRTGSLW 80

                          90
                  ....*....|....*.
gi 2558417448 217 FPIGMHLSWNFFQSIL 232
Cdd:COG1266    81 VPILLHALNNLLALLL 96
 
Name Accession Description Interval E-value
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 137-232 5.08e-18

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 77.52  E-value: 5.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558417448 137 MAILFALFILVSVGEEVLIRGYVLKNFMLSFNKYFALIVSSLLFSIMHGFNphfdFIAFVNLFLAGLVLGISYIYSKNLW 216
Cdd:COG1266     5 LLFLLVVVILAPIAEELLFRGYLLGRLRRRFGPWLAILLSSLLFGLLHLPN----LLGFLPAFLLGLVLGLLYLRTGSLW 80

                          90
                  ....*....|....*.
gi 2558417448 217 FPIGMHLSWNFFQSIL 232
Cdd:COG1266    81 VPILLHALNNLLALLL 96
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 138-228 3.88e-16

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: 72.20  E-value: 3.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558417448 138 AILFALFILVSVGEEVLIRGYVLKNFMLSFNKYFALIVSSLLFSIMHGFNPhfdFIAFVNLFLAGLVLGISYIYSKNLWF 217
Cdd:pfam02517   5 LLLLLLALLAPIGEELLFRGYLLPRLRRRLWPVLAILISSLLFGLAHLPNG---PQLFLLAFLLGLILGYLYLRTGSLWA 81

                          90
                  ....*....|.
gi 2558417448 218 PIGMHLSWNFF 228
Cdd:pfam02517  82 AILLHALNNLL 92
 
Name Accession Description Interval E-value
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 137-232 5.08e-18

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 77.52  E-value: 5.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558417448 137 MAILFALFILVSVGEEVLIRGYVLKNFMLSFNKYFALIVSSLLFSIMHGFNphfdFIAFVNLFLAGLVLGISYIYSKNLW 216
Cdd:COG1266     5 LLFLLVVVILAPIAEELLFRGYLLGRLRRRFGPWLAILLSSLLFGLLHLPN----LLGFLPAFLLGLVLGLLYLRTGSLW 80

                          90
                  ....*....|....*.
gi 2558417448 217 FPIGMHLSWNFFQSIL 232
Cdd:COG1266    81 VPILLHALNNLLALLL 96
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 138-228 3.88e-16

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: 72.20  E-value: 3.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558417448 138 AILFALFILVSVGEEVLIRGYVLKNFMLSFNKYFALIVSSLLFSIMHGFNPhfdFIAFVNLFLAGLVLGISYIYSKNLWF 217
Cdd:pfam02517   5 LLLLLLALLAPIGEELLFRGYLLPRLRRRLWPVLAILISSLLFGLAHLPNG---PQLFLLAFLLGLILGYLYLRTGSLWA 81

                          90
                  ....*....|.
gi 2558417448 218 PIGMHLSWNFF 228
Cdd:pfam02517  82 AILLHALNNLL 92
COG4449 COG4449
Predicted protease, Abi (CAAX) family [General function prediction only];
137-227 2.62e-05

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


Pssm-ID: 443548  Cd Length: 176  Bit Score: 43.85  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558417448 137 MAILFALFILVSVGEEVLIRGYVLKNFM---LSFNKYFALIVSSLLFSIMHGFN-----PH-----FDFIAFVNLFLAGL 203
Cdd:COG4449    60 LAVILILLLFPAIGEELLFRGLLLPHPVelaSGLNWWLWILLSLVLFVLYHPLNaltfyPAgrptfLNPRFLLLAGLLGL 139

                          90       100
                  ....*....|....*....|....
gi 2558417448 204 VLGISYIYSKNLWFPIGMHLSWNF 227
Cdd:COG4449   140 ACTIAYLLTGSLWPAVIIHWLVVV 163
 
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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