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Conserved domains on  [gi|497369062|ref|WP_009683275|]
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MULTISPECIES: SPFH domain-containing protein [Pseudomonas]

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

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List of domain hits

 Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-281 8.47e-81

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 245.13  E-value: 8.47e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   4 LIVVGAIALFVLITVFKGVRIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVaYRLPTKDIILDVQEQEIITKDNAVI 83
Cdd:COG0330    3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  84 VANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSS-REQIKARLREAMSEQTEDWGVTVRSVEIQ 162
Cdd:COG0330   82 DVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 163 DIKPSENMQLAMERQAAAERERKADVTRAEGAKQAAILEAEARLQAARLDAEA----QISLAEASARAISLVKEAVGnet 238
Cdd:COG0330  162 DIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAyreaQILRAEGEAEAFRIVAEAYS--- 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 497369062 239 vPAMYLLGERYVGAMENLAgSNNAKVVVLPADLQETVRGLMGR 281
Cdd:COG0330  239 -AAPFVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLLKS 279
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-281 8.47e-81

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 245.13  E-value: 8.47e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   4 LIVVGAIALFVLITVFKGVRIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVaYRLPTKDIILDVQEQEIITKDNAVI 83
Cdd:COG0330    3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  84 VANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSS-REQIKARLREAMSEQTEDWGVTVRSVEIQ 162
Cdd:COG0330   82 DVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 163 DIKPSENMQLAMERQAAAERERKADVTRAEGAKQAAILEAEARLQAARLDAEA----QISLAEASARAISLVKEAVGnet 238
Cdd:COG0330  162 DIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAyreaQILRAEGEAEAFRIVAEAYS--- 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 497369062 239 vPAMYLLGERYVGAMENLAgSNNAKVVVLPADLQETVRGLMGR 281
Cdd:COG0330  239 -AAPFVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLLKS 279
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 58-168 7.38e-50

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: 160.33  E-value: 7.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  58 AYRLPTKDIILDVQEQEIITKDNAVIVANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSSREQI 137
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 497369062 138 KARLREAMSEQTEDWGVTVRSVEIQDIKPSE 168
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 20-178 9.69e-40

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 135.87  E-value: 9.69e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062    20 KGVRIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVaYRLPTKDIILDVQEQEIITKDNAVIVANALCFAKVVDPQKA 99
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   100 SYGVQNFSFAVT-SLTMTSLRAIVGAMDLDEALSS-REQIKARLREAMSEQTEDWGVTVRSVEIQDIKPSENMQLAMERQ 177
Cdd:smart00244  80 VYRVLDADYAVIeQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159


                   .
gi 497369062   178 A 178
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 ...
 23-195 1.26e-30

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: 112.80  E-value: 1.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   23 RIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVaYRLPTKDIILDVQEQEIITKDNAVIVANALCFAKV--VDPQKAS 100
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  101 YGVQNFSFA---VTSLTMTSLRAIVGAMDLDEALSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIKPSENMQLAMERQ 177
Cdd:pfam01145  80 QNVFGSDDLqelLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*...
gi 497369062  178 AAAERERKADVTRAEGAK 195
Cdd:pfam01145 160 QTAEQEAEAEIARAEAEA 177
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 22-266 1.35e-21

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: 91.31  E-value: 1.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   22 VRIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVaYRLPTKDIILDVQEQEIITKDNAVIVANALCFAKVVDPQKASY 101
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEV-YPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPYKYLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  102 GVQNFSFAVTSLTMTSLRAIVGAMDLDEALSS-REQIKARLREAMSEQTE--DWGVTVRSVEIQDIKPSENMQLAMERQA 178
Cdd:TIGR01933  80 SVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDnyDLGITVTDVNFQSARPPEEVKEAFDDVI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  179 AAeRERKADVTRaEGAKQAAILEAEARLQAARLDAEAQISLAEASARAISLVK--EAVGNETVPAMYLLGER-YVGAMEN 255
Cdd:TIGR01933 160 IA-REDEERYIN-EAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGDVArfTKLLAEYKKAPDVTRERlYLETMEK 237

                         250
                  ....*....|.
gi 497369062  256 LAgSNNAKVVV 266
Cdd:TIGR01933 238 VL-SNTRKVLL 247
PRK10930 PRK10930
FtsH protease activity modulator HflK;
5-270 5.16e-08

