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Conserved domains on  [gi|1958656649|ref|XP_038941191|]
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prohibitin 1 isoform X1 [Rattus norvegicus]

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 1.25e-91

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: 269.00  E-value: 1.25e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  27 LYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRI 106
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 107 YTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAK 186
Cdd:cd03401    81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958656649 187 QVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAA 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 1.25e-91

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: 269.00  E-value: 1.25e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  27 LYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRI 106
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 107 YTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAK 186
Cdd:cd03401    81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958656649 187 QVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAA 221
Cdd:cd03401   161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 26-187 9.25e-36

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 125.47  E-value: 9.25e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649   26 ALYNVDAGHRAVIFDRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVP-VITGSKDLQNVNITLRILFRpVASQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  105 RIYTSigEDYDERVLPSITTEILKSVVARFDAGELIT-QRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAV 183
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 1958656649  184 EAKQ 187
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 12-269 2.49e-34

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 124.95  E-value: 2.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  12 FGLALAVAGGVVNSALYNVDAGHRAVIFdRFRGVQDIVvGEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNV 88
Cdd:COG0330     6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVRTL-EPGLHFKIPFIDRVRKVDVREQVLDVPpqeVLT--KDNNIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  89 NITLRILFRPVasQLPRIYTSIgEDYDERVLPsITTEILKSVVARFDAGELI-TQRELVSRQVSDDLTERAATFGLILDD 167
Cdd:COG0330    82 DVDAVVQYRIT--DPAKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 168 VSLTHLTFGKEFTEAVEAKQVAQQEAERARF-------------------VVEKAEQQKKAAIISAEGDSKAAELIANSL 228
Cdd:COG0330   158 VEIKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAY 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958656649 229 aTAGDGLIELRKLEAAEDIayqLSRSRNITYLPAGQSVLLQ 269
Cdd:COG0330   238 -SAAPFVLFYRSLEALEEV---LSPNSKVIVLPPDGNGFLK 274
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-207 7.84e-32

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: 115.88  E-value: 7.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  30 VDAGHRAVIFdRFrGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVIT-GSKDLQNVNITLRILFRPVASQLPRIYT 108
Cdd:pfam01145   3 VPPGEVGVVT-RF-GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 109 SI-GEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQ 187
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 1958656649 188 VAQQEAERArfvVEKAEQQK 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 1.25e-91

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: 269.00  E-value: 1.25e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  27 LYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRI 106
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 107 YTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAK 186
Cdd:cd03401    81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958656649 187 QVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAA 221
Cdd:cd03401   161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 26-187 9.25e-36

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 125.47  E-value: 9.25e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649   26 ALYNVDAGHRAVIFDRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVP-VITGSKDLQNVNITLRILFRpVASQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  105 RIYTSigEDYDERVLPSITTEILKSVVARFDAGELIT-QRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAV 183
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 1958656649  184 EAKQ 187
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 12-269 2.49e-34

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 124.95  E-value: 2.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  12 FGLALAVAGGVVNSALYNVDAGHRAVIFdRFRGVQDIVvGEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNV 88
Cdd:COG0330     6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVRTL-EPGLHFKIPFIDRVRKVDVREQVLDVPpqeVLT--KDNNIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  89 NITLRILFRPVasQLPRIYTSIgEDYDERVLPsITTEILKSVVARFDAGELI-TQRELVSRQVSDDLTERAATFGLILDD 167
Cdd:COG0330    82 DVDAVVQYRIT--DPAKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 168 VSLTHLTFGKEFTEAVEAKQVAQQEAERARF-------------------VVEKAEQQKKAAIISAEGDSKAAELIANSL 228
Cdd:COG0330   158 VEIKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAY 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958656649 229 aTAGDGLIELRKLEAAEDIayqLSRSRNITYLPAGQSVLLQ 269
Cdd:COG0330   238 -SAAPFVLFYRSLEALEEV---LSPNSKVIVLPPDGNGFLK 274
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-207 7.84e-32

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: 115.88  E-value: 7.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  30 VDAGHRAVIFdRFrGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVIT-GSKDLQNVNITLRILFRPVASQLPRIYT 108
Cdd:pfam01145   3 VPPGEVGVVT-RF-GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 109 SI-GEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQ 187
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 1958656649 188 VAQQEAERArfvVEKAEQQK 207
Cdd:pfam01145 161 TAEQEAEAE---IARAEAEA 177
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 26-227 2.20e-16

