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Conserved domains on  [gi|17537737|ref|NP_494399|]
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Receptor expression-enhancing protein [Caenorhabditis elegans]

Protein Classification

HVA22/TB2/DP1 family protein( domain architecture ID 10504231)

HVA22/TB2/DP1 family protein such as receptor expression enhancing proteins (REEPs), which are membrane shaping adapter proteins that modulate specific G protein-coupled receptor trafficking by affecting ER cargo capacity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TB2_DP1_HVA22 pfam03134
TB2/DP1, HVA22 family; This family includes members from a wide variety of eukaryotes. It ...
 17-95 1.45e-16

TB2/DP1, HVA22 family; This family includes members from a wide variety of eukaryotes. It includes the TB2/DP1 (deleted in polyposis) protein, which in humans is deleted in severe forms of familial adenomatous polyposis, an autosomal dominant oncological inherited disease. The family also includes the plant protein of known similarity to TB2/DP1, the HVA22 abscisic acid-induced protein, which is thought to be a regulatory protein.


:

Pssm-ID: 460820  Cd Length: 77  Bit Score: 72.15  E-value: 1.45e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17537737    17 PVIGSFKVLKKPTKPRLIECMHYWTIYGSFLIVDWFLSTFyvSCFIPFYDFFILTFTVLMAIPHIGFASVLYTKFLAPF 95
Cdd:pfam03134   1 PAYASYKALESPDKDDDTQWLTYWVVFGFFTLVESFADFL--LSWIPFYYEFKLLFLLWLVLPQTQGATYIYEKFLRPF 77
 
Name Accession Description Interval E-value
TB2_DP1_HVA22 pfam03134
TB2/DP1, HVA22 family; This family includes members from a wide variety of eukaryotes. It ...
 17-95 1.45e-16

TB2/DP1, HVA22 family; This family includes members from a wide variety of eukaryotes. It includes the TB2/DP1 (deleted in polyposis) protein, which in humans is deleted in severe forms of familial adenomatous polyposis, an autosomal dominant oncological inherited disease. The family also includes the plant protein of known similarity to TB2/DP1, the HVA22 abscisic acid-induced protein, which is thought to be a regulatory protein.


Pssm-ID: 460820  Cd Length: 77  Bit Score: 72.15  E-value: 1.45e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17537737    17 PVIGSFKVLKKPTKPRLIECMHYWTIYGSFLIVDWFLSTFyvSCFIPFYDFFILTFTVLMAIPHIGFASVLYTKFLAPF 95
Cdd:pfam03134   1 PAYASYKALESPDKDDDTQWLTYWVVFGFFTLVESFADFL--LSWIPFYYEFKLLFLLWLVLPQTQGATYIYEKFLRPF 77
YOP1 COG5052
Protein involved in membrane traffic [Intracellular trafficking and secretion];
8-103 1.11e-04

Protein involved in membrane traffic [Intracellular trafficking and secretion];


Pssm-ID: 227385  Cd Length: 186  Bit Score: 41.71  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537737   8 LSNLIGIVAPVIGSFKVLKKPTKPRLIECMHYWTIYGSFLIVDWFLSTFYVscFIPFYDFFILTFTVLMAIPHIGFASVL 87
Cdd:COG5052  62 LTNVAGFSLPAQLSLVAFYTLNFMDDTQLLTYWMVFGFLSAIEKYSGAILS--KVPFYWTLKNVFLLWLLLPRTEGARII 139

                        90
                ....*....|....*.
gi 17537737  88 YTKFLAPFLRKYERRI 103
Cdd:COG5052 140 YDDIIAPDVSDHGFRT 155
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 55-112 9.54e-03

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 36.75  E-value: 9.54e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17537737  55 TFYVSCFIPFYDFFILTFTVLMAIPHIGFASVLYTKFLAPFLRKYERRIDNISAKLMD 112
Cdd:cd18778 127 TLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQD 184
 
Name Accession Description Interval E-value
TB2_DP1_HVA22 pfam03134
TB2/DP1, HVA22 family; This family includes members from a wide variety of eukaryotes. It ...
 17-95 1.45e-16

TB2/DP1, HVA22 family; This family includes members from a wide variety of eukaryotes. It includes the TB2/DP1 (deleted in polyposis) protein, which in humans is deleted in severe forms of familial adenomatous polyposis, an autosomal dominant oncological inherited disease. The family also includes the plant protein of known similarity to TB2/DP1, the HVA22 abscisic acid-induced protein, which is thought to be a regulatory protein.


Pssm-ID: 460820  Cd Length: 77  Bit Score: 72.15  E-value: 1.45e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17537737    17 PVIGSFKVLKKPTKPRLIECMHYWTIYGSFLIVDWFLSTFyvSCFIPFYDFFILTFTVLMAIPHIGFASVLYTKFLAPF 95
Cdd:pfam03134   1 PAYASYKALESPDKDDDTQWLTYWVVFGFFTLVESFADFL--LSWIPFYYEFKLLFLLWLVLPQTQGATYIYEKFLRPF 77
YOP1 COG5052
Protein involved in membrane traffic [Intracellular trafficking and secretion];
8-103 1.11e-04

Protein involved in membrane traffic [Intracellular trafficking and secretion];


Pssm-ID: 227385  Cd Length: 186  Bit Score: 41.71  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537737   8 LSNLIGIVAPVIGSFKVLKKPTKPRLIECMHYWTIYGSFLIVDWFLSTFYVscFIPFYDFFILTFTVLMAIPHIGFASVL 87
Cdd:COG5052  62 LTNVAGFSLPAQLSLVAFYTLNFMDDTQLLTYWMVFGFLSAIEKYSGAILS--KVPFYWTLKNVFLLWLLLPRTEGARII 139

                        90
                ....*....|....*.
gi 17537737  88 YTKFLAPFLRKYERRI 103
Cdd:COG5052 140 YDDIIAPDVSDHGFRT 155
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 55-112 9.54e-03

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 36.75  E-value: 9.54e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17537737  55 TFYVSCFIPFYDFFILTFTVLMAIPHIGFASVLYTKFLAPFLRKYERRIDNISAKLMD 112
Cdd:cd18778 127 TLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQD 184
 
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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