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 53.29  E-value: 5.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   5 IVVGAIALFVLITVFKGVRIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVV------AYR-LPTKDIILdvqeqeiiT 77
Cdd:PRK10930  80 VVGIAAAAVVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVkpvnveAVReLAASGVML--------T 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  78 KDNAVIVANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSS-REQIKARLREAMSE--QTEDWGV 154
Cdd:PRK10930 152 SDENVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEEtiRPYDMGI 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 155 TVRSVEIQDIKPSENMQLAMErQAAAERERkadvtraegaKQAAILEAEARLQAA--RLDAEAQISLAEASARAISLVKE 232
Cdd:PRK10930 232 TLLDVNFQAARPPEEVKAAFD-DAIAAREN----------EQQYIREAEAYTNEVqpRANGQAQRILEEARAYKAQTILE 300

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 497369062 233 AVGN---------ETVPAMYLLGER-YVGAMEN--------LAGSNNAKVVVLPAD 270
Cdd:PRK10930 301 AQGEvarfakllpEYKAAPEITRERlYIETMEKvlghtrkvLVNDKGGNLMVLPLD 356
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-281 8.47e-81

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 245.13  E-value: 8.47e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   4 LIVVGAIALFVLITVFKGVRIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVaYRLPTKDIILDVQEQEIITKDNAVI 83
Cdd:COG0330    3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  84 VANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSS-REQIKARLREAMSEQTEDWGVTVRSVEIQ 162
Cdd:COG0330   82 DVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 163 DIKPSENMQLAMERQAAAERERKADVTRAEGAKQAAILEAEARLQAARLDAEA----QISLAEASARAISLVKEAVGnet 238
Cdd:COG0330  162 DIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAyreaQILRAEGEAEAFRIVAEAYS--- 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 497369062 239 vPAMYLLGERYVGAMENLAgSNNAKVVVLPADLQETVRGLMGR 281
Cdd:COG0330  239 -AAPFVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLLKS 279
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 58-168 7.38e-50

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: 160.33  E-value: 7.38e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  58 AYRLPTKDIILDVQEQEIITKDNAVIVANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSSREQI 137
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 497369062 138 KARLREAMSEQTEDWGVTVRSVEIQDIKPSE 168
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 66-204 2.44e-45

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: 151.13  E-value: 2.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  66 IILDVQEQEIITKDNAVIVANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSSREQIKARLREAM 145
Cdd:cd08826   14 VTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLSEREEINKRIQEII 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497369062 146 SEQTEDWGVTVRSVEIQDIKPSENMQLAMERQAAAERERKADVTRAEGAKQAAILEAEA 204
Cdd:cd08826   94 DEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEA 152
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 25-270 2.37e-42

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: 144.68  E-value: 2.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  25 VPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVaYRLPTKDIILDVQEQEIITKDNAVIVANALCFAKVVDPQKASYGVQ 104
Cdd:cd13437    9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKI-IQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 105 NFSFAVTSLTMTSLRAIVGAMDLDEALSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIKPSENMQLAMerQAAAERER 184
Cdd:cd13437   88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSL--SSAAKAKR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 185 KAdvtraegakQAAILEAEARLQAARLDAEAQISLAEASARAIslvkeavgnetvpamyllgeRYVGAMENLAGSNNAKV 264
Cdd:cd13437  166 IG---------ESKIISAKADVESAKLMREAADILDSKAAMQI--------------------RYLETLQAIAKSANSKV 216


                 ....*.
gi 497369062 265 VVLPAD 270
Cdd:cd13437  217 IFLPLD 222
PHB smart00244
prohibitin homologues; prohibitin homologues
 20-178 9.69e-40

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 135.87  E-value: 9.69e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062    20 KGVRIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVaYRLPTKDIILDVQEQEIITKDNAVIVANALCFAKVVDPQKA 99
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   100 SYGVQNFSFAVT-SLTMTSLRAIVGAMDLDEALSS-REQIKARLREAMSEQTEDWGVTVRSVEIQDIKPSENMQLAMERQ 177
Cdd:smart00244  80 VYRVLDADYAVIeQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159


                   .
gi 497369062   178 A 178
Cdd:smart00244 160 Q 160
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 73-234 1.15e-33