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: 76.37  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  26 ALYNVDAGHRAVIFdRFRGVQDIVVGEGTHFLIPWVQKPIIFDCR-----SRPRNVPvitgSKDLQNVNITLRILFR--- 97
Cdd:cd03405     1 SVFIVDETEQAVVL-QFGKPVRVITEPGLHFKLPFIQNVRKFDKRiltldGPPEEVL----TKDKKRLIVDSYARWRitd 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  98 PVasqlpRIYTSIGEDYD-ERVLPSITTEILKSVVARFDAGELI-TQRELVSRQVSDDLTERAATFGLILDDVSLTHLTF 175
Cdd:cd03405    76 PL-----RFYQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDL 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656649 176 GKEFTEAV------EAKQVAQQ--------------EAERARfVVEKAEQQKKAAIISAEGDSKAAELIANS 227
Cdd:cd03405   151 PEEVSESVyermraERERIAAEyraegeeeaekiraEADRER-TVILAEAYREAEEIRGEGDAEAARIYAEA 221
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 74-177 1.35e-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: 54.29  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  74 RNVPVIT-GSKDLQNVNITLRILFRPV-ASQLPRIYTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVS 151
Cdd:cd02106     5 DDVRVEPvGTADGVPVAVDLVVQFRITdYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVK 84

                          90       100
                  ....*....|....*....|....*.
gi 1958656649 152 DDLTERAATFGLILDDVSLTHLTFGK 177
Cdd:cd02106    85 EDLEEDLENFGVVISDVDITSIEPPD 110
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 51-248 4.70e-09

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: 55.08  E-value: 4.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  51 GEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNVNITLRILFRpVASQLPRIYTSIGEDYDERVLPSITteiL 127
Cdd:cd13435     6 GPGVFFVLPCIDNYCKVDLRTVSFDVPpqeVLT--KDSVTVTVDAVVYYR-ISDPLNAVIQVANYSHSTRLLAATT---L 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 128 KSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAkqvaqqEAERARfvvekaeqQK 207
Cdd:cd13435    80 RNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAA------EAEAAR--------EA 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958656649 208 KAAIISAEGDSKAAELI--ANSLATAGDGLIELRKLEAAEDIA 248
Cdd:cd13435   146 RAKVIAAEGEMKSSRALkeASDIISASPSALQLRYLQTLSSIS 188
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 30-248 1.24e-07

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


Pssm-ID: 259816 [Multi-domain]  Cd Length: 215  Bit Score: 51.00  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  30 VDAGHRAVIFdrFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPViTG----SKDlqnvNITLRILFRpVASQL-- 103
Cdd:cd13438     1 VPPGERGLLY--RDGKLVRTLEPGRYAFWKFGRKVQVELVDLREQLLEV-SGqeilTAD----KVALRVNLV-ATYRVvd 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 104 PRIYTSIGEDYDErVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKE----F 179
Cdd:cd13438    73 PVKAVETVDDPEE-QLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEireiL 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656649 180 TEAVEAKQVAQQEAERARfvvEKAEQQKKAAiisaegdsKAAELIANSLAtagdgLIELRKLEAAEDIA 248
Cdd:cd13438   152 NQVLEAEKRAQANLIRAR---EETAATRSLL--------NAAKLMEENPA-----LLRLRELEALEKIA 204
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 28-248 1.36e-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: 51.08  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  28 YNVDAGHRAVIfDRFRGVQDIVvGEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNVNITLRILFRPVASQlp 104
Cdd:cd13437     7 KQVKQGSVGLV-ERFGKFYKTV-DPGLHKVNPCTEKIIQVDMKTQVIDLPrqsVMT--KDNVSVTIDSVVYYRIIDPY-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 105 RIYTSIgEDYDERVLP-SITTeiLKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTE-- 181
Cdd:cd13437    81 KAIYRI-DNVKQALIErTQTT--LRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQsl 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656649 182 --AVEAKQVAQQEAERARFVVEKAEQQKKAAIISaegDSKAAelianslatagdglIELRKLEAAEDIA 248
Cdd:cd13437   158 ssAAKAKRIGESKIISAKADVESAKLMREAADIL---DSKAA--------------MQIRYLETLQAIA 209
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 59-248 3.62e-07

