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Conserved domains on  [gi|17569493|ref|NP_509281|]
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Stomatin-1 [Caenorhabditis elegans]

Protein Classification

SPFH domain-containing protein( domain architecture ID 139628)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_like super family cl19107
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 86-283 5.17e-102

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.


The actual alignment was detected with superfamily member cd03403:

Pssm-ID: 473137 [Multi-domain]  Cd Length: 202  Bit Score: 297.93  E-value: 5.17e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  86 KGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILG 165
Cdd:cd03403   5 KGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 166 THTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAEAEATRDAGAKIIAAEGELRASAALAE 245
Cdd:cd03403  85 TKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRALKE 164

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17569493 246 AATIISKSEGAMQLRYLHTLNAISSEKTSTIIFPFPME 283
Cdd:cd03403 165 AADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
 
Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 86-283 5.17e-102

Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; Stomatin (or band 7) is widely expressed and, highly expressed in red blood cells. It localizes predominantly to the plasma membrane and to intracellular vesicles of the endocytic pathway, where it is present in higher order homo-oligomeric complexes (of between 9 and 12 monomers). Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and, is implicated in trafficking of Glut1 glucose transporters. This subgroup found in animals, also contains proteins similar to Caenorhabditis elegans MEC-2. MEC-2 interacts with MEC-4, which is part of the degenerin channel complex required for response to gentle body touch.


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 297.93  E-value: 5.17e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  86 KGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILG 165
Cdd:cd03403   5 KGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 166 THTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAEAEATRDAGAKIIAAEGELRASAALAE 245
Cdd:cd03403  85 TKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRALKE 164

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17569493 246 AATIISKSEGAMQLRYLHTLNAISSEKTSTIIFPFPME 283
Cdd:cd03403 165 AADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
PHB smart00244
prohibitin homologues; prohibitin homologues
 62-220 3.97e-51

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 166.68  E-value: 3.97e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493     62 MCIKIVQEYQRAVVFRLGRLVpDVKGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITS 141
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL-RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493    142 VVGVGNATD-STKLLAQTTLRTILGTHTLSEILSD-REKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAE 219
Cdd:smart00244  80 VYRVLDADYaVIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159


                   .
gi 17569493    220 A 220
Cdd:smart00244 160 Q 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 50-236 3.26e-50

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 168.48  E-value: 3.26e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  50 VLIFLTFPVSVFMCIKIVQEYQRAVVFRLGRLVpDVKGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDA 129
Cdd:COG0330   7 LILLVLVLVLLFSSVYIVPQGERGVVLRFGKYV-RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 130 VVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILS-DREKISADMKISLDEATEPWGIKVERVELRDVRL 208
Cdd:COG0330  86 VVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDP 165

                       170       180
                ....*....|....*....|....*...
gi 17569493 209 PSQMQRAMAAEAEATRDAGAKIIAAEGE 236
Cdd:COG0330 166 PEEVQDAMEDRMKAEREREAAILEAEGY 193
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 65-236 3.99e-38

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: 133.60  E-value: 3.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493    65 KIVQEYQRAVVFRLGRLVpDVKGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKV--FDP---I 139
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLS-RVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPpklV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493   140 TSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAE 219
Cdd:pfam01145  80 QNVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*..
gi 17569493   220 AEATRDAGAKIIAAEGE 236
Cdd:pfam01145 160 QTAEQEAEAEIARAEAE 176
PRK10930 PRK10930
FtsH protease activity modulator HflK;
45-228 4.71e-08

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 54.06  E-value: 4.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493   45 IAMSYVLIFLTFPVSVFMCIKivqEYQRAVVFRLGRLVPDVKgPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVT 124
Cdd:PRK10930  81 VGIAAAAVVIIWAASGFYTIK---EAERGVVTRFGKFSHLVE-PGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENV 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  125 VSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILSD-REKISADMKISLDEATEPW--GIKVERV 201
Cdd:PRK10930 157 VRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYdmGITLLDV 236

                        170       180       190
                 ....*....|....*....|....*....|....
gi 17569493  202 ELRDVRLPSQMQR----AMAA---EAEATRDAGA 228
Cdd:PRK10930 237 NFQAARPPEEVKAafddAIAArenEQQYIREAEA 270
 
Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 86-283 5.17e-102

Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; Stomatin (or band 7) is widely expressed and, highly expressed in red blood cells. It localizes predominantly to the plasma membrane and to intracellular vesicles of the endocytic pathway, where it is present in higher order homo-oligomeric complexes (of between 9 and 12 monomers). Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and, is implicated in trafficking of Glut1 glucose transporters. This subgroup found in animals, also contains proteins similar to Caenorhabditis elegans MEC-2. MEC-2 interacts with MEC-4, which is part of the degenerin channel complex required for response to gentle body touch.


