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Conserved domains on  [gi|571491670|ref|XP_006592010|]
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prohibitin-1, mitochondrial isoform X1 [Glycine max]

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 ...
 37-231 2.83e-89

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


:

Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 263.61  E-value: 2.83e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  37 LYNVEGGHRAIVFNRVVGVKDKVYPEGTHIMIPLFERPVIYDVRARPHLVESTSGSRDLQMVKIGLRVLTRPVPDQLPTV 116
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 117 YRTLGENYNERVLPSIIHETLKAVVAQYNASQLITQRENVSREIRKILTQRASQFNIALDDVSITSLTFGKEFTAAIEAK 196
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 571491670 197 QVAAQEAERAKFVVEKAEQDKQSAVIRAQGEAKSA 231
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 ...
 37-231 2.83e-89

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 263.61  E-value: 2.83e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  37 LYNVEGGHRAIVFNRVVGVKDKVYPEGTHIMIPLFERPVIYDVRARPHLVESTSGSRDLQMVKIGLRVLTRPVPDQLPTV 116
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 117 YRTLGENYNERVLPSIIHETLKAVVAQYNASQLITQRENVSREIRKILTQRASQFNIALDDVSITSLTFGKEFTAAIEAK 196
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 571491670 197 QVAAQEAERAKFVVEKAEQDKQSAVIRAQGEAKSA 231
Cdd:cd03401  161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 36-197 3.04e-34

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 122.00  E-value: 3.04e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670    36 SLYNVEGGHRAIVFNRVVGVKDKVYPeGTHIMIPLFERPVIYDVRARPHLV-ESTSGSRDLQMVKIGLRVLTRpVPDQLP 114
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGP-GLHFLIPFIDDVKKVDLRAQTDDVpPQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670   115 TVYRTlgENYNERVLPSIIHETLKAVVAQYNASQLIT-QRENVSREIRKILTQRASQFNIALDDVSITSLTFGKEFTAAI 193
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 571491670   194 EAKQ 197
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 24-262 9.21e-32

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 118.79  E-value: 9.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  24 IIGGLVVYGAANSLYNVEGGHRAIV--FNRVVgvkdKVYPEGTHIMIPLFERPVIYDVRARPHLVESTSG-SRDLQMVKI 100
Cdd:COG0330    8 ILLVLVLVLLFSSVYIVPQGERGVVlrFGKYV----RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVlTKDNNIVDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 101 GLRVLTRpVPDQLPTVYRTlgENYNERVLPsIIHETLKAVVAQYNASQLI-TQRENVSREIRKILTQRASQFNIALDDVS 179
Cdd:COG0330   84 DAVVQYR-ITDPAKFLYNV--ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 180 ITSLTFGKEFTAAIEAKQVAAQEAERAKF-------------------VVEKAEQDKQSAVIRAQGEAKSAQLIGQAIAN 240
Cdd:COG0330  160 IKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAYSA 239

                        250       260
                 ....*....|....*....|..
gi 571491670 241 NPAFITLRKIEAAREIAQTISN 262
Cdd:COG0330  240 APFVLFYRSLEALEEVLSPNSK 261
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 40-217 1.06e-25

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 100.09  E-value: 1.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670   40 VEGGHRAIVFNRvvGVKDKVYPEGTHIMIPLFERPVIYDVRARPHLVES-TSGSRDLQMVKIGLRVLTRPVPDQLPTVYR 118
Cdd:pfam01145   3 VPPGEVGVVTRF--GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVqTVLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  119 TL-GENYNERVLPSIIHETLKAVVAQYNASQLITQRENVSREIRKILTQRASQFNIALDDVSITSLTFGKEFTAAIEAKQ 197
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 571491670  198 VAAQEAERAkfvVEKAEQDK 217
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 ...
 37-231 2.83e-89

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 263.61  E-value: 2.83e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  37 LYNVEGGHRAIVFNRVVGVKDKVYPEGTHIMIPLFERPVIYDVRARPHLVESTSGSRDLQMVKIGLRVLTRPVPDQLPTV 116
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 117 YRTLGENYNERVLPSIIHETLKAVVAQYNASQLITQRENVSREIRKILTQRASQFNIALDDVSITSLTFGKEFTAAIEAK 196
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 571491670 197 QVAAQEAERAKFVVEKAEQDKQSAVIRAQGEAKSA 231
Cdd:cd03401  161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 36-197 3.04e-34

