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Conserved domains on  [gi|1622157237|ref|XP_028560996|]
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prohibitin [Podarcis muralis]

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 5.08e-90

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: 5.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  27 LYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVTMQLPRI 106
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 107 FTTIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSEDLTERAATFGLILDDVSLTHLTFGKEFTEAVEMK 186
Cdd:cd03401    81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622157237 187 QVAQQEAERARFIVEKAEQQKKAAIISAEGDSKAA 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 5.08e-90

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: 5.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  27 LYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVTMQLPRI 106
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 107 FTTIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSEDLTERAATFGLILDDVSLTHLTFGKEFTEAVEMK 186
Cdd:cd03401    81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622157237 187 QVAQQEAERARFIVEKAEQQKKAAIISAEGDSKAA 221
Cdd:cd03401   161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 26-187 3.34e-36

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 126.62  E-value: 3.34e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237   26 ALYNVDAGHRAVIFDRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVP-VITGSKDLQNVNITLRILFRpVTMQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  105 RIFTTigEDYDERVLPSITTEILKSVVARFDAGELIT-QRELVSRQVSEDLTERAATFGLILDDVSLTHLTFGKEFTEAV 183
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 1622157237  184 EMKQ 187
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 12-269 4.09e-34

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 124.57  E-value: 4.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  12 LGLGLAVAGGVVNSALYNVDAGHRAVIFdRFRGVQDIVvGEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNV 88
Cdd:COG0330     6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVRTL-EPGLHFKIPFIDRVRKVDVREQVLDVPpqeVLT--KDNNIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  89 NITLRILFRPVTmqLPRIFTTIgEDYDERVLPsITTEILKSVVARFDAGELI-TQRELVSRQVSEDLTERAATFGLILDD 167
Cdd:COG0330    82 DVDAVVQYRITD--PAKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 168 VSLTHLTFGKEFTEAVEMKQVAQQEAERARF-------------------IVEKAEQQKKAAIISAEGDSKAAELIATSL 228
Cdd:COG0330   158 VEIKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAY 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1622157237 229 SSVGDgLIELRKLEAAEDIayqLSRSRNITYLPSGQSVLLQ 269
Cdd:COG0330   238 SAAPF-VLFYRSLEALEEV---LSPNSKVIVLPPDGNGFLK 274
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-207 7.03e-31

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: 113.19  E-value: 7.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  30 VDAGHRAVIFdRFrGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVIT-GSKDLQNVNITLRILFRPVTMQLPRIFT 108
Cdd:pfam01145   3 VPPGEVGVVT-RF-GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 109 TI-GEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSEDLTERAATFGLILDDVSLTHLTFGKEFTEAVEMKQ 187
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 1622157237 188 VAQQEAERArfiVEKAEQQK 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 5.08e-90

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: 5.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  27 LYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVTMQLPRI 106
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 107 FTTIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSEDLTERAATFGLILDDVSLTHLTFGKEFTEAVEMK 186
Cdd:cd03401    81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622157237 187 QVAQQEAERARFIVEKAEQQKKAAIISAEGDSKAA 221
Cdd:cd03401   161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 26-187 3.34e-36

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 126.62  E-value: 3.34e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237   26 ALYNVDAGHRAVIFDRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVP-VITGSKDLQNVNITLRILFRpVTMQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  105 RIFTTigEDYDERVLPSITTEILKSVVARFDAGELIT-QRELVSRQVSEDLTERAATFGLILDDVSLTHLTFGKEFTEAV 183
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 1622157237  184 EMKQ 187
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 12-269 4.09e-34

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 124.57  E-value: 4.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  12 LGLGLAVAGGVVNSALYNVDAGHRAVIFdRFRGVQDIVvGEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNV 88
Cdd:COG0330     6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVRTL-EPGLHFKIPFIDRVRKVDVREQVLDVPpqeVLT--KDNNIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  89 NITLRILFRPVTmqLPRIFTTIgEDYDERVLPsITTEILKSVVARFDAGELI-TQRELVSRQVSEDLTERAATFGLILDD 167
Cdd:COG0330    82 DVDAVVQYRITD--PAKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 168 VSLTHLTFGKEFTEAVEMKQVAQQEAERARF-------------------IVEKAEQQKKAAIISAEGDSKAAELIATSL 228
Cdd:COG0330   158 VEIKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAY 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1622157237 229 SSVGDgLIELRKLEAAEDIayqLSRSRNITYLPSGQSVLLQ 269
Cdd:COG0330   238 SAAPF-VLFYRSLEALEEV---LSPNSKVIVLPPDGNGFLK 274
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-207 7.03e-31

