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Conserved domains on  [gi|50593217|ref|NP_011747|]
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prohibitin subunit PHB2 [Saccharomyces cerevisiae S288C]

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 ...
 58-252 1.79e-89

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: 265.15  E-value: 1.79e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217  58 LFNVDGGHRAIVYSRIHGVSSRIFNEGTHFIFPWLDTPIIYDVRAKPRNVASLTGTKDLQMVNITCRVLSRPDVVQLPTI 137
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 138 YRTLGQDYDERVLPSIVNEVLKAVVAQFNASQLITQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNAVEAK 217
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 50593217 218 QIAQQDAQRAAFVVDKARQEKQGMVVRAQGEAKSA 252
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 ...
 58-252 1.79e-89

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: 265.15  E-value: 1.79e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217  58 LFNVDGGHRAIVYSRIHGVSSRIFNEGTHFIFPWLDTPIIYDVRAKPRNVASLTGTKDLQMVNITCRVLSRPDVVQLPTI 137
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 138 YRTLGQDYDERVLPSIVNEVLKAVVAQFNASQLITQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNAVEAK 217
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 50593217 218 QIAQQDAQRAAFVVDKARQEKQGMVVRAQGEAKSA 252
Cdd:cd03401 161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 57-218 8.97e-36

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 126.62  E-value: 8.97e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217     57 ALFNVDGGHRAIVYSRIHGVSsRIFNEGTHFIFPWLDTPIIYDVRAKPRNV-ASLTGTKDLQMVNITCRVLSRpDVVQLP 135
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL-RVLGPGLHFLIPFIDDVKKVDLRAQTDDVpPQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217    136 TIYRTLgqDYDERVLPSIVNEVLKAVVAQFNASQLIT-QREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNAV 214
Cdd:smart00244  79 AVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 50593217    215 EAKQ 218
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 56-293 8.32e-30

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 114.17  E-value: 8.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217  56 NALFNVDGGHRAIVYSRihGVSSRIFNEGTHFIFPWLDTPIIYDVRAKPRNV-ASLTGTKDLQMVNITCRVLSRpdVVQL 134
Cdd:COG0330  19 SSVYIVPQGERGVVLRF--GKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVpPQEVLTKDNNIVDVDAVVQYR--ITDP 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 135 PTIYRTLgQDYDERVLPsIVNEVLKAVVAQFNASQLI-TQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNA 213
Cdd:COG0330  95 AKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDA 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 214 VEAKQIAQQDAQRAAF-------------------VVDKARQEKQGMVVRAQGEAKSAELIGEAIKKSRDYVELKRLDTa 274
Cdd:COG0330 173 MEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYRSLEA- 251

                       250
                ....*....|....*....
gi 50593217 275 rdIAKILASSPNRVILDNE 293
Cdd:COG0330 252 --LEEVLSPNSKVIVLPPD 268
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 61-238 3.24e-25

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 99.32  E-value: 3.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217    61 VDGGHRAIVYSriHGVSSRIFNEGTHFIFPWLDTPIIYDVRAKPRNVASLT-GTKDLQMVNITCRVLSRPDVVQLPTIYR 139
Cdd:pfam01145   3 VPPGEVGVVTR--FGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217   140 TL-GQDYDERVLPSIVNEVLKAVVAQFNASQLITQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNAVEAKQ 218
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 50593217   219 IAQQDAQRAafvVDKARQEK 238
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 ...
 58-252 1.79e-89

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: 265.15  E-value: 1.79e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217  58 LFNVDGGHRAIVYSRIHGVSSRIFNEGTHFIFPWLDTPIIYDVRAKPRNVASLTGTKDLQMVNITCRVLSRPDVVQLPTI 137
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 138 YRTLGQDYDERVLPSIVNEVLKAVVAQFNASQLITQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNAVEAK 217
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 50593217 218 QIAQQDAQRAAFVVDKARQEKQGMVVRAQGEAKSA 252
Cdd:cd03401 161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 57-218 8.97e-36

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 126.62  E-value: 8.97e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217     57 ALFNVDGGHRAIVYSRIHGVSsRIFNEGTHFIFPWLDTPIIYDVRAKPRNV-ASLTGTKDLQMVNITCRVLSRpDVVQLP 135
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL-RVLGPGLHFLIPFIDDVKKVDLRAQTDDVpPQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217    136 TIYRTLgqDYDERVLPSIVNEVLKAVVAQFNASQLIT-QREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNAV 214
Cdd:smart00244  79 AVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 50593217    215 EAKQ 218
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 56-293 8.32e-30

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 114.17  E-value: 8.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217  56 NALFNVDGGHRAIVYSRihGVSSRIFNEGTHFIFPWLDTPIIYDVRAKPRNV-ASLTGTKDLQMVNITCRVLSRpdVVQL 134
Cdd:COG0330  19 SSVYIVPQGERGVVLRF--GKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVpPQEVLTKDNNIVDVDAVVQYR--ITDP 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 135 PTIYRTLgQDYDERVLPsIVNEVLKAVVAQFNASQLI-TQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNA 213
Cdd:COG0330  95 AKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDA 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 214 VEAKQIAQQDAQRAAF-------------------VVDKARQEKQGMVVRAQGEAKSAELIGEAIKKSRDYVELKRLDTa 274
Cdd:COG0330 173 MEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFYRSLEA- 251

                       250
                ....*....|....*....
gi 50593217 275 rdIAKILASSPNRVILDNE 293
Cdd:COG0330 252 --LEEVLSPNSKVIVLPPD 268
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 61-238 3.24e-25

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 99.32  E-value: 3.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217    61 VDGGHRAIVYSriHGVSSRIFNEGTHFIFPWLDTPIIYDVRAKPRNVASLT-GTKDLQMVNITCRVLSRPDVVQLPTIYR 139
Cdd:pfam01145   3 VPPGEVGVVTR--FGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217   140 TL-GQDYDERVLPSIVNEVLKAVVAQFNASQLITQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNAVEAKQ 218
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 50593217   219 IAQQDAQRAafvVDKARQEK 238
Cdd:pfam01145 161 TAEQEAEAE---IARAEAEA 177
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 57-258 3.29e-13

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: 67.90  E-value: 3.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217  57 ALFNVDGGHRAIVySRIHGVSSRIFNEGTHFIFPWLDTPIIYDVR-----AKPRNVasLTGTKDLQMVNITCRVlsrpDV 131
Cdd:cd03405   1 SVFIVDETEQAVV-LQFGKPVRVITEPGLHFKLPFIQNVRKFDKRiltldGPPEEV--LTKDKKRLIVDSYARW----RI 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 132 VQLPTIYRTLGQDYD-ERVLPSIVNEVLKAVVAQFNASQLI-TQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPE 209
Cdd:cd03405  74 TDPLRFYQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEE 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 50593217 210 FTNAV----------EAKQIAQQDAQRAAFVvdKARQEKQGMVVRAQGEAKSAELIGEA 258
Cdd:cd03405 154 VSESVyermraererIAAEYRAEGEEEAEKI--RAEADRERTVILAEAYREAEEIRGEG 210
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 99-202 7.99e-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: 60.84  E-value: 7.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217  99 DVRAKPRnvasltGTKDLQMVNITCRVLSRP-DVVQLPTIYRTLGQDYDERVLPSIVNEVLKAVVAQFNASQLITQREKV 177
Cdd:cd02106   6 DVRVEPV------GTADGVPVAVDLVVQFRItDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEI 79

                        90       100
                ....*....|....*....|....*
gi 50593217 178 SRLIRENLVRRASKFNILLDDVSIT 202
Cdd:cd02106  80 AKAVKEDLEEDLENFGVVISDVDIT 104
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 55-290 4.02e-07

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: 49.92  E-value: 4.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217  55 NNALFNVDGGHRAIVySRIhGVSSRIFNEGTHFIFPWLDTPIIYDVRAKPRNVASLTG-TKDLQMVNITCRVLSRpdVVQ 133
Cdd:cd13437   3 PNPYKQVKQGSVGLV-ERF-GKFYKTVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVmTKDNVSVTIDSVVYYR--IID 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 134 LPT-IYRTlgQDYDERVLpSIVNEVLKAVVAQFNASQLITQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFtn 212
Cdd:cd13437  79 PYKaIYRI--DNVKQALI-ERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDL-- 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 213 aveakqiaQQDAQRAAfvvdKARQEKQGMVVRAQGEAKSAELIGEA--IKKSRDYVELKRLDTARDIAKilaSSPNRVIL 290
Cdd:cd13437 154 --------QQSLSSAA----KAKRIGESKIISAKADVESAKLMREAadILDSKAAMQIRYLETLQAIAK---SANSKVIF 218
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 84-278 6.56e-06

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: 46.22  E-value: 6.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217  84 GTHFIFPWLDTPIIYDVRAKPRNVASLTG-TKDLQMVNITCRV---LSRPdvvqLPTIYRTLGQDYDERVLPSIVnevLK 159
Cdd:cd13435   8 GVFFVLPCIDNYCKVDLRTVSFDVPPQEVlTKDSVTVTVDAVVyyrISDP----LNAVIQVANYSHSTRLLAATT---LR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 160 AVVAQFNASQLITQREKVSRLIRENLVRRASKFNILLDDVSItymtfspeftnaveaKQIAQQDA-QRAAFVVDKARQEK 238
Cdd:cd13435  81 NVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEI---------------KDVSLPDSlQRAMAAEAEAAREA 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 50593217 239 QGMVVRAQGEAKSAELIGEA---IKKSRDYVELKRLDTARDIA 278
Cdd:cd13435 146 RAKVIAAEGEMKSSRALKEAsdiISASPSALQLRYLQTLSSIS 188
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 61-285 4.85e-05

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: 44.04  E-value: 4.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217  61 VDGGHRAIVYsRIhGVSSRIFNEGTHFIFPW-LDTPIIYDVRA-------KPRNVASLTGTKDLQMVNITCRVLSRpdvV 132
Cdd:cd03404  18 VDPGERGVVL-RF-GKYVRTVGPGLHWKLPFpIEVVEKVNVTQvrsveigFRVPEESLMLTGDENIVDVDFVVQYR---I 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 133 QLPTIYRTLGQDYDErVLPSIVNEVLKAVVAQFNASQLIT-QREKVSRLIRENLVRRASKFN--ILLDDVSITYMTFSPE 209
Cdd:cd03404  93 SDPVAYLFNVRDPEE-TLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQEILDRYDlgIEIVQVQLQDADPPEE 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 210 FTNAVEAKQIAQQDAQR--------AAFVVDKARQEKQGM-----------VVRAQGEAKSAELIGEAIKKSRDyVELKR 270
Cdd:cd03404 172 VQDAFDDVNAARQDKERlineaqayANEVIPRARGEAARIiqeaeaykaevVARAEGDAARFLALLAEYRKAPE-VTRER 250

                       250
                ....*....|....*..
gi 50593217 271 --LDTardIAKILASSP 285
Cdd:cd03404 251 lyLET---MEEVLSNAS 264
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 75-263 7.10e-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: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 43.73  E-value: 7.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217  75 GVSSRIFNEGTHFIFPWLDTpIIYDVRAKPR--NVASLTGTKDLQMVNITCRVLSRPDVVQLPTIYRTLgqDYDERVLPS 152
Cdd:cd03407  14 GKFSRIAEPGLHFIIPPIES-VAGRVSLRVQqlDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYKL--TNPEQQIQS 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 153 IVNEVLKAVVAQFNASQLITQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNAVeAKQIAQQDAQRAAfvVD 232
Cdd:cd03407  91 YVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAM-NEINAAQRLREAA--EE 167

                       170       180       190
                ....*....|....*....|....*....|.
gi 50593217 233 KARQEKQGMVVRAQGEAKSAELIGEAIKKSR 263
Cdd:cd03407 168 KAEAEKILQVKAAEAEAEAKRLQGVGIAEQR 198
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 157-278 1.04e-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: 42.12  E-value: 1.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 157 VLKAVVAQFNASQLITQREKVSRLIRENLVRRASKFNIlldDVSitymtfspeftnAVEAKQIA-QQDAQRAAfvvdkAR 235
Cdd:cd08826  65 TLRSVVGQVELDELLSEREEINKRIQEIIDEQTEPWGI---KVT------------AVEIKDVDlPESMQRAM-----AR 124

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 50593217 236 Q-----EKQGMVVRAQGEAKSAELIGEA---IKKSRDYVELKRLDTARDIA 278
Cdd:cd08826 125 QaeaerERRAKIIKAEGELQAAEKLAEAaeiLAKSPGALQLRYLQTLSEIA 175
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
156-282 1.02e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.63  E-value: 1.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593217 156 EVLKAVVAQFNASQLITQREKVSRLIRENLVRRASKFNILLDDVSITYMTFSPEFTNAVEAKQIAQQDAQRAafvVDKAR 235
Cdd:COG2268 131 GALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDAR---IAEAE 207

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 50593217 236 QEKQGMVVRAQG--EAKSAELigeaiKKSRDYVELKRLDTARDIAKILA 282
Cdd:COG2268 208 AERETEIAIAQAnrEAEEAEL-----EQEREIETARIAEAEAELAKKKA 251
 
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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