NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446827246|ref|WP_000904502|]
View 

MULTISPECIES: SPFH domain-containing protein [Enterobacteriaceae]

Protein Classification

SPFH domain-containing protein( domain architecture ID 11417211)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein similar to Homo sapiens mitochondrial stomatin-like protein 2, and Escherichia coli protein QmcA

CATH:  3.30.479.30
Gene Ontology:  GO:0016020
PubMed:  16101677|17766116|10542406|21501885|24782879
TCDB:  8.A.21

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 2-289 4.15e-96

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 284.81  E-value: 4.15e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   2 LIFIPILIFVALVIVGAGVKIVPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANV 81
Cdd:COG0330    3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  82 TIDAVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGSMELDEMLS-QRDSINSRLLRIVDEATNPWGIKVTRIEIR 160
Cdd:COG0330   82 DVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 161 DVRPPAELISSMNAQMKAERTKRAYILEAEGIRQAEILKAEGEKQSQILKAEGERQSAFLQaearersAEAEARATKMVS 240
Cdd:COG0330  162 DIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILR-------AEGEAEAFRIVA 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 446827246 241 EAiasgdIQAVNYFVAQKYTEALQQIGsSSNSKVVMMPLEASSLMGSIA 289
Cdd:COG0330  235 EA-----YSAAPFVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLL 277
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 2-289 4.15e-96

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 284.81  E-value: 4.15e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   2 LIFIPILIFVALVIVGAGVKIVPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANV 81
Cdd:COG0330    3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  82 TIDAVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGSMELDEMLS-QRDSINSRLLRIVDEATNPWGIKVTRIEIR 160
Cdd:COG0330   82 DVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 161 DVRPPAELISSMNAQMKAERTKRAYILEAEGIRQAEILKAEGEKQSQILKAEGERQSAFLQaearersAEAEARATKMVS 240
Cdd:COG0330  162 DIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILR-------AEGEAEAFRIVA 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 446827246 241 EAiasgdIQAVNYFVAQKYTEALQQIGsSSNSKVVMMPLEASSLMGSIA 289
Cdd:COG0330  235 EA-----YSAAPFVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLL 277
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 58-166 2.21e-56

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: 177.67  E-value: 2.21e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  58 KINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGSMELDEMLSQRDSINS 137
Cdd:cd08829    3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                         90       100
                 ....*....|....*....|....*....
gi 446827246 138 RLLRIVDEATNPWGIKVTRIEIRDVRPPA 166
Cdd:cd08829   83 KLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 18-176 1.81e-42

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 143.57  E-value: 1.81e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246    18 AGVKIVPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRA 97
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246    98 AYEVSNLELAII-NLTMTNIRTVLGSMELDEMLS-QRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQ 175
Cdd:smart00244  80 VYRVLDADYAVIeQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159


                   .
gi 446827246   176 M 176
Cdd:smart00244 160 Q 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 21-191 9.80e-36

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: 126.67  E-value: 9.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   21 KIVPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVI--DAPRAA 98
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   99 YEV---SNLELAIINLTMTNIRTVLGSMELDEMLSQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQ 175
Cdd:pfam01145  80 QNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*.
gi 446827246  176 MKAERTKRAYILEAEG 191
Cdd:pfam01145 160 QTAEQEAEAEIARAEA 175
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 31-285 1.18e-16

HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 77.83  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   31 VERFGRYTKTLQPGLSLVVPFMDRIgRKINMmEQVLDIPSQ-EVISKDNANVTIDAVCFIQVIDAPRAAYEVSNLELAII 109
Cdd:TIGR01933  12 VLRFGKYHRTVDPGLNWKPPFIEEV-YPVNV-TAVRNLRKQgLMLTGDENIVNVEMNVQYRITDPYKYLFSVENPEDSLR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  110 NLTMTNIRTVLGSMELDEMLSQ-RDSINSRLLRIVDEATNPW--GIKVTRIEIRDVRPPAELISSMNAQMKAERTKRAYI 186
Cdd:TIGR01933  90 QATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDVIIAREDEERYI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  187 LEAEGIRQAEILKAEGEKQSQILKAEGERQSAFLQAEarersAEAEaRATKMVSEAIASGDIQAvnyfvAQKYTEALQQI 266
Cdd:TIGR01933 170 NEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAK-----GDVA-RFTKLLAEYKKAPDVTR-----ERLYLETMEKV 238

