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Conserved domains on  [gi|529010114|ref|XP_005226181|]
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erlin-2 isoform X1 [Bos taurus]

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 ...
 96-388 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: 607.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114  96 CASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFL 175
Cdd:cd03406    1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 176 VPHAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNI 255
Cdd:cd03406   81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 256 PEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITFGQKVMEKETEKRISEIEDAAFLAREK 335
Cdd:cd03406  161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 529010114 336 AKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDS 388
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 ...
 96-388 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: 607.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114  96 CASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFL 175
Cdd:cd03406    1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 176 VPHAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNI 255
Cdd:cd03406   81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 256 PEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITFGQKVMEKETEKRISEIEDAAFLAREK 335
Cdd:cd03406  161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 529010114 336 AKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDS 388
Cdd:cd03406  241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
PHB smart00244
prohibitin homologues; prohibitin homologues
 101-267 5.07e-30

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 113.52  E-value: 5.07e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114   101 SAVHKIEEGHIGVYYRGGALLTsTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLVPHAV 180
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDA--VVYYRVLDPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114   181 YDIVKNYTADYdkALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAVRVTKPNIPEAIR 260
Cdd:smart00244  78 RAVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAEAW--GIKVEDVEIKDIRLPEEIK 153


                   ....*..
gi 529010114   261 RNYELME 267
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 ...
 105-287 4.88e-27

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: 106.25  E-value: 4.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114  105 KIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLV-PHAVYDI 183
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDV--TVIYRVnPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114  184 VKNY-TADYDKALIFNKIHHELNQFCSVHTLQEVYIElFDQIDENLKLALQQDLtsMAPGLVIQAVRVTKPNIPEAIRRN 262
Cdd:pfam01145  79 VQNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEEL--AKYGVEIIDVQITDIDPPPEIAEA 155

                         170       180
                  ....*....|....*....|....*
gi 529010114  263 yelMESEKTKLLIAAQKQKVVEKEA 287
Cdd:pfam01145 156 ---IEAKQTAEQEAEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 84-388 5.68e-20

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 89.13  E-value: 5.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114  84 LGAVVAVAASFFcasLFSAVHKIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVM 163
Cdd:COG0330    5 LLLILLVLVLVL---LFSSVYIVPQGERGVVLRFGKY-VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 164 IYFD---RIEVVNflvphaVYDIVKNyTADYDKALIfNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMa 240
Cdd:COG0330   81 VDVDavvQYRITD------PAKFLYN-VENAEEALR-QLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDPY- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 241 pGLVIQAVRVTKPNIPEAIRRNYElmesektKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEItfgqkvmEKETEK 320
Cdd:COG0330  152 -GIEVVDVEIKDIDPPEEVQDAME-------DRMKAEREREAAILEAEGYREAAIIRAEGEAQRAII-------EAEAYR 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529010114 321 riseieDAAFLareKAKADAEcyTAMKIAEAnkLKLTPEYLQLM---KYKAIAS-NSKIYF----GKDIPNMFMDS 388
Cdd:COG0330  217 ------EAQIL---RAEGEAE--AFRIVAEA--YSAAPFVLFYRsleALEEVLSpNSKVIVlppdGNGFLKYLLKS 279
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 276-359 1.35e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 276 AAQKQKVVEKEAETERKKALIEAEKVAQVAEITFGQKVMEKETEKRISEIEDAAFLAREKAKADAECYTAMKIAEANKLK 355
Cdd:PRK09510 123 AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202


                 ....
gi 529010114 356 LTPE 359
Cdd:PRK09510 203 AEAE 206
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 96-388 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: 607.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114  96 CASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFL 175
Cdd:cd03406    1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 176 VPHAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNI 255
Cdd:cd03406   81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 256 PEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITFGQKVMEKETEKRISEIEDAAFLAREK 335
Cdd:cd03406  161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 529010114 336 AKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDS 388
Cdd:cd03406  241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
PHB smart00244
prohibitin homologues; prohibitin homologues
 101-267 5.07e-30

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 113.52  E-value: 5.07e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114   101 SAVHKIEEGHIGVYYRGGALLTsTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLVPHAV 180
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDA--VVYYRVLDPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114   181 YDIVKNYTADYdkALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAVRVTKPNIPEAIR 260
Cdd:smart00244  78 RAVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAEAW--GIKVEDVEIKDIRLPEEIK 153


                   ....*..
gi 529010114   261 RNYELME 267
Cdd:smart00244 154 EAMEAQQ 160
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 145-257 4.42e-27

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: 103.98  E-value: 4.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 145 TLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPHAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVyIELFDQI 224
Cdd:cd02106    1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQI-ISGRDEI 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 529010114 225 DENLKLALQQDLTSMapGLVIQAVRVTKPNIPE 257
Cdd:cd02106   80 AKAVKEDLEEDLENF--GVVISDVDITSIEPPD 110
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 105-287 4.88e-27

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: 106.25  E-value: 4.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114  105 KIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLV-PHAVYDI 183
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDV--TVIYRVnPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114  184 VKNY-TADYDKALIFNKIHHELNQFCSVHTLQEVYIElFDQIDENLKLALQQDLtsMAPGLVIQAVRVTKPNIPEAIRRN 262
Cdd:pfam01145  79 VQNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEEL--AKYGVEIIDVQITDIDPPPEIAEA 155

