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Conserved domains on  [gi|1934262584|ref|WP_195477713|]
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FtsH protease activity modulator HflK [Ruminococcus sp. D55t1_190419_H1]

Protein Classification

protease modulator HflK( domain architecture ID 10130454)

protease modulator HflK (high frequency of lysogenization K) is an inner membrane protein and is part of the HflCK complex that modulates FtsH protease

CATH:  3.30.479.30
Gene Symbol:  hflK
Gene Ontology:  GO:0098797|GO:0052547
PubMed:  9159109|8947034|10542406|17766116|20599668|21324212|16834335
SCOP:  4003722

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 30-285 1.10e-106

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: 311.75  E-value: 1.10e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQ-VQKVN-TTIQGFPIGYSmgnnavVENEGIMITSDYNFIDVDFFVE 107
Cdd:cd03404    16 YTVDPGERGVVLRFGKYVRTVGPGLHWKLPFPIEvVEKVNvTQVRSVEIGFR------VPEESLMLTGDENIVDVDFVVQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 108 YRISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMILNQMEEQDLGIQLVNITIQDSEPP 187
Cdd:cd03404    90 YRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEILDRYDLGIEIVQVQLQDADPP 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 188 tEEVMKAFKEVETAKQGKETALNNANKYRNEKLPEAQAQADQIIQDAEAQKQVRINEAEAEVARFNAMYEEYVKNPETTK 267
Cdd:cd03404   170 -EEVQDAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGDAARFLALLAEYRKAPEVTR 248

                         250
                  ....*....|....*...
gi 1934262584 268 MRMFYETMEDVLPGMKIV 285
Cdd:cd03404   249 ERLYLETMEEVLSNASKV 266
 
Name Accession Description Interval E-value
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 30-285 1.10e-106

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: 311.75  E-value: 1.10e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQ-VQKVN-TTIQGFPIGYSmgnnavVENEGIMITSDYNFIDVDFFVE 107
Cdd:cd03404    16 YTVDPGERGVVLRFGKYVRTVGPGLHWKLPFPIEvVEKVNvTQVRSVEIGFR------VPEESLMLTGDENIVDVDFVVQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 108 YRISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMILNQMEEQDLGIQLVNITIQDSEPP 187
Cdd:cd03404    90 YRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEILDRYDLGIEIVQVQLQDADPP 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 188 tEEVMKAFKEVETAKQGKETALNNANKYRNEKLPEAQAQADQIIQDAEAQKQVRINEAEAEVARFNAMYEEYVKNPETTK 267
Cdd:cd03404   170 -EEVQDAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGDAARFLALLAEYRKAPEVTR 248

                         250
                  ....*....|....*...
gi 1934262584 268 MRMFYETMEDVLPGMKIV 285
Cdd:cd03404   249 ERLYLETMEEVLSNASKV 266
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 30-291 2.43e-72

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 224.72  E-value: 2.43e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQVQKVNTTIQGFPIgysmgnnavveNEGIMITSDYNFIDVDFFVEYR 109
Cdd:COG0330    22 YIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDV-----------PPQEVLTKDNNIVDVDAVVQYR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 110 ISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMILNQMEEqdLGIQLVNITIQDSEPPtE 189
Cdd:COG0330    91 ITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDP--YGIEVVDVEIKDIDPP-E 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 190 EVMKAFKEVETAKQGKETALNNANKYRNEKLPEAQAQADQIIQDAEAQKQVRINEAEAEVARFNAMYEEYVKNPETTKMR 269
Cdd:COG0330   168 EVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYR 247

                         250       260
                  ....*....|....*....|....
gi 1934262584 270 MFyETMEDVLPGMK--IVIDNGSG 291
Cdd:COG0330   248 SL-EALEEVLSPNSkvIVLPPDGN 270
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 30-299 1.73e-69

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: 216.88  E-value: 1.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQVQKVN-TTIQGFpigysmgnnavvENEGIMITSDYNFIDVDFFVEY 108
Cdd:TIGR01933   2 YTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNvTAVRNL------------RKQGLMLTGDENIVNVEMNVQY 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 109 RISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMILNQMEEQDLGIQLVNITIQDSEPPt 188
Cdd:TIGR01933  70 RITDPYKYLFSVENPEDSLRQATDSALRGVIGDSTMDDILTEGRSQIREDTKERLNEIIDNYDLGITVTDVNFQSARPP- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 189 EEVMKAFKEVETAKQGKETALNNANKYRNEKLPEAQAQADQIIQDAEAQKQVRINEAEAEVARFNAMYEEYVKNPETTKM 268
Cdd:TIGR01933 149 EEVKEAFDDVIIAREDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGDVARFTKLLAEYKKAPDVTRE 228