                         250
                  ....*....|....*....
gi 446827246  267 gSSSNSKVVMMPLEASSLM 285
Cdd:TIGR01933 239 -LSNTRKVLLDDKKGNNLL 256
PRK10930 PRK10930
FtsH protease activity modulator HflK;
8-248 2.23e-10

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 61.00  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   8 LIFVALVIV--GAGVKIVPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIgRKINMmEQVLDIPSQEVISKDNANVT-ID 84
Cdd:PRK10930  83 IAAAAVVIIwaASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEV-KPVNV-EAVRELAASGVMLTSDENVVrVE 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  85 AVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGSMELDEMLSQ-RDSINSRLLRIVDEATNPW--GIKVTRIEIRD 161
Cdd:PRK10930 161 MNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYdmGITLLDVNFQA 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 162 VRPPAELISSMNAQMKAERTKRAYILEAEGIRQAEILKAEGEKQSQILKAEGERQSAFLQAEARersaeaEARATKMVSE 241
Cdd:PRK10930 241 ARPPEEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGE------VARFAKLLPE 314


                 ....*..
gi 446827246 242 AIASGDI 248
Cdd:PRK10930 315 YKAAPEI 321
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 2-289 4.15e-96

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 284.81  E-value: 4.15e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   2 LIFIPILIFVALVIVGAGVKIVPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANV 81
Cdd:COG0330    3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  82 TIDAVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGSMELDEMLS-QRDSINSRLLRIVDEATNPWGIKVTRIEIR 160
Cdd:COG0330   82 DVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 161 DVRPPAELISSMNAQMKAERTKRAYILEAEGIRQAEILKAEGEKQSQILKAEGERQSAFLQaearersAEAEARATKMVS 240
Cdd:COG0330  162 DIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILR-------AEGEAEAFRIVA 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 446827246 241 EAiasgdIQAVNYFVAQKYTEALQQIGsSSNSKVVMMPLEASSLMGSIA 289
Cdd:COG0330  235 EA-----YSAAPFVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLL 277
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 58-166 2.21e-56

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: 177.67  E-value: 2.21e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  58 KINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGSMELDEMLSQRDSINS 137
Cdd:cd08829    3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                         90       100
                 ....*....|....*....|....*....
gi 446827246 138 RLLRIVDEATNPWGIKVTRIEIRDVRPPA 166
Cdd:cd08829   83 KLLEALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 23-280 9.58e-52

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: 169.72  E-value: 9.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  23 VPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRAAYEVS 102
Cdd:cd13437    9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKI-IQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 103 NLELAIINLTMTNIRTVLGSMELDEMLSQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQMKAERTk 182
Cdd:cd13437   88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRI- 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 183 rayileaegirqaeilkaegeKQSQILKAEGERQSAFLQAEArersaeAEARATKmvseaiASGDIqavnyfvaqKYTEA 262
Cdd:cd13437  167 ---------------------GESKIISAKADVESAKLMREA------ADILDSK------AAMQI---------RYLET 204

                        250
                 ....*....|....*...
gi 446827246 263 LQQIGSSSNSKVVMMPLE 280
Cdd:cd13437  205 LQAIAKSANSKVIFLPLD 222
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 50-195 5.74e-48

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: 158.45  E-value: 5.74e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  50 PFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGSMELDEML 129
Cdd:cd08826    1 PFIDRM-VRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446827246 130 SQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQMKAERTKRAYILEAEGIRQA 195
Cdd:cd08826   80 SEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQA 145
PHB smart00244
prohibitin homologues; prohibitin homologues
 18-176 1.81e-42

