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Conserved domains on  [gi|24585145|ref|NP_724165|]
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lethal (2) 37Cc, isoform A [Drosophila melanogaster]

Protein Classification

SPFH_prohibitin domain-containing protein (domain architecture ID 10130412)

SPFH_prohibitin domain-containing protein

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 2.02e-91

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


:

Pssm-ID: 259799  Cd Length: 195  Bit Score: 272.46  E-value: 2.02e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  27 LYNVEGGHRAVIFDRFTGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVITGSKDLQNVNITLRILYRPIPDQLPKI 106
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145 107 YTILGQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMK 186
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 24585145 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 2.02e-91

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


Pssm-ID: 259799  Cd Length: 195  Bit Score: 272.46  E-value: 2.02e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  27 LYNVEGGHRAVIFDRFTGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVITGSKDLQNVNITLRILYRPIPDQLPKI 106
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145 107 YTILGQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMK 186
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 24585145 187 QVAQQEAEKARFVVEKAEQQKLASIISAEGDAEAA 221
Cdd:cd03401 161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
26-187 4.61e-33

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581  Cd Length: 160  Bit Score: 120.84  E-value: 4.61e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145     26 ALYNVEGGHRAVIFDRFTGIKEnVVGEGTHFFIPWVQRPIIFDIRSQPRNVP-VITGSKDLQNVNITLRILYRpIPDQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145    105 KIYTILgqDYDERVLPSIAPEVLKAVVAQFDAGELIT-QREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAV 183
Cdd:smart00244  79 AVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156

                   ....
gi 24585145    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 2.55e-30

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: 307341  Cd Length: 177  Bit Score: 113.97  E-value: 2.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145    30 VEGGHRAVIFdRFtGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVIT-GSKDLQNVNITLRILYRpIPDQLPKIYT 108
Cdd:pfam01145   3 VPPGEVGVVT-RF-GKLSRVLGPGLHFIIPFIQSVVIVDVRVQTLDVSVQTvLTKDGVPVNVDATVIYR-VPDDPPKLVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145   109 IL--GQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMK 186
Cdd:pfam01145  80 TVgfGSDDLQELIRQVVQSALREVIARYTLEELLSNREELAEEIKAALNEELSKYGVEIIDVQITDIDPPPEYREAIEAK 159
                         170       180
                  ....*....|....*....|.
gi 24585145   187 QVAQQEAEKArfvVEKAEQQK 207
Cdd:pfam01145 160 QTAEQEAEAE---IARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
13-231 1.66e-24

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


Pssm-ID: 223407  Cd Length: 291  Bit Score: 100.60  E-value: 1.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  13 GLGVAVLGGVVNSALYNVEGGHRAVIFdRFTGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNV------PVITGSKDLQ 86
Cdd:COG0330   7 IILLVILIVLLFSSIFVVKEGERGVVL-RFGRYTRTLGEPGLHFKIPFPEAIEEVVVRVDLRERtldvgpPQEVITKDNV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  87 NVNITLRILYRPIPDQLPKIYTilgqDYDERVLPSIAPEVLKAVVAQFDAGELITQREM-VSQRVSQELTVRAKQFGFIL 165
Cdd:COG0330  86 IVSVDAVVQYRVTDPQKAVYNV----ENAEAALRQLVQSALRSVIGRMTLDELLTERRAeINAKIREILDEAADPWGIKV 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24585145 166 DDISLTHLTFGREFTLAVEMKQVAQQEAEKArfvVEKAEQQKLASIISAEGDAEAAGLLAKSFGEA 231
Cdd:COG0330 162 VDVEIKDIDPPEEVQAAMEKQMAAERDKRAE---ILEAEGEAQAAILRAEGEAEAAIILAEAEAEA 224
PRK11029 PRK11029
FtsH protease regulator HflC; Provisional
190-245 4.28e-05

FtsH protease regulator HflC; Provisional


Pssm-ID: 182913  Cd Length: 334  Bit Score: 43.96  E-value: 4.28e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24585145  190 QQEAEKARFVVEK------AEQQKLASIISAEGDAEAAGLLAKSFGEAGDGLVELRRIEAAE 245
Cdd:PRK11029 243 QEEAEKLRATADYevtrtlAEAERQGRIMRGEGDAEAAKLFADAFSQDPDFYAFIRSLRAYE 304
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
18-247 2.63e-04

HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]


