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Conserved domains on  [gi|506420374|ref|WP_015940093|]
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FtsH protease activity modulator HflK [Glaesserella parasuis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10930 super family cl35974
FtsH protease activity modulator HflK;
1-379 4.17e-160

FtsH protease activity modulator HflK;


The actual alignment was detected with superfamily member PRK10930:

Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 456.98  E-value: 4.17e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374   1 MSWNESGNQ---QDPWGkpgqkkpeQEQPSGQ-EKEPNKQSNEPQPPDLEEVFNSLLRKM---GGGKGNGSNQNN----- 68
Cdd:PRK10930   1 MAWNQPGNNgqdRDPWG--------SSKPGGNsGGNGNKGGRDQGPPDLDDIFRKLSKKLgglGGGKGTGSGGGSssqgp 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  69 RPPVSaGKFLPVLLGLGLVVWGASGFYTVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVTPVNIERVLELRTNGSMLT 148
Cdd:PRK10930  73 RPQLG-GRVVGIAAAAVVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 149 QDENMVLVEMTVQYRIEDPAKYLFSVTKPDDSLKQATDSALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKNYDMGL 228
Cdd:PRK10930 152 SDENVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEGRTVIRSDTQRELEETIRPYDMGI 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 229 LITDVNFQYARPPEEVKAAFDDAIKAQEDEQRLIREAEAYARGQEPIARGQAQRILEQANAYKEQVVLNAQGEVQRFTQL 308
Cdd:PRK10930 232 TLLDVNFQAARPPEEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGEVARFAKL 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506420374 309 LPEYKAAPEVTRDRLYIQTMEKVMKNTPKLMVDsSNGNNLTVLPIDKLMAKPTVNEAVKTPSSQPVIQQQP 379
Cdd:PRK10930 312 LPEYKAAPEITRERLYIETMEKVLGHTRKVLVN-DKGGNLMVLPLDQMLKGGNAPAAKSDNGASNLLRLPP 381
 
Name Accession Description Interval E-value
PRK10930 PRK10930
FtsH protease activity modulator HflK;
1-379 4.17e-160

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 456.98  E-value: 4.17e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374   1 MSWNESGNQ---QDPWGkpgqkkpeQEQPSGQ-EKEPNKQSNEPQPPDLEEVFNSLLRKM---GGGKGNGSNQNN----- 68
Cdd:PRK10930   1 MAWNQPGNNgqdRDPWG--------SSKPGGNsGGNGNKGGRDQGPPDLDDIFRKLSKKLgglGGGKGTGSGGGSssqgp 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  69 RPPVSaGKFLPVLLGLGLVVWGASGFYTVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVTPVNIERVLELRTNGSMLT 148
Cdd:PRK10930  73 RPQLG-GRVVGIAAAAVVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 149 QDENMVLVEMTVQYRIEDPAKYLFSVTKPDDSLKQATDSALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKNYDMGL 228
Cdd:PRK10930 152 SDENVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEGRTVIRSDTQRELEETIRPYDMGI 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 229 LITDVNFQYARPPEEVKAAFDDAIKAQEDEQRLIREAEAYARGQEPIARGQAQRILEQANAYKEQVVLNAQGEVQRFTQL 308
Cdd:PRK10930 232 TLLDVNFQAARPPEEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGEVARFAKL 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506420374 309 LPEYKAAPEVTRDRLYIQTMEKVMKNTPKLMVDsSNGNNLTVLPIDKLMAKPTVNEAVKTPSSQPVIQQQP 379
Cdd:PRK10930 312 LPEYKAAPEITRERLYIETMEKVLGHTRKVLVN-DKGGNLMVLPLDQMLKGGNAPAAKSDNGASNLLRLPP 381
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 94-354 9.97e-147

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: 416.80  E-value: 9.97e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374   94 FYTVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVTPVNIERVLELRTNGSMLTQDENMVLVEMTVQYRIEDPAKYLFS 173
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPYKYLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  174 VTKPDDSLKQATDSALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKNYDMGLLITDVNFQYARPPEEVKAAFDDAIK 253
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDILTEGRSQIREDTKERLNEIIDNYDLGITVTDVNFQSARPPEEVKEAFDDVII 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  254 AQEDEQRLIREAEAYARGQEPIARGQAQRILEQANAYKEQVVLNAQGEVQRFTQLLPEYKAAPEVTRDRLYIQTMEKVMK 333
Cdd:TIGR01933 161 AREDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGDVARFTKLLAEYKKAPDVTRERLYLETMEKVLS 240

