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Conserved domains on  [gi|665408704|ref|NP_001163012|]
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prohibitin 1, isoform D [Drosophila melanogaster]

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 6.02e-93

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: 272.46  E-value: 6.02e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  27 LYNVEGGHRAVIFDRFTGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVITGSKDLQNVNITLRILYRPIPDQLPKI 106
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 107 YTILGQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMK 186
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 665408704 187 QVAQQEAEKARFVVEKAEQQKLASIISAEGDAEAA 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 6.02e-93

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: 272.46  E-value: 6.02e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  27 LYNVEGGHRAVIFDRFTGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVITGSKDLQNVNITLRILYRPIPDQLPKI 106
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 107 YTILGQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMK 186
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 665408704 187 QVAQQEAEKARFVVEKAEQQKLASIISAEGDAEAA 221
Cdd:cd03401  161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 26-187 5.71e-34

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 120.84  E-value: 5.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704    26 ALYNVEGGHRAVIFDRFTGIKEnVVGEGTHFFIPWVQRPIIFDIRSQPRNVP-VITGSKDLQNVNITLRILYRpIPDQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704   105 KIYTILgqDYDERVLPSIAPEVLKAVVAQFDAGELIT-QREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAV 183
Cdd:smart00244  79 AVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 665408704   184 EMKQ 187
Cdd:smart00244 157 EAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-207 6.10e-33

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: 118.58  E-value: 6.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704   30 VEGGHRAVIFDrfTGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVIT-GSKDLQNVNITLRILYRPIPDQLPKIY- 107
Cdd:pfam01145   3 VPPGEVGVVTR--FGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVq 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  108 TILGQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMKQ 187
Cdd:pfam01145  81 NVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 665408704  188 VAQQEAEKArfvVEKAEQQK 207
Cdd:pfam01145 161 TAEQEAEAE---IARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 7-248 3.75e-31

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 116.86  E-value: 3.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704   7 NRIGQMGLGVAVLGGVVNSALYNVEGGHRAVIFdRFTGIKEnVVGEGTHFFIPWVQRPIIFDIRSQPRNVP---VITgsK 83
Cdd:COG0330    1 NKLILLLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVR-TLEPGLHFKIPFIDRVRKVDVREQVLDVPpqeVLT--K 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  84 DLQNVNITLRILYRpIPDqlPKIYTILGQDYDERVLPsIAPEVLKAVVAQFDAGELI-TQREMVSQRVSQELTVRAKQFG 162
Cdd:COG0330   77 DNNIVDVDAVVQYR-ITD--PAKFLYNVENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 163 FILDDISLTHLTFGREFTLAVEMKQVAQQEAEKARF-------------------VVEKAEQQKLASIISAEGDAEAAGL 223
Cdd:COG0330  153 IEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRI 232

                        250       260
                 ....*....|....*....|....*
gi 665408704 224 LAKSFGEAGDgLVELRRIEAAEDIA 248
Cdd:COG0330  233 VAEAYSAAPF-VLFYRSLEALEEVL 256
PRK11029 PRK11029
protease modulator HflC;
190-245 4.84e-05

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 43.96  E-value: 4.84e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408704 190 QQEAEKARFVVEK------AEQQKLASIISAEGDAEAAGLLAKSFGEAGDGLVELRRIEAAE 245
Cdd:PRK11029 243 QEEAEKLRATADYevtrtlAEAERQGRIMRGEGDAEAAKLFADAFSQDPDFYAFIRSLRAYE 304
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 27-221 6.02e-93

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: 272.46  E-value: 6.02e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  27 LYNVEGGHRAVIFDRFTGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVITGSKDLQNVNITLRILYRPIPDQLPKI 106
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 107 YTILGQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMK 186
Cdd:cd03401   81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 665408704 187 QVAQQEAEKARFVVEKAEQQKLASIISAEGDAEAA 221
Cdd:cd03401  161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
 26-187 5.71e-34