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1934262584 269 RMFYETMEDVLPGMK--IVIDNGSGVEKILPLD 299
Cdd:TIGR01933 229 RLYLETMEKVLSNTRkvLLDDKKGNNLLYLPLD 261
PRK10930 PRK10930
FtsH protease activity modulator HflK;
30-299 4.37e-51

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 174.24  E-value: 4.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQVQKVNTtiqgfpigysmgnNAVVE--NEGIMITSDYNFIDVDFFVE 107
Cdd:PRK10930   98 YTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVNV-------------EAVRElaASGVMLTSDENVVRVEMNVQ 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 108 YRISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMILNQMEEQDLGIQLVNITIQDSEPP 187
Cdd:PRK10930  165 YRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEGRTVIRSDTQRELEETIRPYDMGITLLDVNFQAARPP 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 188 tEEVMKAFKEVETAKQGKETALNNANKYRNEKLPEAQAQADQIIQDAEAQKQVRINEAEAEVARFNAMYEEYVKNPETTK 267
Cdd:PRK10930  245 -EEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGEVARFAKLLPEYKAAPEITR 323

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1934262584 268 MRMFYETMEDVLPGM-KIVIDNGSGVEKILPLD 299
Cdd:PRK10930  324 ERLYIETMEKVLGHTrKVLVNDKGGNLMVLPLD 356
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-212 4.24e-25

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: 98.93  E-value: 4.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQVQKVNTTIQgfpigysmgnnaVVENEGI-MITSDYNFIDVDFFVEY 108
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTVDVRVQ------------TLEVSVQtVLTKDGVPVNVDVTVIY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 109 RI--SEPVKYLYT---SEQPEDILKNIAQSCIRTVIASYNVDEVLTTgKGEIQSKIKEMILNQMEEqdLGIQLVNITIQD 183
Cdd:pfam01145  69 RVnpDDPPKLVQNvfgSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEELAK--YGVEIIDVQITD 145

                         170       180
                  ....*....|....*....|....*....
gi 1934262584 184 SEPPtEEVMKAFKEVETAKQGKETALNNA 212
Cdd:pfam01145 146 IDPP-PEIAEAIEAKQTAEQEAEAEIARA 173
PHB smart00244
prohibitin homologues; prohibitin homologues
 30-199 7.28e-23

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 92.72  E-value: 7.28e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584   30 YQIQEQEQAVLTTFG-VPKAVTEtGLHFKVPFVQQVQKVNTTIQGFPIgysmgnnavveNEGIMITSDYNFIDVDFFVEY 108
Cdd:smart00244   4 KVVGEGERGVVERLGrVLRVLGP-GLHFLIPFIDDVKKVDLRAQTDDV-----------PPQETITKDNVKVSVDAVVYY 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  109 RISEPVKYLYTSEQPED-ILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMIlnQMEEQDLGIQLVNITIQDSEPP 187
Cdd:smart00244  72 RVLDPLRAVYRVLDADYaVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREEL--NEAAEAWGIKVEDVEIKDIRLP 149

                          170
                   ....*....|..
gi 1934262584  188 tEEVMKAFKEVE 199
Cdd:smart00244 150 -EEIKEAMEAQQ 160
 
Name Accession Description Interval E-value
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 30-285 1.10e-106

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: 311.75  E-value: 1.10e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQ-VQKVN-TTIQGFPIGYSmgnnavVENEGIMITSDYNFIDVDFFVE 107
Cdd:cd03404    16 YTVDPGERGVVLRFGKYVRTVGPGLHWKLPFPIEvVEKVNvTQVRSVEIGFR------VPEESLMLTGDENIVDVDFVVQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 108 YRISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMILNQMEEQDLGIQLVNITIQDSEPP 187
Cdd:cd03404    90 YRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEILDRYDLGIEIVQVQLQDADPP 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 188 tEEVMKAFKEVETAKQGKETALNNANKYRNEKLPEAQAQADQIIQDAEAQKQVRINEAEAEVARFNAMYEEYVKNPETTK 267
Cdd:cd03404   170 -EEVQDAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGDAARFLALLAEYRKAPEVTR 248