                         250       260
                  ....*....|....*....|.
gi 506420374  334 NTPKLMVDSSNGNNLTVLPID 354
Cdd:TIGR01933 241 NTRKVLLDDKKGNNLLYLPLD 261
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 91-338 4.09e-124

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: 359.52  E-value: 4.09e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  91 ASGFYTVQEAERGVVTRFGKLHEIVLPGLNWKPTF-IDNVTPVNIERV------LELRTNGSMLTQDENMVLVEMTVQYR 163
Cdd:cd03404   12 LSGFYTVDPGERGVVLRFGKYVRTVGPGLHWKLPFpIEVVEKVNVTQVrsveigFRVPEESLMLTGDENIVDVDFVVQYR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 164 IEDPAKYLFSVTKPDDSLKQATDSALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKNYDMGLLITDVNFQYARPPEE 243
Cdd:cd03404   92 ISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEILDRYDLGIEIVQVQLQDADPPEE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 244 VKAAFDDAIKAQEDEQRLIREAEAYARGQEPIARGQAQRILEQANAYKEQVVLNAQGEVQRFTQLLPEYKAAPEVTRDRL 323
Cdd:cd03404  172 VQDAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGDAARFLALLAEYRKAPEVTRERL 251

                        250
                 ....*....|....*
gi 506420374 324 YIQTMEKVMKNTPKL 338
Cdd:cd03404  252 YLETMEEVLSNASKV 266
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 91-348 4.13e-96

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 288.66  E-value: 4.13e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  91 ASGFYTVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVTPVNI-ERVLELrTNGSMLTQDENMVLVEMTVQYRIEDPAK 169
Cdd:COG0330   18 FSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKVDVrEQVLDV-PPQEVLTKDNNIVDVDAVVQYRITDPAK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 170 YLFSVTKPDDSLKQATDSALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKNYdmGLLITDVNFQYARPPEEVKAAFD 249
Cdd:COG0330   97 FLYNVENAEEALRQLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDPY--GIEVVDVEIKDIDPPEEVQDAME 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 250 DAIKAQEDEQRLIREAEAYARGQEPIARGQAQRILEQANAYKEQVVLNAQGEVQRFTQLLPEYKAAPEVTRDRlYIQTME 329
Cdd:COG0330  175 DRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYR-SLEALE 253

                        250
                 ....*....|....*....
gi 506420374 330 KVMKNTPKLMVDSSNGNNL 348
Cdd:COG0330  254 EVLSPNSKVIVLPPDGNGF 272
PHB smart00244
prohibitin homologues; prohibitin homologues
 92-250 2.31e-38

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 135.48  E-value: 2.31e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374    92 SGFYTVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVTPVNIERVLELRTNGSMLTQDENMVLVEMTVQYRIEDPAKYL 171
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374   172 FSVTKPDD-SLKQATDSALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKNYdmGLLITDVNFQYARPPEEVKAAFDD 250
Cdd:smart00244  81 YRVLDADYaVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAEAW--GIKVEDVEIKDIRLPEEIKEAMEA 158
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 95-269 3.30e-29

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 111.64  E-value: 3.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374   95 YTVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVTPVNIeRVLELR-TNGSMLTQDENMVLVEMTVQYRI--EDPAKYL 171
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTVDV-RVQTLEvSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  172 FSVTKPDD---SLKQATDSALRYVIGHMTMDDILTTgRAIVREKTWNALRDIIKNYdmGLLITDVNFQYARPPEEVKAAF 248
Cdd:pfam01145  80 QNVFGSDDlqeLLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEELAKY--GVEIIDVQITDIDPPPEIAEAI 156

                         170       180
                  ....*....|....*....|.
gi 506420374  249 DDAIKAQEDEQRLIREAEAYA 269
Cdd:pfam01145 157 EAKQTAEQEAEAEIARAEAEA 177
 
Name Accession Description Interval E-value
PRK10930 PRK10930
FtsH protease activity modulator HflK;
1-379 4.17e-160

