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Conserved domains on  [gi|1405457301|ref|NP_001351406|]
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erlin-2 isoform 2 [Mus musculus]

Protein Classification

erlin( domain architecture ID 10130465)

erlin family protein similar to Homo sapiens erlin-1 and erlin-2, which forms the ERLIN1/ERLIN2 complex that mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 40-332 0e+00

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


:

Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 598.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  40 CASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFL 119
Cdd:cd03406     1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 120 VPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNI 199
Cdd:cd03406    81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 200 PEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREK 279
Cdd:cd03406   161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405457301 280 AKADAECYTALKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDS 332
Cdd:cd03406   241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 40-332 0e+00

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 598.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  40 CASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFL 119
Cdd:cd03406     1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 120 VPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNI 199
Cdd:cd03406    81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 200 PEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREK 279
Cdd:cd03406   161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405457301 280 AKADAECYTALKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDS 332
Cdd:cd03406   241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
PHB smart00244
prohibitin homologues; prohibitin homologues
 45-211 7.06e-30

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 112.37  E-value: 7.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301   45 SAVHKIEEGHIGVYYRGGALLTsTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLVPNAV 124
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDA--VVYYRVLDPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  125 YDIVKNYTADYdkALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAVRVTKPNIPEAIR 204
Cdd:smart00244  78 RAVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAEAW--GIKVEDVEIKDIRLPEEIK 153


                   ....*..
gi 1405457301  205 RNYELME 211
Cdd:smart00244 154 EAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 49-231 2.47e-26

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 103.17  E-value: 2.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  49 KIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLV-PNAVYDI 127
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDV--TVIYRVnPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 128 VKNY-TADYDKALIFNKIHHELNQFCSVHTLQEVYIElFDQIDENLKLALQQDLtsMAPGLVIQAVRVTKPNIPEAIRRN 206
Cdd:pfam01145  79 VQNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEEL--AKYGVEIIDVQITDIDPPPEIAEA 155

                         170       180
                  ....*....|....*....|....*
gi 1405457301 207 yelMESEKTKLLIAAQKQKVVEKEA 231
Cdd:pfam01145 156 ---IEAKQTAEQEAEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 28-332 6.23e-19

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 85.66  E-value: 6.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  28 LGAVVAVASSFFcasLFSAVHKIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVM 107
Cdd:COG0330     5 LLLILLVLVLVL---LFSSVYIVPQGERGVVLRFGKY-VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 108 IYFDriEVVNFLVPNAvYDIVKNyTADYDKALIfNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGL 187
Cdd:COG0330    81 VDVD--AVVQYRITDP-AKFLYN-VENAEEALR-QLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDPY--GI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 188 VIQAVRVTKPNIPEAIRRNYElmesektKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEItygqkvmEKETEKkis 267
Cdd:COG0330   154 EVVDVEIKDIDPPEEVQDAME-------DRMKAEREREAAILEAEGYREAAIIRAEGEAQRAII-------EAEAYR--- 216

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405457301 268 eieDAAFLareKAKADAEcyTALKIAEAnkLKLTPEYLQLM---KYKAIAS-NSKIYF----GKDIPNMFMDS 332
Cdd:COG0330   217 ---EAQIL---RAEGEAE--AFRIVAEA--YSAAPFVLFYRsleALEEVLSpNSKVIVlppdGNGFLKYLLKS 279
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 220-303 6.00e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 6.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 220 AAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTALKIAEANKLK 299
Cdd:PRK09510  123 AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202


                  ....
gi 1405457301 300 LTPE 303
Cdd:PRK09510  203 AEAE 206
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 211-297 5.11e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 38.29  E-value: 5.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 211 ESEKTKLLIAAQKQKVVE---KEAETERK-KALIEAEKVAQVAEITYGQKVMEK-ETEKKISEIEDAAFLAREKAKADAE 285
Cdd:TIGR02794 129 AAEAKAKAEAEAERKAKEeaaKQAEEEAKaKAAAEAKKKAEEAKKKAEAEAKAKaEAEAKAKAEEAKAKAEAAKAKAAAE 208

                          90
                  ....*....|..
gi 1405457301 286 cytALKIAEANK 297
Cdd:TIGR02794 209 ---AAAKAEAEA 217
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 40-332 0e+00