                         170       180
                  ....*....|....*....|....*
gi 529010114  263 yelMESEKTKLLIAAQKQKVVEKEA 287
Cdd:pfam01145 156 ---IEAKQTAEQEAEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 84-388 5.68e-20

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 89.13  E-value: 5.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114  84 LGAVVAVAASFFcasLFSAVHKIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVM 163
Cdd:COG0330    5 LLLILLVLVLVL---LFSSVYIVPQGERGVVLRFGKY-VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 164 IYFD---RIEVVNflvphaVYDIVKNyTADYDKALIfNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMa 240
Cdd:COG0330   81 VDVDavvQYRITD------PAKFLYN-VENAEEALR-QLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDPY- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 241 pGLVIQAVRVTKPNIPEAIRRNYElmesektKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEItfgqkvmEKETEK 320
Cdd:COG0330  152 -GIEVVDVEIKDIDPPEEVQDAME-------DRMKAEREREAAILEAEGYREAAIIRAEGEAQRAII-------EAEAYR 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529010114 321 riseieDAAFLareKAKADAEcyTAMKIAEAnkLKLTPEYLQLM---KYKAIAS-NSKIYF----GKDIPNMFMDS 388
Cdd:COG0330  217 ------EAQIL---RAEGEAE--AFRIVAEA--YSAAPFVLFYRsleALEEVLSpNSKVIVlppdGNGFLKYLLKS 279
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 103-303 5.26e-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: 5.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 103 VHKIEEGHIGV-YYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKnVPCGTSGGVMIyfdRIEV-VNF-LVPHA 179
Cdd:cd03401    1 FYTVDAGEVGVvFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREIT-LTVLSKDGQTV---NIDLsVLYrPDPEK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 180 VYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYI---ELFDQIDENLKLALQQDltsmapGLVIQAVRVTKPNIP 256
Cdd:cd03401   77 LPELYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTkreEVSAEIREALTERLAPF------GIIVDDVLITNIDFP 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 529010114 257 EAIRRNYElmesEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQ 303
Cdd:cd03401  151 DEYEKAIE----AKQVAEQEAERAKFELEKAEQEAERKVIEAEGEAE 193
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 89-306 7.92e-07

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: 50.20  E-value: 7.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114  89 AVAASFFCASLFSAVHKIEEGHIGVYYRGGALlTSTSGPGFHLMLPF-ITSYKSVQTTlQTDEVKNVPCGTSGGVMIYFD 167
Cdd:cd03404    1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGKY-VRTVGPGLHWKLPFpIEVVEKVNVT-QVRSVEIGFRVPEESLMLTGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 168 R-IEVVNFLVPHAVYDIVKnY---TADYDKALIfNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGL 243
Cdd:cd03404   79 EnIVDVDFVVQYRISDPVA-YlfnVRDPEETLR-QAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEILDRYDLGI 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 244 VIQAVRVTKPNIPEAIRRNYELMES---EKTKLLIAAQK--QKVVEKeAETERKKALIEAE--KVAQVAE 306
Cdd:cd03404  157 EIVQVQLQDADPPEEVQDAFDDVNAarqDKERLINEAQAyaNEVIPR-ARGEAARIIQEAEayKAEVVAR 225
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 276-359 1.35e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 276 AAQKQKVVEKEAETERKKALIEAEKVAQVAEITFGQKVMEKETEKRISEIEDAAFLAREKAKADAECYTAMKIAEANKLK 355
Cdd:PRK09510 123 AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202


                 ....
gi 529010114 356 LTPE 359
Cdd:PRK09510 203 AEAE 206
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
231-351 1.83e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.24  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 231 ALQQDLTSMapGLVIQAVRVT-------------KPNIPEAIR-RNYELMESEK-TKLLIAAQKQ--------------- 280
Cdd:COG2268  159 VAGTDLAKN--GLELESVAITdledennyldalgRRKIAEIIRdARIAEAEAEReTEIAIAQANReaeeaeleqereiet 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 281 -KVVEKEAETERKKAL---------IEAEKVAQVAEITFGQKV------MEKETEKRISEIEDAAFLAREKA----KADA 340
Cdd:COG2268  237 aRIAEAEAELAKKKAEerreaetarAEAEAAYEIAEANAEREVqrqleiAEREREIELQEKEAEREEAELEAdvrkPAEA 316

                        170
                 ....*....|.
gi 529010114 341 ECYTAMKIAEA 351
Cdd:COG2268  317 EKQAAEAEAEA 327
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 106-303 3.03e-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: 39.01  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 106 IEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGvmiyfDRIEVVNFlvphAVYDIV- 184
Cdd:cd03405    5 VDETEQAVVLQFGKPVRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDK-----KRLIVDSY----ARWRITd 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529010114 185 --KNYTA--DYDKA--LIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAVRVTKPNIPEA 258
Cdd:cd03405   76 plRFYQSvgGEEGAesRLDDIVDSALRNEIGKRTLAEVVSGGRDELMEEILEQANEEAKEY--GIEVVDVRIKRIDLPEE 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 529010114 259 IRRN-YELMESEKTKL--LIAAQKQKVVEK---EAETERKKALIEAEKVAQ 303
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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