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 456.98  E-value: 4.17e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374   1 MSWNESGNQ---QDPWGkpgqkkpeQEQPSGQ-EKEPNKQSNEPQPPDLEEVFNSLLRKM---GGGKGNGSNQNN----- 68
Cdd:PRK10930   1 MAWNQPGNNgqdRDPWG--------SSKPGGNsGGNGNKGGRDQGPPDLDDIFRKLSKKLgglGGGKGTGSGGGSssqgp 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  69 RPPVSaGKFLPVLLGLGLVVWGASGFYTVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVTPVNIERVLELRTNGSMLT 148
Cdd:PRK10930  73 RPQLG-GRVVGIAAAAVVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 149 QDENMVLVEMTVQYRIEDPAKYLFSVTKPDDSLKQATDSALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKNYDMGL 228
Cdd:PRK10930 152 SDENVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEGRTVIRSDTQRELEETIRPYDMGI 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 229 LITDVNFQYARPPEEVKAAFDDAIKAQEDEQRLIREAEAYARGQEPIARGQAQRILEQANAYKEQVVLNAQGEVQRFTQL 308
Cdd:PRK10930 232 TLLDVNFQAARPPEEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGEVARFAKL 311

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506420374 309 LPEYKAAPEVTRDRLYIQTMEKVMKNTPKLMVDsSNGNNLTVLPIDKLMAKPTVNEAVKTPSSQPVIQQQP 379
Cdd:PRK10930 312 LPEYKAAPEITRERLYIETMEKVLGHTRKVLVN-DKGGNLMVLPLDQMLKGGNAPAAKSDNGASNLLRLPP 381
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 94-354 9.97e-147

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: 416.80  E-value: 9.97e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374   94 FYTVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVTPVNIERVLELRTNGSMLTQDENMVLVEMTVQYRIEDPAKYLFS 173
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPYKYLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  174 VTKPDDSLKQATDSALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKNYDMGLLITDVNFQYARPPEEVKAAFDDAIK 253
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDILTEGRSQIREDTKERLNEIIDNYDLGITVTDVNFQSARPPEEVKEAFDDVII 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  254 AQEDEQRLIREAEAYARGQEPIARGQAQRILEQANAYKEQVVLNAQGEVQRFTQLLPEYKAAPEVTRDRLYIQTMEKVMK 333
Cdd:TIGR01933 161 AREDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGDVARFTKLLAEYKKAPDVTRERLYLETMEKVLS 240

                         250       260
                  ....*....|....*....|.
gi 506420374  334 NTPKLMVDSSNGNNLTVLPID 354
Cdd:TIGR01933 241 NTRKVLLDDKKGNNLLYLPLD 261
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 91-338 4.09e-124

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: 359.52  E-value: 4.09e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  91 ASGFYTVQEAERGVVTRFGKLHEIVLPGLNWKPTF-IDNVTPVNIERV------LELRTNGSMLTQDENMVLVEMTVQYR 163
Cdd:cd03404   12 LSGFYTVDPGERGVVLRFGKYVRTVGPGLHWKLPFpIEVVEKVNVTQVrsveigFRVPEESLMLTGDENIVDVDFVVQYR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 164 IEDPAKYLFSVTKPDDSLKQATDSALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKNYDMGLLITDVNFQYARPPEE 243
Cdd:cd03404   92 ISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEILDRYDLGIEIVQVQLQDADPPEE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 244 VKAAFDDAIKAQEDEQRLIREAEAYARGQEPIARGQAQRILEQANAYKEQVVLNAQGEVQRFTQLLPEYKAAPEVTRDRL 323
Cdd:cd03404  172 VQDAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGDAARFLALLAEYRKAPEVTRERL 251

                        250
                 ....*....|....*
gi 506420374 324 YIQTMEKVMKNTPKL 338
Cdd:cd03404  252 YLETMEEVLSNASKV 266
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 91-348 4.13e-96

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 288.66  E-value: 4.13e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  91 ASGFYTVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVTPVNI-ERVLELrTNGSMLTQDENMVLVEMTVQYRIEDPAK 169
Cdd:COG0330   18 FSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKVDVrEQVLDV-PPQEVLTKDNNIVDVDAVVQYRITDPAK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 170 YLFSVTKPDDSLKQATDSALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKNYdmGLLITDVNFQYARPPEEVKAAFD 249
Cdd:COG0330   97 FLYNVENAEEALRQLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDPY--GIEVVDVEIKDIDPPEEVQDAME 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 250 DAIKAQEDEQRLIREAEAYARGQEPIARGQAQRILEQANAYKEQVVLNAQGEVQRFTQLLPEYKAAPEVTRDRlYIQTME 329
Cdd:COG0330  175 DRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYR-SLEALE 253