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 297.93  E-value: 5.17e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  86 KGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILG 165
Cdd:cd03403   5 KGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 166 THTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAEAEATRDAGAKIIAAEGELRASAALAE 245
Cdd:cd03403  85 TKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRALKE 164

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17569493 246 AATIISKSEGAMQLRYLHTLNAISSEKTSTIIFPFPME 283
Cdd:cd03403 165 AADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 86-286 1.88e-99

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: 291.98  E-value: 1.88e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  86 KGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILG 165
Cdd:cd13435   5 RGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 166 THTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAEAEATRDAGAKIIAAEGELRASAALAE 245
Cdd:cd13435  85 TRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRALKE 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 17569493 246 AATIISKSEGAMQLRYLHTLNAISSEKTSTIIFPFPMEILG 286
Cdd:cd13435 165 ASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLT 205
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 95-272 6.13e-77

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: 233.17  E-value: 6.13e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  95 PCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILS 174
Cdd:cd08826   1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 175 DREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAEAEATRDAGAKIIAAEGELRASAALAEAATIISKSE 254
Cdd:cd08826  81 EREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSP 160

                       170
                ....*....|....*...
gi 17569493 255 GAMQLRYLHTLNAISSEK 272
Cdd:cd08826 161 GALQLRYLQTLSEIASEK 178
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 61-281 8.32e-70

Podocin, 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 vertebrates. 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. Podocin is expressed in the kidney and mutations in the gene have been linked to familial idiopathic nephrotic syndrome. Podocin interacts with the TRP ion channel TRPV-6 and may function as a scaffolding protein in the organization of lipid-protein domains.


Pssm-ID: 259809 [Multi-domain]  Cd Length: 223  Bit Score: 217.06  E-value: 8.32e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  61 FMCIKIVQEYQRAVVFRLGRLVPD-VKGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPI 139
Cdd:cd08827   1 WFCVKVVREYERAVIFRLGHLLQGrARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 140 TSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAE 219
Cdd:cd08827  81 VCLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17569493 220 AEATRDAGAKIIAAEGELRASAALAEAATIISKSEGAMQLRYLHTLNAISSEKTSTIIFPFP 281
Cdd:cd08827 161 AEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLP 222
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 86-237 4.40e-68

Slipin-3 (SLP-3), 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 vertebrates. 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 slipin subgroup remain uncharacterized, except for Caenorhabditis elegans UNC-1. Mutations in the unc-1 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259810 [Multi-domain]  Cd Length: 154  Bit Score: 209.89  E-value: 4.40e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  86 KGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILG 165
Cdd:cd08828   1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17569493 166 THTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAEAEATRDAGAKIIAAEGEL 237
Cdd:cd08828  81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEM 152
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 103-209 1.09e-51

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: 166.21  E-value: 1.09e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 103 IDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILSDREKISAD 182
Cdd:cd13434   1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                        90       100
                ....*....|....*....|....*..
gi 17569493 183 MKISLDEATEPWGIKVERVELRDVRLP 209
Cdd:cd13434  81 LQEILDEATDPWGIKVERVEIKDIILP 107
PHB smart00244
prohibitin homologues; prohibitin homologues
 62-220 3.97e-51

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 166.68  E-value: 3.97e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493     62 MCIKIVQEYQRAVVFRLGRLVpDVKGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITS 141
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL-RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493    142 VVGVGNATD-STKLLAQTTLRTILGTHTLSEILSD-REKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAE 219
Cdd:smart00244  80 VYRVLDADYaVIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159


                   .
gi 17569493    220 A 220
Cdd:smart00244 160 Q 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 50-236 3.26e-50

