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Conserved domains on  [gi|7305503|ref|NP_038470|]
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stomatin-like protein 2, mitochondrial isoform a [Homo sapiens]

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 ...
 41-300 5.99e-77

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 237.82  E-value: 5.99e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVE 120
Cdd:COG0330  24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  121 DPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERR 199
Cdd:COG0330 103 NAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAERE 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  200 KRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAAALTqhngdaAASLTVA 279
Cdd:COG0330 183 REAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLF 245

                       250       260
                ....*....|....*....|.
gi 7305503  280 EQYVSAFSKLAKDSNTILLPS 300
Cdd:COG0330 246 YRSLEALEEVLSPNSKVIVLP 266
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 41-300 5.99e-77

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 237.82  E-value: 5.99e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVE 120
Cdd:COG0330  24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  121 DPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERR 199
Cdd:COG0330 103 NAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAERE 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  200 KRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAAALTqhngdaAASLTVA 279
Cdd:COG0330 183 REAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLF 245

                       250       260
                ....*....|....*....|.
gi 7305503  280 EQYVSAFSKLAKDSNTILLPS 300
Cdd:COG0330 246 YRSLEALEEVLSPNSKVIVLP 266
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 74-184 8.49e-62

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: 193.07  E-value: 8.49e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   74 RYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESL 153
Cdd:cd08829   1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 7305503  154 NASIVDAINQAADCWGIRCLRYEIKDIHVPP 184
Cdd:cd08829  81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 40-194 1.02e-45

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 153.59  E-value: 1.02e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503      40 FVPQQEAWVVERMGRFHRILEPGLNILIPVLDRIrYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:smart00244   5 VVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRV 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7305503     120 EDPEYAVT-QLAQTTMRSELGKLSLDKVFR-ERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQV 194
Cdd:smart00244  84 LDADYAVIeQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 41-209 4.80e-34

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: 123.59  E-value: 4.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503     41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIM--DPYKASYG 118
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLVQN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503    119 VEDPEYA---VTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVE 195
Cdd:pfam01145  82 VFGSDDLqelLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQT 161

                         170
                  ....*....|....
gi 7305503    196 AERRKRATVLESEG 209
Cdd:pfam01145 162 AEQEAEAEIARAEA 175
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 41-243 1.65e-19

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: 86.69  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503     41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQSlkEIVINVPEQSAV-TLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNV--TAVRNLRKQGLMlTGDENIVNVEMNVQYRITDPYKYLFSV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503    120 EDPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCW--GIRCLRYEIKDIHVPPRVKESMQMQVEA 196
Cdd:TIGR01933  82 ENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDVIIA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 7305503    197 ERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 243
Cdd:TIGR01933 162 REDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGD 208
PRK10930 PRK10930
FtsH protease activity modulator HflK;
41-243 1.37e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 46.74  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503    41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIR--YVQSLKEIVinvpeQSAVTL---DNVTLQIDGVLYlRIMDPYKA 115
Cdd:PRK10930 100 IKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKpvNVEAVRELA-----ASGVMLtsdENVVRVEMNVQY-RVTDPEKY 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   116 SYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFREreslNASIVDAINQAADCWGIRCLRYEIKDIHV-------PPRVKE 188
Cdd:PRK10930 174 LFSVTSPDDSLRQATDSALRGVIGKYTMDRILTE----GRTVIRSDTQRELEETIRPYDMGITLLDVnfqaarpPEEVKA 249

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7305503   189 SMQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 243
Cdd:PRK10930 250 AFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGE 304
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 41-300 5.99e-77

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 237.82  E-value: 5.99e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVE 120
Cdd:COG0330  24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  121 DPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERR 199
Cdd:COG0330 103 NAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAERE 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  200 KRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAAALTqhngdaAASLTVA 279
Cdd:COG0330 183 REAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLF 245

                       250       260
                ....*....|....*....|.
gi 7305503  280 EQYVSAFSKLAKDSNTILLPS 300
Cdd:COG0330 246 YRSLEALEEVLSPNSKVIVLP 266
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 74-184 8.49e-62

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: 193.07  E-value: 8.49e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   74 RYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESL 153
Cdd:cd08829   1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 7305503  154 NASIVDAINQAADCWGIRCLRYEIKDIHVPP 184
Cdd:cd08829  81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 40-194 1.02e-45

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 153.59  E-value: 1.02e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503      40 FVPQQEAWVVERMGRFHRILEPGLNILIPVLDRIrYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:smart00244   5 VVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRV 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7305503     120 EDPEYAVT-QLAQTTMRSELGKLSLDKVFR-ERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQV 194
Cdd:smart00244  84 LDADYAVIeQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 68-230 2.37e-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: 153.05  E-value: 2.37e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   68 PVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVF 147
Cdd:cd08826   1 PFIDRMVRV-DLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  148 RERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEGkkqAQIL 227
Cdd:cd08826  80 SEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEA---AEIL 156