                        250
                 ....*....|....*....
gi 506420374 330 KVMKNTPKLMVDSSNGNNL 348
Cdd:COG0330  254 EVLSPNSKVIVLPPDGNGF 272
PHB smart00244
prohibitin homologues; prohibitin homologues
 92-250 2.31e-38

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 135.48  E-value: 2.31e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374    92 SGFYTVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVTPVNIERVLELRTNGSMLTQDENMVLVEMTVQYRIEDPAKYL 171
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374   172 FSVTKPDD-SLKQATDSALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKNYdmGLLITDVNFQYARPPEEVKAAFDD 250
Cdd:smart00244  81 YRVLDADYaVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAEAW--GIKVEDVEIKDIRLPEEIKEAMEA 158
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 94-292 1.34e-29

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: 114.89  E-value: 1.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  94 FYTVQEAERGVVTRFGKL-HEIVLPGLNWKPTFIDNVTPVNIeRVLELRTNGS-MLTQDENMVLVEMTVQYRIEDPAKYL 171
Cdd:cd03405    2 VFIVDETEQAVVLQFGKPvRVITEPGLHFKLPFIQNVRKFDK-RILTLDGPPEeVLTKDKKRLIVDSYARWRITDPLRFY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 172 FSVTKPDDS---LKQATDSALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKNYdmGLLITDVNFQYARPPEEVKAA- 247
Cdd:cd03405   81 QSVGGEEGAesrLDDIVDSALRNEIGKRTLAEVVSGGRDELMEEILEQANEEAKEY--GIEVVDVRIKRIDLPEEVSESv 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506420374 248 FD---------------------DAIKAQEDEQRLIREAEAYARGQEPIARGQAQRILEQANAYKE 292
Cdd:cd03405  159 YErmraereriaaeyraegeeeaEKIRAEADRERTVILAEAYREAEEIRGEGDAEAARIYAEAYGK 224
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 95-269 3.30e-29

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 111.64  E-value: 3.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374   95 YTVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVTPVNIeRVLELR-TNGSMLTQDENMVLVEMTVQYRI--EDPAKYL 171
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTVDV-RVQTLEvSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  172 FSVTKPDD---SLKQATDSALRYVIGHMTMDDILTTgRAIVREKTWNALRDIIKNYdmGLLITDVNFQYARPPEEVKAAF 248
Cdd:pfam01145  80 QNVFGSDDlqeLLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEELAKY--GVEIIDVQITDIDPPPEIAEAI 156

                         170       180
                  ....*....|....*....|.
gi 506420374  249 DDAIKAQEDEQRLIREAEAYA 269
Cdd:pfam01145 157 EAKQTAEQEAEAEIARAEAEA 177
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 94-301 2.92e-19

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: 84.87  E-value: 2.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  94 FYTVQEAERGVVTRFGK--LHEIVLPGLNWKPTFIDNVTPVNIeRVLELRTNGSMLTQDENMVLVEMTVQYRIE-DPAKY 170
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKgvKDEVLGEGLHFKIPWIQVVIIYDV-RTQPREITLTVLSKDGQTVNIDLSVLYRPDpEKLPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 171 LFSVTKPDDS---LKQATDSALRYVIGHMTMDDILTTgRAIVREKTWNALRDIIKNYdmGLLITDVNFQYARPPEEVKAA 247
Cdd:cd03401   80 LYQNLGPDYEervLPPIVREVLKAVVAQYTAEELYTK-REEVSAEIREALTERLAPF--GIIVDDVLITNIDFPDEYEKA 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 506420374 248 FDDAIKAQEDEQRlireaeayargqepiargqAQRILEQANAYKEQVVLNAQGE 301
Cdd:cd03401  157 IEAKQVAEQEAER-------------------AKFELEKAEQEAERKVIEAEGE 191
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 94-265 1.48e-17