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 168.48  E-value: 3.26e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  50 VLIFLTFPVSVFMCIKIVQEYQRAVVFRLGRLVpDVKGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDA 129
Cdd:COG0330   7 LILLVLVLVLLFSSVYIVPQGERGVVLRFGKYV-RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 130 VVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILS-DREKISADMKISLDEATEPWGIKVERVELRDVRL 208
Cdd:COG0330  86 VVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDP 165

                       170       180
                ....*....|....*....|....*...
gi 17569493 209 PSQMQRAMAAEAEATRDAGAKIIAAEGE 236
Cdd:COG0330 166 PEEVQDAMEDRMKAEREREAAILEAEGY 193
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 67-278 1.86e-49

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: 164.71  E-value: 1.86e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  67 VQEYQRAVVFRLGRLVPDVKgPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVGVG 146
Cdd:cd13437   9 VKQGSVGLVERFGKFYKTVD-PGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 147 NATDSTKLLAQTTLRTILGTHTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAEAEATRDA 226
Cdd:cd13437  88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIG 167

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 17569493 227 GAKIIAAEGELRASAALAEAATIISkSEGAMQLRYLHTLNAISSEKTSTIIF 278
Cdd:cd13437 168 ESKIISAKADVESAKLMREAADILD-SKAAMQIRYLETLQAIAKSANSKVIF 218
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 103-279 1.57e-46

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: 155.48  E-value: 1.57e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 103 IDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILSDREKISAD 182
Cdd:cd13775   1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 183 MKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAEAEATRDAGAKIIAAEGELRASAALAEAATIISKSEGAMQLRYL 262
Cdd:cd13775  81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAM 160

                       170
                ....*....|....*..
gi 17569493 263 HTLNAISSEKTSTIIFP 279
Cdd:cd13775 161 NMLYEGLKEKGSMVVVP 177
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 79-208 1.99e-41

Stomatin-like protein 1 (SLP-1), 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 animals. 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. The family contains human SLP-1, which has been found to be expressed in the brain, and Caenorhabditis elegans UNC-24, which is a lipid raft-associated protein required for normal locomotion. It may mediate the correct localization of UNC-1. Mutations in the unc-24 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259814 [Multi-domain]  Cd Length: 131  Bit Score: 140.61  E-value: 1.99e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  79 GRLVPdVKGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQT 158
Cdd:cd13436   1 GRLQK-PRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQT 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17569493 159 TLRTILGTHTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRL 208
Cdd:cd13436  80 SLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 103-210 2.03e-39

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: 134.91  E-value: 2.03e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 103 IDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILSDREKISAD 182
Cdd:cd08829   4 VDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAK 83

                        90       100
                ....*....|....*....|....*...
gi 17569493 183 MKISLDEATEPWGIKVERVELRDVRLPS 210
Cdd:cd08829  84 LLEALDEATDPWGVKVTRVEIKDITPPE 111
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 65-236 3.99e-38

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: 133.60  E-value: 3.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493    65 KIVQEYQRAVVFRLGRLVpDVKGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKV--FDP---I 139
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLS-RVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPpklV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493   140 TSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAE 219
Cdd:pfam01145  80 QNVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*..
gi 17569493   220 AEATRDAGAKIIAAEGE 236
Cdd:pfam01145 160 QTAEQEAEAEIARAEAE 176
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 67-236 2.00e-32

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. 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 SLPs remain uncharacterized.


Pssm-ID: 259816 [Multi-domain]  Cd Length: 215  Bit Score: 119.95  E-value: 2.00e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  67 VQEYQRAVVFRLGRLVpDVKGPGI-FFIIPCID-TFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVG 144
Cdd:cd13438   1 VPPGERGLLYRDGKLV-RTLEPGRyAFWKFGRKvQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVET 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 145 VGNATDSTKLLAQTTLRTILGTHTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAEAEATR 224
Cdd:cd13438  80 VDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEK 159

                       170
                ....*....|..
gi 17569493 225 DAGAKIIAAEGE 236
Cdd:cd13438 160 RAQANLIRAREE 171
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 63-236 1.31e-29