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 143.57  E-value: 1.81e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246    18 AGVKIVPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRA 97
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246    98 AYEVSNLELAII-NLTMTNIRTVLGSMELDEMLS-QRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQ 175
Cdd:smart00244  80 VYRVLDADYAVIeQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159


                   .
gi 446827246   176 M 176
Cdd:smart00244 160 Q 160
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 59-166 3.20e-36

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: 125.77  E-value: 3.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  59 INMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGSMELDEMLSQRDSINSR 138
Cdd:cd13434    1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                         90       100
                 ....*....|....*....|....*...
gi 446827246 139 LLRIVDEATNPWGIKVTRIEIRDVRPPA 166
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDIILPQ 108
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 21-191 9.80e-36

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: 126.67  E-value: 9.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   21 KIVPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVI--DAPRAA 98
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   99 YEV---SNLELAIINLTMTNIRTVLGSMELDEMLSQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQ 175
Cdd:pfam01145  80 QNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*.
gi 446827246  176 MKAERTKRAYILEAEG 191
Cdd:pfam01145 160 QTAEQEAEAEIARAEA 175
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 43-280 1.56e-34

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: 124.80  E-value: 1.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  43 PGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGS 122
Cdd:cd13435    7 PGVFFVLPCIDNY-CKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 123 MELDEMLSQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQMKAERTKRayileaegirqAEILKAEG 202
Cdd:cd13435   86 RNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREAR-----------AKVIAAEG 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446827246 203 EKqsqilkaegerqsaflqaeareRSAEAEARATKMVSEAIASgdiqavnyfVAQKYTEALQQIGSSSNSKVVM-MPLE 280
Cdd:cd13435  155 EM----------------------KSSRALKEASDIISASPSA---------LQLRYLQTLSSISGEKNSTIIFpLPME 202
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 43-195 4.80e-34

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: 123.04  E-value: 4.80e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  43 PGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGS 122
Cdd:cd03403    7 PGLFFILPCIDSY-RKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGT 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446827246 123 MELDEMLSQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQMKAERTKRAYILEAEGIRQA 195
Cdd:cd03403   86 KNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNA 158
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 43-191 3.77e-29

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: 108.97  E-value: 3.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  43 PGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGS 122
Cdd:cd08828    3 PGLILVLPCTDTF-IKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGT 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446827246 123 MELDEMLSQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQMKAERTKRAYILEAEG 191
Cdd:cd08828   82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEG 150
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 59-201 8.77e-29

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: 108.48  E-value: 8.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  59 INMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGSMELDEMLSQRDSINSR 138
Cdd:cd13775    1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446827246 139 LLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQMKAERTKRAYILEAEgirqAEILKAE 201
Cdd:cd13775   81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAE----AEKEIAE 139
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 22-278 2.14e-28

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: 109.98  E-value: 2.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  22 IVPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIGRKINMMEQVLDIpSQEVISKDNANVTIDAVCFIQVID--APRAAY 99
Cdd:cd03407    1 CVSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDV-RVETKTKDNVFVTLVVSVQYRVVPekVYDAFY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 100 EVSNLELAIINLTMTNIRTVLGSMELDEMLSQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQMKAE 179
Cdd:cd03407   80 KLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 180 RTKRAYILEAEGIRQAEILKAEGEKQSQILKAEGerqsaflQAEARERSAEAEARATKMVSEAIASGDIQ-AVNYFVAQK 258
Cdd:cd03407  160 RLREAAEEKAEAEKILQVKAAEAEAEAKRLQGVG-------IAEQRKAIVDGLRESIEDFQEAVPGVSSKeVMDLLLITQ 232

                        250       260
                 ....*....|....*....|
gi 446827246 259 YTEALQQIGSSSNSKVVMMP 278
Cdd:cd03407  233 YFDTLKEVGKSSKSSTVFLP 252
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 22-242 3.79e-28