                         250
                  ....*....|....*...
gi 1934262584 268 MRMFYETMEDVLPGMKIV 285
Cdd:cd03404   249 ERLYLETMEEVLSNASKV 266
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 30-291 2.43e-72

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 224.72  E-value: 2.43e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQVQKVNTTIQGFPIgysmgnnavveNEGIMITSDYNFIDVDFFVEYR 109
Cdd:COG0330    22 YIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDV-----------PPQEVLTKDNNIVDVDAVVQYR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 110 ISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMILNQMEEqdLGIQLVNITIQDSEPPtE 189
Cdd:COG0330    91 ITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDP--YGIEVVDVEIKDIDPP-E 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 190 EVMKAFKEVETAKQGKETALNNANKYRNEKLPEAQAQADQIIQDAEAQKQVRINEAEAEVARFNAMYEEYVKNPETTKMR 269
Cdd:COG0330   168 EVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYR 247

                         250       260
                  ....*....|....*....|....
gi 1934262584 270 MFyETMEDVLPGMK--IVIDNGSG 291
Cdd:COG0330   248 SL-EALEEVLSPNSkvIVLPPDGN 270
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 30-299 1.73e-69

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: 216.88  E-value: 1.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQVQKVN-TTIQGFpigysmgnnavvENEGIMITSDYNFIDVDFFVEY 108
Cdd:TIGR01933   2 YTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNvTAVRNL------------RKQGLMLTGDENIVNVEMNVQY 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 109 RISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMILNQMEEQDLGIQLVNITIQDSEPPt 188
Cdd:TIGR01933  70 RITDPYKYLFSVENPEDSLRQATDSALRGVIGDSTMDDILTEGRSQIREDTKERLNEIIDNYDLGITVTDVNFQSARPP- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 189 EEVMKAFKEVETAKQGKETALNNANKYRNEKLPEAQAQADQIIQDAEAQKQVRINEAEAEVARFNAMYEEYVKNPETTKM 268
Cdd:TIGR01933 149 EEVKEAFDDVIIAREDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGDVARFTKLLAEYKKAPDVTRE 228

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1934262584 269 RMFYETMEDVLPGMK--IVIDNGSGVEKILPLD 299
Cdd:TIGR01933 229 RLYLETMEKVLSNTRkvLLDDKKGNNLLYLPLD 261
PRK10930 PRK10930
FtsH protease activity modulator HflK;
30-299 4.37e-51

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 174.24  E-value: 4.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQVQKVNTtiqgfpigysmgnNAVVE--NEGIMITSDYNFIDVDFFVE 107
Cdd:PRK10930   98 YTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVNV-------------EAVRElaASGVMLTSDENVVRVEMNVQ 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 108 YRISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMILNQMEEQDLGIQLVNITIQDSEPP 187
Cdd:PRK10930  165 YRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEGRTVIRSDTQRELEETIRPYDMGITLLDVNFQAARPP 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 188 tEEVMKAFKEVETAKQGKETALNNANKYRNEKLPEAQAQADQIIQDAEAQKQVRINEAEAEVARFNAMYEEYVKNPETTK 267
Cdd:PRK10930  245 -EEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGEVARFAKLLPEYKAAPEITR 323

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1934262584 268 MRMFYETMEDVLPGM-KIVIDNGSGVEKILPLD 299
Cdd:PRK10930  324 ERLYIETMEKVLGHTrKVLVNDKGGNLMVLPLD 356
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 30-276 9.36e-32

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: 118.74  E-value: 9.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAV-TETGLHFKVPFVQQVQKVNTTIQGFpigysmgNNAVVEnegiMITSDYNFIDVDFFVEY 108
Cdd:cd03405     3 FIVDETEQAVVLQFGKPVRViTEPGLHFKLPFIQNVRKFDKRILTL-------DGPPEE----VLTKDKKRLIVDSYARW 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 109 RISEPVKYlYTS----EQPEDILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMILNQMEEqdLGIQLVNITIQDS 184
Cdd:cd03405    72 RITDPLRF-YQSvggeEGAESRLDDIVDSALRNEIGKRTLAEVVSGGRDELMEEILEQANEEAKE--YGIEVVDVRIKRI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 185 EPPtEEV-------MKAFKEVETAK---QGKEtalnNANKYRNeklpEAQAQADQIIQDAEAQKQVRINEAEAEVAR-FN 253
Cdd:cd03405   149 DLP-EEVsesvyerMRAERERIAAEyraEGEE----EAEKIRA----EADRERTVILAEAYREAEEIRGEGDAEAARiYA 219