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: 120.81  E-value: 1.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  73 QEIITKDNAVIVANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSSREQIKARLREAMSEQTEDW 152
Cdd:cd13775   13 EQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPW 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 153 GVTVRSVEIQDIKPSENMQLAMERQAAAERERKADVTRAEGAKQAaileAEARLQAARLDAEAQISLaeaSARAISLVKE 232
Cdd:cd13775   93 GITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEI----AEMFVEAAEVYENNPIAL---QLRAMNMLYE 165


                 ..
gi 497369062 233 AV 234
Cdd:cd13775  166 GL 167
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 23-195 1.26e-30

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: 112.80  E-value: 1.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   23 RIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVaYRLPTKDIILDVQEQEIITKDNAVIVANALCFAKV--VDPQKAS 100
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  101 YGVQNFSFA---VTSLTMTSLRAIVGAMDLDEALSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIKPSENMQLAMERQ 177
Cdd:pfam01145  80 QNVFGSDDLqelLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*...
gi 497369062  178 AAAERERKADVTRAEGAK 195
Cdd:pfam01145 160 QTAEQEAEAEIARAEAEA 177
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 45-235 1.60e-30

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: 113.63  E-value: 1.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  45 PGLNIVIPYMDVVaYRLPTKDIILDVQEQEIITKDNAVIVANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGA 124
Cdd:cd13435    7 PGVFFVLPCIDNY-CKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 125 MDLDEALSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIKPSENMQLAMERQAAAERERKADVTRAEGAKQAA------ 198
Cdd:cd13435   86 RNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSralkea 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 497369062 199 ---ILEAEARLQAARLDAEAQISLAEASARAISLVKEAVG 235
Cdd:cd13435  166 sdiISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLT 205
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 24-270 2.48e-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: 109.21  E-value: 2.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  24 IVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVAYRLPTKDIILDVQEqEIITKDNaVIVANALCFAKVVDPQKAS--- 100
Cdd:cd03407    1 CVSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDVRV-ETKTKDN-VFVTLVVSVQYRVVPEKVYdaf 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 101 YGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIKPSENMQLAMERQAAA 180
Cdd:cd03407   79 YKLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 181 ERERKADVTRAEGAKQAAILEAEARLQAARLDAEAqisLAEASaRAI---------SLVKEAVGNETVPAMYL-LGERYV 250
Cdd:cd03407  159 QRLREAAEEKAEAEKILQVKAAEAEAEAKRLQGVG---IAEQR-KAIvdglresieDFQEAVPGVSSKEVMDLlLITQYF 234

                        250       260
                 ....*....|....*....|
gi 497369062 251 GAMENLAGSNNAKVVVLPAD 270
Cdd:cd03407  235 DTLKEVGKSSKSSTVFLPHG 254
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 8-226 7.03e-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: 107.98  E-value: 7.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   8 GAIALFVLITVFKGVRIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVAYRLPTKDI------ILDVQEQEIITKDNA 81
Cdd:cd03404    1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGKYVRTVGPGLHWKLPFPIEVVEKVNVTQVrsveigFRVPEESLMLTGDEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  82 VIVANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSS-REQIKARLREAMSEQTEDW--GVTVRS 158
Cdd:cd03404   81 IVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEILDRYdlGIEIVQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497369062 159 VEIQDIKPSENMQLAMErqaaaererkaDVTRAEGAKQAAILEAE---------ARLQAARLDAEAQISLAEASARA 226
Cdd:cd03404  161 VQLQDADPPEEVQDAFD-----------DVNAARQDKERLINEAQayaneviprARGEAARIIQEAEAYKAEVVARA 226
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 66-168 5.25e-27

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: 101.11  E-value: 5.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  66 IILDVQEQEIITKDNAVIVANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSSREQIKARLREAM 145
Cdd:cd13434    6 QSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQEIL 85

                         90       100
                 ....*....|....*....|...
gi 497369062 146 SEQTEDWGVTVRSVEIQDIKPSE 168
Cdd:cd13434   86 DEATDPWGIKVERVEIKDIILPQ 108
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 45-218 2.17e-25

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: 99.93  E-value: 2.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  45 PGLNIVIPYMDVVAyRLPTKDIILDVQEQEIITKDNAVIVANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGA 124
Cdd:cd03403    7 PGLFFILPCIDSYR-KVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 125 MDLDEALSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIKPSENMQLAMERQAAAERERKADVTRAEGAKQAA------ 198
Cdd:cd03403   86 KNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASralkea 165