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: 108.73  E-value: 3.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  22 IVPQGYQWTVERFGRYTKT-LQPGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDaPRAAYE 100
Cdd:cd03405    4 IVDETEQAVVLQFGKPVRViTEPGLHFKLPFIQNV-RKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITD-PLRFYQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 101 -VSNLELA------IINltmTNIRTVLGSMELDEMLS-QRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSM 172
Cdd:cd03405   82 sVGGEEGAesrlddIVD---SALRNEIGKRTLAEVVSgGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESV 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 173 NAQMKAERTKRAYILEAEGIRQAEILKAEGEKQSQILKAEGERQsaflqaeARERSAEAEARATKMVSEA 242
Cdd:cd03405  159 YERMRAERERIAAEYRAEGEEEAEKIRAEADRERTVILAEAYRE-------AEEIRGEGDAEAARIYAEA 221
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 7-240 5.49e-28

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: 108.75  E-value: 5.49e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   7 ILIFVALVIVGAGVKIVPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIGRKINMME-QVLDIP-----SQEVISKDNAN 80
Cdd:cd03404    2 ILLLLLLVWLLSGFYTVDPGERGVVLRFGKYVRTVGPGLHWKLPFPIEVVEKVNVTQvRSVEIGfrvpeESLMLTGDENI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  81 VTIDAVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGSMELDEMLS-QRDSINSRLLRIVDEATNPW--GIKVTRI 157
Cdd:cd03404   82 VDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQEILDRYdlGIEIVQV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 158 EIRDVRPPAELISSMNAQMKAERTKRAYILEAEGIRQAEILKAEGEKQSQILKAEGERQsaflqaearERSAEAEARATK 237
Cdd:cd03404  162 QLQDADPPEEVQDAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKA---------EVVARAEGDAAR 232


                 ...
gi 446827246 238 MVS 240
Cdd:cd03404  233 FLA 235
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 20-206 1.05e-23

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: 96.50  E-value: 1.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  20 VKIVPQGYQWTVERFGRYT--KTLQPGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRA 97
Cdd:cd08827    4 VKVVREYERAVIFRLGHLLqgRARGPGLFFYLPCLDVC-HKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  98 AYEVSNLELAIINLTMTNIRTVLGSMELDEMLSQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQMK 177
Cdd:cd08827   83 LSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 446827246 178 AERTKRAYILEAEGIRQA-EILKAEGEKQS 206
Cdd:cd08827  163 AQRQAKVKVIAAEGEKAAsEALKAAAESLS 192
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 35-193 6.96e-23

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: 94.14  E-value: 6.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  35 GRYTKTLQPGLSLVVPFMDRIGR-KINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRAAYEVSNLELAIINLTM 113
Cdd:cd13438   13 GKLVRTLEPGRYAFWKFGRKVQVeLVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETVDDPEEQLYLALQ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 114 TNIRTVLGSMELDEMLSQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQMKAErtKRAyilEAEGIR 193
Cdd:cd13438   93 LALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAE--KRA---QANLIR 167
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 31-285 1.18e-16

HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 77.83  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   31 VERFGRYTKTLQPGLSLVVPFMDRIgRKINMmEQVLDIPSQ-EVISKDNANVTIDAVCFIQVIDAPRAAYEVSNLELAII 109
Cdd:TIGR01933  12 VLRFGKYHRTVDPGLNWKPPFIEEV-YPVNV-TAVRNLRKQgLMLTGDENIVNVEMNVQYRITDPYKYLFSVENPEDSLR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  110 NLTMTNIRTVLGSMELDEMLSQ-RDSINSRLLRIVDEATNPW--GIKVTRIEIRDVRPPAELISSMNAQMKAERTKRAYI 186
Cdd:TIGR01933  90 QATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDVIIAREDEERYI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  187 LEAEGIRQAEILKAEGEKQSQILKAEGERQSAFLQAEarersAEAEaRATKMVSEAIASGDIQAvnyfvAQKYTEALQQI 266
Cdd:TIGR01933 170 NEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAK-----GDVA-RFTKLLAEYKKAPDVTR-----ERLYLETMEKV 238

                         250
                  ....*....|....*....
gi 446827246  267 gSSSNSKVVMMPLEASSLM 285
Cdd:TIGR01933 239 -LSNTRKVLLDDKKGNNLL 256
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 20-218 4.24e-16