                ...
gi 7305503  228 ASE 230
Cdd:cd08826 157 AKS 159
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 41-237 7.97e-43

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: 148.15  E-value: 7.97e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVE 120
Cdd:cd13437   9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKIIQV-DMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  121 DPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRK 200
Cdd:cd13437  88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIG 167

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 7305503  201 RATVLESEGTRESAinvAEGKKQAQILASEAekAEQI 237
Cdd:cd13437 168 ESKIISAKADVESA---KLMREAADILDSKA--AMQI 199
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 41-209 4.80e-34

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: 123.59  E-value: 4.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503     41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIM--DPYKASYG 118
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLVQN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503    119 VEDPEYA---VTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVE 195
Cdd:pfam01145  82 VFGSDDLqelLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQT 161

                         170
                  ....*....|....
gi 7305503    196 AERRKRATVLESEG 209
Cdd:pfam01145 162 AEQEAEAEIARAEA 175
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 61-237 7.68e-33

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: 121.72  E-value: 7.68e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   61 PGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGK 140
Cdd:cd13435   7 PGVFFVLPCIDNYCKV-DLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGT 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  141 LSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESainvAEG 220
Cdd:cd13435  86 RNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKS----SRA 161

                       170
                ....*....|....*..
gi 7305503  221 KKQAQILASEAEKAEQI 237
Cdd:cd13435 162 LKEASDIISASPSALQL 178
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 79-183 3.37e-31

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: 113.83  E-value: 3.37e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   79 LKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIV 158
Cdd:cd13434   3 LRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQ 82

                        90       100
                ....*....|....*....|....*
gi 7305503  159 DAINQAADCWGIRCLRYEIKDIHVP 183
Cdd:cd13434  83 EILDEATDPWGIKVERVEIKDIILP 107
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 61-237 3.10e-29

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: 111.87  E-value: 3.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   61 PGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGK 140
Cdd:cd03403   7 PGLFFILPCIDSYRKV-DLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGT 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  141 LSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTResaiNVAEG 220
Cdd:cd03403  86 KNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQ----NASRA 161

                       170
                ....*....|....*..
gi 7305503  221 KKQAQILASEAEKAEQI 237
Cdd:cd03403 162 LKEAADVISESPAALQL 178
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 61-209 1.35e-28

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: 108.58  E-value: 1.35e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   61 PGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGK 140
Cdd:cd08828   3 PGLILVLPCTDTFIKV-DLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGT 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305503  141 LSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEG 209
Cdd:cd08828  82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEG 150
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 41-311 3.84e-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: 110.75  E-value: 3.84e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQSLKEIVINVPEQSAvTLDNVTLQIDGVLYLRIMDP--YKASYG 118
Cdd:cd03407   2 VSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDVRVETK-TKDNVFVTLVVSVQYRVVPEkvYDAFYK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  119 VEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAER 198
Cdd:cd03407  81 LTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  199 RKRATVLESEGTRESAINVAEGKKQAQILASEAeKAEQiNQAageasavlakakakaeAIRILAAALT--QHNGDAAASL 276
Cdd:cd03407 161 LREAAEEKAEAEKILQVKAAEAEAEAKRLQGVG-IAEQ-RKA----------------IVDGLRESIEdfQEAVPGVSSK 222

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 7305503  277 TVAE-----QYVSAFSKLAKDS--NTILLPSNPGDVTSMVAQ 311
Cdd:cd03407 223 EVMDlllitQYFDTLKEVGKSSksSTVFLPHGPGGVSDISAQ 264
Band_7_C pfam16200
C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal ...
 259-321 3.01e-25

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: 96.78  E-value: 3.01e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7305503    259 RILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTILLPSNPGDVTSMVAQAMGVYGALTK 321
Cdd:pfam16200   1 EKVAEAIKKPGGQEAVSLRVAEQYVEAFGKLAKESNTVILPANLGDVSSMVAQAMSIYKKVNK 63
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 41-243 3.82e-24

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: 99.51  E-value: 3.82e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   41 VPQQEAWVVERMGRFHRILEPGLNILIP-VLDRIRYVQS----LKEIVINVPEQSAV-TLD-NVtLQIDGVLYLRIMDPY 113
Cdd:cd03404  18 VDPGERGVVLRFGKYVRTVGPGLHWKLPfPIEVVEKVNVtqvrSVEIGFRVPEESLMlTGDeNI-VDVDFVVQYRISDPV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  114 KASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCW--GIRCLRYEIKDIHVPPRVKESM 190
Cdd:cd03404  97 AYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEILDRYdlGIEIVQVQLQDADPPEEVQDAF 176

