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Conserved domains on  [gi|559098408|ref|NP_001273961|]
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stomatin-like protein 2, mitochondrial isoform c [Homo sapiens]

Protein Classification

SPFH domain-containing protein( domain architecture ID 11417211)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein similar to Escherichia coli protein QmcA that has been identified as a multi-copy suppressor of an FtsH/HtpX protease double disruption mutant and may play a role in the quality control of integral membrane proteins

Gene Ontology:  GO:0016020
PubMed:  17766116|10542406

Graphical summary

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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 ...
 2-249 1.78e-70

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 219.71  E-value: 1.78e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   2 GRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQT 81
Cdd:COG0330   36 GKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAES 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  82 TMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTR 160
Cdd:COG0330  115 ALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYR 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408 161 ESAINVAEGKKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAAALTqhngdaAASLTVAEQYVSAFSKLAK 240
Cdd:COG0330  195 EAAIIRAEGEAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLFYRSLEALEEVLS 257


                 ....*....
gi 559098408 241 DSNTILLPS 249
Cdd:COG0330  258 PNSKVIVLP 266
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 2-249 1.78e-70

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 219.71  E-value: 1.78e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   2 GRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQT 81
Cdd:COG0330   36 GKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAES 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  82 TMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTR 160
Cdd:COG0330  115 ALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYR 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408 161 ESAINVAEGKKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAAALTqhngdaAASLTVAEQYVSAFSKLAK 240
Cdd:COG0330  195 EAAIIRAEGEAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLFYRSLEALEEVLS 257


                 ....*....
gi 559098408 241 DSNTILLPS 249
Cdd:COG0330  258 PNSKVIVLP 266
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 23-133 2.12e-61

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: 190.38  E-value: 2.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  23 RYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESL 102
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 559098408 103 NASIVDAINQAADCWGIRCLRYEIKDIHVPP 133
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 1-143 3.41e-39

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 135.10  E-value: 3.41e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408     1 MGRFHRILEPGLNILIPVLDRIrYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVT-QLA 79
Cdd:smart00244  17 LGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRVLDADYAVIeQLA 95

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559098408    80 QTTMRSELGKLSLDKVFR-ERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQV 143
Cdd:smart00244  96 QTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 2-158 2.95e-29

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: 109.72  E-value: 2.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408    2 GRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIM--DPYKASYGVEDPEYA---VT 76
Cdd:pfam01145  15 GKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLVQNVFGSDDLqelLR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   77 QLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLES 156
Cdd:pfam01145  94 RVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQTAEQEAEAEIARA 173


                  ..
gi 559098408  157 EG 158
Cdd:pfam01145 174 EA 175
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 2-192 6.24e-17

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: 78.60  E-value: 6.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408    2 GRFHRILEPGLNILIPVLDRIRYVQSlkEIVINVPEQSAV-TLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQ 80
Cdd:TIGR01933  16 GKYHRTVDPGLNWKPPFIEEVYPVNV--TAVRNLRKQGLMlTGDENIVNVEMNVQYRITDPYKYLFSVENPEDSLRQATD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   81 TTMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCW--GIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESE 157
Cdd:TIGR01933  94 SALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDVIIAREDEERYINEAE 173

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 559098408  158 GTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 192
Cdd:TIGR01933 174 AYANEVVPKARGDAQRIIEEARGYKERRINRAKGD 208
PRK10930 PRK10930
FtsH protease activity modulator HflK;
1-192 7.75e-04

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 40.58  E-value: 7.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   1 MGRFHRILEPGLNILIPVLDRIR--YVQSLKEIVinvpeQSAVTL---DNVTLQIDGVLYlRIMDPYKASYGVEDPEYAV 75
Cdd:PRK10930 111 FGKFSHLVEPGLNWKPTFIDEVKpvNVEAVRELA-----ASGVMLtsdENVVRVEMNVQY-RVTDPEKYLFSVTSPDDSL 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  76 TQLAQTTMRSELGKLSLDKVFREreslNASIVDAINQAADCWGIRCLRYEIKDIHV-------PPRVKESMQMQVEAERR 148
Cdd:PRK10930 185 RQATDSALRGVIGKYTMDRILTE----GRTVIRSDTQRELEETIRPYDMGITLLDVnfqaarpPEEVKAAFDDAIAAREN 260

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 559098408 149 KRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 192
Cdd:PRK10930 261 EQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGE 304
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 2-249 1.78e-70

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 219.71  E-value: 1.78e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   2 GRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQT 81
Cdd:COG0330   36 GKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAES 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  82 TMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTR 160
Cdd:COG0330  115 ALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYR 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408 161 ESAINVAEGKKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAAALTqhngdaAASLTVAEQYVSAFSKLAK 240
Cdd:COG0330  195 EAAIIRAEGEAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLFYRSLEALEEVLS 257