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 120.84  E-value: 5.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704    26 ALYNVEGGHRAVIFDRFTGIKEnVVGEGTHFFIPWVQRPIIFDIRSQPRNVP-VITGSKDLQNVNITLRILYRpIPDQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704   105 KIYTILgqDYDERVLPSIAPEVLKAVVAQFDAGELIT-QREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAV 183
Cdd:smart00244  79 AVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156


                   ....
gi 665408704   184 EMKQ 187
Cdd:smart00244 157 EAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-207 6.10e-33

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: 118.58  E-value: 6.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704   30 VEGGHRAVIFDrfTGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVIT-GSKDLQNVNITLRILYRPIPDQLPKIY- 107
Cdd:pfam01145   3 VPPGEVGVVTR--FGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPKLVq 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  108 TILGQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMKQ 187
Cdd:pfam01145  81 NVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQ 160

                         170       180
                  ....*....|....*....|
gi 665408704  188 VAQQEAEKArfvVEKAEQQK 207
Cdd:pfam01145 161 TAEQEAEAE---IARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 7-248 3.75e-31

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 116.86  E-value: 3.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704   7 NRIGQMGLGVAVLGGVVNSALYNVEGGHRAVIFdRFTGIKEnVVGEGTHFFIPWVQRPIIFDIRSQPRNVP---VITgsK 83
Cdd:COG0330    1 NKLILLLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVR-TLEPGLHFKIPFIDRVRKVDVREQVLDVPpqeVLT--K 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  84 DLQNVNITLRILYRpIPDqlPKIYTILGQDYDERVLPsIAPEVLKAVVAQFDAGELI-TQREMVSQRVSQELTVRAKQFG 162
Cdd:COG0330   77 DNNIVDVDAVVQYR-ITD--PAKFLYNVENAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 163 FILDDISLTHLTFGREFTLAVEMKQVAQQEAEKARF-------------------VVEKAEQQKLASIISAEGDAEAAGL 223
Cdd:COG0330  153 IEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILeaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRI 232

                        250       260
                 ....*....|....*....|....*
gi 665408704 224 LAKSFGEAGDgLVELRRIEAAEDIA 248
Cdd:COG0330  233 VAEAYSAAPF-VLFYRSLEALEEVL 256
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 26-230 6.51e-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: 75.22  E-value: 6.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  26 ALYNVEGGHRAVIFdRFTGIKENVVGEGTHFFIPWVQRPIIFDIR-----SQPRNVPvitgSKDLQNVNITLRILYRpIP 100
Cdd:cd03405    1 SVFIVDETEQAVVL-QFGKPVRVITEPGLHFKLPFIQNVRKFDKRiltldGPPEEVL----TKDKKRLIVDSYARWR-IT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 101 DQLpKIYTILGQDYD-ERVLPSIAPEVLKAVVAQFDAGELI-TQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGRE 178
Cdd:cd03405   75 DPL-RFYQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEE 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408704 179 FTLAV------EMKQVAQQ--------------EAEKARfVVEKAEQQKLASIISAEGDAEAAGLLAKSFGE 230
Cdd:cd03405  154 VSESVyermraERERIAAEyraegeeeaekiraEADRER-TVILAEAYREAEEIRGEGDAEAARIYAEAYGK 224
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 59-248 4.03e-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: 4.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  59 PWVQRPIIFDIRSQPRNVP---VITgsKDlqnvNITLRI---LYRPIPDQLPKIYTIlgQDYDERVLpSIAPEVLKAVVA 132
Cdd:cd08826    1 PFIDRMVRVDLRTVTLDVPpqeVIT--KD----NVTVKVnavVYFRVVDPEKAVLAV--EDYRYATS-QLAQTTLRSVVG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 133 QFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLthltfgREFTLAVEMKQVAQQEAEkarfvvekAEQQKLASII 212
Cdd:cd08826   72 QVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEI------KDVDLPESMQRAMARQAE--------AERERRAKII 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 665408704 213 SAEGDAEAAGLLAksfgEAGD------GLVELRRIEAAEDIA 248
Cdd:cd08826  138 KAEGELQAAEKLA----EAAEilakspGALQLRYLQTLSEIA 175
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 51-248 3.62e-09

Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in arthropods. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this divergent slipin subgroup remain largely uncharacterized. It contains Drosophila Mec2, the gene for which was identified in a screen for genes required for nephrocyte function; it may function together with Sns in maintaining nephrocyte diaphragm.


