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Conserved domains on  [gi|15219569|ref|NP_171882|]
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prohibitin 2 [Arabidopsis thaliana]

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 ...
 36-230 4.47e-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: 265.53  E-value: 4.47e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569  36 LYNVDGGHRAVMFNRLTGIKEKVYPEGTHFMVPWFERPIIYDVRARPYLVESTTGSHDLQMVKIGLRVLTRPMGDRLPQI 115
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 116 YRTLGENYSERVLPSIIHETLKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSITTLTFGKEFTAAIEAK 195
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15219569 196 QVAAQEAERAKFIVEKAEQDRRSAVIRAQGEAKSA 230
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 ...
 36-230 4.47e-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: 265.53  E-value: 4.47e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569  36 LYNVDGGHRAVMFNRLTGIKEKVYPEGTHFMVPWFERPIIYDVRARPYLVESTTGSHDLQMVKIGLRVLTRPMGDRLPQI 115
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 116 YRTLGENYSERVLPSIIHETLKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSITTLTFGKEFTAAIEAK 195
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15219569 196 QVAAQEAERAKFIVEKAEQDRRSAVIRAQGEAKSA 230
Cdd:cd03401 161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 35-196 1.09e-36

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 128.16  E-value: 1.09e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569     35 SLYNVDGGHRAVMFNRLTGIKEKVYPeGTHFMVPWFERPIIYDVRARPYLV-ESTTGSHDLQMVKIGLRVLTRpMGDRLP 113
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGP-GLHFLIPFIDDVKKVDLRAQTDDVpPQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569    114 QIYRTlgENYSERVLPSIIHETLKAVVAQYNASQLIT-QREAVSREIRKILTERASNFDIALDDVSITTLTFGKEFTAAI 192
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 15219569    193 EAKQ 196
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 23-256 2.22e-30

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 114.94  E-value: 2.22e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569  23 VIGGLGVYALTNSLYNVDGGHRAVMFnRLtGIKEKVYPEGTHFMVPWFERPIIYDVRARPYLVESTTG-SHDLQMVKIGL 101
Cdd:COG0330   8 ILLVLVLVLLFSSVYIVPQGERGVVL-RF-GKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVlTKDNNIVDVDA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 102 RVLTRPMGdrLPQIYRTLgENYSERVLPsIIHETLKAVVAQYNASQLI-TQREAVSREIRKILTERASNFDIALDDVSIT 180
Cdd:COG0330  86 VVQYRITD--PAKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIK 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 181 TLTFGKEFTAAIEAKQVAAQEAERAKF-------------------IVEKAEQDRRSAVIRAQGEAKSAQLIGQAIANNQ 241
Cdd:COG0330 162 DIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAP 241

                       250
                ....*....|....*
gi 15219569 242 AFITLRKIEAAREIA 256
Cdd:COG0330 242 FVLFYRSLEALEEVL 256
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 39-216 5.66e-27

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: 103.56  E-value: 5.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569    39 VDGGHRAVMFNrlTGIKEKVYPEGTHFMVPWFERPIIYDVRARPYLVES-TTGSHDLQMVKIGLRVLTRPMGDRLPQIYR 117
Cdd:pfam01145   3 VPPGEVGVVTR--FGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVqTVLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569   118 TL-GENYSERVLPSIIHETLKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSITTLTFGKEFTAAIEAKQ 196
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 15219569   197 VAAQEAERAkfiVEKAEQDR 216
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 ...
 36-230 4.47e-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: 265.53  E-value: 4.47e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569  36 LYNVDGGHRAVMFNRLTGIKEKVYPEGTHFMVPWFERPIIYDVRARPYLVESTTGSHDLQMVKIGLRVLTRPMGDRLPQI 115
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 116 YRTLGENYSERVLPSIIHETLKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSITTLTFGKEFTAAIEAK 195
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                       170       180       190
                ....*....|....*....|....*....|....*
gi 15219569 196 QVAAQEAERAKFIVEKAEQDRRSAVIRAQGEAKSA 230
Cdd:cd03401 161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 35-196 1.09e-36

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 128.16  E-value: 1.09e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569     35 SLYNVDGGHRAVMFNRLTGIKEKVYPeGTHFMVPWFERPIIYDVRARPYLV-ESTTGSHDLQMVKIGLRVLTRpMGDRLP 113
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGP-GLHFLIPFIDDVKKVDLRAQTDDVpPQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569    114 QIYRTlgENYSERVLPSIIHETLKAVVAQYNASQLIT-QREAVSREIRKILTERASNFDIALDDVSITTLTFGKEFTAAI 192
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 15219569    193 EAKQ 196
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 23-256 2.22e-30