                         250       260
                  ....*....|....*....|...
gi 1934262584 254 AMYEeyvKNPETTKmrmFYETME 276
Cdd:cd03405   220 EAYG---KDPEFYS---FYRSLE 236
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-212 4.24e-25

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: 98.93  E-value: 4.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQVQKVNTTIQgfpigysmgnnaVVENEGI-MITSDYNFIDVDFFVEY 108
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTVDVRVQ------------TLEVSVQtVLTKDGVPVNVDVTVIY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 109 RI--SEPVKYLYT---SEQPEDILKNIAQSCIRTVIASYNVDEVLTTgKGEIQSKIKEMILNQMEEqdLGIQLVNITIQD 183
Cdd:pfam01145  69 RVnpDDPPKLVQNvfgSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEELAK--YGVEIIDVQITD 145

                         170       180
                  ....*....|....*....|....*....
gi 1934262584 184 SEPPtEEVMKAFKEVETAKQGKETALNNA 212
Cdd:pfam01145 146 IDPP-PEIAEAIEAKQTAEQEAEAEIARA 173
PHB smart00244
prohibitin homologues; prohibitin homologues
 30-199 7.28e-23

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 92.72  E-value: 7.28e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584   30 YQIQEQEQAVLTTFG-VPKAVTEtGLHFKVPFVQQVQKVNTTIQGFPIgysmgnnavveNEGIMITSDYNFIDVDFFVEY 108
Cdd:smart00244   4 KVVGEGERGVVERLGrVLRVLGP-GLHFLIPFIDDVKKVDLRAQTDDV-----------PPQETITKDNVKVSVDAVVYY 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  109 RISEPVKYLYTSEQPED-ILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMIlnQMEEQDLGIQLVNITIQDSEPP 187
Cdd:smart00244  72 RVLDPLRAVYRVLDADYaVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREEL--NEAAEAWGIKVEDVEIKDIRLP 149

                          170
                   ....*....|..
gi 1934262584  188 tEEVMKAFKEVE 199
Cdd:smart00244 150 -EEIKEAMEAQQ 160
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 30-248 1.61e-21

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: 89.88  E-value: 1.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFG--VPKAVTETGLHFKVPFVQQVQKVNTTIQGFPIGYSMGnnavvenegimiTSDYNFIDVDFFVE 107
Cdd:cd03401     2 YTVDAGEVGVVFRRGkgVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVL------------SKDGQTVNIDLSVL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 108 YRIS-EPVKYLYTS---EQPEDILKNIAQSCIRTVIASYNVDEVLTTgKGEIQSKIKEMILNQMEEQdlGIQLVNITIQD 183
Cdd:cd03401    70 YRPDpEKLPELYQNlgpDYEERVLPPIVREVLKAVVAQYTAEELYTK-REEVSAEIREALTERLAPF--GIIVDDVLITN 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934262584 184 SEPPtEEVMKAFKEVETAKQgketalnnankyrneklpEAQaQADQIIQDAEAQKQVRINEAEAE 248
Cdd:cd03401   147 IDFP-DEYEKAIEAKQVAEQ------------------EAE-RAKFELEKAEQEAERKVIEAEGE 191
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 32-248 4.34e-13

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: 68.00  E-value: 4.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  32 IQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQV-QKVNTTIQGFpigysmgnNAVVENEgimiTSDYNFIDVDFFVEYRI 110
Cdd:cd03407     2 VSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVaGRVSLRVQQL--------DVRVETK----TKDNVFVTLVVSVQYRV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 111 SEPVKYL--YTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTgKGEIQSKIKEMILNQMEEqdLGIQLVNITIQDSEPPt 188
Cdd:cd03407    70 VPEKVYDafYKLTNPEQQIQSYVFDVVRASVPKLTLDEVFES-KDEIAKAVKEELAKVMSE--YGYEIVKTLVTDIEPD- 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 189 EEVMKAFKEVetakqgketalnNANKYRNEKlpeaqaqadqIIQDAEAQKQVRINEAEAE 248
Cdd:cd03407   146 ASVKAAMNEI------------NAAQRLREA----------AEEKAEAEKILQVKAAEAE 183
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 30-208 1.23e-12

