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Conserved domains on  [gi|20127652|ref|NP_061092|]
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presenilin-associated rhomboid-like protein, mitochondrial isoform 1 precursor [Homo sapiens]

Protein Classification

rhomboid family protein( domain architecture ID 10483871)

rhomboid family protein may be an intramembrane serine protease that catalyzes regulated intramembrane proteolysis, resulting in the release of functional polypeptides from their membrane anchors, or an inactive rhomboid protein that lacks the conserved active sites and has no peptidase activity

CATH:  1.20.1540.10
Gene Ontology:  GO:0016020
MEROPS:  S54
PubMed:  24099005|22035660|26527717|12620104
SCOP:  4000471

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 209-350 8.80e-30

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


:

Pssm-ID: 426384  Cd Length: 147  Bit Score: 111.93  E-value: 8.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20127652   209 MLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFMAVYLSAGVISNFVSYvgkVATGRYGPSLGASGAIMTVLAAVC 288
Cdd:pfam01694  10 LITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSY---LFSPLSTPSVGASGAIFGLLGALL 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20127652   289 TKIPEGRLAIIFLPMFTFtagnALKAIIAMDTAGMILGWKFFDHAAHLGGALFGIWYVTYGH 350
Cdd:pfam01694  87 VLGPRNRILLFGLIGALL----ALLLFILLNLVLGLLPGNGVSNLAHLGGLLVGLLLGFILL 144
 
Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 209-350 8.80e-30

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


Pssm-ID: 426384  Cd Length: 147  Bit Score: 111.93  E-value: 8.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20127652   209 MLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFMAVYLSAGVISNFVSYvgkVATGRYGPSLGASGAIMTVLAAVC 288
Cdd:pfam01694  10 LITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSY---LFSPLSTPSVGASGAIFGLLGALL 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20127652   289 TKIPEGRLAIIFLPMFTFtagnALKAIIAMDTAGMILGWKFFDHAAHLGGALFGIWYVTYGH 350
Cdd:pfam01694  87 VLGPRNRILLFGLIGALL----ALLLFILLNLVLGLLPGNGVSNLAHLGGLLVGLLLGFILL 144
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
 169-345 3.05e-27

Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 106.48  E-value: 3.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20127652 169 VTGIIAANVLVFCLWRVpsLQRTMIRYFTSNPASKVLCSP--MLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFM 246
Cdd:COG0705   6 TLALIALNVLVFLLQLL--LGGELLNWLALVPARLLLGELwrLLTSMFLHGGFLHLLFNMLALWVFGPLLERRLGSKRFL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20127652 247 AVYLSAGVISNFVSYVgkVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPM--FTFTAGnalkaIIAMDTAGMI 324
Cdd:COG0705  84 LLYLLSGLGGGLLQLL--FSPGSGYPLVGASGAIFGLLGALLVLGPRRRVLLLFIPIpaLLFLLV-----WLLLGLLFGL 156

                       170       180
                ....*....|....*....|.
gi 20127652 325 LGWKFFDHAAHLGGALFGIWY 345
Cdd:COG0705 157 LGGGGIAWEAHLGGLLAGLLL 177
 
Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 209-350 8.80e-30

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


Pssm-ID: 426384  Cd Length: 147  Bit Score: 111.93  E-value: 8.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20127652   209 MLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFMAVYLSAGVISNFVSYvgkVATGRYGPSLGASGAIMTVLAAVC 288
Cdd:pfam01694  10 LITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSY---LFSPLSTPSVGASGAIFGLLGALL 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20127652   289 TKIPEGRLAIIFLPMFTFtagnALKAIIAMDTAGMILGWKFFDHAAHLGGALFGIWYVTYGH 350
Cdd:pfam01694  87 VLGPRNRILLFGLIGALL----ALLLFILLNLVLGLLPGNGVSNLAHLGGLLVGLLLGFILL 144
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
 169-345 3.05e-27

Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 106.48  E-value: 3.05e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20127652 169 VTGIIAANVLVFCLWRVpsLQRTMIRYFTSNPASKVLCSP--MLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFM 246
Cdd:COG0705   6 TLALIALNVLVFLLQLL--LGGELLNWLALVPARLLLGELwrLLTSMFLHGGFLHLLFNMLALWVFGPLLERRLGSKRFL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20127652 247 AVYLSAGVISNFVSYVgkVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPM--FTFTAGnalkaIIAMDTAGMI 324
Cdd:COG0705  84 LLYLLSGLGGGLLQLL--FSPGSGYPLVGASGAIFGLLGALLVLGPRRRVLLLFIPIpaLLFLLV-----WLLLGLLFGL 156

                       170       180
                ....*....|....*....|.
gi 20127652 325 LGWKFFDHAAHLGGALFGIWY 345
Cdd:COG0705 157 LGGGGIAWEAHLGGLLAGLLL 177
 
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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