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Conserved domains on  [gi|193210507|ref|NP_001123162|]
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Band 7 domain-containing protein [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 ...
 79-279 2.11e-103

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: 299.85  E-value: 2.11e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  79 GGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRN 158
Cdd:cd03403    2 GGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 159 ALGMKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQLTRAMAAEAEAAREARAKVVAAEGEQKASRA 238
Cdd:cd03403   82 VLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 193210507 239 LKEAADVIQANPVALQLRHLQALNSIAAEHNSTIVFPVPVE 279
Cdd:cd03403  162 LKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
 
Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 79-279 2.11e-103

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: 299.85  E-value: 2.11e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  79 GGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRN 158
Cdd:cd03403    2 GGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 159 ALGMKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQLTRAMAAEAEAAREARAKVVAAEGEQKASRA 238
Cdd:cd03403   82 VLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 193210507 239 LKEAADVIQANPVALQLRHLQALNSIAAEHNSTIVFPVPVE 279
Cdd:cd03403  162 LKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
PHB smart00244
prohibitin homologues; prohibitin homologues
 58-207 1.52e-43

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 145.88  E-value: 1.52e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507    58 CLKVIKEYERVVIFRIGRLVfgGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIAS 137
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193210507   138 VNNVDDA-IYSTKLLAQTTLRNALGMKTLTEMLT-EREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQ 207
Cdd:smart00244  80 VYRVLDAdYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEE 151
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 45-287 1.16e-38

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 136.89  E-value: 1.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  45 ILIIVTFPFSMCVclKVIKEYERVVIFRIGRLVfgGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVD 124
Cdd:COG0330    9 LLVLVLVLLFSSV--YIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 125 AVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRNALGMKTLTEMLTE-REAIAQLCETILDEGTEHWGVKVERVEVKDIR 203
Cdd:COG0330   85 AVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDID 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 204 LPQQLT----------------------RAMAAEAEAAREARAKVVAAEGEQKASRALKEA--------ADVIQANPVAL 253
Cdd:COG0330  165 PPEEVQdamedrmkaerereaaileaegYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGeaeafrivAEAYSAAPFVL 244

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 193210507 254 QLRHLQALNSIAAEHNSTIVFPVP-VEMFGAFMKK 287
Cdd:COG0330  245 FYRSLEALEEVLSPNSKVIVLPPDgNGFLKYLLKS 279
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 60-208 5.44e-23

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: 92.77  E-value: 5.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507   60 KVIKEYERVVIFRIGRLVfgGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFR--TSDPIAS 137
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLS--RVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRvnPDDPPKL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193210507  138 VNNVDDAIYSTKLL---AQTTLRNALGMKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQL 208
Cdd:pfam01145  79 VQNVFGSDDLQELLrrvLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEI 152
PRK10930 PRK10930
FtsH protease activity modulator HflK;
62-182 2.17e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 45.59  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  62 IKEYERVVIFRIGRlvFGGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIA---SV 138
Cdd:PRK10930 100 IKEAERGVVTRFGK--FSHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTDPEKylfSV 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193210507 139 NNVDDAiystklLAQTT---LRNALGMKTLTEMLTEREAIAQ------LCETI 182
Cdd:PRK10930 178 TSPDDS------LRQATdsaLRGVIGKYTMDRILTEGRTVIRsdtqreLEETI 224
 
Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 79-279 2.11e-103

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: 299.85  E-value: 2.11e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  79 GGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRN 158
Cdd:cd03403    2 GGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 159 ALGMKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQLTRAMAAEAEAAREARAKVVAAEGEQKASRA 238
Cdd:cd03403   82 VLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 193210507 239 LKEAADVIQANPVALQLRHLQALNSIAAEHNSTIVFPVPVE 279
Cdd:cd03403  162 LKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 79-285 4.03e-100

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: 4.03e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  79 GGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRN 158
Cdd:cd13435    2 GGARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 159 ALGMKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQLTRAMAAEAEAAREARAKVVAAEGEQKASRA 238
Cdd:cd13435   82 VLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 193210507 239 LKEAADVIQANPVALQLRHLQALNSIAAEHNSTIVFPVPVEMFGAFM 285
Cdd:cd13435  162 LKEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLTPLL 208
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 58-277 1.19e-66