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: 66.10  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFGVPKAVTETGLHFKVPFVQQVQKVNTTIQgfpigysmgnnaVVE-NEGIMITSDYNFIDVDFFVEY 108
Cdd:cd13437     7 KQVKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKIIQVDMKTQ------------VIDlPRQSVMTKDNVSVTIDSVVYY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 109 RISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTgKGEIQSKIKEMILNQMEeqDLGIQLVNITIQD----- 183
Cdd:cd13437    75 RIIDPYKAIYRIDNVKQALIERTQTTLRSVIGERTLQDLLEK-REEIADEIEEIVEEVAK--EWGVYVESILIKDivlsk 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1934262584 184 ------SEPPTEE------VMKAFKEVETAKQGKETA 208
Cdd:cd13437   152 dlqqslSSAAKAKrigeskIISAKADVESAKLMREAA 188
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 30-286 3.57e-12

HflC 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. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]


Pssm-ID: 273883 [Multi-domain]  Cd Length: 317  Bit Score: 65.96  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQAVLTTFG-------VPKAVTETGLHFKVPFVQQVQKVNTTIQgfpigySMGNNAvveneGIMITSDYNFIDV 102
Cdd:TIGR01932  21 FIIKEGERGIITRFGkilkdnnHHVLVYEPGLHFKIPFIEHVKIFDAKIQ------TMDGRP-----DRIPTKEKKDIII 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 103 DFFVEYRISEPVKYlYTS------EQPEDILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMILNQMEE------- 169
Cdd:TIGR01932  90 DTYIRWRIEDFKKY-YLStgggtiSAAEVLIKRKIDDRLRSEIGVLGLKEIVRSSNDQLDTLVSKLALNRGGKinkiamt 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 170 --------------------QDLGIQLVNITIQDSEPPTEEVMKAFKEVETAKQGKetalnnANKYRN---EKLPEAQAQ 226
Cdd:TIGR01932 169 itkgreilareisqiansqlKDIGIEVVDVRIKKINYSDELSESIYNRMRSEREQI------ARMHRSqgeEKAEEILGK 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934262584 227 AD----QIIQDAEAQKQVRINEAEAEVARFNAmyEEYVKNPETTKMRMFYETMEDVLPGMKIVI 286
Cdd:TIGR01932 243 AEyevrKILSEAYRTARIIKGEGDAEAAKIYS--DAYGKDPEFYSFWRSLEAYEKSFKDNQDEK 304
PRK11029 PRK11029
protease modulator HflC;
49-254 2.47e-09

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 57.44  E-value: 2.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  49 VTETGLHFKVPFVQQVQKVNTTIQgfpigySMGNNAvveneGIMITSDYNFIDVDFFVEYRISEPVKY-LYTS----EQP 123
Cdd:PRK11029   47 VYAPGLHFKIPFIETVKMLDARIQ------TMDNQA-----DRFVTKEKKDLIVDSYIKWRISDFSRYyLATGggdiSQA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 124 EDILKNIAQSCIRTVIASYNVDEVLTTGKGEIQSKIKEMiLN-------------------------QMEEQD------- 171
Cdd:PRK11029  116 EVLLKRKFSDRLRSEIGRLDVKDIVTDSRGRLTLDVRDA-LNsgsagtedevatpaaddaiasaaerVEAETKgkvpvin 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 172 ------LGIQLVNITIQDSEPPTE------EVMKAFKEVETAK---QGKETAlnnankyrnEKLpeaQAQADQIIQD--A 234
Cdd:PRK11029  195 pnsmaaLGIEVVDVRIKQINLPTEvsdaiyNRMRAEREAVARRhrsQGQEEA---------EKL---RATADYEVTRtlA 262

                         250       260
                  ....*....|....*....|..
gi 1934262584 235 EAQKQVRI--NEAEAEVARFNA 254
Cdd:PRK11029  263 EAERQGRImrGEGDAEAAKLFA 284
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 93-187 3.79e-09