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 7305503  191 QMQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 243
Cdd:cd03404 177 DDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGD 229
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 89-214 3.05e-22

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: 92.30  E-value: 3.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   89 QSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCW 168
Cdd:cd13775  13 EQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPW 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 7305503  169 GIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESA 214
Cdd:cd13775  93 GITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIA 138
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 41-202 1.32e-19

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: 86.05  E-value: 1.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   41 VPQQEAWVVERMGRFHRILEPGL--------NILIPVLDriryvqsLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDP 112
Cdd:cd13438   1 VPPGERGLLYRDGKLVRTLEPGRyafwkfgrKVQVELVD-------LREQLLEVSGQEILTADKVALRVNLVATYRVVDP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  113 YKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQM 192
Cdd:cd13438  74 VKAVETVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQ 153

                       170
                ....*....|
gi 7305503  193 QVEAERRKRA 202
Cdd:cd13438 154 VLEAEKRAQA 163
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 41-243 1.65e-19

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: 86.69  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503     41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQSlkEIVINVPEQSAV-TLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNV--TAVRNLRKQGLMlTGDENIVNVEMNVQYRITDPYKYLFSV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503    120 EDPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCW--GIRCLRYEIKDIHVPPRVKESMQMQVEA 196
Cdd:TIGR01933  82 ENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDVIIA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 7305503    197 ERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 243
Cdd:TIGR01933 162 REDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGD 208
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 38-211 9.70e-19

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: 83.78  E-value: 9.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   38 VLFVPQQEAWVVERMGRF--HRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKA 115
Cdd:cd08827   4 VKVVREYERAVIFRLGHLlqGRARGPGLFFYLPCLDVCHKV-DIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  116 SYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVE 195
Cdd:cd08827  83 LSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                       170
                ....*....|....*.
gi 7305503  196 AERRKRATVLESEGTR 211
Cdd:cd08827 163 AQRQAKVKVIAAEGEK 178
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 41-267 1.13e-18

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: 84.08  E-value: 1.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   41 VPQQEAWVVERMGR-FHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDP---YKAs 116
Cdd:cd03405   5 VDETEQAVVLQFGKpVRVITEPGLHFKLPFIQNVRKF-DKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPlrfYQS- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  117 ygVEDPEYAVTQLAQ---TTMRSELGKLSLDKVFR-ERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQM 192
Cdd:cd03405  83 --VGGEEGAESRLDDivdSALRNEIGKRTLAEVVSgGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESVYE 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7305503  193 QVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAE-KAEQI-NQAAGEAsavlakakakaeaIRILAAALTQ 267
Cdd:cd03405 161 RMRAERERIAAEYRAEGEEEAEKIRAEADRERTVILAEAYrEAEEIrGEGDAEA-------------ARIYAEAYGK 224
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 53-182 4.85e-13

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: 65.50  E-value: 4.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   53 GRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQT 132
Cdd:cd13436   1 GRLQKPRGPGIVLILPCIDNFTRV-DMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQT 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 7305503  133 TMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHV 182
Cdd:cd13436  80 SLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 83-184 1.20e-07

core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons, and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259797 [Multi-domain]  Cd Length: 110  Bit Score: 49.67  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   83 VINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKA-----SYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASI 157
Cdd:cd02106   4 FDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAV 83

                        90       100
                ....*....|....*....|....*..
gi 7305503  158 VDAINQAADCWGIRCLRYEIKDIHVPP 184
Cdd:cd02106  84 KEDLEEDLENFGVVISDVDITSIEPPD 110
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 41-243 3.14e-06

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: 47.12  E-value: 3.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   41 VPQQEAWVVERMGRFH--RILEPGLNILIPVLDR-IRYVQSLKEIVINVpeqSAVTLDNVTLQID-GVLYlRImDPYKA- 115
Cdd:cd03401   4 VDAGEVGVVFRRGKGVkdEVLGEGLHFKIPWIQVvIIYDVRTQPREITL---TVLSKDGQTVNIDlSVLY-RP-DPEKLp 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  116 ----SYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKEsmq 191
Cdd:cd03401  79 elyqNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEK--- 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7305503  192 mqveaerrkratvlesegtresAInvaEGKKQAQILASEA----EKAEQ-----INQAAGE 243
Cdd:cd03401 156 ----------------------AI---EAKQVAEQEAERAkfelEKAEQeaerkVIEAEGE 191
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 41-197 6.01e-06

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: 46.78  E-value: 6.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   41 VPQQEAWVVERMGRFHR-ILEPGLNILIPVLDRIRYvqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:cd03402  13 VQPNEAAVLTLFGRYRGtVRRPGLRWVNPFYRKKRV--SLRVRNFESEPLKVNDANGNPIEIAAVVVWRVVDTAKAVFDV 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  120 EDPEYAVTQLAQTTMR----------SELGKLSLDKvfrERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKES 189
Cdd:cd03402  91 DDYEEFVSIQSEAALRrvasrypydsFEDGEPSLRG---NSDEVSEELRRELQERLAVAGVEVIEARITHLAYAPEIAQA 167