Pssm-ID: 259813 [Multi-domain]  Cd Length: 208  Bit Score: 55.47  E-value: 3.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  51 GEGTHFFIPWVQRPIIFDIRSQPRNVP---VITgsKDLQNVNITLRILYRpIPDQLPKIYTILGQDYDERVLpsiAPEVL 127
Cdd:cd13435    6 GPGVFFVLPCIDNYCKVDLRTVSFDVPpqeVLT--KDSVTVTVDAVVYYR-ISDPLNAVIQVANYSHSTRLL---AATTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 128 KAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLthltfgREFTLAVEMKQVAQQEAEKARfvvekaeqQK 207
Cdd:cd13435   80 RNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEI------KDVSLPDSLQRAMAAEAEAAR--------EA 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 665408704 208 LASIISAEGDAEAAGLL--AKSFGEAGDGLVELRRIEAAEDIA 248
Cdd:cd13435  146 RAKVIAAEGEMKSSRALkeASDIISASPSALQLRYLQTLSSIS 188
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 28-224 3.49e-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: 3.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  28 YNVEGGHRAVI--FDRFtgikENVVGEGTHFFIPWVQRPIIFDIRSQPRNVP---VITgsKDLQNVNITLRILYRpIPDQ 102
Cdd:cd13437    7 KQVKQGSVGLVerFGKF----YKTVDPGLHKVNPCTEKIIQVDMKTQVIDLPrqsVMT--KDNVSVTIDSVVYYR-IIDP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 103 LPKIYTIlgQDYDERVLpSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFtla 182
Cdd:cd13437   80 YKAIYRI--DNVKQALI-ERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDL--- 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 665408704 183 vemkqvaQQEAEKArfvvekAEQQKLAS--IISAEGDAEAAGLL 224
Cdd:cd13437  154 -------QQSLSSA------AKAKRIGEskIISAKADVESAKLM 184
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
9-221 9.15e-08

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 52.57  E-value: 9.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704   9 IGQMGLGVAVLGGVVNSALYNVEGGHRAVIFDRFTGIKenVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVITG--SKDLQ 86
Cdd:COG2268   10 IGVIVVVLLLLLIILARFYRKVPPNEALVITGRGGGYK--VVTGGGAFVLPVLHRAERMSLSTMTIEVERTEGliTKDGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  87 NVNI----TLRIlyRPIPDQLPK-IYTILGQDYDE--RVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAK 159
Cdd:COG2268   88 RVDVdavfYVKV--NSDPEDIANaAERFLGRDPEEieELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLA 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408704 160 QFGFILDDISLTHLTFGREFTLAVEMKQVAQ--QEAEKARfvvekAEQQKLASIISAEGDAEAA 221
Cdd:COG2268  166 KNGLELESVAITDLEDENNYLDALGRRKIAEiiRDARIAE-----AEAERETEIAIAQANREAE 224
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 36-240 1.89e-07

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: 51.05  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  36 AVIFDRFtGIKENVVGEGTHFFIPWVQRpiIFD---IRSQPRNVPVITGSKDLQNVNITLRILYRPIPDQLPKIYTILgq 112
Cdd:cd03407    7 VAIVERF-GKFSRIAEPGLHFIIPPIES--VAGrvsLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYKL-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 113 DYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMKQVAQQE 192
Cdd:cd03407   82 TNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 665408704 193 AEKArfvVEKAEQQKLASIISAEGDAEAAGLlaksfgeAGDGLVELRR 240
Cdd:cd03407  162 REAA---EEKAEAEKILQVKAAEAEAEAKRL-------QGVGIAEQRK 199
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 70-173 2.25e-07