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: 113.19  E-value: 7.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  30 VDAGHRAVIFdRFrGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVIT-GSKDLQNVNITLRILFRPVTMQLPRIFT 108
Cdd:pfam01145   3 VPPGEVGVVT-RF-GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 109 TI-GEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSEDLTERAATFGLILDDVSLTHLTFGKEFTEAVEMKQ 187
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 1622157237 188 VAQQEAERArfiVEKAEQQK 207
Cdd:pfam01145 161 TAEQEAEAE---IARAEAEA 177
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 26-225 8.24e-17

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: 77.53  E-value: 8.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  26 ALYNVDAGHRAVIFdRFRGVQDIVVGEGTHFLIPWVQKPIIFDCR-----SRPRNVPvitgSKDLQNVNITLRILFR--- 97
Cdd:cd03405     1 SVFIVDETEQAVVL-QFGKPVRVITEPGLHFKLPFIQNVRKFDKRiltldGPPEEVL----TKDKKRLIVDSYARWRitd 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  98 PVTMqlpriFTTIGEDYD-ERVLPSITTEILKSVVARFDAGELI-TQRELVSRQVSEDLTERAATFGLILDDVSLTHLTF 175
Cdd:cd03405    76 PLRF-----YQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622157237 176 GKEFTEAV------EMKQVAQQE----AERARFI---------VEKAEQQKKAAIISAEGDSKAAELIA 225
Cdd:cd03405   151 PEEVSESVyermraERERIAAEYraegEEEAEKIraeadrertVILAEAYREAEEIRGEGDAEAARIYA 219
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 51-248 1.22e-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: 56.62  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  51 GEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNVNITLRILFRpVTMQLPRIFTTIGEDYDERVLPSITteiL 127
Cdd:cd13435     6 GPGVFFVLPCIDNYCKVDLRTVSFDVPpqeVLT--KDSVTVTVDAVVYYR-ISDPLNAVIQVANYSHSTRLLAATT---L 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 128 KSVVARFDAGELITQRELVSRQVSEDLTERAATFGLILDDVSLthltfgKEFTEAVEMKQVAQQEAERARfivekaeqQK 207
Cdd:cd13435    80 RNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEI------KDVSLPDSLQRAMAAEAEAAR--------EA 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622157237 208 KAAIISAEGDSKAAELI--ATSLSSVGDGLIELRKLEAAEDIA 248
Cdd:cd13435   146 RAKVIAAEGEMKSSRALkeASDIISASPSALQLRYLQTLSSIS 188
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 74-177 5.60e-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: 52.75  E-value: 5.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  74 RNVPVIT-GSKDLQNVNITLRILFRPVTMQ-LPRIFTTIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVS 151
Cdd:cd02106     5 DDVRVEPvGTADGVPVAVDLVVQFRITDYNaLPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVK 84

                          90       100
                  ....*....|....*....|....*.
gi 1622157237 152 EDLTERAATFGLILDDVSLTHLTFGK 177
Cdd:cd02106    85 EDLEEDLENFGVVISDVDITSIEPPD 110
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 59-248 1.70e-08

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: 52.90  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  59 PWVQKPIIFDCRSRPRNVP---VITgsKDlqnvNITLR----ILFRPVTMQlpRIFTTIgEDYDERVLP-SITTeiLKSV 130
Cdd:cd08826     1 PFIDRMVRVDLRTVTLDVPpqeVIT--KD----NVTVKvnavVYFRVVDPE--KAVLAV-EDYRYATSQlAQTT--LRSV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 131 VARFDAGELITQRELVSRQVSEDLTERAATFGLILDDVSLTHLtfgkEFTEavEMKQVAQQEAErarfivekAEQQKKAA 210
Cdd:cd08826    70 VGQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDV----DLPE--SMQRAMARQAE--------AERERRAK 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1622157237 211 IISAEGD-------SKAAELIATSLSSvgdglIELRKLEAAEDIA 248
Cdd:cd08826   136 IIKAEGElqaaeklAEAAEILAKSPGA-----LQLRYLQTLSEIA 175
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 28-248 3.60e-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: 52.62  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  28 YNVDAGHRAVIfDRFRGVQDIVvGEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNVNITLRILFRPVTmqlP 104
Cdd:cd13437     7 KQVKQGSVGLV-ERFGKFYKTV-DPGLHKVNPCTEKIIQVDMKTQVIDLPrqsVMT--KDNVSVTIDSVVYYRIID---P 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 105 R--IFTTigEDYDERVLP-SITTeiLKSVVARFDAGELITQRELVSRQVSEDLTERAATFGLILDDVSLTHLTFGKEFTE 181
Cdd:cd13437    80 YkaIYRI--DNVKQALIErTQTT--LRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQ 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 182 AVEMKQVAQQEAErarfivekaeqqkkAAIISAEGDSKAAELI---ATSLSSvgDGLIELRKLEAAEDIA 248
Cdd:cd13437   156 SLSSAAKAKRIGE--------------SKIISAKADVESAKLMreaADILDS--KAAMQIRYLETLQAIA 209
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 30-197 1.07e-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: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  30 VDAGHRAVIFdrFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPViTG----SKDlqnvNITLRILFRpVTMQL-- 103
Cdd:cd13438     1 VPPGERGLLY--RDGKLVRTLEPGRYAFWKFGRKVQVELVDLREQLLEV-SGqeilTAD----KVALRVNLV-ATYRVvd 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 104 PRIFTTIGEDYDErVLPSITTEILKSVVARFDAGELITQRELVSRQVSEDLTERAATFGLILDDVSLTHLTFGKE----F 179
Cdd:cd13438    73 PVKAVETVDDPEE-QLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEireiL 151