                 ....*....
gi 559098408 241 DSNTILLPS 249
Cdd:COG0330  258 PNSKVIVLP 266
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 23-133 2.12e-61

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: 190.38  E-value: 2.12e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  23 RYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESL 102
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 559098408 103 NASIVDAINQAADCWGIRCLRYEIKDIHVPP 133
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 17-179 8.04e-46

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: 8.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  17 PVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVF 96
Cdd:cd08826    1 PFIDRMVRV-DLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  97 RERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEGkkqAQIL 176
Cdd:cd08826   80 SEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEA---AEIL 156


                 ...
gi 559098408 177 ASE 179
Cdd:cd08826  157 AKS 159
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 2-186 1.02e-39

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: 138.52  E-value: 1.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   2 GRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQT 81
Cdd:cd13437   21 GKFYKTVDPGLHKVNPCTEKIIQV-DMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRIDNVKQALIERTQT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  82 TMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRE 161
Cdd:cd13437  100 TLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIGESKIISAKADVE 179

                        170       180
                 ....*....|....*....|....*
gi 559098408 162 SAinvAEGKKQAQILASEAekAEQI 186
Cdd:cd13437  180 SA---KLMREAADILDSKA--AMQI 199
PHB smart00244
prohibitin homologues; prohibitin homologues
 1-143 3.41e-39

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 135.10  E-value: 3.41e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408     1 MGRFHRILEPGLNILIPVLDRIrYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVT-QLA 79
Cdd:smart00244  17 LGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRVLDADYAVIeQLA 95

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 559098408    80 QTTMRSELGKLSLDKVFR-ERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQV 143
Cdd:smart00244  96 QTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 10-186 1.73e-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: 122.11  E-value: 1.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  10 PGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGK 89
Cdd:cd13435    7 PGVFFVLPCIDNYCKV-DLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  90 LSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESainvAEG 169
Cdd:cd13435   86 RNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKS----SRA 161

                        170
                 ....*....|....*..
gi 559098408 170 KKQAQILASEAEKAEQI 186
Cdd:cd13435  162 LKEASDIISASPSALQL 178
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 28-132 3.60e-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: 112.67  E-value: 3.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  28 LKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIV 107
Cdd:cd13434    3 LRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQ 82

                         90       100
                 ....*....|....*....|....*
gi 559098408 108 DAINQAADCWGIRCLRYEIKDIHVP 132
Cdd:cd13434   83 EILDEATDPWGIKVERVEIKDIILP 107
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 10-186 8.99e-30

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: 8.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  10 PGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGK 89
Cdd:cd03403    7 PGLFFILPCIDSYRKV-DLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  90 LSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTResaiNVAEG 169
Cdd:cd03403   86 KNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQ----NASRA 161

                        170
                 ....*....|....*..
gi 559098408 170 KKQAQILASEAEKAEQI 186
Cdd:cd03403  162 LKEAADVISESPAALQL 178
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 2-158 2.95e-29

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: 109.72  E-value: 2.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408    2 GRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIM--DPYKASYGVEDPEYA---VT 76
Cdd:pfam01145  15 GKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLVQNVFGSDDLqelLR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   77 QLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLES 156
Cdd:pfam01145  94 RVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQTAEQEAEAEIARA 173


                  ..
gi 559098408  157 EG 158
Cdd:pfam01145 174 EA 175
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 10-158 4.85e-29

Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this slipin subgroup remain uncharacterized, except for Caenorhabditis elegans UNC-1. Mutations in the unc-1 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259810 [Multi-domain]  Cd Length: 154  Bit Score: 108.58  E-value: 4.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  10 PGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGK 89
Cdd:cd08828    3 PGLILVLPCTDTFIKV-DLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGT 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 559098408  90 LSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEG 158
Cdd:cd08828   82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEG 150
Band_7_C pfam16200
C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal ...
 208-270 1.87e-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: 96.01  E-value: 1.87e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559098408  208 RILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTILLPSNPGDVTSMVAQAMGVYGALTK 270
Cdd:pfam16200   1 EKVAEAIKKPGGQEAVSLRVAEQYVEAFGKLAKESNTVILPANLGDVSSMVAQAMSIYKKVNK 63
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 38-163 1.46e-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: 91.92  E-value: 1.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  38 QSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCW 117
Cdd:cd13775   13 EQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPW 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 559098408 118 GIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESA 163
Cdd:cd13775   93 GITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIA 138
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 2-260 1.52e-22