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 114.94  E-value: 2.22e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569  23 VIGGLGVYALTNSLYNVDGGHRAVMFnRLtGIKEKVYPEGTHFMVPWFERPIIYDVRARPYLVESTTG-SHDLQMVKIGL 101
Cdd:COG0330   8 ILLVLVLVLLFSSVYIVPQGERGVVL-RF-GKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVlTKDNNIVDVDA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 102 RVLTRPMGdrLPQIYRTLgENYSERVLPsIIHETLKAVVAQYNASQLI-TQREAVSREIRKILTERASNFDIALDDVSIT 180
Cdd:COG0330  86 VVQYRITD--PAKFLYNV-ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIK 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 181 TLTFGKEFTAAIEAKQVAAQEAERAKF-------------------IVEKAEQDRRSAVIRAQGEAKSAQLIGQAIANNQ 241
Cdd:COG0330 162 DIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAP 241

                       250
                ....*....|....*
gi 15219569 242 AFITLRKIEAAREIA 256
Cdd:COG0330 242 FVLFYRSLEALEEVL 256
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 39-216 5.66e-27

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: 103.56  E-value: 5.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569    39 VDGGHRAVMFNrlTGIKEKVYPEGTHFMVPWFERPIIYDVRARPYLVES-TTGSHDLQMVKIGLRVLTRPMGDRLPQIYR 117
Cdd:pfam01145   3 VPPGEVGVVTR--FGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVqTVLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569   118 TL-GENYSERVLPSIIHETLKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSITTLTFGKEFTAAIEAKQ 196
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 15219569   197 VAAQEAERAkfiVEKAEQDR 216
Cdd:pfam01145 161 TAEQEAEAE---IARAEAEA 177
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 77-186 6.56e-19

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: 80.10  E-value: 6.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569  77 DVRARPYLVEsTTGSHDLQMVKIGLRVLTRPM-GDRLPQIYRTLGENYSERVLPSIIHETLKAVVAQYNASQLITQREAV 155
Cdd:cd02106   1 RPQFDDVRVE-PVGTADGVPVAVDLVVQFRITdYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEI 79

                        90       100       110
                ....*....|....*....|....*....|.
gi 15219569 156 SREIRKILTERASNFDIALDDVSITTLTFGK 186
Cdd:cd02106  80 AKAVKEDLEEDLENFGVVISDVDITSIEPPD 110
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 35-238 2.25e-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: 76.76  E-value: 2.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569  35 SLYNVDGGHRAVMFnRLTGIKEKVYPEGTHFMVPWFERPIIYDVRARPYLVESTtgshdlqmvkiglRVLTRpmgDRLP- 113
Cdd:cd03405   1 SVFIVDETEQAVVL-QFGKPVRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPE-------------EVLTK---DKKRl 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 114 --------QI------YRTLG-ENYSERVLPSIIHETLKAVVAQYNASQLI-TQREAVSREIRKILTERASNFDIALDDV 177
Cdd:cd03405  64 ivdsyarwRItdplrfYQSVGgEEGAESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDV 143

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15219569 178 SITTLTFGKEFTAAI----------EAKQVAAQEAERAKFIveKAEQDRRSAVIRAQGEAKSAQLIGQAIA 238
Cdd:cd03405 144 RIKRIDLPEEVSESVyermraererIAAEYRAEGEEEAEKI--RAEADRERTVILAEAYREAEEIRGEGDA 212
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 135-257 4.59e-10

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: 57.52  E-value: 4.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 135 TLKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSIttltfgKEFTAAIEAKQVAAQEAErakfivekAEQ 214
Cdd:cd08826  65 TLRSVVGQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEI------KDVDLPESMQRAMARQAE--------AER 130

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15219569 215 DRRSAVIRAQGEAKSAQLIGQA---IANNQAFITLRKIEAAREIAQ 257
Cdd:cd08826 131 ERRAKIIKAEGELQAAEKLAEAaeiLAKSPGALQLRYLQTLSEIAS 176
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 62-256 9.41e-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: 54.31  E-value: 9.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569  62 GTHFMVPWFERPIIYDVRARPYLV-ESTTGSHDLQMVKIGLRVLTRpMGDRLPQIYRTLGENYSERVLPSIiheTLKAVV 140
Cdd:cd13435   8 GVFFVLPCIDNYCKVDLRTVSFDVpPQEVLTKDSVTVTVDAVVYYR-ISDPLNAVIQVANYSHSTRLLAAT---TLRNVL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 141 AQYNASQLITQREAVSREIRKILTERASNFDIALDDVSIttltfgKEFTAAIEAKQVAAQEAERAKfivekaeqDRRSAV 220
Cdd:cd13435  84 GTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEI------KDVSLPDSLQRAMAAEAEAAR--------EARAKV 149

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15219569 221 IRAQGEAKSAQLIGQA---IANNQAFITLRKIEAAREIA 256
Cdd:cd13435 150 IAAEGEMKSSRALKEAsdiISASPSALQLRYLQTLSSIS 188
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 23-253 1.35e-07

