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Conserved domains on  [gi|1260004914|gb|PEV52136|]
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CPBP family intramembrane metalloprotease domain-containing protein [Bacillus thuringiensis]

Protein Classification

CPBP family intramembrane glutamic endopeptidase( domain architecture ID 11441546)

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, ...
 126-214 1.70e-24

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


:

Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 95.24  E-value: 1.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260004914 126 VYMTIFTFISACVLAPIMEEVIFRGFFLQRMAHKWGIKKAVIISSIIFGLGHFD----VIGAFMFGVVMCLLYIKTKNIW 201
Cdd:COG1266     1 LLWLLLFLLVVVILAPIAEELLFRGYLLGRLRRRFGPWLAILLSSLLFGLLHLPnllgFLPAFLLGLVLGLLYLRTGSLW 80

                          90
                  ....*....|...
gi 1260004914 202 TNIAVHALNNLIA 214
Cdd:COG1266    81 VPILLHALNNLLA 93
MazE COG2336
Antitoxin component MazE of the MazEF toxin-antitoxin module [Defense mechanisms];
301-337 6.13e-04

Antitoxin component MazE of the MazEF toxin-antitoxin module [Defense mechanisms];


:

Pssm-ID: 441907  Cd Length: 80  Bit Score: 37.94  E-value: 6.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1260004914 301 AIELPDEAVNKLRLEENDYVTVAVEEDKIVIKKAHNR 337
Cdd:COG2336    13 GVRIPKALLEQLGLKEGDEVELEVEDGRIVIRPVRRP 49
 
Name Accession Description Interval E-value
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 126-214 1.70e-24

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 95.24  E-value: 1.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260004914 126 VYMTIFTFISACVLAPIMEEVIFRGFFLQRMAHKWGIKKAVIISSIIFGLGHFD----VIGAFMFGVVMCLLYIKTKNIW 201
Cdd:COG1266     1 LLWLLLFLLVVVILAPIAEELLFRGYLLGRLRRRFGPWLAILLSSLLFGLLHLPnllgFLPAFLLGLVLGLLYLRTGSLW 80

                          90
                  ....*....|...
gi 1260004914 202 TNIAVHALNNLIA 214
Cdd:COG1266    81 VPILLHALNNLLA 93
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 130-213 3.61e-21

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: 86.45  E-value: 3.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260004914 130 IFTFISACVLAPIMEEVIFRGFFLQRMAHKWGIKKAVIISSIIFGLGHF-----DVIGAFMFGVVMCLLYIKTKNIWTNI 204
Cdd:pfam02517   4 LLLLLLLALLAPIGEELLFRGYLLPRLRRRLWPVLAILISSLLFGLAHLpngpqLFLLAFLLGLILGYLYLRTGSLWAAI 83


                  ....*....
gi 1260004914 205 AVHALNNLI 213
Cdd:pfam02517  84 LLHALNNLL 92
pepcterm_CAAX TIGR03008
CAAX prenyl protease-related protein; The CAAX prenyl protease, in eukaryotes, catalyzes three ...
 128-213 2.73e-08

CAAX prenyl protease-related protein; The CAAX prenyl protease, in eukaryotes, catalyzes three covalent modifications, including cleavage and acylation, at the C-terminus of certain proteins in a process connected to protein sorting. This family describes a bacterial protein family homologous to one domain of the CAAX-processing enzyme. Members of this protein family are found in genomes that carry a predicted protein sorting system, PEP-CTERM/exosortase, usually in the vicinity of the EpsH homolog that is the hallmark of the system. The function of this protein is unknown, but it may relate to protein motification. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 163100  Cd Length: 222  Bit Score: 53.64  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260004914 128 MTIFTFISACVLAPIMEEVIFRGFFLQRMAHK-----------WgikKAVIISSIIFGLGHFDVIGAFMFGVVMCLLYIK 196
Cdd:TIGR03008 115 LIAFRLAGATLVVPVMEELFWRSFLLRYLQQSdfesvpggrfhW---PSFLAVTLLFGLEHHLIVAGLIAGLAYNLLLLR 191

                          90
                  ....*....|....*..
gi 1260004914 197 TKNIWTNIAVHALNNLI 213
Cdd:TIGR03008 192 TGSIMACILAHAVTNGL 208
MazE COG2336
Antitoxin component MazE of the MazEF toxin-antitoxin module [Defense mechanisms];
301-337 6.13e-04

Antitoxin component MazE of the MazEF toxin-antitoxin module [Defense mechanisms];


Pssm-ID: 441907  Cd Length: 80  Bit Score: 37.94  E-value: 6.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1260004914 301 AIELPDEAVNKLRLEENDYVTVAVEEDKIVIKKAHNR 337
Cdd:COG2336    13 GVRIPKALLEQLGLKEGDEVELEVEDGRIVIRPVRRP 49
SpoVT_AbrB smart00966
SpoVT / AbrB like domain; This domain is found in AbrB from Bacillus subtilis. The product of ...
 301-334 4.71e-03

SpoVT / AbrB like domain; This domain is found in AbrB from Bacillus subtilis. The product of the abrB gene is an ambiactive repressor and activator of the transcription of genes expressed during the transition state between vegetative growth and the onset of stationary phase and sporulation. AbrB is thought to interact directly with the transcription initiation regions of genes under its control. AbrB contains a helix-turn-helix structure, but this domain ends before the helix-turn-helix begins. The product of the B. subtilis gene spoVT is another member of this family and is also a transcriptional regulator. DNA-binding activity in this AbrB homologue requires hexamerisation. Another family member has been isolated from the Sulfolobus solfataricus and has been identified as a homologue of bacterial repressor-like proteins. The Escherichia coli family member SohA or Prl1F appears to be bifunctional and is able to regulate its own expression as well as relieve the export block imposed by high-level synthesis of beta-galactosidase hybrid proteins.