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: 48.13  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  70 RSQPRNVPVIT-GSKDLQNVNITLRILYRPIPDQ-LPKIYTILGQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVS 147
Cdd:cd02106    1 RPQFDDVRVEPvGTADGVPVAVDLVVQFRITDYNaLPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                         90       100
                 ....*....|....*....|....*.
gi 665408704 148 QRVSQELTVRAKQFGFILDDISLTHL 173
Cdd:cd02106   81 KAVKEDLEEDLENFGVVISDVDITSI 106
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 12-253 6.74e-06

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: 46.35  E-value: 6.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  12 MGLGVAVLGGVVnSALYNVEGGHRAVIFdRFtGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVITG--------SK 83
Cdd:cd03404    1 LILLLLLLVWLL-SGFYTVDPGERGVVL-RF-GKYVRTVGPGLHWKLPFPIEVVEKVNVTQVRSVEIGFRvpeeslmlTG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  84 DLQNVNITLRILYRpIPDqlPKIYTILGQDYDErVLPSIAPEVLKAVVAQFDAGELIT-QREMVSQRVSQELTVrakqfg 162
Cdd:cd03404   78 DENIVDVDFVVQYR-ISD--PVAYLFNVRDPEE-TLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQE------ 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 163 fILDD----ISLThltfgreftlAVEMKQVAQQEAEKARFV-VEKAEQQKLASIisAEGDAEAAGLLAKSFGEAgdglve 237
Cdd:cd03404  148 -ILDRydlgIEIV----------QVQLQDADPPEEVQDAFDdVNAARQDKERLI--NEAQAYANEVIPRARGEA------ 208

                        250
                 ....*....|....*.
gi 665408704 238 LRRIEAAEdiAYQLSR 253
Cdd:cd03404  209 ARIIQEAE--AYKAEV 222
PRK11029 PRK11029
protease modulator HflC;
190-245 4.84e-05

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 43.96  E-value: 4.84e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665408704 190 QQEAEKARFVVEK------AEQQKLASIISAEGDAEAAGLLAKSFGEAGDGLVELRRIEAAE 245
Cdd:PRK11029 243 QEEAEKLRATADYevtrtlAEAERQGRIMRGEGDAEAAKLFADAFSQDPDFYAFIRSLRAYE 304
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 30-248 6.47e-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: 42.91  E-value: 6.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704  30 VEGGHRAVIFdrFTGIKENVVGEGTHFFipW-VQRPI---IFDIRSQprnVPVITG----SKDLQNVNITLRILYRpIPD 101
Cdd:cd13438    1 VPPGERGLLY--RDGKLVRTLEPGRYAF--WkFGRKVqveLVDLREQ---LLEVSGqeilTADKVALRVNLVATYR-VVD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 102 qlPKIYTILGQDYDErVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLthltfgREFTL 181
Cdd:cd13438   73 --PVKAVETVDDPEE-QLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGV------KDIIL 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665408704 182 AVEMKQVAQQEAEkarfvvekAEQQKLASIISAEG-------DAEAAGLLaksfgEAGDGLVELRRIEAAEDIA 248
Cdd:cd13438  144 PGEIREILNQVLE--------AEKRAQANLIRAREetaatrsLLNAAKLM-----EENPALLRLRELEALEKIA 204
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
177-248 3.49e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.32  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665408704 177 REFTLAVEMKQVAQQEAEKARFVVEKAEQQKLASIISAEGDAEAAG-----------LLAKSFGEAGDGLVELRRIEAAE 245
Cdd:COG2268  288 REREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRakglaeaegkrALAEAWNKLGDAAILLMLIEKLP 367


                 ...
gi 665408704 246 DIA 248
Cdd:COG2268  368 EIA 370
 
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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