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Conserved domains on  [gi|916740054|ref|WP_051347110|]
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JDVT-CTERM system glutamic-type intramembrane protease [Thiomicrorhabdus chilensis]

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 NF033192
JDVT-CTERM system glutamic-type intramembrane protease; See NF033191.
 56-153 1.09e-35

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


:

Pssm-ID: 467988 [Multi-domain]  Cd Length: 98  Bit Score: 119.36  E-value: 1.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916740054  56 LFIMVFWQPLIEELFFRGLLQGKLFQQTWFQESLAGISRANIVVSILFVATHFIYHPPLWALAVFIPSLIFGWFRDRYDS 135
Cdd:NF033192   1 LLSLVLLQPLLEEWVFRGGLQEWLLRRTWGRARLGGISLANLLTSAAFALAHLVAHPWLWALAVFVPSLLFGLFYERSRS 80

                         90
                 ....*....|....*...
gi 916740054 136 VLPSILLHAFYNASFLTV 153
Cdd:NF033192  81 LGPCIALHAFYNAGFLAV 98
 
Name Accession Description Interval E-value
JDVT-CAAX NF033192
JDVT-CTERM system glutamic-type intramembrane protease; See NF033191.
 56-153 1.09e-35

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


Pssm-ID: 467988 [Multi-domain]  Cd Length: 98  Bit Score: 119.36  E-value: 1.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916740054  56 LFIMVFWQPLIEELFFRGLLQGKLFQQTWFQESLAGISRANIVVSILFVATHFIYHPPLWALAVFIPSLIFGWFRDRYDS 135
Cdd:NF033192   1 LLSLVLLQPLLEEWVFRGGLQEWLLRRTWGRARLGGISLANLLTSAAFALAHLVAHPWLWALAVFVPSLLFGLFYERSRS 80

                         90
                 ....*....|....*...
gi 916740054 136 VLPSILLHAFYNASFLTV 153
Cdd:NF033192  81 LGPCIALHAFYNAGFLAV 98
Mrt_core NF040914
myxosortase core domain;
53-147 8.32e-17

myxosortase core domain;


Pssm-ID: 468849 [Multi-domain]  Cd Length: 108  Bit Score: 71.07  E-value: 8.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916740054  53 WMALFIMVFWQPLIEELFFRGLLQGKL---FQQTWFQESLAGISRANIVVSILFVATHFIYHPPLWALAVFIPSLIFGWF 129
Cdd:NF040914   1 LLLVLTQLLLVALPEEFFYRGYLQTRLdqlWPPRRRRLLGAPLGPAILLTSALFALGHLLTIPHPARLAVFFPSLLFGWL 80

                         90
                 ....*....|....*...
gi 916740054 130 RDRYDSVLPSILLHAFYN 147
Cdd:NF040914  81 RERTGGIGAPVVFHALCN 98
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 53-154 5.21e-11

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 55.95  E-value: 5.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916740054  53 WMALFIMVFWQPLIEELFFRGLLQGKLFQQTwfqeslaGISRANIVVSILFVATHFIYhpPLWALAVFIPSLIFGWFRDR 132
Cdd:COG1266    5 LLFLLVVVILAPIAEELLFRGYLLGRLRRRF-------GPWLAILLSSLLFGLLHLPN--LLGFLPAFLLGLVLGLLYLR 75

                         90       100
                 ....*....|....*....|..
gi 916740054 133 YDSVLPSILLHAFYNASFLTVF 154
Cdd:COG1266   76 TGSLWVPILLHALNNLLALLLL 97
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 53-148 7.01e-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: 52.94  E-value: 7.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916740054   53 WMALFIMVFWQPLIEELFFRGLLQGKLFQQTWFqeslagiSRANIVVSILFVATHFiYHPPLWALAVFIPSLIFGWFRDR 132
Cdd:pfam02517   4 LLLLLLLALLAPIGEELLFRGYLLPRLRRRLWP-------VLAILISSLLFGLAHL-PNGPQLFLLAFLLGLILGYLYLR 75

                          90
                  ....*....|....*.
gi 916740054  133 YDSVLPSILLHAFYNA 148
Cdd:pfam02517  76 TGSLWAAILLHALNNL 91
 
Name Accession Description Interval E-value
JDVT-CAAX NF033192
JDVT-CTERM system glutamic-type intramembrane protease; See NF033191.
 56-153 1.09e-35

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


Pssm-ID: 467988 [Multi-domain]  Cd Length: 98  Bit Score: 119.36  E-value: 1.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916740054  56 LFIMVFWQPLIEELFFRGLLQGKLFQQTWFQESLAGISRANIVVSILFVATHFIYHPPLWALAVFIPSLIFGWFRDRYDS 135
Cdd:NF033192   1 LLSLVLLQPLLEEWVFRGGLQEWLLRRTWGRARLGGISLANLLTSAAFALAHLVAHPWLWALAVFVPSLLFGLFYERSRS 80

                         90
                 ....*....|....*...
gi 916740054 136 VLPSILLHAFYNASFLTV 153
Cdd:NF033192  81 LGPCIALHAFYNAGFLAV 98
Mrt_core NF040914
myxosortase core domain;
53-147 8.32e-17

myxosortase core domain;


Pssm-ID: 468849 [Multi-domain]  Cd Length: 108  Bit Score: 71.07  E-value: 8.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916740054  53 WMALFIMVFWQPLIEELFFRGLLQGKL---FQQTWFQESLAGISRANIVVSILFVATHFIYHPPLWALAVFIPSLIFGWF 129
Cdd:NF040914   1 LLLVLTQLLLVALPEEFFYRGYLQTRLdqlWPPRRRRLLGAPLGPAILLTSALFALGHLLTIPHPARLAVFFPSLLFGWL 80

                         90
                 ....*....|....*...
gi 916740054 130 RDRYDSVLPSILLHAFYN 147
Cdd:NF040914  81 RERTGGIGAPVVFHALCN 98
YdiL COG1266
Membrane protease YdiL, CAAX protease family [Posttranslational modification, protein turnover, ...
 53-154 5.21e-11

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


Pssm-ID: 440877 [Multi-domain]  Cd Length: 97  Bit Score: 55.95  E-value: 5.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916740054  53 WMALFIMVFWQPLIEELFFRGLLQGKLFQQTwfqeslaGISRANIVVSILFVATHFIYhpPLWALAVFIPSLIFGWFRDR 132
Cdd:COG1266    5 LLFLLVVVILAPIAEELLFRGYLLGRLRRRF-------GPWLAILLSSLLFGLLHLPN--LLGFLPAFLLGLVLGLLYLR 75

                         90       100
                 ....*....|....*....|..
gi 916740054 133 YDSVLPSILLHAFYNASFLTVF 154
Cdd:COG1266   76 TGSLWVPILLHALNNLLALLLL 97
Rce1-like pfam02517
Type II CAAX prenyl endopeptidase Rce1-like; This family (also known as the ABI (abortive ...
 53-148 7.01e-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: 52.94  E-value: 7.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 916740054   53 WMALFIMVFWQPLIEELFFRGLLQGKLFQQTWFqeslagiSRANIVVSILFVATHFiYHPPLWALAVFIPSLIFGWFRDR 132
Cdd:pfam02517   4 LLLLLLLALLAPIGEELLFRGYLLPRLRRRLWP-------VLAILISSLLFGLAHL-PNGPQLFLLAFLLGLILGYLYLR 75

                          90
                  ....*....|....*.
gi 916740054  133 YDSVLPSILLHAFYNA 148
Cdd:pfam02517  76 TGSLWAAILLHALNNL 91
 
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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