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: 207.43  E-value: 1.19e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  58 CLKVIKEYERVVIFRIGRLVFGGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDP--- 134
Cdd:cd08827    3 CVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAsvc 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 135 IASVNNVDDAIystKLLAQTTLRNALGMKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQLTRAMAA 214
Cdd:cd08827   83 LSSFASISDAM---QALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193210507 215 EAEAAREARAKVVAAEGEQKASRALKEAADVIQANPVALQLRHLQALNSIAAEHNSTIVFPVP 277
Cdd:cd08827  160 EAEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLP 222
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 91-268 3.46e-65

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: 201.97  E-value: 3.46e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  91 PCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRNALGMKTLTEMLT 170
Cdd:cd08826    1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 171 EREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQLTRAMAAEAEAAREARAKVVAAEGEQKASRALKEAADVIQANP 250
Cdd:cd08826   81 EREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSP 160

                        170
                 ....*....|....*...
gi 193210507 251 VALQLRHLQALNSIAAEH 268
Cdd:cd08826  161 GALQLRYLQTLSEIASEK 178
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 82-235 3.66e-57

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: 180.61  E-value: 3.66e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  82 RGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRNALG 161
Cdd:cd08828    1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193210507 162 MKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQLTRAMAAEAEAAREARAKVVAAEGEQKA 235
Cdd:cd08828   81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 99-206 3.03e-54

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: 171.61  E-value: 3.03e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  99 IDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRNALGMKTLTEMLTEREAIAQL 178
Cdd:cd13434    1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                         90       100
                 ....*....|....*....|....*...
gi 193210507 179 CETILDEGTEHWGVKVERVEVKDIRLPQ 206
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDIILPQ 108
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 84-274 6.68e-46

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: 153.92  E-value: 6.68e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  84 PGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRNALGMK 163
Cdd:cd13437   29 PGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRIDNVKQALIERTQTTLRSVIGER 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 164 TLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQLTRAMAAEAEAAREARAKVVAAEGEQKASRALKEAA 243
Cdd:cd13437  109 TLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIGESKIISAKADVESAKLMREAA 188

                        170       180       190
                 ....*....|....*....|....*....|.
gi 193210507 244 DvIQANPVALQLRHLQALNSIAAEHNSTIVF 274
Cdd:cd13437  189 D-ILDSKAAMQIRYLETLQAIAKSANSKVIF 218
PHB smart00244
prohibitin homologues; prohibitin homologues
 58-207 1.52e-43

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 145.88  E-value: 1.52e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507    58 CLKVIKEYERVVIFRIGRLVfgGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIAS 137
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193210507   138 VNNVDDA-IYSTKLLAQTTLRNALGMKTLTEMLT-EREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQ 207
Cdd:smart00244  80 VYRVLDAdYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEE 151
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 45-287 1.16e-38

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 136.89  E-value: 1.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  45 ILIIVTFPFSMCVclKVIKEYERVVIFRIGRLVfgGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVD 124
Cdd:COG0330    9 LLVLVLVLLFSSV--YIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 125 AVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRNALGMKTLTEMLTE-REAIAQLCETILDEGTEHWGVKVERVEVKDIR 203
Cdd:COG0330   85 AVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDID 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 204 LPQQLT----------------------RAMAAEAEAAREARAKVVAAEGEQKASRALKEA--------ADVIQANPVAL 253
Cdd:COG0330  165 PPEEVQdamedrmkaerereaaileaegYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGeaeafrivAEAYSAAPFVL 244

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 193210507 254 QLRHLQALNSIAAEHNSTIVFPVP-VEMFGAFMKK 287
Cdd:COG0330  245 FYRSLEALEEVLSPNSKVIVLPPDgNGFLKYLLKS 279
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 98-206 3.01e-36