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: 80.74  E-value: 1.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  94 FYTVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVTPVNIE-RVLELRTNgSMLTQDENMVLVEMTVQYRIEDPAKYLF 172
Cdd:cd13437    6 YKQVKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKIIQVDMKtQVIDLPRQ-SVMTKDNVSVTIDSVVYYRIIDPYKAIY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 173 SVTKPDDSLKQATDSALRYVIGHMTMDDILTTgraivREKTWNALRDIIKNY--DMG-----LLITDVNF------QYAR 239
Cdd:cd13437   85 RIDNVKQALIERTQTTLRSVIGERTLQDLLEK-----REEIADEIEEIVEEVakEWGvyvesILIKDIVLskdlqqSLSS 159

                        170       180
                 ....*....|....*....|....*...
gi 506420374 240 PPEEVKAAFDDAIKAQEDEQ--RLIREA 265
Cdd:cd13437  160 AAKAKRIGESKIISAKADVEsaKLMREA 187
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 94-344 1.07e-16

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: 80.21  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374   94 FYTVQEAERGVVTRFGK-------LHEIVLPGLNWKPTFIDNVTPVNiERVleLRTNG---SMLTQDENMVLVEMTVQYR 163
Cdd:TIGR01932  20 FFIIKEGERGIITRFGKilkdnnhHVLVYEPGLHFKIPFIEHVKIFD-AKI--QTMDGrpdRIPTKEKKDIIIDTYIRWR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  164 IEDPAKYLFSVTKPDDS-----LKQATDSALRYVIGHMTMDDIL-----------------------------TTGRAIV 209
Cdd:TIGR01932  97 IEDFKKYYLSTGGGTISaaevlIKRKIDDRLRSEIGVLGLKEIVrssndqldtlvsklalnrggkinkiamtiTKGREIL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  210 REKTWNALRDIIKnyDMGLLITDVNFQYARPPEEVKAAFDDaikaqedeqRLIREAEAYARGQEPIARGQAQRILEQAN- 288
Cdd:TIGR01932 177 AREISQIANSQLK--DIGIEVVDVRIKKINYSDELSESIYN---------RMRSEREQIARMHRSQGEEKAEEILGKAEy 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506420374  289 --------AYKEQVVLNAQGEVQRFTQLLPEYKAAPEVTRDRLYIQTMEKVMKNTPKLMVDSSN 344
Cdd:TIGR01932 246 evrkilseAYRTARIIKGEGDAEAAKIYSDAYGKDPEFYSFWRSLEAYEKSFKDNQDEKVLSTD 309
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 97-291 8.79e-14

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: 69.87  E-value: 8.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  97 VQEAERGVVTRFGKLHEIVLPGLN--WKPTFIDNVTPVNI-ERVLELrTNGSMLTQDENMVLVEMTVQYRIEDPAKYLFS 173
Cdd:cd13438    1 VPPGERGLLYRDGKLVRTLEPGRYafWKFGRKVQVELVDLrEQLLEV-SGQEILTADKVALRVNLVATYRVVDPVKAVET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 174 VTKPDDSLKQATDSALRYVIGHMTMDDILTTGRAIVREKTwNALRDIIKNYDMGLL---ITDVNFqyarpPEEVKAAFDD 250
Cdd:cd13438   80 VDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLL-AAVKEAAAELGVEVLsvgVKDIIL-----PGEIREILNQ 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 506420374 251 AIKAQedeqrliREAEA---YARGQEpiargQAQRILeqANAYK 291
Cdd:cd13438  154 VLEAE-------KRAQAnliRAREET-----AATRSL--LNAAK 183
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 96-300 2.66e-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: 69.54  E-value: 2.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  96 TVQEAERGVVTRFGKLHEIVLPGLNWKPTFIDNVT-PVNIeRVLELRTNGSMLTQDENMVLVEMTVQYRIEDPAKYL--F 172
Cdd:cd03407    1 CVSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAgRVSL-RVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDafY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 173 SVTKPDDSLKQATDSALRYVIGHMTMDDILTTGRAI---VREktwnALRDIIKNYD---MGLLITDVNfqyarPPEEVKA 246
Cdd:cd03407   80 KLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIakaVKE----ELAKVMSEYGyeiVKTLVTDIE-----PDASVKA 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 506420374 247 AFDDAIKAQedeqrliREAEAYArgqepiARGQAQRIL--EQANAYKEQVVLNAQG 300
Cdd:cd03407  151 AMNEINAAQ-------RLREAAE------EKAEAEKILqvKAAEAEAEAKRLQGVG 193
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 134-242 2.45e-12

