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Conserved domains on  [gi|187951379|gb|AAI39182|]
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RIKEN cDNA 1700071K01 gene [Mus musculus]

Protein Classification

prohibitin family protein( domain architecture ID 10130412)

prohibitin family protein similar to Homo sapiens prohibitin, a lipid raft-associated integral membrane protein that inhibits DNA synthesis and has a role in regulating proliferation

CATH:  3.30.479.30
Gene Ontology:  GO:0005743|GO:0035632|GO:0016020
PubMed:  31522117|17766116|10542406|16101677
SCOP:  4003722

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 27-221 8.23e-92

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: 269.38  E-value: 8.23e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  27 LYNVDAGHRAVIFDRFHGVQDIVVGEGTHFLIPWVQKPVIFDCRSQPRNIPVITGSKDLQNVNITLRILFRPVASQLPHI 106
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 107 YTNIGQDYDERVLPSITSEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAK 186
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 187951379 187 QVAQQEAETARFVVEKAEQQKVAAIISAEGDAKAA 221
Cdd:cd03401  161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 27-221 8.23e-92

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: 269.38  E-value: 8.23e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  27 LYNVDAGHRAVIFDRFHGVQDIVVGEGTHFLIPWVQKPVIFDCRSQPRNIPVITGSKDLQNVNITLRILFRPVASQLPHI 106
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 107 YTNIGQDYDERVLPSITSEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAK 186
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 187951379 187 QVAQQEAETARFVVEKAEQQKVAAIISAEGDAKAA 221
Cdd:cd03401  161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 26-187 4.36e-35

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 123.54  E-value: 4.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379    26 ALYNVDAGHRAVIFDRFHGVQDiVVGEGTHFLIPWVQKPVIFDCRSQPRNIP-VITGSKDLQNVNITLRILFRpVASQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379   105 HIYTNigQDYDERVLPSITSEILKSVVARFDAGELIT-QRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAV 183
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 187951379   184 EAKQ 187
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 12-263 1.55e-33

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 123.03  E-value: 1.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  12 FGLALAVAGGVVSSALYNVDAGHRAVIFdRFHGVQDIVvGEGTHFLIPWVQKPVIFDCRSQPRNIP---VITgsKDLQNV 88
Cdd:COG0330    6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVRTL-EPGLHFKIPFIDRVRKVDVREQVLDVPpqeVLT--KDNNIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  89 NITLRILFRPVasQLPHIYTNIgQDYDERVLPsITSEILKSVVARFDAGELI-TQRELVSRQVSDDLTERAATFGLILDD 167
Cdd:COG0330   82 DVDAVVQYRIT--DPAKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 168 VSLTHLTFGKEFTEAVEAKQVAQQEAETARF--------VVEKAEQQKVAAIISAE-----------GDAKAAELIANSL 228
Cdd:COG0330  158 VEIKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaAIIRAEGEAQRAIIEAEayreaqilraeGEAEAFRIVAEAY 237

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 187951379 229 aTAGDGLIELRKLEAAEDIayqLSRSQNVTYLPVG 263
Cdd:COG0330  238 -SAAPFVLFYRSLEALEEV---LSPNSKVIVLPPD 268
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-207 4.29e-33

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 118.96  E-value: 4.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379   30 VDAGHRAVIFdRFHGVQDiVVGEGTHFLIPWVQKPVIFDCRSQPRNIPVIT-GSKDLQNVNITLRILFRPVASQLPHIYT 108
Cdd:pfam01145   3 VPPGEVGVVT-RFGKLSR-VLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  109 NI-GQDYDERVLPSITSEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQ 187
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 187951379  188 VAQQEAETArfvVEKAEQQK 207
Cdd:pfam01145 161 TAEQEAEAE---IARAEAEA 177
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 27-221 8.23e-92

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: 269.38  E-value: 8.23e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  27 LYNVDAGHRAVIFDRFHGVQDIVVGEGTHFLIPWVQKPVIFDCRSQPRNIPVITGSKDLQNVNITLRILFRPVASQLPHI 106
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 107 YTNIGQDYDERVLPSITSEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAK 186
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 187951379 187 QVAQQEAETARFVVEKAEQQKVAAIISAEGDAKAA 221
Cdd:cd03401  161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 26-187 4.36e-35

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 123.54  E-value: 4.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379    26 ALYNVDAGHRAVIFDRFHGVQDiVVGEGTHFLIPWVQKPVIFDCRSQPRNIP-VITGSKDLQNVNITLRILFRpVASQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379   105 HIYTNigQDYDERVLPSITSEILKSVVARFDAGELIT-QRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAV 183
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 187951379   184 EAKQ 187
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 12-263 1.55e-33

