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Conserved domains on  [gi|493801038|ref|WP_006748948|]
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JDVT-CTERM system glutamic-type intramembrane protease [Thioalkalivibrio paradoxus]

Protein Classification

JDVT-CTERM system glutamic-type intramembrane protease( domain architecture ID 14337512)

JDVT-CTERM system glutamic-type intramembrane protease is a homolog of eukaryotic type II CAAX prenylation site proteases, which proteolytically remove C-terminal residues of farnesylated and geranylated proteins

EC:  3.4.-.-
Gene Ontology:  GO:0070007

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
JDVT-CAAX super family cl38957
JDVT-CTERM system glutamic-type intramembrane protease; See NF033191.
50-143 5.45e-20

JDVT-CTERM system glutamic-type intramembrane protease; See NF033191.


The actual alignment was detected with superfamily member NF033192:

Pssm-ID: 467988 [Multi-domain]  Cd Length: 98  Bit Score: 78.91  E-value: 5.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493801038  50 FLSAVLVYPVLEEIVFRGLLQGWLLERNWGRSRLGPVTAANAIAALLFALAHLIHQPPAWAAAVILPALVFGYFRERHG- 128
Cdd:NF033192   1 LLSLVLLQPLLEEWVFRGGLQEWLLRRTWGRARLGGISLANLLTSAAFALAHLVAHPWLWALAVFVPSLLFGLFYERSRs 80
                         90
                 ....*....|....*
gi 493801038 129 LWTAIMLHVLYNSGF 143
Cdd:NF033192  81 LGPCIALHAFYNAGF 95
 
Name Accession Description Interval E-value
JDVT-CAAX NF033192
JDVT-CTERM system glutamic-type intramembrane protease; See NF033191.
50-143 5.45e-20

JDVT-CTERM system glutamic-type intramembrane protease; See NF033191.


Pssm-ID: 467988 [Multi-domain]  Cd Length: 98  Bit Score: 78.91  E-value: 5.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493801038  50 FLSAVLVYPVLEEIVFRGLLQGWLLERNWGRSRLGPVTAANAIAALLFALAHLIHQPPAWAAAVILPALVFGYFRERHG- 128
Cdd:NF033192   1 LLSLVLLQPLLEEWVFRGGLQEWLLRRTWGRARLGGISLANLLTSAAFALAHLVAHPWLWALAVFVPSLLFGLFYERSRs 80
                         90
                 ....*....|....*
gi 493801038 129 LWTAIMLHVLYNSGF 143
Cdd:NF033192  81 LGPCIALHAFYNAGF 95
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
47-141 2.30e-05

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 40.93  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493801038  47 PWFFLSAVLVYPVLEEIVFRGLLQGWLlernwgRSRLGPVtaanAIAALLFALAHLIHQP-PAWAAAVILPALVFGYFRE 125
Cdd:COG1266    5 LLFLLVVVILAPIAEELLFRGYLLGRL------RRRFGPW----LAILLSSLLFGLLHLPnLLGFLPAFLLGLVLGLLYL 74
                         90
                 ....*....|....*..
gi 493801038 126 RHG-LWTAIMLHVLYNS 141
Cdd:COG1266   75 RTGsLWVPILLHALNNL 91
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
48-140 6.62e-05

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: 39.46  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493801038   48 WFFLSAVLVYPVLEEIVFRGLLQGWLLERNWGRsrlgpvtaANAIAALLFALAHLIHQPPAWAAAVILPALVFGYFRERH 127
Cdd:pfam02517   5 LLLLLLALLAPIGEELLFRGYLLPRLRRRLWPV--------LAILISSLLFGLAHLPNGPQLFLLAFLLGLILGYLYLRT 76
                          90
                  ....*....|....
gi 493801038  128 G-LWTAIMLHVLYN 140
Cdd:pfam02517  77 GsLWAAILLHALNN 90
 
Name Accession Description Interval E-value
JDVT-CAAX NF033192
JDVT-CTERM system glutamic-type intramembrane protease; See NF033191.
50-143 5.45e-20

JDVT-CTERM system glutamic-type intramembrane protease; See NF033191.


Pssm-ID: 467988 [Multi-domain]  Cd Length: 98  Bit Score: 78.91  E-value: 5.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493801038  50 FLSAVLVYPVLEEIVFRGLLQGWLLERNWGRSRLGPVTAANAIAALLFALAHLIHQPPAWAAAVILPALVFGYFRERHG- 128
Cdd:NF033192   1 LLSLVLLQPLLEEWVFRGGLQEWLLRRTWGRARLGGISLANLLTSAAFALAHLVAHPWLWALAVFVPSLLFGLFYERSRs 80
                         90
                 ....*....|....*
gi 493801038 129 LWTAIMLHVLYNSGF 143
Cdd:NF033192  81 LGPCIALHAFYNAGF 95
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
47-141 2.30e-05

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 40.93  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493801038  47 PWFFLSAVLVYPVLEEIVFRGLLQGWLlernwgRSRLGPVtaanAIAALLFALAHLIHQP-PAWAAAVILPALVFGYFRE 125
Cdd:COG1266    5 LLFLLVVVILAPIAEELLFRGYLLGRL------RRRFGPW----LAILLSSLLFGLLHLPnLLGFLPAFLLGLVLGLLYL 74
                         90
                 ....*....|....*..
gi 493801038 126 RHG-LWTAIMLHVLYNS 141
Cdd:COG1266   75 RTGsLWVPILLHALNNL 91
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
48-140 6.62e-05

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: 39.46  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493801038   48 WFFLSAVLVYPVLEEIVFRGLLQGWLLERNWGRsrlgpvtaANAIAALLFALAHLIHQPPAWAAAVILPALVFGYFRERH 127
Cdd:pfam02517   5 LLLLLLALLAPIGEELLFRGYLLPRLRRRLWPV--------LAILISSLLFGLAHLPNGPQLFLLAFLLGLILGYLYLRT 76
                          90
                  ....*....|....
gi 493801038  128 G-LWTAIMLHVLYN 140
Cdd:pfam02517  77 GsLWAAILLHALNN 90
 
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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