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: 63.15  E-value: 2.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 134 IERVLELRtNGSMLTQDENMVLVEMTVQYRIEDPAK-YLFSVTK----PDDSLKQATDSALRYVIGHMTMDDILtTGRAI 208
Cdd:cd02106    1 RPQFDDVR-VEPVGTADGVPVAVDLVVQFRITDYNAlPAFYLVDfvkdIKADIRRKIADVLRAAIGRMTLDQII-SGRDE 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 506420374 209 VREKTWNALRDIIKNYdmGLLITDVNFQYARPPE 242
Cdd:cd02106   79 IAKAVKEDLEEDLENF--GVVISDVDITSIEPPD 110
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 146-242 2.53e-09

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: 54.51  E-value: 2.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 146 MLTQDENMVLVEMTVQYRIEDPAKYLFSVTKPDDSLKQATDSALRYVIGHMTMDDILTTgraivREKTWNALRDIIKNY- 224
Cdd:cd13434   15 ILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSE-----REEISQQLQEILDEAt 89

                         90
                 ....*....|....*....
gi 506420374 225 -DMGLLITDVNFQYARPPE 242
Cdd:cd13434   90 dPWGIKVERVEIKDIILPQ 108
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 135-242 3.12e-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: 54.02  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 135 ERVLELrTNGSMLTQDENMVLVEMTVQYRIEDPAKYLFSVTKPDDSLKQATDSALRYVIGHMTMDDILtTGRAIVREKTW 214
Cdd:cd08829    8 EQVLDI-PPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETL-SSREEINAKLL 85

                         90       100
                 ....*....|....*....|....*...
gi 506420374 215 NALRDIIKNYdmGLLITDVNFQYARPPE 242
Cdd:cd08829   86 EALDEATDPW--GVKVTRVEIKDITPPE 111
HflK_N pfam12221
Bacterial membrane protein N terminal; This domain is found in bacteria. This domain is ...
 2-63 8.19e-08

Bacterial membrane protein N terminal; This domain is found in bacteria. This domain is typically between 65 to 81 amino acids in length. This domain is found associated with pfam01145. This domain is the N terminal of the bacterial membrane protein HflK. HflK complexes with HflC to form a membrane protease which is modulated by the GTPase HflX. The N terminal domain of HflK is the membrane spanning region which anchors the protein in the bacterial membrane.


Pssm-ID: 463497  Cd Length: 43  Bit Score: 48.05  E-value: 8.19e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506420374    2 SWNESG-NQQDPWGKPGqkkpeqeqpsgqekepnkqsNEPQPPDLEEVFNSLLRKMGGGKGNG 63
Cdd:pfam12221   1 AWNEPGgNGRDPWGGGG--------------------GGQGPPDLDELLRKLQDKLGGLFGGG 43
PRK11029 PRK11029
protease modulator HflC;
92-303 3.12e-07

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 51.67  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  92 SGFYTVQEAERGVVTRFGKLHE-------IVLPGLNWKPTFIDNVtpvnieRVLELRTNgSM-------LTQDENMVLVE 157
Cdd:PRK11029  18 MSVFVVKEGERGIVLRFGKVLRdddnkplVYAPGLHFKIPFIETV------KMLDARIQ-TMdnqadrfVTKEKKDLIVD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 158 MTVQYRIEDPAKYLFSVTKPDDS-----LKQATDSALRYVIGHMTMDDILTTGR----AIVRE-------------KTWN 215
Cdd:PRK11029  91 SYIKWRISDFSRYYLATGGGDISqaevlLKRKFSDRLRSEIGRLDVKDIVTDSRgrltLDVRDalnsgsagtedevATPA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 216 ALRDIIKNYD--------------------MGLLITDVNFQYARPPEEVKaafdDAIKaqedeQRLIREAEAYAR----- 270
Cdd:PRK11029 171 ADDAIASAAErveaetkgkvpvinpnsmaaLGIEVVDVRIKQINLPTEVS----DAIY-----NRMRAEREAVARrhrsq 241

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 506420374 271 GQEPIARGQAQ------RILeqANAYKEQVVLNAQGEVQ 303
Cdd:PRK11029 242 GQEEAEKLRATadyevtRTL--AEAERQGRIMRGEGDAE 278
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 92-195 1.03e-05

