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Conserved domains on  [gi|1370511817|ref|XP_024302826|]
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erlin-2 isoform X1 [Homo sapiens]

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 ...
16-308 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: 593.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  16 CASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFL 95
Cdd:cd03406     1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  96 VPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNI 175
Cdd:cd03406    81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 176 PEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREK 255
Cdd:cd03406   161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370511817 256 AKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDS 308
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 ...
16-308 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: 593.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  16 CASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFL 95
Cdd:cd03406     1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  96 VPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNI 175
Cdd:cd03406    81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 176 PEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREK 255
Cdd:cd03406   161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370511817 256 AKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDS 308
Cdd:cd03406   241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
PHB smart00244
prohibitin homologues; prohibitin homologues
21-187 1.10e-29

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 111.21  E-value: 1.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817   21 SAVHKIEEGHIGVYYRGGALLTsTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLVPNAV 100
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDA--VVYYRVLDPL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  101 YDIVKNYTADYdkALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAVRVTKPNIPEAIR 180
Cdd:smart00244  78 RAVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAEAW--GIKVEDVEIKDIRLPEEIK 153

                   ....*..
gi 1370511817  181 RNYELME 187
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 ...
25-211 8.37e-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: 307341 [Multi-domain]  Cd Length: 177  Bit Score: 103.95  E-value: 8.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  25 KIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLVPNAVYDIV 104
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLGPGLHFIIPFIQSVVIVDVRVQTLDVSVQTVLTKDGVPVNVDA--TVIYRVPDDPPKLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 105 KNY--TADYDKALIFNKIHHELNQFCSVHTLQEVYIElFDQIDENLKLALQQDLTSMapGLVIQAVRVTKPNIPEAIRRN 182
Cdd:pfam01145  79 QTVgfGSDDLQELIRQVVQSALREVIARYTLEELLSN-REELAEEIKAALNEELSKY--GVEIIDVQITDIDPPPEYREA 155
                         170       180
                  ....*....|....*....|....*....
gi 1370511817 183 YElmesektKLLIAAQKQKVVEKEAETER 211
Cdd:pfam01145 156 IE-------AKQTAEQEAEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
14-256 3.97e-07

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


Pssm-ID: 223407 [Multi-domain]  Cd Length: 291  Bit Score: 50.52  E-value: 3.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  14 FFCASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEV-----KNVPCGTSGGVMIYFDr 88
Cdd:COG0330    12 ILIVLLFSSIFVVKEGERGVVLRFGRYTRTLGEPGLHFKIPFPEAIEEVVVRVDLRERtldvgPPQEVITKDNVIVSVD- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  89 iEVVNFLVPNAVYDIvknYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAV 168
Cdd:COG0330    91 -AVVQYRVTDPQKAV---YNVENAEAALRQLVQSALRSVIGRMTLDELLTERRAEINAKIREILDEAADPW--GIKVVDV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 169 RVTKPNIPEAIRRnyelmeseKTKLLIAAQKQKVVEK-EAETERKKALIEAEKVAQVAEI---TYGQKVMEKETEKKISE 244
Cdd:COG0330   165 EIKDIDPPEEVQA--------AMEKQMAAERDKRAEIlEAEGEAQAAILRAEGEAEAAIIlaeAEAEAEVIARAEADAAK 236
                         250
                  ....*....|..
gi 1370511817 245 IEDAAFLAREKA 256
Cdd:COG0330   237 IIAAALREAPAA 248
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
196-279 8.28e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 196 AAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTAMKIAEANKLK 275
Cdd:PRK09510  123 AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202

                  ....
gi 1370511817 276 LTPE 279
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 ...
16-308 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: 593.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  16 CASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFL 95
Cdd:cd03406     1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  96 VPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNI 175
Cdd:cd03406    81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 176 PEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREK 255
Cdd:cd03406   161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370511817 256 AKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDS 308
Cdd:cd03406   241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
PHB smart00244
prohibitin homologues; prohibitin homologues
21-187 1.10e-29

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 111.21  E-value: 1.10e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817   21 SAVHKIEEGHIGVYYRGGALLTsTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLVPNAV 100
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDA--VVYYRVLDPL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  101 YDIVKNYTADYdkALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAVRVTKPNIPEAIR 180
Cdd:smart00244  78 RAVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAEAW--GIKVEDVEIKDIRLPEEIK 153

                   ....*..
gi 1370511817  181 RNYELME 187
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 ...
25-211 8.37e-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: 307341 [Multi-domain]  Cd Length: 177  Bit Score: 103.95  E-value: 8.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  25 KIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLVPNAVYDIV 104
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLGPGLHFIIPFIQSVVIVDVRVQTLDVSVQTVLTKDGVPVNVDA--TVIYRVPDDPPKLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 105 KNY--TADYDKALIFNKIHHELNQFCSVHTLQEVYIElFDQIDENLKLALQQDLTSMapGLVIQAVRVTKPNIPEAIRRN 182
Cdd:pfam01145  79 QTVgfGSDDLQELIRQVVQSALREVIARYTLEELLSN-REELAEEIKAALNEELSKY--GVEIIDVQITDIDPPPEYREA 155
                         170       180
                  ....*....|....*....|....*....
gi 1370511817 183 YElmesektKLLIAAQKQKVVEKEAETER 211
Cdd:pfam01145 156 IE-------AKQTAEQEAEAEIARAEAEA 177
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
65-177 4.18e-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: 100.13  E-value: 4.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  65 TLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVyIELFDQI 144
Cdd:cd02106     1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQI-ISGRDEI 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1370511817 145 DENLKLALQQDLTSMapGLVIQAVRVTKPNIPE 177
Cdd:cd02106    80 AKAVKEDLEEDLENF--GVVISDVDITSIEPPD 110
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
23-223 8.61e-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: 74.47  E-value: 8.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  23 VHKIEEGHIGV-YYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKnVPCGTSGGVMIyfdRIEV-VNF-LVPNA 99
Cdd:cd03401     1 FYTVDAGEVGVvFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREIT-LTVLSKDGQTV---NIDLsVLYrPDPEK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 100 VYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYI---ELFDQIDENLKLALQQDltsmapGLVIQAVRVTKPNIP 176
Cdd:cd03401    77 LPELYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTkreEVSAEIREALTERLAPF------GIIVDDVLITNIDFP 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370511817 177 EAIRRNYElmesEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQ 223
Cdd:cd03401   151 DEYEKAIE----AKQVAEQEAERAKFELEKAEQEAERKVIEAEGEAE 193
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
14-256 3.97e-07

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


Pssm-ID: 223407 [Multi-domain]  Cd Length: 291  Bit Score: 50.52  E-value: 3.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  14 FFCASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEV-----KNVPCGTSGGVMIYFDr 88
Cdd:COG0330    12 ILIVLLFSSIFVVKEGERGVVLRFGRYTRTLGEPGLHFKIPFPEAIEEVVVRVDLRERtldvgPPQEVITKDNVIVSVD- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  89 iEVVNFLVPNAVYDIvknYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAV 168
Cdd:COG0330    91 -AVVQYRVTDPQKAV---YNVENAEAALRQLVQSALRSVIGRMTLDELLTERRAEINAKIREILDEAADPW--GIKVVDV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 169 RVTKPNIPEAIRRnyelmeseKTKLLIAAQKQKVVEK-EAETERKKALIEAEKVAQVAEI---TYGQKVMEKETEKKISE 244
Cdd:COG0330   165 EIKDIDPPEEVQA--------AMEKQMAAERDKRAEIlEAEGEAQAAILRAEGEAEAAIIlaeAEAEAEVIARAEADAAK 236
                         250
                  ....*....|..
gi 1370511817 245 IEDAAFLAREKA 256
Cdd:COG0330   237 IIAAALREAPAA 248
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
4-226 5.11e-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  Cd Length: 266  Bit Score: 47.12  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817   4 LGAVVAVAssffcASLFSAVHKIEEGHIGVYYRGGALlTSTSGPGFHLMLPF-ITSYKSVQTTlQTDEVKNVPCGTSGGV 82
Cdd:cd03404     1 LILLLLLL-----VWLLSGFYTVDPGERGVVLRFGKY-VRTVGPGLHWKLPFpIEVVEKVNVT-QVRSVEIGFRVPEESL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  83 MIYFDR-IEVVNFLVpnaVYDIV--KNY---TADYDKALIfNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDL 156
Cdd:cd03404    74 MLTGDEnIVDVDFVV---QYRISdpVAYlfnVRDPEETLR-QAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEIL 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370511817 157 TSMAPGLVIQAVRVTKPNIPEAIRRNYELMES---EKTKLLIAAQK--QKVVEKeAETERKKALIEAE--KVAQVAE 226
Cdd:cd03404   150 DRYDLGIEIVQVQLQDADPPEEVQDAFDDVNAarqDKERLINEAQAyaNEVIPR-ARGEAARIIQEAEayKAEVVAR 225
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
177-275 5.35e-04

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 334246 [Multi-domain]  Cd Length: 243  Bit Score: 40.66  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 177 EAIRRNYELMESEKTKLLIaAQKQKVVEKEA---ETERKKALIEAEKVAQVAEITygqkvmEKETEKKISEIEDAAFLAR 253
Cdd:pfam00769  20 EARRAQEELRESEETAELL-EEKRRVAEEEAellEQKAAEAEEEKERLEESAEKT------EEEKEQLERELREAEEEAA 92
                          90       100
                  ....*....|....*....|..
gi 1370511817 254 EKAKAdaecyTAMKIAEANKLK 275
Cdd:pfam00769  93 RLEEE-----SERKEEEAERLQ 109
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
26-227 5.75e-04

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: 40.55  E-value: 5.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817  26 IEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGvmiyfDRIEVVNFlvpnAVYDIV- 104
Cdd:cd03405     5 VDETEQAVVLQFGKPVRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDK-----KRLIVDSY----ARWRITd 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 105 --KNYTA--DYDKA--LIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMapGLVIQAVRVTKPNIPEA 178
Cdd:cd03405    76 plRFYQSvgGEEGAesRLDDIVDSALRNEIGKRTLAEVVSGGRDELMEEILEQANEEAKEY--GIEVVDVRIKRIDLPEE 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370511817 179 IRRN-YELMESEKTKllIAAQ-----KQKVVEKEAETERKKALIEAEKVAQVAEI 227
Cdd:cd03405   154 VSESvYERMRAERER--IAAEyraegEEEAEKIRAEADRERTVILAEAYREAEEI 206
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
196-279 8.28e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.56  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 196 AAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTAMKIAEANKLK 275
Cdd:PRK09510  123 AAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202

                  ....
gi 1370511817 276 LTPE 279
Cdd:PRK09510  203 AEAE 206
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
129-272 3.98e-03

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


Pssm-ID: 225177 [Multi-domain]  Cd Length: 548  Bit Score: 38.66  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 129 SVHTLQEVYIELFDQIDENLklalQQDLTSMapGLVIQAVRVTKPNIPEAIRRNYEL-MESE----KTKLLIAAQKQKV- 202
Cdd:COG2268   156 TVEELNEDRLGFAQVVQEVV----GDDLSKM--GLVLDSLAINDINDTSKENQDPNNyLDALgrrrIAQVLQDAEIAENe 229
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370511817 203 VEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTAMKIAEAN 272
Cdd:COG2268   230 AEKETEIAIAEANRDAKLVELEVEQQPAGKTAEQTREVKIILAETEAEVAAWKAETRREAEQAEILAEQA 299
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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