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: 53.63  E-value: 3.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  93 ITSDYNFIDVDFFVEYRISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTgkgeiQSKIKEMILNQMEE--Q 170
Cdd:cd08829    19 ITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSS-----REEINAKLLEALDEatD 93

                          90
                  ....*....|....*..
gi 1934262584 171 DLGIQLVNITIQDSEPP 187
Cdd:cd08829    94 PWGVKVTRVEIKDITPP 110
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 102-218 1.04e-07

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: 51.77  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 102 VDFFVEYRISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLtTGKGEIQSKIKEMILNQMEEqdLGIQLVNITI 181
Cdd:cd13438    62 VNLVATYRVVDPVKAVETVDDPEEQLYLALQLALREAVAARTLDELL-EDREDLSEFLLAAVKEAAAE--LGVEVLSVGV 138

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1934262584 182 QD-SEPPteEVMKAFKEVETAKQGKETALNNAnkyRNE 218
Cdd:cd13438   139 KDiILPG--EIREILNQVLEAEKRAQANLIRA---REE 171
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 92-187 1.72e-07

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: 48.73  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  92 MITSDYNFIDVDFFVEYRISEPVKYLYTSEQPEDILKNIAQSCIRTVIASYNVDEVLtTGKGEIQSKIKEMILNQMEEqd 171
Cdd:cd13434    15 ILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELL-SEREEISQQLQEILDEATDP-- 91

                          90
                  ....*....|....*.
gi 1934262584 172 LGIQLVNITIQDSEPP 187
Cdd:cd13434    92 WGIKVERVEIKDIILP 107
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 53-241 4.49e-07

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: 49.69  E-value: 4.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  53 GLHFKVPFVQQVQKVNTTIQGFPigysmgnnaVVENEgiMITSDYNFIDVDFFVEYRISEPVKYLYTSEQPEDILKNIAQ 132
Cdd:cd13435     8 GVFFVLPCIDNYCKVDLRTVSFD---------VPPQE--VLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 133 SCIRTVIASYNVDEVLTtgKGEIQSKIKEMILNQMEEQdLGIQLVNITIQDSEPPT--EEVMKAfkEVETAKQGKETALN 210
Cdd:cd13435    77 TTLRNVLGTRNLSELLT--ERETISHSMQVTLDEATDP-WGVQVERVEIKDVSLPDslQRAMAA--EAEAAREARAKVIA 151

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1934262584 211 NANKYRNEKlpeAQAQADQIIQDAEAQKQVR 241
Cdd:cd13435   152 AEGEMKSSR---ALKEASDIISASPSALQLR 179
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 59-193 3.68e-06

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: 46.35  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  59 PFVQQVQKVNTTIQGFPigysmgnnavVENEGImITSDYNFIDVDFFVEYRISEPVKYLYTSEQPEDILKNIAQSCIRTV 138
Cdd:cd08826     1 PFIDRMVRVDLRTVTLD----------VPPQEV-ITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSV 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1934262584 139 IASYNVDEVLTTgKGEIQSKIKEMILNQMEEqdLGIQLVNITIQDSEPPteEVMK 193
Cdd:cd08826    70 VGQVELDELLSE-REEINKRIQEIIDEQTEP--WGIKVTAVEIKDVDLP--ESMQ 119
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
30-250 9.33e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 43.71  E-value: 9.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  30 YQIQEQEQA-VLTTFGVPKAVTETGLHFKVPFVQQVQKVNTTIQGFPIgySMGNNAvvenegimITSDYNFIDVD--FFV 106
Cdd:COG2268    28 YRKVPPNEAlVITGRGGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEV--ERTEGL--------ITKDGIRVDVDavFYV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 107 eyRISEPVKYLYT---------SEQPEDILKNIAQSCIRTVIASYNVDEvLTTGKGEIQSKIKEMILNQMEEqdLGIQLV 177
Cdd:COG2268    98 --KVNSDPEDIANaaerflgrdPEEIEELAEEKLEGALRAVAAQMTVEE-LNEDREKFAEKVQEVAGTDLAK--NGLELE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 178 NITIQDSE-----------PPTEEVMKAfKEVETAKQGKETALNNANKYRNEKLPE------------AQAQADQIIQDA 234
Cdd:COG2268   173 SVAITDLEdennyldalgrRKIAEIIRD-ARIAEAEAERETEIAIAQANREAEEAEleqereietariAEAEAELAKKKA 251