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 74.86  E-value: 4.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  20 VKIVPQGYQWTVERFGRYTK--TLQPGLSLVVPFMDRIgRKINMMEQVLDIPSqEVISKDNANVTIDavcfIQV---IDA 94
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKdeVLGEGLHFKIPWIQVV-IIYDVRTQPREITL-TVLSKDGQTVNID----LSVlyrPDP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  95 PRAAYEVSNL-----ELAIINLTMTNIRTVLGSMELDEMLSQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELI 169
Cdd:cd03401   75 EKLPELYQNLgpdyeERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446827246 170 SSMNAQMKAE-RTKRAyileaegirQAEILKAEGEKQSQILKAEGERQSA 218
Cdd:cd03401  155 KAIEAKQVAEqEAERA---------KFELEKAEQEAERKVIEAEGEAEAQ 195
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 35-163 1.87e-14

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: 68.97  E-value: 1.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  35 GRYTKTLQPGLSLVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAPRAAYEVSNLELAIINLTMT 114
Cdd:cd13436    1 GRLQKPRGPGIVLILPCIDNF-TRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446827246 115 NIRTVLGSMELDEMLSQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVR 163
Cdd:cd13436   80 SLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVK 128
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 63-165 7.40e-12

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: 61.23  E-value: 7.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  63 EQVLDIPSQEVISKDNANVTIDAVCFIQVIDaPRAAYEVSNL------ELAIINLTMTNIRTVLGSMELDEMLSQRDSIN 136
Cdd:cd02106    2 PQFDDVRVEPVGTADGVPVAVDLVVQFRITD-YNALPAFYLVdfvkdiKADIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                         90       100
                 ....*....|....*....|....*....
gi 446827246 137 SRLLRIVDEATNPWGIKVTRIEIRDVRPP 165
Cdd:cd02106   81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
2-266 9.95e-12

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 64.89  E-value: 9.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   2 LIFIPILIFVALVIVGAGV----KIVPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIGRkINMMEQVLDI-PSQEVISK 76
Cdd:COG2268    6 ILIIIGVIVVVLLLLLIILarfyRKVPPNEALVITGRGGGYKVVTGGGAFVLPVLHRAER-MSLSTMTIEVeRTEGLITK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  77 DNANVTIDAVCFIQVIDAP----RAAYEVSNLELAIINLTMT-----NIRTVLGSMELDEMLSQRDSINSRLLRIVDEAT 147
Cdd:COG2268   85 DGIRVDVDAVFYVKVNSDPediaNAAERFLGRDPEEIEELAEeklegALRAVAAQMTVEELNEDREKFAEKVQEVAGTDL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 148 NPWGIKVTRIEIRDVRPPAELISSMNAQMKAERTKRAYILEAEGIRQAEILKAEGEKQSQILKAEGERQSAFLQ------ 221
Cdd:COG2268  165 AKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARiaeaea 244

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446827246 222 --------AEARERSAEAEARATKMVSEAIASGDIQAVNYFVAQKYTEALQQI 266
Cdd:COG2268  245 elakkkaeERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEK 297
PRK10930 PRK10930
FtsH protease activity modulator HflK;
8-248 2.23e-10

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 61.00  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   8 LIFVALVIV--GAGVKIVPQGYQWTVERFGRYTKTLQPGLSLVVPFMDRIgRKINMmEQVLDIPSQEVISKDNANVT-ID 84
Cdd:PRK10930  83 IAAAAVVIIwaASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEV-KPVNV-EAVRELAASGVMLTSDENVVrVE 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  85 AVCFIQVIDAPRAAYEVSNLELAIINLTMTNIRTVLGSMELDEMLSQ-RDSINSRLLRIVDEATNPW--GIKVTRIEIRD 161
Cdd:PRK10930 161 MNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYdmGITLLDVNFQA 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 162 VRPPAELISSMNAQMKAERTKRAYILEAEGIRQAEILKAEGEKQSQILKAEGERQSAFLQAEARersaeaEARATKMVSE 241
Cdd:PRK10930 241 ARPPEEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGE------VARFAKLLPE 314