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: 51.36  E-value: 1.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569  23 VIGGLGVYALTnSLYNVDGGHRAV--MFNRLTGIKEkvypEGTHFMVPW-FERPIIYDVRA-------RPYLVESTTGSH 92
Cdd:cd03404   3 LLLLLLVWLLS-GFYTVDPGERGVvlRFGKYVRTVG----PGLHWKLPFpIEVVEKVNVTQvrsveigFRVPEESLMLTG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569  93 DLQMVKIGLRVltrpmgdrlpqIYR-TLGENY------SERVLPSIIHETLKAVVAQYNASQLIT-QREAVSREIRKILT 164
Cdd:cd03404  78 DENIVDVDFVV-----------QYRiSDPVAYlfnvrdPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQ 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 165 ERASNFD--IALDDVSITTLTFGKEFTAAIEAKQVAAQEAERAkfiVEKAEQDRRSAVIRAQGEAksAQLIGQAIANNQA 242
Cdd:cd03404 147 EILDRYDlgIEIVQVQLQDADPPEEVQDAFDDVNAARQDKERL---INEAQAYANEVIPRARGEA--ARIIQEAEAYKAE 221

                       250
                ....*....|.
gi 15219569 243 FITLRKIEAAR 253
Cdd:cd03404 222 VVARAEGDAAR 232
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 135-265 2.80e-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: 50.31  E-value: 2.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 135 TLKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSITTLTFGKEFTAAIEakqvAAQEAERakfiveKAEq 214
Cdd:cd13437 100 TLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLS----SAAKAKR------IGE- 168

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15219569 215 drrSAVIRAQGEAKSAQLIGQA--IANNQAFITLRKIEAareiAQTIAQSANK 265
Cdd:cd13437 169 ---SKIISAKADVESAKLMREAadILDSKAAMQIRYLET----LQAIAKSANS 214
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 136-259 5.52e-05

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria. 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: 43.29  E-value: 5.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 136 LKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSITTLTFGKE----FTAAIEAKQVAAQEAERAkfiveK 211
Cdd:cd13438  95 LREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEireiLNQVLEAEKRAQANLIRA-----R 169

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15219569 212 AEqdrrSAVIRAQgeAKSAQLigqaIANNQAFITLRKIEAAREIAQTI 259
Cdd:cd13438 170 EE----TAATRSL--LNAAKL----MEENPALLRLRELEALEKIAEKV 207
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
134-254 4.37e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.40  E-value: 4.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 134 ETLKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSITTLT--------FGKEFTAAIEAKQ-VAAQEAER 204
Cdd:COG2268 131 GALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEdennyldaLGRRKIAEIIRDArIAEAEAER 210

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15219569 205 AKfIVEKAEQDRRSAVIRAQGEAKSAQLIgqaIANNQAFITLRKIEAARE 254
Cdd:COG2268 211 ET-EIAIAQANREAEEAELEQEREIETAR---IAEAEAELAKKKAEERRE 256
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 48-244 5.78e-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: 5.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569  48 FNRLTGikekvypEGTHFMVPWFERpIIYDVRARPYLVEST--TGSHDLQMVKIGLRVLTRPMGDRLPQIYRTLGenYSE 125
Cdd:cd03407  16 FSRIAE-------PGLHFIIPPIES-VAGRVSLRVQQLDVRveTKTKDNVFVTLVVSVQYRVVPEKVYDAFYKLT--NPE 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 126 RVLPSIIHETLKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSITTLTFGKEFTAAIEAKQVAAQEAERA 205
Cdd:cd03407  86 QQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRLREAA 165

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15219569 206 kfiVEKAEQDRRSAVIRAQGEAKSAQLIGQAIANN-QAFI 244
Cdd:cd03407 166 ---EEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQrKAIV 202
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
186-266 9.58e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 40.24  E-value: 9.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 186 KEFTAAIEAKQVAAQEAERAKFIVEKAEQDRRSAVIRAQGEAKSAQLIGQAIA------------NNQAFITLRKIEAAR 253
Cdd:COG2268 288 REREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAegkralaeawnkLGDAAILLMLIEKLP 367

                        90
                ....*....|...
gi 15219569 254 EIAQTIAQSANKV 266
Cdd:COG2268 368 EIAEAAAKPLEKI 380
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 122-256 1.32e-03

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: 39.07  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 122 NYSERVLPSIiheTLKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSITTLTFGKEFTAAIEAKQVAAQE 201
Cdd:cd03403  68 DRSTRLLAQT---TLRNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAARE 144

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15219569 202 AeRAKfivekaeqdrrsaVIRAQGEAKSAQLIGQA---IANNQAFITLRKIEAAREIA 256
Cdd:cd03403 145 A-RAK-------------VIAAEGEQNASRALKEAadvISESPAALQLRYLQTLNTIS 188
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 121-215 5.05e-03

Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of the SPFH family (stomatin, prohibitin, flotillin, and HflK/C); 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.


Pssm-ID: 259817 [Multi-domain]  Cd Length: 177  Bit Score: 37.22  E-value: 5.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219569 121 ENYSERVlpSIIHET-LKAVVAQYNASQLITQREAVSREIRKILTERASNFDIALDDVSITTLTFGKEFTAAIeAKQVAA 199
Cdd:cd13775  44 EDYRAAV--SLAAQTaLRDAIGRSELAELLSRREQIDEELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAM-SREAQA 120

                        90
                ....*....|....*.
gi 15219569 200 QEAERAKFIVEKAEQD 215
Cdd:cd13775 121 EREKNARVILAEAEKE 136
 
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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