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Conserved domains on  [gi|1034634388|ref|XP_016862291|]
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presenilin-associated rhomboid-like protein, mitochondrial isoform X4 [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
Rhomboid super family cl21536
Rhomboid family; This family contains integral membrane proteins that are related to ...
219-266 5.79e-04

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.


The actual alignment was detected with superfamily member pfam01694:

Pssm-ID: 451297  Cd Length: 147  Bit Score: 39.51  E-value: 5.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1034634388 219 RYGPSLGAALKAIIAMDTAGMILGWKFFDHAAHLGGALFGMISLYTWR 266
Cdd:pfam01694  97 FGLIGALLALLLFILLNLVLGLLPGNGVSNLAHLGGLLVGLLLGFILL 144
 
Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
219-266 5.79e-04

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: 39.51  E-value: 5.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1034634388 219 RYGPSLGAALKAIIAMDTAGMILGWKFFDHAAHLGGALFGMISLYTWR 266
Cdd:pfam01694  97 FGLIGALLALLLFILLNLVLGLLPGNGVSNLAHLGGLLVGLLLGFILL 144
 
Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
219-266 5.79e-04

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: 39.51  E-value: 5.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1034634388 219 RYGPSLGAALKAIIAMDTAGMILGWKFFDHAAHLGGALFGMISLYTWR 266
Cdd:pfam01694  97 FGLIGALLALLLFILLNLVLGLLPGNGVSNLAHLGGLLVGLLLGFILL 144
 
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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