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Conserved domains on  [gi|2462577713|ref|XP_054200149|]
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rhomboid-related protein 4 isoform X5 [Homo sapiens]

Protein Classification

rhomboid family protein( domain architecture ID 229382)

rhomboid family protein may be a membrane-bound serine protease that catalyzes regulated intramembrane proteolysis, resulting in the release of functional polypeptides from their membrane anchors

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlpG super family cl42100
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
 26-150 1.22e-09

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


The actual alignment was detected with superfamily member COG0705:

Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 55.25  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462577713  26 NIPPVTLATLALN--IWFFLNPQKPLYSSCLS-VEKCYQQKDWQRLLLSPLHHADDWHLYFNMASMLWKGINLERRLGSR 102
Cdd:COG0705     1 RLPPVTLALIALNvlVFLLQLLLGGELLNWLAlVPARLLLGELWRLLTSMFLHGGFLHLLFNMLALWVFGPLLERRLGSK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462577713 103 WFAyvitAFSVLTGVVYLLLQFAVAEFMDEPdfkrscAVGFSGVLFAL 150
Cdd:COG0705    81 RFL----LLYLLSGLGGGLLQLLFSPGSGYP------LVGASGAIFGL 118
 
Name Accession Description Interval E-value
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
 26-150 1.22e-09

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


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 55.25  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462577713  26 NIPPVTLATLALN--IWFFLNPQKPLYSSCLS-VEKCYQQKDWQRLLLSPLHHADDWHLYFNMASMLWKGINLERRLGSR 102
Cdd:COG0705     1 RLPPVTLALIALNvlVFLLQLLLGGELLNWLAlVPARLLLGELWRLLTSMFLHGGFLHLLFNMLALWVFGPLLERRLGSK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462577713 103 WFAyvitAFSVLTGVVYLLLQFAVAEFMDEPdfkrscAVGFSGVLFAL 150
Cdd:COG0705    81 RFL----LLYLLSGLGGGLLQLLFSPGSGYP------LVGASGAIFGL 118
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 65-150 2.41e-08

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: 50.68  E-value: 2.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462577713  65 WQRLLLSPLHHADDWHLYFNMASMLWKGINLERRLGSRWFAYVITAFSVLTGVVYLLLqfavaefmdepDFKRSCAVGFS 144
Cdd:pfam01694   7 LWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLF-----------SPLSTPSVGAS 75


                  ....*.
gi 2462577713 145 GVLFAL 150
Cdd:pfam01694  76 GAIFGL 81
 
Name Accession Description Interval E-value
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
 26-150 1.22e-09

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


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 55.25  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462577713  26 NIPPVTLATLALN--IWFFLNPQKPLYSSCLS-VEKCYQQKDWQRLLLSPLHHADDWHLYFNMASMLWKGINLERRLGSR 102
Cdd:COG0705     1 RLPPVTLALIALNvlVFLLQLLLGGELLNWLAlVPARLLLGELWRLLTSMFLHGGFLHLLFNMLALWVFGPLLERRLGSK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462577713 103 WFAyvitAFSVLTGVVYLLLQFAVAEFMDEPdfkrscAVGFSGVLFAL 150
Cdd:COG0705    81 RFL----LLYLLSGLGGGLLQLLFSPGSGYP------LVGASGAIFGL 118
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 65-150 2.41e-08

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: 50.68  E-value: 2.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462577713  65 WQRLLLSPLHHADDWHLYFNMASMLWKGINLERRLGSRWFAYVITAFSVLTGVVYLLLqfavaefmdepDFKRSCAVGFS 144
Cdd:pfam01694   7 LWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLF-----------SPLSTPSVGAS 75


                  ....*.
gi 2462577713 145 GVLFAL 150
Cdd:pfam01694  76 GAIFGL 81
 
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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