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: 46.39  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  92 SGFYTVQEAERGVVTRFGK-LHEIVLPGLNWkptfidnVTPVNIERVLELRT---NGSMLT---QDENMVLVEMTVQYRI 164
Cdd:cd03402    8 GGFFVVQPNEAAVLTLFGRyRGTVRRPGLRW-------VNPFYRKKRVSLRVrnfESEPLKvndANGNPIEIAAVVVWRV 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 506420374 165 EDPAKYLFSVTKPDDSLKQATDSALRYVIGH 195
Cdd:cd03402   81 VDTAKAVFDVDDYEEFVSIQSEAALRRVASR 111
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 117-208 2.90e-05

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: 44.68  E-value: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 117 PGLNWKPTFIDNVTPVNIERVLELRTNGSMLTQDENMVLVEMTVQYRIEDPAKYLFSVTKPDDSLKQATDSALRYVIGHM 196
Cdd:cd13435    7 PGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGTR 86

                         90
                 ....*....|..
gi 506420374 197 TMDDILTTGRAI 208
Cdd:cd13435   87 NLSELLTERETI 98
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 147-267 3.94e-04

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: 40.96  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 147 LTQDENMVLVEMTVQYRIEDPAKYLFSVTKPDDSLKQATDSALRYVIGHMTMDDILTTgraivREKTWNALRDIIKNYDM 226
Cdd:cd08826   24 ITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLSE-----REEINKRIQEIIDEQTE 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 506420374 227 --GLLITDVnfqyarppeEVKaafddAIKAQEDEQRLI-REAEA 267
Cdd:cd08826   99 pwGIKVTAV---------EIK-----DVDLPESMQRAMaRQAEA 128
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 97-267 6.96e-04

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: 40.64  E-value: 6.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374  97 VQEAERGVVTRFGKL--HEIVLPGLNWKPTFIDNVTPVNIE-RVLELRTNgSMLTQDenMVLVEMTV--QYRIEDPAKYL 171
Cdd:cd08827    7 VREYERAVIFRLGHLlqGRARGPGLFFYLPCLDVCHKVDIRlQTLEIPFH-MIVTKD--LVCTEIDAicYYRIENASVCL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 172 FSVTKPDDSLKQATDSALRYVIGHMTMDDILTTGRAIVREKTWnALRDIIKNYdmGLLITDVNFQYARPPEEVKAAFDDA 251
Cdd:cd08827   84 SSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKV-ALDSGTCRW--GIKVERAEIKDVNLPPELQHSFAVE 160

                        170
                 ....*....|....*.
gi 506420374 252 IKAQEDEQRLIREAEA 267
Cdd:cd08827  161 AEAQRQAKVKVIAAEG 176
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
114-304 2.80e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.86  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 114 IVLPGLNwkptfidNVTPVNIERV-LELRTNGSMLTQDeNM-VLVEMTVQYRI----EDPAKYL--FSVTKPDDSLKQAT 185
Cdd:COG2268   55 FVLPVLH-------RAERMSLSTMtIEVERTEGLITKD-GIrVDVDAVFYVKVnsdpEDIANAAerFLGRDPEEIEELAE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506420374 186 D---SALRYVIGHMTMDDILTTGRAIVREKTWNALRDIIKnydMGLLITDVNFQYARPP------------EEVKAafdD 250
Cdd:COG2268  127 EkleGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAK---NGLELESVAITDLEDEnnyldalgrrkiAEIIR---D 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 506420374 251 AIKAQEDEQRLIREAEAYARGQEPIARGQAQRILE-----QANAYKEQVVLNAQGEVQR 304
Cdd:COG2268  201 ARIAEAEAERETEIAIAQANREAEEAELEQEREIEtariaEAEAELAKKKAEERREAET 259
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 242-304 9.34e-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: 36.26  E-value: 9.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506420374 242 EEVKAAFDDAIKAQEDEQRLIREAEAYARGqepiARGQAQRILEQANAY----KEQVVLNAQGEVQR 304
Cdd:cd06503   33 EKIAESLEEAEKAKEEAEELLAEYEEKLAE----ARAEAQEIIEEARKEaekiKEEILAEAKEEAER 95
 
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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