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 122.00  E-value: 3.04e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670    36 SLYNVEGGHRAIVFNRVVGVKDKVYPeGTHIMIPLFERPVIYDVRARPHLV-ESTSGSRDLQMVKIGLRVLTRpVPDQLP 114
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGP-GLHFLIPFIDDVKKVDLRAQTDDVpPQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670   115 TVYRTlgENYNERVLPSIIHETLKAVVAQYNASQLIT-QRENVSREIRKILTQRASQFNIALDDVSITSLTFGKEFTAAI 193
Cdd:smart00244  79 AVYRV--LDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 571491670   194 EAKQ 197
Cdd:smart00244 157 EAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 24-262 9.21e-32

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 118.79  E-value: 9.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  24 IIGGLVVYGAANSLYNVEGGHRAIV--FNRVVgvkdKVYPEGTHIMIPLFERPVIYDVRARPHLVESTSG-SRDLQMVKI 100
Cdd:COG0330    8 ILLVLVLVLLFSSVYIVPQGERGVVlrFGKYV----RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVlTKDNNIVDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 101 GLRVLTRpVPDQLPTVYRTlgENYNERVLPsIIHETLKAVVAQYNASQLI-TQRENVSREIRKILTQRASQFNIALDDVS 179
Cdd:COG0330   84 DAVVQYR-ITDPAKFLYNV--ENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 180 ITSLTFGKEFTAAIEAKQVAAQEAERAKF-------------------VVEKAEQDKQSAVIRAQGEAKSAQLIGQAIAN 240
Cdd:COG0330  160 IKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIVAEAYSA 239

                        250       260
                 ....*....|....*....|..
gi 571491670 241 NPAFITLRKIEAAREIAQTISN 262
Cdd:COG0330  240 APFVLFYRSLEALEEVLSPNSK 261
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 40-217 1.06e-25

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 100.09  E-value: 1.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670   40 VEGGHRAIVFNRvvGVKDKVYPEGTHIMIPLFERPVIYDVRARPHLVES-TSGSRDLQMVKIGLRVLTRPVPDQLPTVYR 118
Cdd:pfam01145   3 VPPGEVGVVTRF--GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVqTVLTKDGVPVNVDVTVIYRVNPDDPPKLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  119 TL-GENYNERVLPSIIHETLKAVVAQYNASQLITQRENVSREIRKILTQRASQFNIALDDVSITSLTFGKEFTAAIEAKQ 197
Cdd:pfam01145  81 NVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 571491670  198 VAAQEAERAkfvVEKAEQDK 217
Cdd:pfam01145 161 TAEQEAEAE---IARAEAEA 177
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 88-187 6.98e-18

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: 77.40  E-value: 6.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  88 STSGSRDLQMVKIGLRVLTRPVPDQ-LPTVYRTLGENYNERVLPSIIHETLKAVVAQYNASQLITQRENVSREIRKILTQ 166
Cdd:cd02106   10 EPVGTADGVPVAVDLVVQFRITDYNaLPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVKEDLEE 89

                         90       100
                 ....*....|....*....|.
gi 571491670 167 RASQFNIALDDVSITSLTFGK 187
Cdd:cd02106   90 DLENFGVVISDVDITSIEPPD 110
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 36-256 3.24e-15

High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259803 [Multi-domain]  Cd Length: 249  Bit Score: 73.29  E-value: 3.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  36 SLYNVEGGHRAIV--FNRVVGVKDKvyPeGTHIMIPLFERPVIYDVRarphlVESTSGSRDlqmvkiglRVLTRpvpDQL 113
Cdd:cd03405    1 SVFIVDETEQAVVlqFGKPVRVITE--P-GLHFKLPFIQNVRKFDKR-----ILTLDGPPE--------EVLTK---DKK 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 114 PTV---------------YRTLGENYN-ERVLPSIIHETLKAVVAQYNASQLI-TQRENVSREIRKILTQRASQFNIALD 176
Cdd:cd03405   62 RLIvdsyarwritdplrfYQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVV 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 177 DVSITSLTFGKEFTAAI----------EAKQVAAQEAERAKFVveKAEQDKQSAVIRAQGEAKSAQLIGQAIA------- 239
Cdd:cd03405  142 DVRIKRIDLPEEVSESVyermraererIAAEYRAEGEEEAEKI--RAEADRERTVILAEAYREAEEIRGEGDAeaariya 219

                        250       260
                 ....*....|....*....|..
gi 571491670 240 ----NNPAFIT-LRKIEAAREI 256
Cdd:cd03405  220 eaygKDPEFYSfYRSLEAYRAS 241
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 96-258 1.19e-11

