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Conserved domains on  [gi|516407531|ref|WP_017796929|]
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MULTISPECIES: CPBP family intramembrane glutamic endopeptidase [Oceanobacillus]

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.-.-
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, ...
97-184 9.04e-12

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


:

Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 58.65  E-value: 9.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407531  97 ILFIIGFTLLVAICEELLFRGTIQTTF--------GYVFASLLFALVHIRYLkktVLFLSIVLVSFFIGWIFERTENLLI 168
Cdd:COG1266    5 LLFLLVVVILAPIAEELLFRGYLLGRLrrrfgpwlAILLSSLLFGLLHLPNL---LGFLPAFLLGLVLGLLYLRTGSLWV 81
                         90
                 ....*....|....*.
gi 516407531 169 TITAHFIIDLVLGLII 184
Cdd:COG1266   82 PILLHALNNLLALLLL 97
 
Name Accession Description Interval E-value
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
97-184 9.04e-12

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 58.65  E-value: 9.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407531  97 ILFIIGFTLLVAICEELLFRGTIQTTF--------GYVFASLLFALVHIRYLkktVLFLSIVLVSFFIGWIFERTENLLI 168
Cdd:COG1266    5 LLFLLVVVILAPIAEELLFRGYLLGRLrrrfgpwlAILLSSLLFGLLHLPNL---LGFLPAFLLGLVLGLLYLRTGSLWV 81
                         90
                 ....*....|....*.
gi 516407531 169 TITAHFIIDLVLGLII 184
Cdd:COG1266   82 PILLHALNNLLALLLL 97
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
96-179 2.84e-10

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: 54.48  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407531   96 PILFIIGFTLLVAICEELLFRGTIQTTF--------GYVFASLLFALVHIRYLkkTVLFLSIVLVSFFIGWIFERTENLL 167
Cdd:pfam02517   3 LLLLLLLLALLAPIGEELLFRGYLLPRLrrrlwpvlAILISSLLFGLAHLPNG--PQLFLLAFLLGLILGYLYLRTGSLW 80
                          90
                  ....*....|..
gi 516407531  168 ITITAHFIIDLV 179
Cdd:pfam02517  81 AAILLHALNNLL 92
ABC_perm_CPBP NF041647
ABC transporter permease subunit/CPBP intramembrane protease; The C-terminal region of this ...
13-186 7.30e-08

ABC transporter permease subunit/CPBP intramembrane protease; The C-terminal region of this ABC transporter permease contains a CPBP family glutamic-type intramembrane protease domain, related to the eukaryotic type 2 CAAX prenyl protease Rce1.


Pssm-ID: 469529 [Multi-domain]  Cd Length: 641  Bit Score: 51.37  E-value: 7.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407531  13 KELRYQLVFSQILFLVISIVLSLILF------------PSWKVWLDyfdanvneILLIGFGSAFIVIVFDIILMS-VFP- 78
Cdd:NF041647 455 RNLLVGLLVTQWGLILLPVLLLLYYKkddfrktlslrlPSLRALLG--------AVLLGAGAWVLVFALSALLSNrLLPp 526
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407531  79 --------NESFDDGGINKRIFkkqPILFIIGftLLVAICEELLFRGTIQTTF--------GYVFASLLFALVHIRYLKk 142
Cdd:NF041647 527 ppelaealEELLSLLLSGAPLW---LLLLVVA--LSPAICEELLFRGFILSGLrrrmspwaAILLSALLFGLFHLSLYR- 600
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 516407531 143 tvlFLSIVLVSFFIGWIFERTENLLITITAHFIIDLVLGLIIRF 186
Cdd:NF041647 601 ---LLPTALLGILLGYLVYRSGSIFPSMLMHFLNNGLAVLLSRY 641
 
Name Accession Description Interval E-value
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
97-184 9.04e-12

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 58.65  E-value: 9.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407531  97 ILFIIGFTLLVAICEELLFRGTIQTTF--------GYVFASLLFALVHIRYLkktVLFLSIVLVSFFIGWIFERTENLLI 168
Cdd:COG1266    5 LLFLLVVVILAPIAEELLFRGYLLGRLrrrfgpwlAILLSSLLFGLLHLPNL---LGFLPAFLLGLVLGLLYLRTGSLWV 81
                         90
                 ....*....|....*.
gi 516407531 169 TITAHFIIDLVLGLII 184
Cdd:COG1266   82 PILLHALNNLLALLLL 97
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
96-179 2.84e-10

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: 54.48  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407531   96 PILFIIGFTLLVAICEELLFRGTIQTTF--------GYVFASLLFALVHIRYLkkTVLFLSIVLVSFFIGWIFERTENLL 167
Cdd:pfam02517   3 LLLLLLLLALLAPIGEELLFRGYLLPRLrrrlwpvlAILISSLLFGLAHLPNG--PQLFLLAFLLGLILGYLYLRTGSLW 80
                          90
                  ....*....|..
gi 516407531  168 ITITAHFIIDLV 179
Cdd:pfam02517  81 AAILLHALNNLL 92
ABC_perm_CPBP NF041647
ABC transporter permease subunit/CPBP intramembrane protease; The C-terminal region of this ...
13-186 7.30e-08

ABC transporter permease subunit/CPBP intramembrane protease; The C-terminal region of this ABC transporter permease contains a CPBP family glutamic-type intramembrane protease domain, related to the eukaryotic type 2 CAAX prenyl protease Rce1.


Pssm-ID: 469529 [Multi-domain]  Cd Length: 641  Bit Score: 51.37  E-value: 7.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407531  13 KELRYQLVFSQILFLVISIVLSLILF------------PSWKVWLDyfdanvneILLIGFGSAFIVIVFDIILMS-VFP- 78
Cdd:NF041647 455 RNLLVGLLVTQWGLILLPVLLLLYYKkddfrktlslrlPSLRALLG--------AVLLGAGAWVLVFALSALLSNrLLPp 526
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516407531  79 --------NESFDDGGINKRIFkkqPILFIIGftLLVAICEELLFRGTIQTTF--------GYVFASLLFALVHIRYLKk 142
Cdd:NF041647 527 ppelaealEELLSLLLSGAPLW---LLLLVVA--LSPAICEELLFRGFILSGLrrrmspwaAILLSALLFGLFHLSLYR- 600
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 516407531 143 tvlFLSIVLVSFFIGWIFERTENLLITITAHFIIDLVLGLIIRF 186
Cdd:NF041647 601 ---LLPTALLGILLGYLVYRSGSIFPSMLMHFLNNGLAVLLSRY 641
 
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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