                        170       180
                 ....*....|....*....|...
gi 497369062 199 ---ILEAEARLQAARLDAEAQIS 218
Cdd:cd03403  166 advISESPAALQLRYLQTLNTIS 188
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 24-226 4.31e-24

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: 97.56  E-value: 4.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  24 IVPQGEEWIVERLGR-YHSTLKPGLNIVIPYMDVVaYRLPTKDIILDVQEQEIITKDNAVIVANAlcFAK--VVDPQKAS 100
Cdd:cd03405    4 IVDETEQAVVLQFGKpVRVITEPGLHFKLPFIQNV-RKFDKRILTLDGPPEEVLTKDKKRLIVDS--YARwrITDPLRFY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 101 YGVQNFSFAVTSLTM---TSLRAIVGAMDLDEALSS-REQIKARLREAMSEQTEDWGVTVRSVEIQDIK-PSENMQLAME 175
Cdd:cd03405   81 QSVGGEEGAESRLDDivdSALRNEIGKRTLAEVVSGgRDELMEEILEQANEEAKEYGIEVVDVRIKRIDlPEEVSESVYE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497369062 176 RQAAaERERKADVTRAEGAKQAAILEAEArlqaarlDAEAQISLAEASARA 226
Cdd:cd03405  161 RMRA-ERERIAAEYRAEGEEEAEKIRAEA-------DRERTVILAEAYREA 203
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 25-211 2.91e-22

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: 91.83  E-value: 2.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  25 VPQGEEWIVERLGRYHSTLKPGLNIV-IPYMDVVAYRLPTKDIILDVQEQEIITKDNAVIVANALCFAKVVDPQKASYGV 103
Cdd:cd13438    1 VPPGERGLLYRDGKLVRTLEPGRYAFwKFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 104 QNFSFAVTSLTMTSLRAIVGAMDLDEALSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIKPSENMQLAMERQAAAERE 183
Cdd:cd13438   81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKR 160

                        170       180
                 ....*....|....*....|....*...
gi 497369062 184 RKADVTRAEGaKQAAileAEARLQAARL 211
Cdd:cd13438  161 AQANLIRARE-ETAA---TRSLLNAAKL 184
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 22-266 1.35e-21

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: 91.31  E-value: 1.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   22 VRIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVaYRLPTKDIILDVQEQEIITKDNAVIVANALCFAKVVDPQKASY 101
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEV-YPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPYKYLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  102 GVQNFSFAVTSLTMTSLRAIVGAMDLDEALSS-REQIKARLREAMSEQTE--DWGVTVRSVEIQDIKPSENMQLAMERQA 178
Cdd:TIGR01933  80 SVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDnyDLGITVTDVNFQSARPPEEVKEAFDDVI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  179 AAeRERKADVTRaEGAKQAAILEAEARLQAARLDAEAQISLAEASARAISLVK--EAVGNETVPAMYLLGER-YVGAMEN 255
Cdd:TIGR01933 160 IA-REDEERYIN-EAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGDVArfTKLLAEYKKAPDVTRERlYLETMEK 237

                         250
                  ....*....|.
gi 497369062  256 LAgSNNAKVVV 266
Cdd:TIGR01933 238 VL-SNTRKVLL 247
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 45-197 5.15e-20

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: 84.31  E-value: 5.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  45 PGLNIVIPYMDVVAyRLPTKDIILDVQEQEIITKDNAVIVANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGA 124
Cdd:cd08828    3 PGLILVLPCTDTFI-KVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGT 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497369062 125 MDLDEALSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIKPSENMQLAMERQAAAERERKADVTRAEGAKQA 197
Cdd:cd08828   82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 22-226 6.22e-18

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: 79.48  E-value: 6.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  22 VRIVPQGEEWIVERLGRYHS--TLKPGLNIVIPYMDVVayrlptkdIILDVQEQ------EIITKD-NAVIVANALCFAk 92
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKdeVLGEGLHFKIPWIQVV--------IIYDVRTQpreitlTVLSKDgQTVNIDLSVLYR- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  93 vVDPQKA-----SYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIKPS 167
Cdd:cd03401   72 -PDPEKLpelyqNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFP 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497369062 168 ENMQLAMERQAAAErerkadvtraegakQAAiLEAEARLQAARLDAEAQISLAEASARA 226
Cdd:cd03401  151 DEYEKAIEAKQVAE--------------QEA-ERAKFELEKAEQEAERKVIEAEGEAEA 194
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 22-198 3.08e-16

