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Conserved domains on  [gi|12963591|ref|NP_075720|]
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stomatin-like protein 2, mitochondrial isoform c [Mus musculus]

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 ...
 41-300 7.49e-75

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 232.42  E-value: 7.49e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  41 VPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVE 120
Cdd:COG0330  24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 121 DPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERR 199
Cdd:COG0330 103 NAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAERE 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 200 KRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAGALTqhngdaAASLTVA 279
Cdd:COG0330 183 REAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLF 245

                       250       260
                ....*....|....*....|.
gi 12963591 280 EQYVSAFSKLAKDSNTVLLPS 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 7.49e-75

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 232.42  E-value: 7.49e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  41 VPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVE 120
Cdd:COG0330  24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 121 DPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERR 199
Cdd:COG0330 103 NAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAERE 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 200 KRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAGALTqhngdaAASLTVA 279
Cdd:COG0330 183 REAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLF 245

                       250       260
                ....*....|....*....|.
gi 12963591 280 EQYVSAFSKLAKDSNTVLLPS 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 1.54e-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: 192.30  E-value: 1.54e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  74 RYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESL 153
Cdd:cd08829   1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 12963591 154 NANIVDAINQAADCWGIRCLRYEIKDIHVPP 184
Cdd:cd08829  81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 40-194 7.54e-45

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 151.27  E-value: 7.54e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591     40 FVPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIrYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:smart00244   5 VVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRV 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12963591    120 EDPEYAVT-QLAQTTMRSELGKLSLDKVFR-ERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQV 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 7.26e-33

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: 120.50  E-value: 7.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591    41 VPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIM--DPYKASYG 118
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLVQN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591   119 VEDPEYA---VTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVE 195
Cdd:pfam01145  82 VFGSDDLqelLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQT 161

                         170
                  ....*....|....
gi 12963591   196 AERRKRATVLESEG 209
Cdd:pfam01145 162 AEQEAEAEIARAEA 175
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 38-243 2.62e-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: 86.30  E-value: 2.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591    38 ILFVPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIRYVQSlkEIVINVPEQSAV-TLDNVTLQIDGVLYLRIMDPYKAS 116
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNV--TAVRNLRKQGLMlTGDENIVNVEMNVQYRITDPYKYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591   117 YGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNANIVDAINQAADCW--GIRCLRYEIKDIHVPPRVKESMQMQ 193
Cdd:TIGR01933  79 FSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDV 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 12963591   194 VEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 243
Cdd:TIGR01933 159 IIAREDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGD 208
PRK10930 PRK10930
FtsH protease activity modulator HflK;
41-243 2.76e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 45.59  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591   41 VPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIR--YVQSLKEIVinvpeQSAVTL---DNVTLQIDGVLYlRIMDPYKA 115
Cdd:PRK10930 100 IKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKpvNVEAVRELA-----ASGVMLtsdENVVRVEMNVQY-RVTDPEKY 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  116 SYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNANIVDAINQAADCW--GIRCLRYEIKDIHVPPRVKESMQM 192
Cdd:PRK10930 174 LFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYdmGITLLDVNFQAARPPEEVKAAFDD 253

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 12963591  193 QVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 243
Cdd:PRK10930 254 AIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGE 304
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 41-300 7.49e-75

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 232.42  E-value: 7.49e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  41 VPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVE 120
Cdd:COG0330  24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 121 DPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERR 199
Cdd:COG0330 103 NAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAERE 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 200 KRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAGALTqhngdaAASLTVA 279
Cdd:COG0330 183 REAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLF 245

                       250       260
                ....*....|....*....|.
gi 12963591 280 EQYVSAFSKLAKDSNTVLLPS 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 1.54e-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: 192.30  E-value: 1.54e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  74 RYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESL 153
Cdd:cd08829   1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 12963591 154 NANIVDAINQAADCWGIRCLRYEIKDIHVPP 184
Cdd:cd08829  81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 68-230 2.06e-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: 153.44  E-value: 2.06e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  68 PVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVF 147
Cdd:cd08826   1 PFIDRMVRV-DLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 148 RERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEGkkqAQIL 227
Cdd:cd08826  80 SEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEA---AEIL 156


                ...
gi 12963591 228 ASE 230
Cdd:cd08826 157 AKS 159
PHB smart00244
prohibitin homologues; prohibitin homologues
 40-194 7.54e-45

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 151.27  E-value: 7.54e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591     40 FVPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIrYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:smart00244   5 VVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRV 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12963591    120 EDPEYAVT-QLAQTTMRSELGKLSLDKVFR-ERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQV 194
Cdd:smart00244  84 LDADYAVIeQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 41-237 6.34e-42

Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in some eukaryotes and viruses. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This diverse subgroup of the SLPs remains largely uncharacterized.