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria 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: 49.05  E-value: 3.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  59 PWVQKPIIFDCRSRPRNVP---VITgsKDlqnvNITLR----ILFRPVASQlpRIYTSIgEDYDERVLP-SITTeiLKSV 130
Cdd:cd08826     1 PFIDRMVRVDLRTVTLDVPpqeVIT--KD----NVTVKvnavVYFRVVDPE--KAVLAV-EDYRYATSQlAQTT--LRSV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 131 VARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVeAKQVaqqEAERarfvvekaeqQKKAA 210
Cdd:cd08826    70 VGQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAM-ARQA---EAER----------ERRAK 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958656649 211 IISAEGDSKAAElianSLATAGD------GLIELRKLEAAEDIA 248
Cdd:cd08826   136 IIKAEGELQAAE----KLAEAAEilakspGALQLRYLQTLSEIA 175
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 36-241 2.59e-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: 44.50  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  36 AVIFDRFrGVQDIVVGEGTHFLIPWVQKpiIFD---CRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIYTSIge 112
Cdd:cd03407     7 VAIVERF-GKFSRIAEPGLHFIIPPIES--VAGrvsLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYKL-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 113 DYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQE 192
Cdd:cd03407    82 TNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRL 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958656649 193 AERArfvVEKAEQQKKAAIISAEGDSKAAELianslatAGDGLIELRKL 241
Cdd:cd03407   162 REAA---EEKAEAEKILQVKAAEAEAEAKRL-------QGVGIAEQRKA 200
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
9-222 3.03e-05

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.86  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649   9 IGKFGLALAVAGGVVNSALYNVDAGHRAVIFDRFRGvQDIVVGEGThFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNV 88
Cdd:COG2268    10 IGVIVVVLLLLLIILARFYRKVPPNEALVITGRGGG-YKVVTGGGA-FVLPVLHRAERMSLSTMTIEVERTEGLITKDGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  89 NITLRILFR-PVASQLPRIYTSI------GEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATF 161
Cdd:COG2268    88 RVDVDAVFYvKVNSDPEDIANAAerflgrDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKN 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958656649 162 GLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERArfvVEKAEQQKKAAIISAEGDSKAAE 222
Cdd:COG2268   168 GLELESVAITDLEDENNYLDALGRRKIAEIIRDAR---IAEAEAERETEIAIAQANREAEE 225
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 51-248 7.20e-04

Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; Stomatin (or band 7) is widely expressed and, highly expressed in red blood cells. It localizes predominantly to the plasma membrane and to intracellular vesicles of the endocytic pathway, where it is present in higher order homo-oligomeric complexes (of between 9 and 12 monomers). Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and, is implicated in trafficking of Glut1 glucose transporters. This subgroup found in animals, also contains proteins similar to Caenorhabditis elegans MEC-2. MEC-2 interacts with MEC-4, which is part of the degenerin channel complex required for response to gentle body touch.


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 39.84  E-value: 7.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  51 GEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNVNITLRILFRpvaSQLPRIYTSIGEDYDE--RVLPSITte 125
Cdd:cd03403     6 GPGLFFILPCIDSYRKVDLRTVSFDVPpqeILT--KDSVTVAVDAVVYYR---VQNATIAVTNVENADRstRLLAQTT-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 126 iLKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLthltfgKEFTEAVEAKQVAQQEAERARfvvekaeq 205
Cdd:cd03403    79 -LRNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEI------KDVRLPVQLQRAMAAEAEAAR-------- 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958656649 206 QKKAAIISAEGDSKAAELI--ANSLATAGDGLIELRKLEAAEDIA 248
Cdd:cd03403   144 EARAKVIAAEGEQNASRALkeAADVISESPAALQLRYLQTLNTIS 188
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 13-257 1.23e-03

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: 39.42  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  13 GLALAVAGGVVNSALYNVDAGHRAVIFdRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITG--------SKD 84
Cdd:cd03404     1 LILLLLLLVWLLSGFYTVDPGERGVVL-RFGKYVR-TVGPGLHWKLPFPIEVVEKVNVTQVRSVEIGFRvpeeslmlTGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649  85 LQNVNITLRILFRpvasqlpriytsIGEDYD--------ERVLPSITTEILKSVVARFDAGELIT-QRELVSRQVSDDLT 155
Cdd:cd03404    79 ENIVDVDFVVQYR------------ISDPVAylfnvrdpEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQ 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656649 156 ERAATF--GLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARF-------------------VVEKAEQQKKAAIISA 214
Cdd:cd03404   147 EILDRYdlGIEIVQVQLQDADPPEEVQDAFDDVNAARQDKERLINeaqayaneviprargeaarIIQEAEAYKAEVVARA 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958656649 215 EGDSKAAELIANSLATAGDGLIELRKLEAAEDIayqLSRSRNI 257
Cdd:cd03404   227 EGDAARFLALLAEYRKAPEVTRERLYLETMEEV---LSNASKV 266
 
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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