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: 75.69  E-value: 3.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  22 VRIVPQGEEWIVERLGRYHS--TLKPGLNIVIPYMDV---VAYRLPTkdiiLDVQEQEIITKDNAVIVANALCFAKVVDP 96
Cdd:cd08827    4 VKVVREYERAVIFRLGHLLQgrARGPGLFFYLPCLDVchkVDIRLQT----LEIPFHMIVTKDLVCTEIDAICYYRIENA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  97 QKASYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIKPSENMQLAMER 176
Cdd:cd08827   80 SVCLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAV 159

                        170       180
                 ....*....|....*....|..
gi 497369062 177 QAAAERERKADVTRAEGAKQAA 198
Cdd:cd08827  160 EAEAQRQAKVKVIAAEGEKAAS 181
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 37-165 2.68e-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: 68.20  E-value: 2.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  37 GRYHSTLKPGLNIVIPYMDVVAyRLPTKDIILDVQEQEIITKDNAVIVANALCFAKVVDPQKASYGVQNFSFAVTSLTMT 116
Cdd:cd13436    1 GRLQKPRGPGIVLILPCIDNFT-RVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 497369062 117 SLRAIVGAMDLDEALSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIK 165
Cdd:cd13436   80 SLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVK 128
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 68-166 1.15e-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: 54.68  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  68 LDVQEQEIITKDNAVIVANALCFAKVVDPQKA-----SYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSSREQIKARLR 142
Cdd:cd02106    5 DDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVK 84

                         90       100
                 ....*....|....*....|....
gi 497369062 143 EAMSEQTEDWGVTVRSVEIQDIKP 166
Cdd:cd02106   85 EDLEEDLENFGVVISDVDITSIEP 108
PRK10930 PRK10930
FtsH protease activity modulator HflK;
5-270 5.16e-08

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 53.29  E-value: 5.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   5 IVVGAIALFVLITVFKGVRIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVV------AYR-LPTKDIILdvqeqeiiT 77
Cdd:PRK10930  80 VVGIAAAAVVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVkpvnveAVReLAASGVML--------T 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  78 KDNAVIVANALCFAKVVDPQKASYGVQNFSFAVTSLTMTSLRAIVGAMDLDEALSS-REQIKARLREAMSE--QTEDWGV 154
Cdd:PRK10930 152 SDENVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEEtiRPYDMGI 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 155 TVRSVEIQDIKPSENMQLAMErQAAAERERkadvtraegaKQAAILEAEARLQAA--RLDAEAQISLAEASARAISLVKE 232
Cdd:PRK10930 232 TLLDVNFQAARPPEEVKAAFD-DAIAAREN----------EQQYIREAEAYTNEVqpRANGQAQRILEEARAYKAQTILE 300

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 497369062 233 AVGN---------ETVPAMYLLGER-YVGAMEN--------LAGSNNAKVVVLPAD 270
Cdd:PRK10930 301 AQGEvarfakllpEYKAAPEITRERlYIETMEKvlghtrkvLVNDKGGNLMVLPLD 356
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 14-205 7.50e-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: 49.09  E-value: 7.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  14 VLITVFKGVRIVPQGEEWIVERLGRYHSTLK-PGLNIVIPYMdvVAYRLPTKDIILDVQEQEIITKDNAVIVANALCFAK 92
Cdd:cd03402    2 VGIILLGGFFVVQPNEAAVLTLFGRYRGTVRrPGLRWVNPFY--RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  93 VVDPQKASYGVQNFSFAVTSLTMTSLRAIVG--AMDLDEA-----LSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIK 165
Cdd:cd03402   80 VVDTAKAVFDVDDYEEFVSIQSEAALRRVASryPYDSFEDgepslRGNSDEVSEELRRELQERLAVAGVEVIEARITHLA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 497369062 166 -PSENMQlAMER--QAAAERE-RKADVTRAEGAKQAAILEAEAR 205
Cdd:cd03402  160 yAPEIAQ-AMLQrqQASAIIAaRQTIVEGAVGMVEMALARLEER 202
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1-234 8.20e-07