Pssm-ID: 259815 [Multi-domain]  Cd Length: 222  Bit Score: 145.83  E-value: 6.34e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  41 VPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVE 120
Cdd:cd13437   9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKIIQV-DMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 121 DPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRK 200
Cdd:cd13437  88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIG 167

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 12963591 201 RATVLESEGTRESAinvAEGKKQAQILASEAekAEQI 237
Cdd:cd13437 168 ESKIISAKADVESA---KLMREAADILDSKA--AMQI 199
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 61-237 5.06e-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: 5.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  61 PGLNVLIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGK 140
Cdd:cd13435   7 PGVFFVLPCIDNYCKV-DLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGT 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 141 LSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESainvAEG 220
Cdd:cd13435  86 RNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKS----SRA 161

                       170
                ....*....|....*..
gi 12963591 221 KKQAQILASEAEKAEQI 237
Cdd:cd13435 162 LKEASDIISASPSALQL 178
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 41-209 7.26e-33

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: 120.50  E-value: 7.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591    41 VPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIM--DPYKASYG 118
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLVQN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591   119 VEDPEYA---VTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVE 195
Cdd:pfam01145  82 VFGSDDLqelLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQT 161

                         170
                  ....*....|....
gi 12963591   196 AERRKRATVLESEG 209
Cdd:pfam01145 162 AEQEAEAEIARAEA 175
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 79-183 6.58e-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: 113.06  E-value: 6.58e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  79 LKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIV 158
Cdd:cd13434   3 LRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQ 82

                        90       100
                ....*....|....*....|....*
gi 12963591 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 6.07e-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: 111.10  E-value: 6.07e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  61 PGLNVLIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGK 140
Cdd:cd03403   7 PGLFFILPCIDSYRKV-DLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGT 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 141 LSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTResaiNVAEG 220
Cdd:cd03403  86 KNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQ----NASRA 161

                       170
                ....*....|....*..
gi 12963591 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 4.24e-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: 107.04  E-value: 4.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  61 PGLNVLIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGK 140
Cdd:cd08828   3 PGLILVLPCTDTFIKV-DLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGT 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12963591 141 LSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEG 209
Cdd:cd08828  82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEG 150
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 41-311 1.13e-26

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: 106.52  E-value: 1.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  41 VPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIRYVQSLKEIVINVPEQSAvTLDNVTLQIDGVLYLRIMDP--YKASYG 118
Cdd:cd03407   2 VSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDVRVETK-TKDNVFVTLVVSVQYRVVPEkvYDAFYK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 119 VEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAER 198
Cdd:cd03407  81 LTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 199 RKRATVLESEGTRESAINVAEGKKQAQILASEAeKAEQiNQAageasavlakakakaeairILAG------ALTQHNGDA 272
Cdd:cd03407 161 LREAAEEKAEAEKILQVKAAEAEAEAKRLQGVG-IAEQ-RKA-------------------IVDGlresieDFQEAVPGV 219

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 12963591 273 AAS----LTVAEQYVSAFSKLAKDS--NTVLLPSNPSDVTSMVAQ 311
Cdd:cd03407 220 SSKevmdLLLITQYFDTLKEVGKSSksSTVFLPHGPGGVSDISAQ 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 1.86e-24

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: 94.47  E-value: 1.86e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12963591   259 RILAGALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTVLLPSNPSDVTSMVAQAMGVYGALTK 321
Cdd:pfam16200   1 EKVAEAIKKPGGQEAVSLRVAEQYVEAFGKLAKESNTVILPANLGDVSSMVAQAMSIYKKVNK 63
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 41-243 7.40e-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: 98.74  E-value: 7.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  41 VPQQEAWVVERMGRFHRILEPGLNVLIP-VLDRIRYVQS----LKEIVINVPEQSAV-TLDNVTLQIDGVLYLRIMDPYK 114
Cdd:cd03404  18 VDPGERGVVLRFGKYVRTVGPGLHWKLPfPIEVVEKVNVtqvrSVEIGFRVPEESLMlTGDENIVDVDFVVQYRISDPVA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 115 ASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNANIVDAINQAADCW--GIRCLRYEIKDIHVPPRVKESMQ 191
Cdd:cd03404  98 YLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEILDRYdlGIEIVQVQLQDADPPEEVQDAFD 177