                         250
                  ....*....|....*.
gi 1934262584 235 EAQKQVRINEAEAEVA 250
Cdd:COG2268   252 EERREAETARAEAEAA 267
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 90-187 7.48e-04

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: 38.50  E-value: 7.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  90 GIMITSDYNFIDVDFFVEYRISEPVKY-----LYTSEQPEDILKNIAQSCIRTVIASYNVDEVLtTGKGEIQSKIKEmIL 164
Cdd:cd02106    10 EPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQII-SGRDEIAKAVKE-DL 87

                          90       100
                  ....*....|....*....|...
gi 1934262584 165 NQMEEqDLGIQLVNITIQDSEPP 187
Cdd:cd02106    88 EEDLE-NFGVVISDVDITSIEPP 109
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 196-251 1.46e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.19  E-value: 1.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 196 KEVETAKQGKETALNNANKYRnEKLPEAQAQADQIIQDA----EAQKQVRINEAEAEVAR 251
Cdd:cd06503    37 ESLEEAEKAKEEAEELLAEYE-EKLAEARAEAQEIIEEArkeaEKIKEEILAEAKEEAER 95
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 32-205 2.04e-03

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: 38.72  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584  32 IQEQEQAVLTTFG--VPKAVTETGLHFKVPFVQQVQKVNTTIQGFPIGYSMgnnavvenegiMITSDYNFIDVDFFVEYR 109
Cdd:cd08827     7 VREYERAVIFRLGhlLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHM-----------IVTKDLVCTEIDAICYYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 110 IsEPVKYLYTS-EQPEDILKNIAQSCIRTVIASYNVDEVLTTGKgEIQSKIKeMILNQMEEQdLGIQLVNITIQDSEPPt 188
Cdd:cd08827    76 I-ENASVCLSSfASISDAMQALVQTTVKRLLAHRAFTDILLERK-SIAQEIK-VALDSGTCR-WGIKVERAEIKDVNLP- 150

                         170
                  ....*....|....*...
gi 1934262584 189 EEVMKAFK-EVETAKQGK 205
Cdd:cd08827   151 PELQHSFAvEAEAQRQAK 168
SPFH_like_u1 cd03408
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 108-202 4.18e-03

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: 259806  Cd Length: 217  Bit Score: 37.92  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 108 YRISEPVKYL---------YTSEQPEDILKNIAQSCIRTVIASYNVDEVLTTGKG---EIQSKIKEMIlnQMEEQDLGIQ 175
Cdd:cd03408   110 FRVTDPALFLtevvgtqgtFTTDEIEEQLRSEIVQALKDAIAELSISGLDLALEAnldELSAALKEKL--APEFEKYGLE 187

                          90       100
                  ....*....|....*....|....*..
gi 1934262584 176 LVNITIQDSEPPtEEVMKAFKEVETAK 202
Cdd:cd03408   188 LTSFGIESISLP-EEVQKRIDKRASMA 213
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 189-251 5.38e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 37.24  E-value: 5.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934262584 189 EEVMKAFKEVETAKQGKETALNNANKyrneKLPEAQAQADQIIQDAEAQKQVRINE----AEAEVAR 251
Cdd:PRK07352   53 EAILQALKEAEERLRQAAQALAEAQQ----KLAQAQQEAERIRADAKARAEAIRAEiekqAIEDMAR 115
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 189-251 5.55e-03

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 36.52  E-value: 5.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934262584 189 EEVMKAFKEVETAKQGKETALNNANKyrneKLPEAQAQADQIIQDAEAQKQVRINEAEAEVAR 251
Cdd:pfam00430  33 ELIADEIAEAEERRKDAAAALAEAEQ----QLKEARAEAQEIIENAKKRAEKLKEEIVAAAEA 91
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 196-251 8.81e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 36.30  E-value: 8.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934262584 196 KEVETAKQGKETALNNANKYRnEKLPEAQAQADQIIQDA----EAQKQVRINEAEAEVAR 251
Cdd:COG0711    38 DGLAEAERAKEEAEAALAEYE-EKLAEARAEAAEIIAEArkeaEAIAEEAKAEAEAEAER 96
 
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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