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 123.03  E-value: 1.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  12 FGLALAVAGGVVSSALYNVDAGHRAVIFdRFHGVQDIVvGEGTHFLIPWVQKPVIFDCRSQPRNIP---VITgsKDLQNV 88
Cdd:COG0330    6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVRTL-EPGLHFKIPFIDRVRKVDVREQVLDVPpqeVLT--KDNNIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  89 NITLRILFRPVasQLPHIYTNIgQDYDERVLPsITSEILKSVVARFDAGELI-TQRELVSRQVSDDLTERAATFGLILDD 167
Cdd:COG0330   82 DVDAVVQYRIT--DPAKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 168 VSLTHLTFGKEFTEAVEAKQVAQQEAETARF--------VVEKAEQQKVAAIISAE-----------GDAKAAELIANSL 228
Cdd:COG0330  158 VEIKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaAIIRAEGEAQRAIIEAEayreaqilraeGEAEAFRIVAEAY 237

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 187951379 229 aTAGDGLIELRKLEAAEDIayqLSRSQNVTYLPVG 263
Cdd:COG0330  238 -SAAPFVLFYRSLEALEEV---LSPNSKVIVLPPD 268
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-207 4.29e-33

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 118.96  E-value: 4.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379   30 VDAGHRAVIFdRFHGVQDiVVGEGTHFLIPWVQKPVIFDCRSQPRNIPVIT-GSKDLQNVNITLRILFRPVASQLPHIYT 108
Cdd:pfam01145   3 VPPGEVGVVT-RFGKLSR-VLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  109 NI-GQDYDERVLPSITSEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQ 187
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 187951379  188 VAQQEAETArfvVEKAEQQK 207
Cdd:pfam01145 161 TAEQEAEAE---IARAEAEA 177
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 26-231 4.08e-15

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: 72.91  E-value: 4.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  26 ALYNVDAGHRAVIFdRFHGVQDIVVGEGTHFLIPWVQKPVIFDCR-----SQPRNIPvitgSKDLQNVNITLRILFR--- 97
Cdd:cd03405    1 SVFIVDETEQAVVL-QFGKPVRVITEPGLHFKLPFIQNVRKFDKRiltldGPPEEVL----TKDKKRLIVDSYARWRitd 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  98 PVAsqlphIYTNIGQDYD-ERVLPSITSEILKSVVARFDAGELI-TQRELVSRQVSDDLTERAATFGLILDDVSLTHLTF 175
Cdd:cd03405   76 PLR-----FYQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDL 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 187951379 176 GKEFTEAVEAKQVAQQEAETARFvveKAEQQKVAAIISAEGDAKAAELIANSLATA 231
Cdd:cd03405  151 PEEVSESVYERMRAERERIAAEY---RAEGEEEAEKIRAEADRERTVILAEAYREA 203
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 77-177 3.31e-09

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: 53.52  E-value: 3.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  77 PVITGSKDLQNVNITLRILFRPV-ASQLPHIYTNIGQDYDERVLPSITSEILKSVVARFDAGELITQRELVSRQVSDDLT 155
Cdd:cd02106    9 VEPVGTADGVPVAVDLVVQFRITdYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVKEDLE 88

                         90       100
                 ....*....|....*....|..
gi 187951379 156 ERAATFGLILDDVSLTHLTFGK 177
Cdd:cd02106   89 EDLENFGVVISDVDITSIEPPD 110
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 112-248 6.71e-09

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: 54.46  E-value: 6.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 112 QDYDErVLPSITSEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKE----FTEAVEAKQ 187
Cdd:cd13438   81 DDPEE-QLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEireiLNQVLEAEK 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187951379 188 VAQQEAETARfvvekaeqQKVAAIISaegDAKAAELIANSLAtagdgLIELRKLEAAEDIA 248
Cdd:cd13438  160 RAQANLIRAR--------EETAATRS---LLNAAKLMEENPA-----LLRLRELEALEKIA 204
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 51-268 1.31e-08

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: 53.93  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  51 GEGTHFLIPWVQKPVIFDCRSQPRNIP---VITgsKDLQNVNITLRILFRpVASQLPHIYTNIGQDYDERVLPSITseiL 127
Cdd:cd13435    6 GPGVFFVLPCIDNYCKVDLRTVSFDVPpqeVLT--KDSVTVTVDAVVYYR-ISDPLNAVIQVANYSHSTRLLAATT---L 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 128 KSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAkqvaqqEAETARfvvekaeqQK 207
Cdd:cd13435   80 RNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAA------EAEAAR--------EA 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187951379 208 VAAIISAEGDAKAAELI--ANSLATAGDGLIELRKLEAAEDIAYQlSRSQNVTYLPVGQTVPL 268
Cdd:cd13435  146 RAKVIAAEGEMKSSRALkeASDIISASPSALQLRYLQTLSSISGE-KNSTIIFPLPMELLTPL 207
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 36-241 3.54e-08