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: 94.19  E-value: 1.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   2 GRFHRILEPGLNILIPVLDRIRYVQSLKEIVINVPEQSAvTLDNVTLQIDGVLYLRIMDP--YKASYGVEDPEYAVTQLA 79
Cdd:cd03407   14 GKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDVRVETK-TKDNVFVTLVVSVQYRVVPEkvYDAFYKLTNPEQQIQSYV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  80 QTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGT 159
Cdd:cd03407   93 FDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRLREAAEEKAEAE 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408 160 RESAINVAEGKKQAQILASEAeKAEQiNQAageasavlakakakaeAIRILAAALT--QHNGDAAASLTVAE-----QYV 232
Cdd:cd03407  173 KILQVKAAEAEAEAKRLQGVG-IAEQ-RKA----------------IVDGLRESIEdfQEAVPGVSSKEVMDlllitQYF 234

                        250       260       270
                 ....*....|....*....|....*....|
gi 559098408 233 SAFSKLAKDS--NTILLPSNPGDVTSMVAQ 260
Cdd:cd03407  235 DTLKEVGKSSksSTVFLPHGPGGVSDISAQ 264
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 2-192 1.02e-20

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: 89.11  E-value: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   2 GRFHRILEPGLNILIP-VLDRIRYVQS----LKEIVINVPEQSAV-TLD-NVtLQIDGVLYLRIMDPYKASYGVEDPEYA 74
Cdd:cd03404   30 GKYVRTVGPGLHWKLPfPIEVVEKVNVtqvrSVEIGFRVPEESLMlTGDeNI-VDVDFVVQYRISDPVAYLFNVRDPEET 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  75 VTQLAQTTMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCW--GIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRA 151
Cdd:cd03404  109 LRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEILDRYdlGIEIVQVQLQDADPPEEVQDAFDDVNAARQDKER 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 559098408 152 TVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 192
Cdd:cd03404  189 LINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGD 229
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 2-151 1.91e-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: 84.51  E-value: 1.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   2 GRFHRILEPGL--------NILIPVLDriryvqsLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEY 73
Cdd:cd13438   13 GKLVRTLEPGRyafwkfgrKVQVELVD-------LREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETVDDPEE 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559098408  74 AVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRA 151
Cdd:cd13438   86 QLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKRAQA 163
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 10-160 6.38e-18

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: 80.70  E-value: 6.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  10 PGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGK 89
Cdd:cd08827   29 PGLFFYLPCLDVCHKV-DIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVCLSSFASISDAMQALVQTTVKRLLAH 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 559098408  90 LSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTR 160
Cdd:cd08827  108 RAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAEAQRQAKVKVIAAEGEK 178
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 7-216 2.41e-17

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: 79.45  E-value: 2.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   7 ILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDP---YKAsygVEDPEYAVTQLAQ--- 80
Cdd:cd03405   23 ITEPGLHFKLPFIQNVRKF-DKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPlrfYQS---VGGEEGAESRLDDivd 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  81 TTMRSELGKLSLDKVFR-ERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGT 159
Cdd:cd03405   99 SALRNEIGKRTLAEVVSgGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESVYERMRAERERIAAEYRAEGE 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 559098408 160 RESAINVAEGKKQAQILASEAE-KAEQI-NQAAGEAsavlakakakaeaIRILAAALTQ 216
Cdd:cd03405  179 EEAEKIRAEADRERTVILAEAYrEAEEIrGEGDAEA-------------ARIYAEAYGK 224
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 2-192 6.24e-17

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: 78.60  E-value: 6.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408    2 GRFHRILEPGLNILIPVLDRIRYVQSlkEIVINVPEQSAV-TLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQ 80
Cdd:TIGR01933  16 GKYHRTVDPGLNWKPPFIEEVYPVNV--TAVRNLRKQGLMlTGDENIVNVEMNVQYRITDPYKYLFSVENPEDSLRQATD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   81 TTMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCW--GIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESE 157
Cdd:TIGR01933  94 SALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDVIIAREDEERYINEAE 173

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 559098408  158 GTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 192
Cdd:TIGR01933 174 AYANEVVPKARGDAQRIIEEARGYKERRINRAKGD 208
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 2-131 2.47e-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: 65.88  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   2 GRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQT 81
Cdd:cd13436    1 GRLQKPRGPGIVLILPCIDNFTRV-DMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQT 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 559098408  82 TMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHV 131
Cdd:cd13436   80 SLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 32-133 2.22e-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: 48.51  E-value: 2.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  32 VINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKA-----SYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASI 106
Cdd:cd02106    4 FDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAV 83

                         90       100
                 ....*....|....*....|....*..
gi 559098408 107 VDAINQAADCWGIRCLRYEIKDIHVPP 133
Cdd:cd02106   84 KEDLEEDLENFGVVISDVDITSIEPPD 110
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 16-129 2.99e-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: 43.26  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  16 IPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIM-DPYKASYGVE----DPEYAVTQLAQTTM----RSE 86
Cdd:cd03399    3 IPFLQRVQRL-SLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGsDPEEIAAAAErflgKSTEEIRELVKETLeghlRAI 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 559098408  87 LGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDI 129
Cdd:cd03399   82 VGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDI 124
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 6-192 1.31e-04