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 49.87  E-value: 8.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   1 MTSLIVVGAIALFVLITVF---KGVRIVPQGEEWIVERLGRYHSTLKPGLNIVIPYMDVVAyRLPTKDIILDVQ-EQEII 76
Cdd:COG2268    4 LGILIIIGVIVVVLLLLLIilaRFYRKVPPNEALVITGRGGGYKVVTGGGAFVLPVLHRAE-RMSLSTMTIEVErTEGLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  77 TKDNAVIVANALCFAKVvdpQKASYGVQNFsfAVTSLTMTS--------------LRAIVGAMDLDEALSSREQIKARLR 142
Cdd:COG2268   83 TKDGIRVDVDAVFYVKV---NSDPEDIANA--AERFLGRDPeeieelaeeklegaLRAVAAQMTVEELNEDREKFAEKVQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 143 EAMSEQTEDWGVTVRSVEIQDIKPSEN-----------MQLAMERQAAAERERKADVTRAEGAKQAAILEAEARLQAARL 211
Cdd:COG2268  158 EVAGTDLAKNGLELESVAITDLEDENNyldalgrrkiaEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETA 237

                        250       260
                 ....*....|....*....|....*.
gi 497369062 212 D---AEAQISLAEASARAISLVKEAV 234
Cdd:COG2268  238 RiaeAEAELAKKKAEERREAETARAE 263
PRK11029 PRK11029
protease modulator HflC;
9-270 2.28e-05

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 45.12  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062   9 AIALFVLITVFKGVRIVPQGEEWIVERLGRY-----HSTL--KPGLNIVIPY-------------MDVVAYRLPT---KD 65
Cdd:PRK11029   7 AIIIIVLVVLYMSVFVVKEGERGIVLRFGKVlrdddNKPLvyAPGLHFKIPFietvkmldariqtMDNQADRFVTkekKD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  66 IILDVQEQEII---------TKDNAVIVANALCFAKVVDPQKASYGVQNFSFAVT---SLTMTSLRAIV--GAMDLDEAL 131
Cdd:PRK11029  87 LIVDSYIKWRIsdfsryylaTGGGDISQAEVLLKRKFSDRLRSEIGRLDVKDIVTdsrGRLTLDVRDALnsGSAGTEDEV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062 132 SSREQIKARLREAMSEQTEDW--------------GVTVRSVEIQDIK-PSEnMQLAMERQAAAERERKADVTRAEGAKQ 196
Cdd:PRK11029 167 ATPAADDAIASAAERVEAETKgkvpvinpnsmaalGIEVVDVRIKQINlPTE-VSDAIYNRMRAEREAVARRHRSQGQEE 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497369062 197 AAILEAEARLQAARLDAEAQ----ISLAEASARAISLVKEAVGNEtvPAMYLLgERYVGAMENlAGSNNAKVVVLPAD 270
Cdd:PRK11029 246 AEKLRATADYEVTRTLAEAErqgrIMRGEGDAEAAKLFADAFSQD--PDFYAF-IRSLRAYEN-SFSGNQDVMVLSPD 319
PTZ00491 PTZ00491
major vault protein; Provisional
 171-233 1.38e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 40.00  E-value: 1.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497369062 171 QLAMERQAAAERERKAdVTRAEGAKQA------AILEAEARLQAARLDAEAQISLAEASARAISLVKEA 233
Cdd:PTZ00491 685 RQKMHDKAKAEEQRTK-LLELQAESAAvessgqSRAEALAEAEARLIEAEAEVEQAELRAKALRIEAEA 752
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 58-183 1.46e-03

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: 38.25  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497369062  58 AYRLPTKDIILDVQEQEIITKDNAVIVANALCFAKV-VDPQKASYGVQNF----SFAVTSLTMT----SLRAIVGAMDLD 128
Cdd:cd03399    9 VQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVgSDPEEIAAAAERFlgksTEEIRELVKEtlegHLRAIVGTMTVE 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 497369062 129 EALSSREQIKARLREAMSEQTEDWGVTVRSVEIQDIKPSENMQ--LAMERQAAAERE 183
Cdd:cd03399   89 EIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLesLGRKQAAEVKKD 145
 
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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