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 598.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  40 CASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFL 119
Cdd:cd03406     1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 120 VPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNI 199
Cdd:cd03406    81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 200 PEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREK 279
Cdd:cd03406   161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1405457301 280 AKADAECYTALKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDS 332
Cdd:cd03406   241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
PHB smart00244
prohibitin homologues; prohibitin homologues
 45-211 7.06e-30

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 112.37  E-value: 7.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301   45 SAVHKIEEGHIGVYYRGGALLTsTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLVPNAV 124
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDA--VVYYRVLDPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  125 YDIVKNYTADYdkALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAVRVTKPNIPEAIR 204
Cdd:smart00244  78 RAVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAEAW--GIKVEDVEIKDIRLPEEIK 153


                   ....*..
gi 1405457301  205 RNYELME 211
Cdd:smart00244 154 EAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 49-231 2.47e-26

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 103.17  E-value: 2.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  49 KIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLV-PNAVYDI 127
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDV--TVIYRVnPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 128 VKNY-TADYDKALIFNKIHHELNQFCSVHTLQEVYIElFDQIDENLKLALQQDLtsMAPGLVIQAVRVTKPNIPEAIRRN 206
Cdd:pfam01145  79 VQNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEEL--AKYGVEIIDVQITDIDPPPEIAEA 155

                         170       180
                  ....*....|....*....|....*
gi 1405457301 207 yelMESEKTKLLIAAQKQKVVEKEA 231
Cdd:pfam01145 156 ---IEAKQTAEQEAEAEIARAEAEA 177
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 89-201 3.78e-26

core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons, and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259797 [Multi-domain]  Cd Length: 110  Bit Score: 100.90  E-value: 3.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  89 TLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVyIELFDQI 168
Cdd:cd02106     1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQI-ISGRDEI 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1405457301 169 DENLKLALQQDLTSMapGLVIQAVRVTKPNIPE 201
Cdd:cd02106    80 AKAVKEDLEEDLENF--GVVISDVDITSIEPPD 110
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 28-332 6.23e-19

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 85.66  E-value: 6.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  28 LGAVVAVASSFFcasLFSAVHKIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVM 107
Cdd:COG0330     5 LLLILLVLVLVL---LFSSVYIVPQGERGVVLRFGKY-VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 108 IYFDriEVVNFLVPNAvYDIVKNyTADYDKALIfNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGL 187
Cdd:COG0330    81 VDVD--AVVQYRITDP-AKFLYN-VENAEEALR-QLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDPY--GI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 188 VIQAVRVTKPNIPEAIRRNYElmesektKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEItygqkvmEKETEKkis 267
Cdd:COG0330   154 EVVDVEIKDIDPPEEVQDAME-------DRMKAEREREAAILEAEGYREAAIIRAEGEAQRAII-------EAEAYR--- 216

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405457301 268 eieDAAFLareKAKADAEcyTALKIAEAnkLKLTPEYLQLM---KYKAIAS-NSKIYF----GKDIPNMFMDS 332
Cdd:COG0330   217 ---EAQIL---RAEGEAE--AFRIVAEA--YSAAPFVLFYRsleALEEVLSpNSKVIVlppdGNGFLKYLLKS 279
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 47-247 2.96e-16

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 76.01  E-value: 2.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  47 VHKIEEGHIGV-YYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKnVPCGTSGGVMIyfdRIEV-VNF-LVPNA 123
Cdd:cd03401     1 FYTVDAGEVGVvFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREIT-LTVLSKDGQTV---NIDLsVLYrPDPEK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 124 VYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYI---ELFDQIDENLKLALQQDltsmapGLVIQAVRVTKPNIP 200
Cdd:cd03401    77 LPELYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTkreEVSAEIREALTERLAPF------GIIVDDVLITNIDFP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1405457301 201 EAIRRNYElmesEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQ 247
Cdd:cd03401   151 DEYEKAIE----AKQVAEQEAERAKFELEKAEQEAERKVIEAEGEAE 193
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 28-250 2.85e-06

High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 48.28  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  28 LGAVVAVAssffcASLFSAVHKIEEGHIGVYYRGGALlTSTSGPGFHLMLPF-ITSYKSVQTTlQTDEVKNVPCGTSGGV 106
Cdd:cd03404     1 LILLLLLL-----VWLLSGFYTVDPGERGVVLRFGKY-VRTVGPGLHWKLPFpIEVVEKVNVT-QVRSVEIGFRVPEESL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 107 MIYFDR-IEVVNFLVpnaVYDIV--KNY---TADYDKALIfNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDL 180
Cdd:cd03404    74 MLTGDEnIVDVDFVV---QYRISdpVAYlfnVRDPEETLR-QAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEIL 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1405457301 181 TSMAPGLVIQAVRVTKPNIPEAIRRNYELMES---EKTKLLIAAQK--QKVVEKeAETERKKALIEAE--KVAQVAE 250
Cdd:cd03404   150 DRYDLGIEIVQVQLQDADPPEEVQDAFDDVNAarqDKERLINEAQAyaNEVIPR-ARGEAARIIQEAEayKAEVVAR 225
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 220-303 6.00e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 6.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 220 AAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTALKIAEANKLK 299
Cdd:PRK09510  123 AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202


                  ....
gi 1405457301 300 LTPE 303
Cdd:PRK09510  203 AEAE 206
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
175-295 3.53e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.09  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 175 ALQQDLTSMapGLVIQAVRVT-------------KPNIPEAIR-RNYELMESEK-TKLLIAAQKQ--------------- 224
Cdd:COG2268   159 VAGTDLAKN--GLELESVAITdledennyldalgRRKIAEIIRdARIAEAEAEReTEIAIAQANReaeeaeleqereiet 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 225 -KVVEKEAETERKKAL---------IEAEKVAQVAEITYGQKV------MEKETEKKISEIEDAAFLAREKA----KADA 284
Cdd:COG2268   237 aRIAEAEAELAKKKAEerreaetarAEAEAAYEIAEANAEREVqrqleiAEREREIELQEKEAEREEAELEAdvrkPAEA 316

                         170
                  ....*....|.
gi 1405457301 285 ECYTALKIAEA 295
Cdd:COG2268   317 EKQAAEAEAEA 327
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
201-297 4.35e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 38.87  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 201 EAIRRNYELMESEKTKLLIAAQK--QKVVEKEAETERKKALIEAEKVAQVAE----ITYGQKVMEKETEKKISEIEDAAF 274
Cdd:COG3064    30 EAEQKAKEEAEEERLAELEAKRQaeEEAREAKAEAEQRAAELAAEAAKKLAEaekaAAEAEKKAAAEKAKAAKEAEAAAA 109

                          90       100
                  ....*....|....*....|...
gi 1405457301 275 LAREKAKADAEcytalKIAEANK 297
Cdd:COG3064   110 AEKAAAAAEKE-----KAEEAKR 127
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 211-297 5.11e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 38.29  E-value: 5.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 211 ESEKTKLLIAAQKQKVVE---KEAETERK-KALIEAEKVAQVAEITYGQKVMEK-ETEKKISEIEDAAFLAREKAKADAE 285
Cdd:TIGR02794 129 AAEAKAKAEAEAERKAKEeaaKQAEEEAKaKAAAEAKKKAEEAKKKAEAEAKAKaEAEAKAKAEEAKAKAEAAKAKAAAE 208

                          90
                  ....*....|..
gi 1405457301 286 cytALKIAEANK 297
Cdd:TIGR02794 209 ---AAAKAEAEA 217
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 50-247 7.53e-03

High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259803 [Multi-domain]  Cd Length: 249  Bit Score: 37.47  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301  50 IEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGvmiyfDRIEVVNFlvpnAVYDIV- 128
Cdd:cd03405     5 VDETEQAVVLQFGKPVRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDK-----KRLIVDSY----ARWRITd 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457301 129 --KNYTA--DYDKA--LIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAVRVTKPNIPEA 202
Cdd:cd03405    76 plRFYQSvgGEEGAesRLDDIVDSALRNEIGKRTLAEVVSGGRDELMEEILEQANEEAKEY--GIEVVDVRIKRIDLPEE 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1405457301 203 IRRN-YELMESEKTKL--LIAAQKQKVVEK---EAETERKKALIEAEKVAQ 247
Cdd:cd03405   154 VSESvYERMRAERERIaaEYRAEGEEEAEKiraEADRERTVILAEAYREAE 204
 
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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