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 12963591 192 MQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 243
Cdd:cd03404 178 DVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGD 229
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 89-214 3.63e-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: 3.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  89 QSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCW 168
Cdd:cd13775  13 EQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPW 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 12963591 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 9.59e-20

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: 86.44  E-value: 9.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  41 VPQQEAWVVERMGRFHRILEPGLNV-LIPVLDRIRYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:cd13438   1 VPPGERGLLYRDGKLVRTLEPGRYAfWKFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 120 EDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERR 199
Cdd:cd13438  81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKR 160


                ...
gi 12963591 200 KRA 202
Cdd:cd13438 161 AQA 163
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 38-243 2.62e-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: 86.30  E-value: 2.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591    38 ILFVPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIRYVQSlkEIVINVPEQSAV-TLDNVTLQIDGVLYLRIMDPYKAS 116
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNV--TAVRNLRKQGLMlTGDENIVNVEMNVQYRITDPYKYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591   117 YGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNANIVDAINQAADCW--GIRCLRYEIKDIHVPPRVKESMQMQ 193
Cdd:TIGR01933  79 FSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDV 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 12963591   194 VEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 243
Cdd:TIGR01933 159 IIAREDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGD 208
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 41-211 1.94e-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: 83.01  E-value: 1.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  41 VPQQEAWVVERMGRF--HRILEPGLNVLIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYG 118
Cdd:cd08827   7 VREYERAVIFRLGHLlqGRARGPGLFFYLPCLDVCHKV-DIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVCLSS 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 119 VEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAER 198
Cdd:cd08827  86 FASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAEAQR 165

                       170
                ....*....|...
gi 12963591 199 RKRATVLESEGTR 211
Cdd:cd08827 166 QAKVKVIAAEGEK 178
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 41-267 3.83e-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: 82.54  E-value: 3.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  41 VPQQEAWVVERMGR-FHRILEPGLNVLIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDP---YKAs 116
Cdd:cd03405   5 VDETEQAVVLQFGKpVRVITEPGLHFKLPFIQNVRKF-DKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPlrfYQS- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 117 ygVEDPEYAVTQLAQ---TTMRSELGKLSLDKVFR-ERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQM 192
Cdd:cd03405  83 --VGGEEGAESRLDDivdSALRNEIGKRTLAEVVSgGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESVYE 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12963591 193 QVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAE-KAEQI-NQAAGEAsavlakakakaeaIRILAGALTQ 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 8.00e-14

Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in animals. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. The family contains human SLP-1, which has been found to be expressed in the brain, and Caenorhabditis elegans UNC-24, which is a lipid raft-associated protein required for normal locomotion. It may mediate the correct localization of UNC-1. Mutations in the unc-24 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259814 [Multi-domain]  Cd Length: 131  Bit Score: 67.42  E-value: 8.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  53 GRFHRILEPGLNVLIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQT 132
Cdd:cd13436   1 GRLQKPRGPGIVLILPCIDNFTRV-DMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQT 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 12963591 133 TMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHV 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 5.78e-08

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: 50.44  E-value: 5.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  83 VINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKA-----SYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANI 157
Cdd:cd02106   4 FDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAV 83

                        90       100
                ....*....|....*....|....*..
gi 12963591 158 VDAINQAADCWGIRCLRYEIKDIHVPP 184
Cdd:cd02106  84 KEDLEEDLENFGVVISDVDITSIEPPD 110
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 41-197 5.40e-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: 5.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  41 VPQQEAWVVERMGRFHR-ILEPGLNVLIPVLDRIRYvqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:cd03402  13 VQPNEAAVLTLFGRYRGtVRRPGLRWVNPFYRKKRV--SLRVRNFESEPLKVNDANGNPIEIAAVVVWRVVDTAKAVFDV 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 120 EDPEYAVTQLAQTTMR----------SELGKLSLDKvfrERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKES 189
Cdd:cd03402  91 DDYEEFVSIQSEAALRrvasrypydsFEDGEPSLRG---NSDEVSEELRRELQERLAVAGVEVIEARITHLAYAPEIAQA 167