                         170
                  ....*....|....*...
gi 1622157237 180 TEAVEMKQVAQQEAERAR 197
Cdd:cd13438   152 NQVLEAEKRAQANLIRAR 169
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
127-222 1.51e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 48.72  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 127 LKSVVARFDAGELITQRELVSRQVSEDLTERAATFGLILDDVSLTHLTFGKEFTEAVEMKQVAQQEAERarfIVEKAEQQ 206
Cdd:COG2268   133 LRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDA---RIAEAEAE 209

                          90
                  ....*....|....*.
gi 1622157237 207 KKAAIISAEGDSKAAE 222
Cdd:COG2268   210 RETEIAIAQANREAEE 225
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 51-248 3.08e-05

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: 43.69  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  51 GEGTHFLIPWVQKPIIFDCRSRPRNVP---VITgsKDLQNVNITLRILFRpvtMQLPRIFTTIGEDYDE--RVLPSITte 125
Cdd:cd03403     6 GPGLFFILPCIDSYRKVDLRTVSFDVPpqeILT--KDSVTVAVDAVVYYR---VQNATIAVTNVENADRstRLLAQTT-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 126 iLKSVVARFDAGELITQRELVSRQVSEDLTERAATFGLILDDVSLthltfgKEFTEAVEMKQVAQQEAERARfivekaeq 205
Cdd:cd03403    79 -LRNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEI------KDVRLPVQLQRAMAAEAEAAR-------- 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622157237 206 QKKAAIISAEGDSK-------AAELIATSLSSVgdgliELRKLEAAEDIA 248
Cdd:cd03403   144 EARAKVIAAEGEQNasralkeAADVISESPAAL-----QLRYLQTLNTIS 188
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 12-227 1.35e-04

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: 42.50  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  12 LGLGLAVAGGVVnSALYNVDAGHRAVIFdRFRGVQDiVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITG--------SK 83
Cdd:cd03404     1 LILLLLLLVWLL-SGFYTVDPGERGVVL-RFGKYVR-TVGPGLHWKLPFPIEVVEKVNVTQVRSVEIGFRvpeeslmlTG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  84 DLQNVNITLRILFRpvtMQLPRIFTTIGEDYDErVLPSITTEILKSVVARFDAGELIT-QRELVSRQVSEDLTERAATF- 161
Cdd:cd03404    78 DENIVDVDFVVQYR---ISDPVAYLFNVRDPEE-TLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQEILDRYd 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622157237 162 -GLILDDVSLTHLTFGKEFTEAVEMKQVAQQEAERARF--------IVEKAEQQKKAAIISAEGDskAAELIATS 227
Cdd:cd03404   154 lGIEIVQVQLQDADPPEEVQDAFDDVNAARQDKERLINeaqayaneVIPRARGEAARIIQEAEAY--KAEVVARA 226
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 36-223 4.47e-04

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: 40.65  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237  36 AVIFDRFrGVQDIVVGEGTHFLIPWVQKpiIFD---CRSRPRNVPVITGSKDLQNVNITLRILFRPVTMQLPRIFTTIge 112
Cdd:cd03407     7 VAIVERF-GKFSRIAEPGLHFIIPPIES--VAGrvsLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYKL-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622157237 113 DYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSEDLTERAATFGLILDDVSLTHLTFGKEFTEAveMKQVaqQE 192
Cdd:cd03407    82 TNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAA--MNEI--NA 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622157237 193 AERARF-IVEKAEQQKKAAIISAEGDSKAAEL 223
Cdd:cd03407   158 AQRLREaAEEKAEAEKILQVKAAEAEAEAKRL 189
 
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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