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: 52.97  E-value: 3.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  36 AVIFDRFhGVQDIVVGEGTHFLIPWVQKpvIFD---CRSQPRNIPVITGSKDLQNVNITLRILFRPVASQLPHIYTNIgq 112
Cdd:cd03407    7 VAIVERF-GKFSRIAEPGLHFIIPPIES--VAGrvsLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYKL-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 113 DYDERVLPSITSEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQE 192
Cdd:cd03407   82 TNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 187951379 193 AETArfvVEKAEQQKVAAIISAEGDAKAAELianslatAGDGLIELRKL 241
Cdd:cd03407  162 REAA---EEKAEAEKILQVKAAEAEAEAKRL-------QGVGIAEQRKA 200
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 28-261 6.56e-08

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: 51.85  E-value: 6.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  28 YNVDAGHRAVIfDRFHGVQDIVvGEGTHFLIPWVQKPVIFDCRSQPRNIP---VITgsKDLQNVNITLRILFRPVAsqlP 104
Cdd:cd13437    7 KQVKQGSVGLV-ERFGKFYKTV-DPGLHKVNPCTEKIIQVDMKTQVIDLPrqsVMT--KDNVSVTIDSVVYYRIID---P 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 105 H--IYT--NIGQDYDERvlpsiTSEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFT 180
Cdd:cd13437   80 YkaIYRidNVKQALIER-----TQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 181 EAVEAKQVAQQEAEtarfvvekaeqqkvAAIISAEGDAKAAELI---ANSLATagDGLIELRKLEAAEDIAyqlsRSQN- 256
Cdd:cd13437  155 QSLSSAAKAKRIGE--------------SKIISAKADVESAKLMreaADILDS--KAAMQIRYLETLQAIA----KSANs 214


                 ....*.
gi 187951379 257 -VTYLP 261
Cdd:cd13437  215 kVIFLP 220
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 13-257 6.72e-06

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: 46.35  E-value: 6.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  13 GLALAVAGGVVSSALYNVDAGHRAVI--FDRFHGVqdivVGEGTHFLIPWVQKPVIFDCRSQPRNIPVITG--------S 82
Cdd:cd03404    1 LILLLLLLVWLLSGFYTVDPGERGVVlrFGKYVRT----VGPGLHWKLPFPIEVVEKVNVTQVRSVEIGFRvpeeslmlT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  83 KDLQNVNITLRILFR---PVASQLphiytNIgQDYDErVLPSITSEILKSVVARFDAGELIT-QRELVSRQVSDDLTERA 158
Cdd:cd03404   77 GDENIVDVDFVVQYRisdPVAYLF-----NV-RDPEE-TLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQEIL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 159 ATF--GLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAETARF-------------------VVEKAEQQKVAAIISAEGD 217
Cdd:cd03404  150 DRYdlGIEIVQVQLQDADPPEEVQDAFDDVNAARQDKERLINeaqayaneviprargeaarIIQEAEAYKAEVVARAEGD 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 187951379 218 AKAAELIANSLATAGDGLIELRKLEAAEDIayqLSRSQNV 257
Cdd:cd03404  230 AARFLALLAEYRKAPEVTRERLYLETMEEV---LSNASKV 266
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 59-248 5.25e-05

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: 42.89  E-value: 5.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379  59 PWVQKPVIFDCRSQPRNIP---VITgsKDlqnvNITLR----ILFRPVAsqlPHIYTNIGQDYDERVLpSITSEILKSVV 131
Cdd:cd08826    1 PFIDRMVRVDLRTVTLDVPpqeVIT--KD----NVTVKvnavVYFRVVD---PEKAVLAVEDYRYATS-QLAQTTLRSVV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 132 ARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVeAKQvaqqeAEtarfvvekAEQQKVAAI 211
Cdd:cd08826   71 GQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAM-ARQ-----AE--------AERERRAKI 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 187951379 212 ISAEGD-------AKAAELIANSLATagdglIELRKLEAAEDIA 248
Cdd:cd08826  137 IKAEGElqaaeklAEAAEILAKSPGA-----LQLRYLQTLSEIA 175
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
127-222 1.80e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.55  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187951379 127 LKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQ--QEAEtarfvVEKAE 204
Cdd:COG2268  133 LRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEiiRDAR-----IAEAE 207

                         90
                 ....*....|....*...
gi 187951379 205 QQKVAAIISAEGDAKAAE 222
Cdd:COG2268  208 AERETEIAIAQANREAEE 225
 
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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