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: 42.12  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   6 RILEPGLNILIPVLDR-IRYVQSLKEIVINVpeqSAVTLDNVTLQID-GVLYlRImDPYKA-----SYGVEDPEYAVTQL 78
Cdd:cd03401   22 EVLGEGLHFKIPWIQVvIIYDVRTQPREITL---TVLSKDGQTVNIDlSVLY-RP-DPEKLpelyqNLGPDYEERVLPPI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  79 AQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKEsmqmqveaerrkratvleseg 158
Cdd:cd03401   97 VREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEK--------------------- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 559098408 159 tresAInvaEGKKQAQILASEA----EKAEQ-----INQAAGE 192
Cdd:cd03401  156 ----AI---EAKQVAEQEAERAkfelEKAEQeaerkVIEAEGE 191
PRK10930 PRK10930
FtsH protease activity modulator HflK;
1-192 7.75e-04

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 40.58  E-value: 7.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   1 MGRFHRILEPGLNILIPVLDRIR--YVQSLKEIVinvpeQSAVTL---DNVTLQIDGVLYlRIMDPYKASYGVEDPEYAV 75
Cdd:PRK10930 111 FGKFSHLVEPGLNWKPTFIDEVKpvNVEAVRELA-----ASGVMLtsdENVVRVEMNVQY-RVTDPEKYLFSVTSPDDSL 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  76 TQLAQTTMRSELGKLSLDKVFREreslNASIVDAINQAADCWGIRCLRYEIKDIHV-------PPRVKESMQMQVEAERR 148
Cdd:PRK10930 185 RQATDSALRGVIGKYTMDRILTE----GRTVIRSDTQRELEETIRPYDMGITLLDVnfqaarpPEEVKAAFDDAIAAREN 260

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 559098408 149 KRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 192
Cdd:PRK10930 261 EQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGE 304
PRK11029 PRK11029
protease modulator HflC;
7-181 1.74e-03

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 39.34  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408   7 ILEPGLNILIPVLDRIRYVQSLkeivINVPEQSA---VTLDNVTLQIDGVLYLRIMD---PYKASYG--VEDPEYAVTQL 78
Cdd:PRK11029  47 VYAPGLHFKIPFIETVKMLDAR----IQTMDNQAdrfVTKEKKDLIVDSYIKWRISDfsrYYLATGGgdISQAEVLLKRK 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  79 AQTTMRSELGKLSLDKVFRE---------RESLNASIV------------DAINQAAD-------------------CWG 118
Cdd:PRK11029 123 FSDRLRSEIGRLDVKDIVTDsrgrltldvRDALNSGSAgtedevatpaadDAIASAAErveaetkgkvpvinpnsmaALG 202

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 559098408 119 IRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRES-----------AINVAEGKKQAQILASEAE 181
Cdd:PRK11029 203 IEVVDVRIKQINLPTEVSDAIYNRMRAEREAVARRHRSQGQEEAeklratadyevTRTLAEAERQGRIMRGEGD 276
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
14-213 2.59e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.09  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  14 ILIPVLDRIRYVqSLKEIVINV-PEQSAVTLDNVTLQIDGVLYLRIMDPYKA------SYGVEDPEyAVTQLAQTT---- 82
Cdd:COG2268   55 FVLPVLHRAERM-SLSTMTIEVeRTEGLITKDGIRVDVDAVFYVKVNSDPEDianaaeRFLGRDPE-EIEELAEEKlega 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408  83 MRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRES 162
Cdd:COG2268  133 LRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERET 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 559098408 163 AINVAEGKKQAQI--LASEAEKAE-QINQAAGEASAVLAKAKAKAEAIRILAAA 213
Cdd:COG2268  213 EIAIAQANREAEEaeLEQEREIETaRIAEAEAELAKKKAEERREAETARAEAEA 266
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
134-294 8.94e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 37.54  E-value: 8.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408 134 RVKESMQMQVEAERRKRATVLEsegtrESAINVAEGKKQAQILAS-EAEKAEQINQAAGEASAVLAKAKAKAEAIRILAA 212
Cdd:COG2268  274 NAEREVQRQLEIAEREREIELQ-----EKEAEREEAELEADVRKPaEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAE 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098408 213 ALtQHNGDAAASLTVAEQYVSAFSKLAK-----DSNTILLPSN-----PGDVTSMVAQAMGVYGALTKAPVPGTPDSLSS 282
Cdd:COG2268  349 AW-NKLGDAAILLMLIEKLPEIAEAAAKplekiDKITIIDGGNggngaGSAVAEALAPLLESLLEETGLDLPGLLKGLTG 427

                        170
                 ....*....|..
gi 559098408 283 GSSRDVQGTDAS 294
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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