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: 113.35  E-value: 1.31e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  63 CIKIVQEYQRAVVFRLGRLVPDVKGPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSV 142
Cdd:cd03405   1 SVFIVDETEQAVVLQFGKPVRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRFY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 143 VGVGNATDSTKLLAQ---TTLRTILGTHTLSEILSD-REKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRA--- 215
Cdd:cd03405  81 QSVGGEEGAESRLDDivdSALRNEIGKRTLAEVVSGgRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESvye 160

                       170       180
                ....*....|....*....|..
gi 17569493 216 -MAAEaeatRDAGAKIIAAEGE 236
Cdd:cd03405 161 rMRAE----RERIAAEYRAEGE 178
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 64-236 7.43e-22

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: 91.04  E-value: 7.43e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  64 IKIVQEYQRAVVFRLGRLVPD-VKGPGIFFIIPCIDTFLNIDLRVASYNVPSqEILSRDSVTVSVDAVVYFKVfDPiTSV 142
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDeVLGEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRP-DP-EKL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 143 V----GVGNATDSTKL--LAQTTLRTILGTHTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRA- 215
Cdd:cd03401  78 PelyqNLGPDYEERVLppIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAi 157

                       170       180       190
                ....*....|....*....|....*....|....
gi 17569493 216 ---MAAEAEATR----------DAGAKIIAAEGE 236
Cdd:cd03401 158 eakQVAEQEAERakfelekaeqEAERKVIEAEGE 191
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 50-236 1.08e-15

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: 75.63  E-value: 1.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  50 VLIFLTFPVSVFMCIKIVQEYQRAVVFRLGRLVpDVKGPGIFFIIPC-IDTFLNIDL-RVASYNVP-----SQEILSRDS 122
Cdd:cd03404   1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGKYV-RTVGPGLHWKLPFpIEVVEKVNVtQVRSVEIGfrvpeESLMLTGDE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 123 VTVSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILS-DREKISADMKISLDEATEPW--GIKVE 199
Cdd:cd03404  80 NIVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQEILDRYdlGIEIV 159

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 17569493 200 RVELRDVRLPSQMQRAMAAEAEATRDAGAKIIAAEGE 236
Cdd:cd03404 160 QVQLQDADPPEEVQDAFDDVNAARQDKERLINEAQAY 196
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 66-236 3.23e-12

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: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 65.68  E-value: 3.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  66 IVQEYQRAVVFRLGRLVpDVKGPGIFFIIPCID-TFLNIDLRVASYNVpSQEILSRDSVTVSVDAVV------------Y 132
Cdd:cd03407   1 CVSQSTVAIVERFGKFS-RIAEPGLHFIIPPIEsVAGRVSLRVQQLDV-RVETKTKDNVFVTLVVSVqyrvvpekvydaF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 133 FKVFDP---ITSVVgvgnatdstkllaQTTLRTILGTHTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLP 209
Cdd:cd03407  79 YKLTNPeqqIQSYV-------------FDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPD 145

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17569493 210 SQMQRAM-----------AAEAEATRDAGAKIIAAEGE 236
Cdd:cd03407 146 ASVKAAMneinaaqrlreAAEEKAEAEKILQVKAAEAE 183
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 65-203 1.54e-10

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: 60.26  E-value: 1.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  65 KIVQEYQRAVVFRLGRLVPDVKGPGIFFIIPCIDTfLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVFDPITSVVG 144
Cdd:cd03402  11 FVVQPNEAAVLTLFGRYRGTVRRPGLRWVNPFYRK-KRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWRVVDTAKAVFD 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17569493 145 VGNATDSTKLLAQTTLRTILGTH----------TLSeilSDREKISADMKISLDEATEPWGIKVERVEL 203
Cdd:cd03402  90 VDDYEEFVSIQSEAALRRVASRYpydsfedgepSLR---GNSDEVSEELRRELQERLAVAGVEVIEARI 155
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 111-209 3.46e-10

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: 56.60  E-value: 3.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 111 NVPSQEILSRDSVTVSVDAVVYFKVFDP-----ITSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILSDREKISADMKI 185
Cdd:cd02106   6 DVRVEPVGTADGVPVAVDLVVQFRITDYnalpaFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVKE 85

                        90       100
                ....*....|....*....|....
gi 17569493 186 SLDEATEPWGIKVERVELRDVRLP 209
Cdd:cd02106  86 DLEEDLENFGVVISDVDITSIEPP 109
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 92-225 9.24e-10

Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; The flotillin (reggie) like proteins are lipid raft-associated. Individual proteins of this SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. In addition, microdomains formed from flotillin proteins may be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and interact with a variety of proteins. They may play a role 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.