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: 62.15  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  96 QMVKIGLRVLTRPVPDQLP------TV-------YRTLG--------ENYNERVLpSIIHETLKAVVAQYNASQLITQRE 154
Cdd:cd08826    5 RMVRVDLRTVTLDVPPQEVitkdnvTVkvnavvyFRVVDpekavlavEDYRYATS-QLAQTTLRSVVGQVELDELLSERE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 155 NVSREIRKILTQRASQFNIALDDVSItsltfgKEFTAAIEAKQVAAQEAErakfvvekAEQDKQSAVIRAQGEAKSAQLI 234
Cdd:cd08826   84 EINKRIQEIIDEQTEPWGIKVTAVEI------KDVDLPESMQRAMARQAE--------AERERRAKIIKAEGELQAAEKL 149

                        170       180
                 ....*....|....*....|....*..
gi 571491670 235 GQA---IANNPAFITLRKIEAAREIAQ 258
Cdd:cd08826  150 AEAaeiLAKSPGALQLRYLQTLSEIAS 176
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 73-257 4.39e-10

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: 58.16  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  73 RPVIYDVRARPHLvestsgSRDLQMVKIGLRVLTRpVPDQLPTVYRTLGENYNERVLPSIiheTLKAVVAQYNASQLITQ 152
Cdd:cd13435   25 RTVSFDVPPQEVL------TKDSVTVTVDAVVYYR-ISDPLNAVIQVANYSHSTRLLAAT---TLRNVLGTRNLSELLTE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 153 RENVSREIRKILTQRASQFNIALDDVSITSLTFGKEFTAAIEAKQVAAQEAeRAKfvvekaeqdkqsaVIRAQGEAKSAQ 232
Cdd:cd13435   95 RETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREA-RAK-------------VIAAEGEMKSSR 160

                        170       180
                 ....*....|....*....|....*...
gi 571491670 233 LIGQA---IANNPAFITLRKIEAAREIA 257
Cdd:cd13435  161 ALKEAsdiISASPSALQLRYLQTLSSIS 188
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 136-266 9.76e-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: 48.76  E-value: 9.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 136 TLKAVVAQYNASQLITQRENVSREIRKILTQRASQFNIALDDVSITSLTFGKEFTAAIEAkqvAAQEAERAkfvvekaeq 215
Cdd:cd13437  100 TLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSS---AAKAKRIG--------- 167

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 571491670 216 dkQSAVIRAQGEAKSAQLIGQA--IANNPAFITLRKIEAareiAQTISNSANK 266
Cdd:cd13437  168 --ESKIISAKADVESAKLMREAadILDSKAAMQIRYLET----LQAIAKSANS 214
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 137-262 7.66e-06

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: 45.99  E-value: 7.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 137 LKAVVAQYNASQLITQRENVSREIRKILTQRASQFNIALDDVSITSLTFGKE----FTAAIEAKQVAAQEAERAKfvvek 212
Cdd:cd13438   95 LREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEireiLNQVLEAEKRAQANLIRAR----- 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 571491670 213 aeqdKQSAVIRAQgeAKSAQLigqaIANNPAFITLRKIEAAREIAQTISN 262
Cdd:cd13438  170 ----EETAATRSL--LNAAKL----MEENPALLRLRELEALEKIAEKVGH 209
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 48-240 3.06e-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: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  48 VFNRVVGvkdkvypEGTHIMIPLFERpVIYDVRARPHLVEST--SGSRDLQMVKIGLRVLTRPVPDQLPTVYRTLGenYN 125
Cdd:cd03407   15 KFSRIAE-------PGLHFIIPPIES-VAGRVSLRVQQLDVRveTKTKDNVFVTLVVSVQYRVVPEKVYDAFYKLT--NP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 126 ERVLPSIIHETLKAVVAQYNASQLITQRENVSREIRKILTQRASQFNIALDDVSITSLTFGKEFTAAIEAKQVAAQEAER 205
Cdd:cd03407   85 EQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRLREA 164