                ....*...
gi 12963591 190 MQMQVEAE 197
Cdd:cd03402 168 MLQRQQAS 175
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 41-243 1.48e-05

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: 45.20  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  41 VPQQEAWVVERMGRFH--RILEPGLNVLIPVLDR-IRYVQSLKEIVINVpeqSAVTLDNVTLQID-GVLYlRImDPYKA- 115
Cdd:cd03401   4 VDAGEVGVVFRRGKGVkdEVLGEGLHFKIPWIQVvIIYDVRTQPREITL---TVLSKDGQTVNIDlSVLY-RP-DPEKLp 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 116 ----SYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKEsmq 191
Cdd:cd03401  79 elyqNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEK--- 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12963591 192 mqveaerrkratvlesegtresAInvaEGKKQAQILASEA----EKAEQ-----INQAAGE 243
Cdd:cd03401 156 ----------------------AI---EAKQVAEQEAERAkfelEKAEQeaerkVIEAEGE 191
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 67-180 2.28e-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: 43.65  E-value: 2.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  67 IPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIM-DPYKASYGVE----DPEYAVTQLAQTTM----RSE 137
Cdd:cd03399   3 IPFLQRVQRL-SLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGsDPEEIAAAAErflgKSTEEIRELVKETLeghlRAI 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 12963591 138 LGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDI 180
Cdd:cd03399  82 VGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDI 124
PRK10930 PRK10930
FtsH protease activity modulator HflK;
41-243 2.76e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 45.59  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591   41 VPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIR--YVQSLKEIVinvpeQSAVTL---DNVTLQIDGVLYlRIMDPYKA 115
Cdd:PRK10930 100 IKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKpvNVEAVRELA-----ASGVMLtsdENVVRVEMNVQY-RVTDPEKY 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  116 SYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNANIVDAINQAADCW--GIRCLRYEIKDIHVPPRVKESMQM 192
Cdd:PRK10930 174 LFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYdmGITLLDVNFQAARPPEEVKAAFDD 253

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 12963591  193 QVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 243
Cdd:PRK10930 254 AIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGE 304
PRK11029 PRK11029
protease modulator HflC;
39-232 7.94e-04

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 40.88  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591   39 LFVPQQ-EAWVVERMGRFHR-------ILEPGLNVLIPVLDRIRYVQSLkeivINVPEQSA---VTLDNVTLQIDGVLYL 107
Cdd:PRK11029  20 VFVVKEgERGIVLRFGKVLRdddnkplVYAPGLHFKIPFIETVKMLDAR----IQTMDNQAdrfVTKEKKDLIVDSYIKW 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  108 RIMD---PYKASYG--VEDPEYAVTQLAQTTMRSELGKLSLDKVFRE---------RESLNANIV------------DAI 161
Cdd:PRK11029  96 RISDfsrYYLATGGgdISQAEVLLKRKFSDRLRSEIGRLDVKDIVTDsrgrltldvRDALNSGSAgtedevatpaadDAI 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  162 NQAAD-------------------CWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRES--------- 213
Cdd:PRK11029 176 ASAAErveaetkgkvpvinpnsmaALGIEVVDVRIKQINLPTEVSDAIYNRMRAEREAVARRHRSQGQEEAeklratady 255

                        250       260
                 ....*....|....*....|.
gi 12963591  214 --AINVAEGKKQAQILASEAE 232
Cdd:PRK11029 256 evTRTLAEAERQGRIMRGEGD 276
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
41-262 9.05e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.01  E-value: 9.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591  41 VPQQEAWVVERMGRFHRILEPGLNVLIPVLDRIRYVqSLKEIVINV-PEQSAVTLDNVTLQIDGVLYLRIMDPYKA---- 115
Cdd:COG2268  31 VPPNEALVITGRGGGYKVVTGGGAFVLPVLHRAERM-SLSTMTIEVeRTEGLITKDGIRVDVDAVFYVKVNSDPEDiana 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12963591 116 --SYGVEDPEyAVTQLAQTT----MRSELGKLSLDKVFRERESLNANIVDAINQAADCWGIRCLRYEIKDIHVPPRVKES 189
Cdd:COG2268 110 aeRFLGRDPE-EIEELAEEKlegaLRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDA 188

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12963591 190 MQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQI--LASEAEKAE-QINQAAGEASAVLAKAKAKAEAIRILA 262
Cdd:COG2268 189 LGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEaeLEQEREIETaRIAEAEAELAKKKAEERREAETARAEA 264
 
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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