Pssm-ID: 259798 [Multi-domain]  Cd Length: 145  Bit Score: 56.36  E-value: 9.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  92 FIIPCIDTFLNIDLRVASYNVPSQEILSRDSVTVSVDAVVYFKVfdpITSVVGVGNA--------TDSTKLLAQTT---- 159
Cdd:cd03399   1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKV---GSDPEEIAAAaerflgksTEEIRELVKETlegh 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17569493 160 LRTILGTHTLSEILSDREKISADMKISLDEATEPWGIKVERVELRDVRLPSQMQRAMAAE--AEATRD 225
Cdd:cd03399  78 LRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKqaAEVKKD 145
PRK10930 PRK10930
FtsH protease activity modulator HflK;
45-228 4.71e-08

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 54.06  E-value: 4.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493   45 IAMSYVLIFLTFPVSVFMCIKivqEYQRAVVFRLGRLVPDVKgPGIFFIIPCIDTFLNIDLRVASYNVPSQEILSRDSVT 124
Cdd:PRK10930  81 VGIAAAAVVIIWAASGFYTIK---EAERGVVTRFGKFSHLVE-PGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENV 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  125 VSVDAVVYFKVFDPITSVVGVGNATDSTKLLAQTTLRTILGTHTLSEILSD-REKISADMKISLDEATEPW--GIKVERV 201
Cdd:PRK10930 157 VRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYdmGITLLDV 236

                        170       180       190
                 ....*....|....*....|....*....|....
gi 17569493  202 ELRDVRLPSQMQR----AMAA---EAEATRDAGA 228
Cdd:PRK10930 237 NFQAARPPEEVKAafddAIAArenEQQYIREAEA 270
PRK11029 PRK11029
protease modulator HflC;
47-191 2.03e-06

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 48.58  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493   47 MSYVLIFLTFPVSVFMC--IKIVQEYQRAVVFRLGRLV------PDVKGPGIFFIIPCIDTFLNIDLRVASYNVPSQEIL 118
Cdd:PRK11029   1 MRKSVIAIIIIVLVVLYmsVFVVKEGERGIVLRFGKVLrdddnkPLVYAPGLHFKIPFIETVKMLDARIQTMDNQADRFV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17569493  119 SRDSVTVSVDAVVYFKV--FDPITSVVGVGNATDSTKLLAQT---TLRTILGTHTLSEILSD-REKISADMKISLDEAT 191
Cdd:PRK11029  81 TKEKKDLIVDSYIKWRIsdFSRYYLATGGGDISQAEVLLKRKfsdRLRSEIGRLDVKDIVTDsRGRLTLDVRDALNSGS 159
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
45-234 1.36e-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: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493  45 IAMSYVLIFLTFPVSVFMCIKIVQEYQRAVVFRLGRLVPDVKGPGIFfIIPCIDTFLNIDLRVASYNV-PSQEILSRDSV 123
Cdd:COG2268   9 IIGVIVVVLLLLLIILARFYRKVPPNEALVITGRGGGYKVVTGGGAF-VLPVLHRAERMSLSTMTIEVeRTEGLITKDGI 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569493 124 TVSVDAVVYFKVfdpITSVVGVGNA--------TDSTKLLAQTT----LRTILGTHTLSEILSDREK--------ISADM 183
Cdd:COG2268  88 RVDVDAVFYVKV---NSDPEDIANAaerflgrdPEEIEELAEEKlegaLRAVAAQMTVEELNEDREKfaekvqevAGTDL 164

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17569493 184 K--------ISLDEATEPWG-------------IKVERVELRDVRLPSQMQRAMA------AEAEATRDAGAKIIAAE 234
Cdd:COG2268 165 AknglelesVAITDLEDENNyldalgrrkiaeiIRDARIAEAEAERETEIAIAQAnreaeeAELEQEREIETARIAEA 242
 
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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