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Conserved domains on  [gi|18404792|ref|NP_566788|]
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CAAX amino terminal protease family protein [Arabidopsis thaliana]

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, ...
 194-282 2.96e-18

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


:

Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 77.91  E-value: 2.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404792 194 YLVVAMLPGISEELLFRGALMPLFGTNWN---GIVAVGLIFGLLHLGSgrkYSFAVWASIVGIVYGYAAVLSSSLIVPMA 270
Cdd:COG1266   8 LLVVVILAPIAEELLFRGYLLGRLRRRFGpwlAILLSSLLFGLLHLPN---LLGFLPAFLLGLVLGLLYLRTGSLWVPIL 84

                        90
                ....*....|..
gi 18404792 271 SHALNNLVGGLL 282
Cdd:COG1266  85 LHALNNLLALLL 96
 
Name Accession Description Interval E-value
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 194-282 2.96e-18

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 77.91  E-value: 2.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404792 194 YLVVAMLPGISEELLFRGALMPLFGTNWN---GIVAVGLIFGLLHLGSgrkYSFAVWASIVGIVYGYAAVLSSSLIVPMA 270
Cdd:COG1266   8 LLVVVILAPIAEELLFRGYLLGRLRRRFGpwlAILLSSLLFGLLHLPN---LLGFLPAFLLGLVLGLLYLRTGSLWVPIL 84

                        90
                ....*....|..
gi 18404792 271 SHALNNLVGGLL 282
Cdd:COG1266  85 LHALNNLLALLL 96
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 188-278 3.77e-17

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: 74.89  E-value: 3.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404792   188 SLEPLDYLVVAMLPGISEELLFRGALMPLFGTNWNGIVAV---GLIFGLLHLGSGrkYSFAVWASIVGIVYGYAAVLSSS 264
Cdd:pfam02517   1 LLLLLLLLLLALLAPIGEELLFRGYLLPRLRRRLWPVLAIlisSLLFGLAHLPNG--PQLFLLAFLLGLILGYLYLRTGS 78

                          90
                  ....*....|....
gi 18404792   265 LIVPMASHALNNLV 278
Cdd:pfam02517  79 LWAAILLHALNNLL 92
 
Name Accession Description Interval E-value
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 194-282 2.96e-18

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 77.91  E-value: 2.96e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404792 194 YLVVAMLPGISEELLFRGALMPLFGTNWN---GIVAVGLIFGLLHLGSgrkYSFAVWASIVGIVYGYAAVLSSSLIVPMA 270
Cdd:COG1266   8 LLVVVILAPIAEELLFRGYLLGRLRRRFGpwlAILLSSLLFGLLHLPN---LLGFLPAFLLGLVLGLLYLRTGSLWVPIL 84

                        90
                ....*....|..
gi 18404792 271 SHALNNLVGGLL 282
Cdd:COG1266  85 LHALNNLLALLL 96
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 188-278 3.77e-17

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: 74.89  E-value: 3.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404792   188 SLEPLDYLVVAMLPGISEELLFRGALMPLFGTNWNGIVAV---GLIFGLLHLGSGrkYSFAVWASIVGIVYGYAAVLSSS 264
Cdd:pfam02517   1 LLLLLLLLLLALLAPIGEELLFRGYLLPRLRRRLWPVLAIlisSLLFGLAHLPNG--PQLFLLAFLLGLILGYLYLRTGS 78

                          90
                  ....*....|....
gi 18404792   265 LIVPMASHALNNLV 278
Cdd:pfam02517  79 LWAAILLHALNNLL 92
COG4449 COG4449
Predicted protease, Abi (CAAX) family [General function prediction only];
187-283 2.44e-05

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


Pssm-ID: 443548  Cd Length: 176  Bit Score: 43.85  E-value: 2.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404792 187 TSLEPLDYLVVAM----LPGISEELLFRGALMPLFGTNWN------GIVAVGLIFGLLHLGSGRKYS-----------FA 245
Cdd:COG4449  52 WAASPLSLLAVILilllFPAIGEELLFRGLLLPHPVELASglnwwlWILLSLVLFVLYHPLNALTFYpagrptflnprFL 131

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 18404792 246 VWASIVGIVYGYAAVLSSSLIVPMASHALNNLVGGLLW 283
Cdd:COG4449 132 LLAGLLGLACTIAYLLTGSLWPAVIIHWLVVVVWLLLL 169
 
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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