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: 125.28  E-value: 3.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  98 KIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRNALGMKTLTEMLTEREAIAQ 177
Cdd:cd08829    3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                         90       100
                 ....*....|....*....|....*....
gi 193210507 178 LCETILDEGTEHWGVKVERVEVKDIRLPQ 206
Cdd:cd08829   83 KLLEALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 99-275 2.57e-35

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: 125.05  E-value: 2.57e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  99 IDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRNALGMKTLTEMLTEREAIAQL 178
Cdd:cd13775    1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 179 CETILDEGTEHWGVKVERVEVKDIRLPQQLTRAMAAEAEAAREARAKVVAAEGEQKASRALKEAADVIQANPVALQLRHL 258
Cdd:cd13775   81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAM 160

                        170
                 ....*....|....*..
gi 193210507 259 QALNSIAAEHNSTIVFP 275
Cdd:cd13775  161 NMLYEGLKEKGSMVVVP 177
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 81-206 2.97e-34

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: 120.97  E-value: 2.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  81 ARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIASVNNVDDAIYSTKLLAQTTLRNAL 160
Cdd:cd13436    6 PRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTSLTNSL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 193210507 161 GMKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQ 206
Cdd:cd13436   86 SKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKVLK 131
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 62-274 1.05e-33

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: 122.26  E-value: 1.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  62 IKEYERVVIFRIGRLVfgGARGPGMI-FIIPCIDTYR-KIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIA--- 136
Cdd:cd13438    1 VPPGERGLLYRDGKLV--RTLEPGRYaFWKFGRKVQVeLVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKave 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 137 SVNNVDDAIYstkLLAQTTLRNALGMKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQLTRAMAAEA 216
Cdd:cd13438   79 TVDDPEEQLY---LALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193210507 217 EAAREARAKVVAAEGEQKASRALKEAADVIQANPVALQLRHLQALNSIAAEHNSTIVF 274
Cdd:cd13438  156 EAEKRAQANLIRAREETAATRSLLNAAKLMEENPALLRLRELEALEKIAEKVGHISVS 213
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 60-208 5.44e-23

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: 92.77  E-value: 5.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507   60 KVIKEYERVVIFRIGRLVfgGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFR--TSDPIAS 137
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLS--RVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRvnPDDPPKL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193210507  138 VNNVDDAIYSTKLL---AQTTLRNALGMKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQL 208
Cdd:pfam01145  79 VQNVFGSDDLQELLrrvLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEI 152
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 58-209 2.15e-20

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: 87.54  E-value: 2.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  58 CLKVIKEYERVVIFRIGRLVfGGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDP--- 134
Cdd:cd03405    1 SVFIVDETEQAVVLQFGKPV-RVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPlrf 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193210507 135 IASVNNVDDAiysTKLLAQ---TTLRNALGMKTLTEML-TEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQLT 209
Cdd:cd03405   80 YQSVGGEEGA---ESRLDDivdSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVS 155
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 59-209 3.28e-14

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: 69.46  E-value: 3.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  59 LKVIKEYERVVIFRIGRLVFGGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPqEILSKDSVTVSVDAVVYFRTSDPIAS- 137
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRPDPEKLPe 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193210507 138 -VNNVDDAIYSTKL--LAQTTLRNALGMKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQLT 209
Cdd:cd03401   80 lYQNLGPDYEERVLppIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYE 154
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 61-207 1.08e-10

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: 60.60  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  61 VIKEYERVVIFRIGRLVfgGARGPGMIFIIPC-IDTYRKIDL----RVVSYAVPPQE--ILSKDSVTVSVDAVVYFRTSD 133
Cdd:cd03404   17 TVDPGERGVVLRFGKYV--RTVGPGLHWKLPFpIEVVEKVNVtqvrSVEIGFRVPEEslMLTGDENIVDVDFVVQYRISD 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193210507 134 PIASVNNVDDAIYSTKLLAQTTLRNALGMKTLTEMLTE-REAIA----QLCETILDEgtEHWGVKVERVEVKDIRLPQQ 207
Cdd:cd03404   95 PVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAadvrELLQEILDR--YDLGIEIVQVQLQDADPPEE 171
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 108-206 2.12e-09