                ....*...
gi 7305503  190 MQMQVEAE 197
Cdd:cd03402 168 MLQRQQAS 175
PRK10930 PRK10930
FtsH protease activity modulator HflK;
41-243 1.37e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 46.74  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503    41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIR--YVQSLKEIVinvpeQSAVTL---DNVTLQIDGVLYlRIMDPYKA 115
Cdd:PRK10930 100 IKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKpvNVEAVRELA-----ASGVMLtsdENVVRVEMNVQY-RVTDPEKY 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   116 SYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFREreslNASIVDAINQAADCWGIRCLRYEIKDIHV-------PPRVKE 188
Cdd:PRK10930 174 LFSVTSPDDSLRQATDSALRGVIGKYTMDRILTE----GRTVIRSDTQRELEETIRPYDMGITLLDVnfqaarpPEEVKA 249

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 7305503   189 SMQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 243
Cdd:PRK10930 250 AFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGE 304
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 67-180 2.13e-05

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: 44.03  E-value: 2.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   67 IPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDpykasygveDPEYAVT--------------QLAQT 132
Cdd:cd03399   3 IPFLQRVQRL-SLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGS---------DPEEIAAaaerflgksteeirELVKE 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 7305503  133 TM----RSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDI 180
Cdd:cd03399  73 TLeghlRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDI 124
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
41-264 2.58e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.55  E-value: 2.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVqSLKEIVINV-PEQSAVTLDNVTLQIDGVLYLRIMDPYKA---- 115
Cdd:COG2268  31 VPPNEALVITGRGGGYKVVTGGGAFVLPVLHRAERM-SLSTMTIEVeRTEGLITKDGIRVDVDAVFYVKVNSDPEDiana 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  116 --SYGVEDPEyAVTQLAQTT----MRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKES 189
Cdd:COG2268 110 aeRFLGRDPE-EIEELAEEKlegaLRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDA 188

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7305503  190 MQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQI--LASEAEKAE-QINQAAGEASAVLAKAKAKAEAIRILAAA 264
Cdd:COG2268 189 LGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEaeLEQEREIETaRIAEAEAELAKKKAEERREAETARAEAEA 266
PRK11029 PRK11029
protease modulator HflC;
39-232 3.03e-04

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 42.04  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503    39 LFVPQQ-EAWVVERMGRFHR-------ILEPGLNILIPVLDRIRYVQSLkeivINVPEQSA---VTLDNVTLQIDGVLYL 107
Cdd:PRK11029  20 VFVVKEgERGIVLRFGKVLRdddnkplVYAPGLHFKIPFIETVKMLDAR----IQTMDNQAdrfVTKEKKDLIVDSYIKW 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   108 RIMD---PYKASYG--VEDPEYAVTQLAQTTMRSELGKLSLDKVFRE---------RESLNASIV------------DAI 161
Cdd:PRK11029  96 RISDfsrYYLATGGgdISQAEVLLKRKFSDRLRSEIGRLDVKDIVTDsrgrltldvRDALNSGSAgtedevatpaadDAI 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503   162 NQAAD-------------------CWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRES--------- 213
Cdd:PRK11029 176 ASAAErveaetkgkvpvinpnsmaALGIEVVDVRIKQINLPTEVSDAIYNRMRAEREAVARRHRSQGQEEAeklratady 255

                        250       260
                 ....*....|....*....|.
gi 7305503   214 --AINVAEGKKQAQILASEAE 232
Cdd:PRK11029 256 evTRTLAEAERQGRIMRGEGD 276
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
185-345 8.87e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 37.93  E-value: 8.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  185 RVKESMQMQVEAERRKRATVLEsegtrESAINVAEGKKQAQILAS-EAEKAEQINQAAGEASAVLAKAKAKAEAIRILAA 263
Cdd:COG2268 274 NAEREVQRQLEIAEREREIELQ-----EKEAEREEAELEADVRKPaEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAE 348

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305503  264 ALtQHNGDAAASLTVAEQYVSAFSKLAK-----DSNTILLPSN-----PGDVTSMVAQAMGVYGALTKAPVPGTPDSLSS 333
Cdd:COG2268 349 AW-NKLGDAAILLMLIEKLPEIAEAAAKplekiDKITIIDGGNggngaGSAVAEALAPLLESLLEETGLDLPGLLKGLTG 427

                       170
                ....*....|..
gi 7305503  334 GSSRDVQGTDAS 345
Cdd:COG2268 428 AGAAAPAGEPAE 439
 
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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