Pssm-ID: 198034 [Multi-domain]  Cd Length: 45  Bit Score: 34.41  E-value: 4.71e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1260004914  301 AIELPDEAVNKLRLEENDYVTVAVEEDKIVIKKA 334
Cdd:smart00966   8 QVTIPKEVREKLGIKEGDEVELEVDGDGIILEPV 41
 
Name Accession Description Interval E-value
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 126-214 1.70e-24

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 95.24  E-value: 1.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260004914 126 VYMTIFTFISACVLAPIMEEVIFRGFFLQRMAHKWGIKKAVIISSIIFGLGHFD----VIGAFMFGVVMCLLYIKTKNIW 201
Cdd:COG1266     1 LLWLLLFLLVVVILAPIAEELLFRGYLLGRLRRRFGPWLAILLSSLLFGLLHLPnllgFLPAFLLGLVLGLLYLRTGSLW 80

                          90
                  ....*....|...
gi 1260004914 202 TNIAVHALNNLIA 214
Cdd:COG1266    81 VPILLHALNNLLA 93
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 130-213 3.61e-21

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: 86.45  E-value: 3.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260004914 130 IFTFISACVLAPIMEEVIFRGFFLQRMAHKWGIKKAVIISSIIFGLGHF-----DVIGAFMFGVVMCLLYIKTKNIWTNI 204
Cdd:pfam02517   4 LLLLLLLALLAPIGEELLFRGYLLPRLRRRLWPVLAILISSLLFGLAHLpngpqLFLLAFLLGLILGYLYLRTGSLWAAI 83


                  ....*....
gi 1260004914 205 AVHALNNLI 213
Cdd:pfam02517  84 LLHALNNLL 92
pepcterm_CAAX TIGR03008
CAAX prenyl protease-related protein; The CAAX prenyl protease, in eukaryotes, catalyzes three ...
 128-213 2.73e-08

CAAX prenyl protease-related protein; The CAAX prenyl protease, in eukaryotes, catalyzes three covalent modifications, including cleavage and acylation, at the C-terminus of certain proteins in a process connected to protein sorting. This family describes a bacterial protein family homologous to one domain of the CAAX-processing enzyme. Members of this protein family are found in genomes that carry a predicted protein sorting system, PEP-CTERM/exosortase, usually in the vicinity of the EpsH homolog that is the hallmark of the system. The function of this protein is unknown, but it may relate to protein motification. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 163100  Cd Length: 222  Bit Score: 53.64  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260004914 128 MTIFTFISACVLAPIMEEVIFRGFFLQRMAHK-----------WgikKAVIISSIIFGLGHFDVIGAFMFGVVMCLLYIK 196
Cdd:TIGR03008 115 LIAFRLAGATLVVPVMEELFWRSFLLRYLQQSdfesvpggrfhW---PSFLAVTLLFGLEHHLIVAGLIAGLAYNLLLLR 191

                          90
                  ....*....|....*..
gi 1260004914 197 TKNIWTNIAVHALNNLI 213
Cdd:TIGR03008 192 TGSIMACILAHAVTNGL 208
MazE COG2336
Antitoxin component MazE of the MazEF toxin-antitoxin module [Defense mechanisms];
301-337 6.13e-04

Antitoxin component MazE of the MazEF toxin-antitoxin module [Defense mechanisms];


Pssm-ID: 441907  Cd Length: 80  Bit Score: 37.94  E-value: 6.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1260004914 301 AIELPDEAVNKLRLEENDYVTVAVEEDKIVIKKAHNR 337
Cdd:COG2336    13 GVRIPKALLEQLGLKEGDEVELEVEDGRIVIRPVRRP 49
SpoVT_AbrB smart00966
SpoVT / AbrB like domain; This domain is found in AbrB from Bacillus subtilis. The product of ...
 301-334 4.71e-03

SpoVT / AbrB like domain; This domain is found in AbrB from Bacillus subtilis. The product of the abrB gene is an ambiactive repressor and activator of the transcription of genes expressed during the transition state between vegetative growth and the onset of stationary phase and sporulation. AbrB is thought to interact directly with the transcription initiation regions of genes under its control. AbrB contains a helix-turn-helix structure, but this domain ends before the helix-turn-helix begins. The product of the B. subtilis gene spoVT is another member of this family and is also a transcriptional regulator. DNA-binding activity in this AbrB homologue requires hexamerisation. Another family member has been isolated from the Sulfolobus solfataricus and has been identified as a homologue of bacterial repressor-like proteins. The Escherichia coli family member SohA or Prl1F appears to be bifunctional and is able to regulate its own expression as well as relieve the export block imposed by high-level synthesis of beta-galactosidase hybrid proteins.


Pssm-ID: 198034 [Multi-domain]  Cd Length: 45  Bit Score: 34.41  E-value: 4.71e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1260004914  301 AIELPDEAVNKLRLEENDYVTVAVEEDKIVIKKA 334
Cdd:smart00966   8 QVTIPKEVREKLGIKEGDEVELEVDGDGIILEPV 41
 
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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