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: 53.91  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 108 VPPQEILSKDSVTVSVDAVVYFRTSDP-----IASVNNVDDAIYSTKLLAQTTLRNALGMKTLTEMLTEREAIAQLCETI 182
Cdd:cd02106    7 VRVEPVGTADGVPVAVDLVVQFRITDYnalpaFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVKED 86

                         90       100
                 ....*....|....*....|....
gi 193210507 183 LDEGTEHWGVKVERVEVKDIRLPQ 206
Cdd:cd02106   87 LEEDLENFGVVISDVDITSIEPPD 110
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 88-177 2.16e-06

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: 46.34  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  88 FIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFR-TSDPIASVNNV-------DDAIYStkLLAQT---TL 156
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKvGSDPEEIAAAAerflgksTEEIRE--LVKETlegHL 78

                         90       100
                 ....*....|....*....|.
gi 193210507 157 RNALGMKTLTEMLTEREAIAQ 177
Cdd:cd03399   79 RAIVGTMTVEEIYQDREKFAE 99
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 59-202 1.02e-05

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: 45.62  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  59 LKVIKEYERVVIFRIGRLVfGGARGPGMIFIIPCIDTyRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIASV 138
Cdd:cd03402   10 FFVVQPNEAAVLTLFGRYR-GTVRRPGLRWVNPFYRK-KRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWRVVDTAKAV 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193210507 139 NNVDDAIYSTKLLAQTTLRNALGM--------KTLTeMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDI 202
Cdd:cd03402   88 FDVDDYEEFVSIQSEAALRRVASRypydsfedGEPS-LRGNSDEVSEELRRELQERLAVAGVEVIEARITHL 158
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 61-242 1.66e-05

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: 45.27  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  61 VIKEYERVVIFRIGRlvFGGARGPGMIFIIPCIDTYR-KIDLRVVSYAVPpQEILSKDSVTVSVDAVVYFRTSDpiasvN 139
Cdd:cd03407    1 CVSQSTVAIVERFGK--FSRIAEPGLHFIIPPIESVAgRVSLRVQQLDVR-VETKTKDNVFVTLVVSVQYRVVP-----E 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507 140 NVDDAIYS-TKLLAQ------TTLRNALGMKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIRLPQQLTram 212
Cdd:cd03407   73 KVYDAFYKlTNPEQQiqsyvfDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVK--- 149

                        170       180       190
                 ....*....|....*....|....*....|
gi 193210507 213 aaeaeaarEARAKVVAAEGEQKASRALKEA 242
Cdd:cd03407  150 --------AAMNEINAAQRLREAAEEKAEA 171
PRK10930 PRK10930
FtsH protease activity modulator HflK;
62-182 2.17e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 45.59  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  62 IKEYERVVIFRIGRlvFGGARGPGMIFIIPCIDTYRKIDLRVVSYAVPPQEILSKDSVTVSVDAVVYFRTSDPIA---SV 138
Cdd:PRK10930 100 IKEAERGVVTRFGK--FSHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTDPEKylfSV 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193210507 139 NNVDDAiystklLAQTT---LRNALGMKTLTEMLTEREAIAQ------LCETI 182
Cdd:PRK10930 178 TSPDDS------LRQATdsaLRGVIGKYTMDRILTEGRTVIRsdtqreLEETI 224
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
75-203 1.62e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.47  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193210507  75 RLVFGGArgpgmIFIIPCIDTYRKIDLRVVSYAVPPQE-ILSKDSVTVSVDAVVYFRTSDPIASVNNV--------DDAI 145
Cdd:COG2268   47 KVVTGGG-----AFVLPVLHRAERMSLSTMTIEVERTEgLITKDGIRVDVDAVFYVKVNSDPEDIANAaerflgrdPEEI 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193210507 146 ysTKLLAQT---TLRNALGMKTLTEMLTEREAIAQLCETILDEGTEHWGVKVERVEVKDIR 203
Cdd:COG2268  122 --EELAEEKlegALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLE 180
 
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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