                 ....*..
gi 446827246 242 AIASGDI 248
Cdd:PRK10930 315 YKAAPEI 321
PRK11029 PRK11029
protease modulator HflC;
3-242 4.89e-10

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 59.37  E-value: 4.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246   3 IFIPILIFVaLVIVGAGVKIVPQGYQWTVERFGRY-----TKTL--QPGLSLVVPFMDRIgRKINMMEQVLDIPSQEVIS 75
Cdd:PRK11029   4 SVIAIIIIV-LVVLYMSVFVVKEGERGIVLRFGKVlrdddNKPLvyAPGLHFKIPFIETV-KMLDARIQTMDNQADRFVT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  76 KDNANVTIDAVCFIQVID------------------------APRAAYEVSNLELAII-----NLTMTNIRTVL--GSME 124
Cdd:PRK11029  82 KEKKDLIVDSYIKWRISDfsryylatgggdisqaevllkrkfSDRLRSEIGRLDVKDIvtdsrGRLTLDVRDALnsGSAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246 125 LDEMLSQR---DSINSRLLRIVDE------ATNP-----WGIKVTRIEIRDVRPPAELISSMNAQMKAERTKRAYILEAE 190
Cdd:PRK11029 162 TEDEVATPaadDAIASAAERVEAEtkgkvpVINPnsmaaLGIEVVDVRIKQINLPTEVSDAIYNRMRAEREAVARRHRSQ 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446827246 191 GIRQAEILKAEGEKQSQILKAEGERQSAFLQaearersAEAEARATKMVSEA 242
Cdd:PRK11029 242 GQEEAEKLRATADYEVTRTLAEAERQGRIMR-------GEGDAEAAKLFADA 286
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 47-183 2.57e-08

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: 52.12  E-value: 2.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  47 LVVPFMDRIgRKINMMEQVLDIPSQEVISKDNANVTIDAVCFIQVIDAP---RAAYE--VSNLELAIINLTMT----NIR 117
Cdd:cd03399    1 FVIPFLQRV-QRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPeeiAAAAErfLGKSTEEIRELVKEtlegHLR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446827246 118 TVLGSMELDEMLSQRDSINSRLLRIVDEATNPWGIKVTRIEIRDVRPPAELISSMNAQmKAERTKR 183
Cdd:cd03399   80 AIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRK-QAAEVKK 144
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 11-154 4.98e-07

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: 49.86  E-value: 4.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446827246  11 VALVIVGAGVKIVPQGYQWTVERFGRYTKTL-QPGLSLVVPFMDRigRKINMMEQVLDIPSQEVISKDNANVTIDAVCFI 89
Cdd:cd03402    1 VVGIILLGGFFVVQPNEAAVLTLFGRYRGTVrRPGLRWVNPFYRK--KRVSLRVRNFESEPLKVNDANGNPIEIAAVVVW 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446827246  90 QVIDAPRAAYEVSNLELAIINLTMTNIRTVLGSMELDEM----LSQR---DSINSRLLRIVDEATNPWGIKV 154
Cdd:cd03402   79 RVVDTAKAVFDVDDYEEFVSIQSEAALRRVASRYPYDSFedgePSLRgnsDEVSEELRRELQERLAVAGVEV 150
Band_7_C pfam16200
C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal ...
 237-296 3.39e-04

C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal extension of the Band_7 family, pfam01145. It is found in proteins fro bacteria to fungi, plants and mammals.


Pssm-ID: 465062  Cd Length: 63  Bit Score: 38.23  E-value: 3.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446827246  237 KMVSEAIAS-GDIQAVNYFVAQKYTEALQQIGSSSNSkvVMMPLEASSLMGSIAGIAELVK 296
Cdd:pfam16200   1 EKVAEAIKKpGGQEAVSLRVAEQYVEAFGKLAKESNT--VILPANLGDVSSMVAQAMSIYK 59
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH