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Conserved domains on  [gi|446583346|ref|WP_000660692|]
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MULTISPECIES: SPFH domain-containing protein [Bacillus]

Protein Classification

SPFH domain-containing protein( domain architecture ID 10130451)

uncharacterized SPFH domain-containing protein similar to stomatin, prohibitin, or paraslipin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
42-273 6.36e-127

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: 259800  Cd Length: 231  Bit Score: 360.33  E-value: 6.36e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346  42 ILASVLATGIGIVQPNQAKVITFFGNYLGTIRQNGLFLTIPFAFRQTVSLRVENFNSKKLKVNDVEGNPIEIAAVIVYKV 121
Cdd:cd03402    1 VVGIILLGGFFVVQPNEAAVLTLFGRYRGTVRRPGLRWVNPFYRKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 122 VDSAKAMFGVEHYDRFVEIQSETAIRHVATKYPYDNFQDETcITLRGNTEEISEELKRELEARLEIAGVEVLETRLTHLA 201
Cdd:cd03402   81 VDTAKAVFDVDDYEEFVSIQSEAALRRVASRYPYDSFEDGE-PSLRGNSDEVSEELRRELQERLAVAGVEVIEARITHLA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446583346 202 YATEIAHAMLQRQQAKAVLAARKEIVEGAVKMAKDSIHMLDEEGVLELDDERKANMVNNLLVAIVSDKGAQP 273
Cdd:cd03402  160 YAPEIAQAMLQRQQASAIIAARQTIVEGAVGMVEMALARLEERGVVELDEERKAALVSNLLVVLCSERGAQP 231
 
Name Accession Description Interval E-value
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
42-273 6.36e-127

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: 259800  Cd Length: 231  Bit Score: 360.33  E-value: 6.36e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346  42 ILASVLATGIGIVQPNQAKVITFFGNYLGTIRQNGLFLTIPFAFRQTVSLRVENFNSKKLKVNDVEGNPIEIAAVIVYKV 121
Cdd:cd03402    1 VVGIILLGGFFVVQPNEAAVLTLFGRYRGTVRRPGLRWVNPFYRKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 122 VDSAKAMFGVEHYDRFVEIQSETAIRHVATKYPYDNFQDETcITLRGNTEEISEELKRELEARLEIAGVEVLETRLTHLA 201
Cdd:cd03402   81 VDTAKAVFDVDDYEEFVSIQSEAALRRVASRYPYDSFEDGE-PSLRGNSDEVSEELRRELQERLAVAGVEVIEARITHLA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446583346 202 YATEIAHAMLQRQQAKAVLAARKEIVEGAVKMAKDSIHMLDEEGVLELDDERKANMVNNLLVAIVSDKGAQP 273
Cdd:cd03402  160 YAPEIAQAMLQRQQASAIIAARQTIVEGAVGMVEMALARLEERGVVELDEERKAALVSNLLVVLCSERGAQP 231
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
33-229 5.41e-25

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 100.68  E-value: 5.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346  33 MFVIAILALILASVLATGIGIVQPNQAKVITFFGNYLGTIRQnGLFLTIPFAFR-QTVSLRVENFNSKKLKVNDVEGNPI 111
Cdd:COG0330    3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEP-GLHFKIPFIDRvRKVDVREQVLDVPPQEVLTKDNNIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 112 EIAAVIVYKVVDSAKAMFGVEHYDRFVEIQSETAIRHVATKYPYDNfqdetciTLRGNTEEISEELKRELEARLEIAGVE 191
Cdd:COG0330   82 DVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDE-------VLSTGRDEINAEIREELQEALDPYGIE 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446583346 192 VLETRLTHLAYATEIAHAMLQRQQAKAVLAARKEIVEG 229
Cdd:COG0330  155 VVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEG 192
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
53-229 1.05e-20

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: 86.61  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346   53 IVQPNQAKVITFFGNYLGTIrQNGLFLTIPF-AFRQTVSLRVENFNSKKLKVNDVEGNPIEIAAVIVYKV--VDSAKA-- 127
Cdd:pfam01145   2 IVPPGEVGVVTRFGKLSRVL-EPGLHFIIPFiQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLvq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346  128 -MFGVEHYDRFVEIQSETAIRHVATKYpydnfqdeTCITLRGNTEEISEELKRELEARLEIAGVEVLETRLTHLAYATEI 206
Cdd:pfam01145  81 nVFGSDDLQELLRRVLESALREIIARY--------TLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEI 152
                         170       180
                  ....*....|....*....|...
gi 446583346  207 AHAMLQRQQAKAVLAARKEIVEG 229
Cdd:pfam01145 153 AEAIEAKQTAEQEAEAEIARAEA 175
PHB smart00244
prohibitin homologues; prohibitin homologues
53-214 1.16e-11

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 61.52  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346    53 IVQPNQAKVITFFGNYLGTIRQnGLFLTIPFAFR-QTVSLRVENFNSKKLKVNDVEGNPIEIAAVIVYKVVDSAKAMFGV 131
Cdd:smart00244   5 VVGEGERGVVERLGRVLRVLGP-GLHFLIPFIDDvKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346   132 EHYDRFVEIQ-SETAIRHVATKYPYDNFqdetcitLRGNTEEISEELKRELEARLEIAGVEVLETRLTHLAYATEIAHAM 210
Cdd:smart00244  84 LDADYAVIEQlAQTTLRSVIGKRTLDEL-------LTDQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156

                   ....
gi 446583346   211 LQRQ 214
Cdd:smart00244 157 EAQQ 160
 
Name Accession Description Interval E-value
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
42-273 6.36e-127

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: 259800  Cd Length: 231  Bit Score: 360.33  E-value: 6.36e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346  42 ILASVLATGIGIVQPNQAKVITFFGNYLGTIRQNGLFLTIPFAFRQTVSLRVENFNSKKLKVNDVEGNPIEIAAVIVYKV 121
Cdd:cd03402    1 VVGIILLGGFFVVQPNEAAVLTLFGRYRGTVRRPGLRWVNPFYRKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 122 VDSAKAMFGVEHYDRFVEIQSETAIRHVATKYPYDNFQDETcITLRGNTEEISEELKRELEARLEIAGVEVLETRLTHLA 201
Cdd:cd03402   81 VDTAKAVFDVDDYEEFVSIQSEAALRRVASRYPYDSFEDGE-PSLRGNSDEVSEELRRELQERLAVAGVEVIEARITHLA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446583346 202 YATEIAHAMLQRQQAKAVLAARKEIVEGAVKMAKDSIHMLDEEGVLELDDERKANMVNNLLVAIVSDKGAQP 273
Cdd:cd03402  160 YAPEIAQAMLQRQQASAIIAARQTIVEGAVGMVEMALARLEERGVVELDEERKAALVSNLLVVLCSERGAQP 231
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
33-229 5.41e-25

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 100.68  E-value: 5.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346  33 MFVIAILALILASVLATGIGIVQPNQAKVITFFGNYLGTIRQnGLFLTIPFAFR-QTVSLRVENFNSKKLKVNDVEGNPI 111
Cdd:COG0330    3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEP-GLHFKIPFIDRvRKVDVREQVLDVPPQEVLTKDNNIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 112 EIAAVIVYKVVDSAKAMFGVEHYDRFVEIQSETAIRHVATKYPYDNfqdetciTLRGNTEEISEELKRELEARLEIAGVE 191
Cdd:COG0330   82 DVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDE-------VLSTGRDEINAEIREELQEALDPYGIE 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446583346 192 VLETRLTHLAYATEIAHAMLQRQQAKAVLAARKEIVEG 229
Cdd:COG0330  155 VVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEG 192
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
53-229 1.05e-20

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: 86.61  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346   53 IVQPNQAKVITFFGNYLGTIrQNGLFLTIPF-AFRQTVSLRVENFNSKKLKVNDVEGNPIEIAAVIVYKV--VDSAKA-- 127
Cdd:pfam01145   2 IVPPGEVGVVTRFGKLSRVL-EPGLHFIIPFiQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLvq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346  128 -MFGVEHYDRFVEIQSETAIRHVATKYpydnfqdeTCITLRGNTEEISEELKRELEARLEIAGVEVLETRLTHLAYATEI 206
Cdd:pfam01145  81 nVFGSDDLQELLRRVLESALREIIARY--------TLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEI 152
                         170       180
                  ....*....|....*....|...
gi 446583346  207 AHAMLQRQQAKAVLAARKEIVEG 229
Cdd:pfam01145 153 AEAIEAKQTAEQEAEAEIARAEA 175
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
37-197 9.82e-13

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: 66.38  E-value: 9.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346  37 AILALILASVLATGIGIVQPNQAKVITFFGNYLGTIrQNGLFLTIPFAFRQTVSLRVENFNSKKLKVNDVE--------G 108
Cdd:cd03404    1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGKYVRTV-GPGLHWKLPFPIEVVEKVNVTQVRSVEIGFRVPEeslmltgdE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 109 NPIEIAAVIVYKVVDSAKAMFGVEHYDRFVEIQSETAIRHVATKYPYDNFqdetcitLRGNTEEISEELKRELEARLEI- 187
Cdd:cd03404   80 NIVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDV-------LTEGRAEIAADVRELLQEILDRy 152
                        170
                 ....*....|.
gi 446583346 188 -AGVEVLETRL 197
Cdd:cd03404  153 dLGIEIVQVQL 163
PHB smart00244
prohibitin homologues; prohibitin homologues
53-214 1.16e-11

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 61.52  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346    53 IVQPNQAKVITFFGNYLGTIRQnGLFLTIPFAFR-QTVSLRVENFNSKKLKVNDVEGNPIEIAAVIVYKVVDSAKAMFGV 131
Cdd:smart00244   5 VVGEGERGVVERLGRVLRVLGP-GLHFLIPFIDDvKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346   132 EHYDRFVEIQ-SETAIRHVATKYPYDNFqdetcitLRGNTEEISEELKRELEARLEIAGVEVLETRLTHLAYATEIAHAM 210
Cdd:smart00244  84 LDADYAVIEQlAQTTLRSVIGKRTLDEL-------LTDQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156

                   ....
gi 446583346   211 LQRQ 214
Cdd:smart00244 157 EAQQ 160
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
107-202 1.22e-07

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: 48.90  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 107 EGNPIEIAAVIVYKVVDSAKA-----MFGVEHYDRFVEIQSETAIRHVATKYPYDNFQDetcitlrgNTEEISEELKREL 181
Cdd:cd02106   16 DGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIIS--------GRDEIAKAVKEDL 87
                         90       100
                 ....*....|....*....|.
gi 446583346 182 EARLEIAGVEVLETRLTHLAY 202
Cdd:cd02106   88 EEDLENFGVVISDVDITSIEP 108
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
53-227 8.91e-07

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: 48.28  E-value: 8.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346  53 IVQPNQAKVITFFGNYLGT-IRQNGLFLTIPFAFR-QTVSLRVENFNSKkLKVNDVEGNPIEIAAVIVYKVvDSAKAM-- 128
Cdd:cd03401    3 TVDAGEVGVVFRRGKGVKDeVLGEGLHFKIPWIQVvIIYDVRTQPREIT-LTVLSKDGQTVNIDLSVLYRP-DPEKLPel 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 129 ---FGVEHYDRFVEIQSETAIRHVATKYPYDNFqdetcITLRgntEEISEELKRELEARLEIAGVEVLETRLTHLAYATE 205
Cdd:cd03401   81 yqnLGPDYEERVLPPIVREVLKAVVAQYTAEEL-----YTKR---EEVSAEIREALTERLAPFGIIVDDVLITNIDFPDE 152
                        170       180
                 ....*....|....*....|..
gi 446583346 206 IAHAMLQRQQAKaVLAARKEIV 227
Cdd:cd03401  153 YEKAIEAKQVAE-QEAERAKFE 173
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
53-216 1.80e-06

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: 47.87  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346  53 IVQPNQAKVITFFGNYLGTIRQNGLFLTIPFAfrQTVSL---RVENFNSKKLKVNDVEGNPIEIAAVIVYKVVDSAK--- 126
Cdd:cd03405    4 IVDETEQAVVLQFGKPVRVITEPGLHFKLPFI--QNVRKfdkRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRfyq 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 127 AMFGVEHYDRFVEIQSETAIRHVATKYPYDNFqdetcitLRGNTEEISEELKRELEARLEIAGVEVLETRLTHLAYATEI 206
Cdd:cd03405   82 SVGGEEGAESRLDDIVDSALRNEIGKRTLAEV-------VSGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEV 154
                        170
                 ....*....|
gi 446583346 207 AHAMLQRQQA 216
Cdd:cd03405  155 SESVYERMRA 164
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
110-192 1.85e-06

Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, podocin, and other members of the stomatin-like protein family (SLPs or slipins). The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. 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. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome. Bacterial and archaebacterial SLPs and many of the eukaryotic family members remain uncharacterized.


Pssm-ID: 259812 [Multi-domain]  Cd Length: 108  Bit Score: 45.65  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 110 PIEIAAVIVYKVVDSAKAMFGVEHYDRFVEIQSETAIRHVATKYPYDNfqdetcitLRGNTEEISEELKRELEARLEIAG 189
Cdd:cd13434   22 TVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDE--------LLSEREEISQQLQEILDEATDPWG 93

                 ...
gi 446583346 190 VEV 192
Cdd:cd13434   94 IKV 96
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
111-242 1.99e-06

Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in some eukaryotes and viruses. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This diverse subgroup of the SLPs remains largely uncharacterized.


Pssm-ID: 259815 [Multi-domain]  Cd Length: 222  Bit Score: 47.61  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 111 IEIAAVIVYKVVDSAKAMFGVEHYDRFVEIQSETAIRHVATKYpydNFQDetCITLRgntEEISEELKRELEARLEIAGV 190
Cdd:cd13437   66 VTIDSVVYYRIIDPYKAIYRIDNVKQALIERTQTTLRSVIGER---TLQD--LLEKR---EEIADEIEEIVEEVAKEWGV 137
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446583346 191 EVLETRLTHLAYATEI----AHAMLQRQQAKA-VLAARKEiVEGAvKMAKDSIHMLD 242
Cdd:cd13437  138 YVESILIKDIVLSKDLqqslSSAAKAKRIGESkIISAKAD-VESA-KLMREAADILD 192
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
110-259 6.22e-06

Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of the SPFH family (stomatin, prohibitin, flotillin, and HflK/C); This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized.


Pssm-ID: 259817 [Multi-domain]  Cd Length: 177  Bit Score: 45.69  E-value: 6.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 110 PIEIAAVIVYKVVDSAKAMFGVEHYDRFVEIQSETAIRHVATKYPYDnfqdetciTLRGNTEEISEELKRELEARLEIAG 189
Cdd:cd13775   22 PVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELA--------ELLSRREQIDEELQDIIDEKTTPWG 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446583346 190 VEVLETRLTHLAYATEIAHAML------QRQQAKAVLA-ARKEIVEGAVKMAKDSIHmldEEGVLELddeRKANMVN 259
Cdd:cd13775   94 ITVQSVEIRDIIIPKELQDAMSreaqaeREKNARVILAeAEKEIAEMFVEAAEVYEN---NPIALQL---RAMNMLY 164
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
110-193 1.55e-05

Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in all three kingdoms of life. The conserved domain common to these families has also been referred to as the Band 7 domain. Individual proteins of the SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This subgroup of the SLPs remains largely uncharacterized. It includes human SLP-2 which is upregulated and involved in the progression and development in several types of cancer, including esophageal squamous cell carcinoma, endometrial adenocarcinoma, breast cancer, and glioma.


Pssm-ID: 259811 [Multi-domain]  Cd Length: 111  Bit Score: 43.23  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 110 PIEIAAVIVYKVVDSAKAMFGVEHYDRFVEIQSETAIRHVATKYPYDNfqdetciTLRgNTEEISEELKRELEARLEIAG 189
Cdd:cd08829   25 TVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDE-------TLS-SREEINAKLLEALDEATDPWG 96

                 ....
gi 446583346 190 VEVL 193
Cdd:cd08829   97 VKVT 100
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
87-249 1.66e-05

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized. This subgroup contains PH1511 from the hyperthermophilic archaeon Pyrococcus horikoshi.


Pssm-ID: 259808 [Multi-domain]  Cd Length: 178  Bit Score: 44.43  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346  87 QTVSLRVENFNSKKLKVNDVEGNPIEIAAVIVYKVVDSAKAMFGVEHYDRFVEIQSETAIRHVATKYPYDnfqdetciTL 166
Cdd:cd08826    7 VRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELD--------EL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 167 RGNTEEISEELKRELEARLEIAGVEVLETRLTHLAYATEIAHAMlqRQQAKA-------VLAARKEiVEGAVKMAKDSIH 239
Cdd:cd08826   79 LSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAM--ARQAEAererrakIIKAEGE-LQAAEKLAEAAEI 155
                        170
                 ....*....|
gi 446583346 240 MLDEEGVLEL 249
Cdd:cd08826  156 LAKSPGALQL 165
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
70-235 3.55e-05

Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in arthropods. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this divergent slipin subgroup remain largely uncharacterized. It contains Drosophila Mec2, the gene for which was identified in a screen for genes required for nephrocyte function; it may function together with Sns in maintaining nephrocyte diaphragm.


Pssm-ID: 259813 [Multi-domain]  Cd Length: 208  Bit Score: 43.91  E-value: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346  70 GTIRQNGLFLTIPFA--FRQtVSLRVENFNSKKLKVNDVEGNPIEIAAVIVYKVVDSAKAMFGVEHYDRFVEIQSETAIR 147
Cdd:cd13435    2 GGARGPGVFFVLPCIdnYCK-VDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446583346 148 HV-ATKypydNFQDetcitLRGNTEEISEELKRELEARLEIAGVEVLETRLTHLAYATEIAHAMlqRQQAKAVLAARKEI 226
Cdd:cd13435   81 NVlGTR----NLSE-----LLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAM--AAEAEAAREARAKV 149
                        170
                 ....*....|.
gi 446583346 227 V--EGAVKMAK 235
Cdd:cd13435  150 IaaEGEMKSSR 160
 
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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