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Conserved domains on  [gi|119574303|gb|EAW53918|]
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chromosome 16 open reading frame 45, isoform CRA_a [Homo sapiens]

Protein Classification

bMERB family protein( domain architecture ID 581919)

bMERB (bivalent Mical/EHBP Rab binding) family protein is a DUF3585 domain-containing protein; similar to Homo sapiens bMERB domain-containing protein 1 and Schistosoma mansoni circulating cathodic antigen

Gene Ontology:  GO:0032482|GO:0031267
PubMed:  27552051

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bMERB_dom super family cl48129
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
 51-148 8.36e-21

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


The actual alignment was detected with superfamily member pfam12130:

Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 83.72  E-value: 8.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574303   51 EEIELEMAKIQRLREVLVRRESELRFMMDDIQLCKDIMDLKQELQNLVAIPEKEKTKLQKQREDELIQKIHKLVQKRDFL 130
Cdd:pfam12130  34 EQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELRELMSKPDWLKTEEDKQREEELLEELVEIVEQRDAL 113

                          90
                  ....*....|....*...
gi 119574303  131 VDDAEVERLREQEEDKEM 148
Cdd:pfam12130 114 VDSLEEDRLREEEEDEEL 131
 
Name Accession Description Interval E-value
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
 51-148 8.36e-21

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 83.72  E-value: 8.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574303   51 EEIELEMAKIQRLREVLVRRESELRFMMDDIQLCKDIMDLKQELQNLVAIPEKEKTKLQKQREDELIQKIHKLVQKRDFL 130
Cdd:pfam12130  34 EQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELRELMSKPDWLKTEEDKQREEELLEELVEIVEQRDAL 113

                          90
                  ....*....|....*...
gi 119574303  131 VDDAEVERLREQEEDKEM 148
Cdd:pfam12130 114 VDSLEEDRLREEEEDEEL 131
 
Name Accession Description Interval E-value
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
 51-148 8.36e-21

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 83.72  E-value: 8.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119574303   51 EEIELEMAKIQRLREVLVRRESELRFMMDDIQLCKDIMDLKQELQNLVAIPEKEKTKLQKQREDELIQKIHKLVQKRDFL 130
Cdd:pfam12130  34 EQLLQEWFKLVNEKNALVRRESELMYLAKEQDLEERQARLEQELRELMSKPDWLKTEEDKQREEELLEELVEIVEQRDAL 113

                          90
                  ....*....|....*...
gi 119574303  131 VDDAEVERLREQEEDKEM 148
Cdd:pfam12130 114 VDSLEEDRLREEEEDEEL 131
 
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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