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 571491670 206 AkfvVEKAEQDKQSAVIRAQGEAKSAQLIGQAIAN 240
Cdd:cd03407  165 A---EEKAEAEKILQVKAAEAEAEAKRLQGVGIAE 196
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 112-257 1.13e-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: 42.15  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 112 QLPTVYRTLGENYNE--RVLPSIiheTLKAVVAQYNASQLITQRENVSREIRKILTQRASQFNIALDDVSITSLTFGKEF 189
Cdd:cd03403   55 QNATIAVTNVENADRstRLLAQT---TLRNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQL 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 571491670 190 TAAIEAKQVAAQEAeRAKfvvekaeqdkqsaVIRAQGEAKSAQLIGQA---IANNPAFITLRKIEAAREIA 257
Cdd:cd03403  132 QRAMAAEAEAAREA-RAK-------------VIAAEGEQNASRALKEAadvISESPAALQLRYLQTLNTIS 188
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 24-228 2.99e-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: 41.34  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  24 IIGGLVVYGAANSLYNVEGGHRAIV--FNRVVGVKDkvypEGTHIMIPL-FERPVIYDVRA-------RPHLVESTSGSR 93
Cdd:cd03404    2 ILLLLLLVWLLSGFYTVDPGERGVVlrFGKYVRTVG----PGLHWKLPFpIEVVEKVNVTQvrsveigFRVPEESLMLTG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  94 DLQMVKIGLRVLTRpVPDQLPTVYRTlgENYnERVLPSIIHETLKAVVAQYNASQLIT-QRENVSREIRKILTQRASQFN 172
Cdd:cd03404   78 DENIVDVDFVVQYR-ISDPVAYLFNV--RDP-EETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQEILDRYD 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 571491670 173 --IALDDVSITSLTFGKEFTAAIEAKQVAAQEAERAKF-------------------VVEKAEQDKQSAVIRAQGEA 228
Cdd:cd03404  154 lgIEIVQVQLQDADPPEEVQDAFDDVNAARQDKERLINeaqayaneviprargeaarIIQEAEAYKAEVVARAEGDA 230
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 136-260 4.70e-04

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: 40.30  E-value: 4.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 136 TLKAVVAQYNASQLITQRENVSREIRKILTQRASQFNIALDDVSITSLTFGKEFTAAIEAKqvaAQeaerakfvvekAEQ 215
Cdd:cd13775   57 ALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSRE---AQ-----------AER 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 571491670 216 DKQSAVIRAQGEAKSAQLIGQA---IANNPAFITLRKI----EAAREIAQTI 260
Cdd:cd13775  123 EKNARVILAEAEKEIAEMFVEAaevYENNPIALQLRAMnmlyEGLKEKGSMV 174
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
12-255 1.14e-03

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: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  12 PGGGVAALLKVSIIGGLVVYGAANSLYNVEGGHRAIVFNRVVGvKDKVYPEGTHIMIPLFERPVIYDVRARPHLVESTSG 91
Cdd:COG2268    2 ETLGILIIIGVIVVVLLLLLIILARFYRKVPPNEALVITGRGG-GYKVVTGGGAFVLPVLHRAERMSLSTMTIEVERTEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670  92 SRDLQ----------MVKIGlrvltrPVPDQLPTVYRTLGE---NYNERVLPSIIHETLKAVVAQYNASQLITQRENVSR 158
Cdd:COG2268   81 LITKDgirvdvdavfYVKVN------SDPEDIANAAERFLGrdpEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 159 EIRKILTQRASQFNIALDDVSITSLT--------FGKEFTAAIEAKQ-VAAQEAERAKfVVEKAEQDKQSAVIRAQGEAK 229
Cdd:COG2268  155 KVQEVAGTDLAKNGLELESVAITDLEdennyldaLGRRKIAEIIRDArIAEAEAERET-EIAIAQANREAEEAELEQERE 233

                        250       260
                 ....*....|....*....|....*.
gi 571491670 230 SAQLIgqaIANNPAFITLRKIEAARE 255
Cdd:COG2268  234 IETAR---IAEAEAELAKKKAEERRE 256
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
135-261 1.92e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.47  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 135 ETLKAVVAQYNAS-QLITQRENVSREIRKILTQRA--SQFNIALDDVSITSLTFGKEFTAAIEAKQVAAQEAERAKFVVE 211
Cdd:COG2268  233 EIETARIAEAEAElAKKKAEERREAETARAEAEAAyeIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRK 312

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 571491670 212 KAEQDKQSAVIRAQGEAKSAQLIGQAIA------------NNPAFITLRKIEAAREIAQTIS 261
Cdd:COG2268  313 PAEAEKQAAEAEAEAEAEAIRAKGLAEAegkralaeawnkLGDAAILLMLIEKLPEIAEAAA 374
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 136-216 3.07e-03

Slipin-3 (SLP-3), 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 vertebrates. 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 slipin subgroup remain uncharacterized, except for Caenorhabditis elegans UNC-1. Mutations in the unc-1 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259810 [Multi-domain]  Cd Length: 154  Bit Score: 37.32  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571491670 136 TLKAVVAQYNASQLITQRENVSREIRKILTQRASQFNIALDDVSITSLTFGKEFTAAIEAKQVAAQEAeRAKFVVEKAEQ 215
Cdd:cd08828   74 TLRNVLGTQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREA-RAKVVAAEGEM 152


                 .
gi 571491670 216 D 216
Cdd:cd08828  153 N 153
 
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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