Pssm-ID: 273883  Cd Length: 317  Bit Score: 41.69  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145    18 VLGGVVNSALYNVEGGHRAVIFdRFTGI------KENVVGEGTHFFIPWVQRPIIFDIR-----SQPRNVPvitgSKDLQ 86
Cdd:TIGR01932  11 LLIVVLFQPFFIIKEGERGIIT-RFGKIlkdnnhHVLVYEPGLHFKIPFIEHVKIFDAKiqtmdGRPDRIP----TKEKK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145    87 NVNITLRILYRpIPDqLPKIYTILGQD---YDERVLPSIAPEVLKAVVAQFDAGELITQ--------------------- 142
Cdd:TIGR01932  86 DIIIDTYIRWR-IED-FKKYYLSTGGGtisAAEVLIKRKIDDRLRSEIGVLGLKEIVRSsndqldtlvsklalnrggkin 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145   143 ---------REMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAV------EMKQVAQQ-------EAEKARFVV 200
Cdd:TIGR01932 164 kiamtitkgREILAREISQIANSQLKDIGIEVVDVRIKKINYSDELSESIynrmrsEREQIARMhrsqgeeKAEEILGKA 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24585145   201 EK------AEQQKLASIISAEGDAEAAGLLAKSFGEAGDGLVELRRIEAAEDI 247
Cdd:TIGR01932 244 EYevrkilSEAYRTARIIKGEGDAEAAKIYSDAYGKDPEFYSFWRSLEAYEKS 296
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
27-221 2.02e-91

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


Pssm-ID: 259799  Cd Length: 195  Bit Score: 272.46  E-value: 2.02e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  27 LYNVEGGHRAVIFDRFTGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVITGSKDLQNVNITLRILYRPIPDQLPKI 106
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145 107 YTILGQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMK 186
Cdd:cd03401  81 YQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAK 160
                       170       180       190
                ....*....|....*....|....*....|....*
gi 24585145 187 QVAQQEAEKARFVVEKAEQQKLASIISAEGDAEAA 221
Cdd:cd03401 161 QVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
PHB smart00244
prohibitin homologues; prohibitin homologues
26-187 4.61e-33

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581  Cd Length: 160  Bit Score: 120.84  E-value: 4.61e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145     26 ALYNVEGGHRAVIFDRFTGIKEnVVGEGTHFFIPWVQRPIIFDIRSQPRNVP-VITGSKDLQNVNITLRILYRpIPDQLP 104
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPpQETITKDNVKVSVDAVVYYR-VLDPLR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145    105 KIYTILgqDYDERVLPSIAPEVLKAVVAQFDAGELIT-QREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAV 183
Cdd:smart00244  79 AVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156

                   ....
gi 24585145    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 2.55e-30

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: 307341  Cd Length: 177  Bit Score: 113.97  E-value: 2.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145    30 VEGGHRAVIFdRFtGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVIT-GSKDLQNVNITLRILYRpIPDQLPKIYT 108
Cdd:pfam01145   3 VPPGEVGVVT-RF-GKLSRVLGPGLHFIIPFIQSVVIVDVRVQTLDVSVQTvLTKDGVPVNVDATVIYR-VPDDPPKLVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145   109 IL--GQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMK 186
Cdd:pfam01145  80 TVgfGSDDLQELIRQVVQSALREVIARYTLEELLSNREELAEEIKAALNEELSKYGVEIIDVQITDIDPPPEYREAIEAK 159
                         170       180
                  ....*....|....*....|.
gi 24585145   187 QVAQQEAEKArfvVEKAEQQK 207
Cdd:pfam01145 160 QTAEQEAEAE---IARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
13-231 1.66e-24

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


Pssm-ID: 223407  Cd Length: 291  Bit Score: 100.60  E-value: 1.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  13 GLGVAVLGGVVNSALYNVEGGHRAVIFdRFTGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNV------PVITGSKDLQ 86
Cdd:COG0330   7 IILLVILIVLLFSSIFVVKEGERGVVL-RFGRYTRTLGEPGLHFKIPFPEAIEEVVVRVDLRERtldvgpPQEVITKDNV 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  87 NVNITLRILYRPIPDQLPKIYTilgqDYDERVLPSIAPEVLKAVVAQFDAGELITQREM-VSQRVSQELTVRAKQFGFIL 165
Cdd:COG0330  86 IVSVDAVVQYRVTDPQKAVYNV----ENAEAALRQLVQSALRSVIGRMTLDELLTERRAeINAKIREILDEAADPWGIKV 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24585145 166 DDISLTHLTFGREFTLAVEMKQVAQQEAEKArfvVEKAEQQKLASIISAEGDAEAAGLLAKSFGEA 231
Cdd:COG0330 162 VDVEIKDIDPPEEVQAAMEKQMAAERDKRAE---ILEAEGEAQAAILRAEGEAEAAIILAEAEAEA 224
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
26-230 4.73e-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  Cd Length: 249  Bit Score: 75.22  E-value: 4.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  26 ALYNVEGGHRAVIFdRFTGIKENVVGEGTHFFIPWVQRPIIFDIR-----SQPRNVPvitgSKDLQNVNITLRILYRpIP 100
Cdd:cd03405   1 SVFIVDETEQAVVL-QFGKPVRVITEPGLHFKLPFIQNVRKFDKRiltldGPPEEVL----TKDKKRLIVDSYARWR-IT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145 101 DQLpKIYTILGQDYD-ERVLPSIAPEVLKAVVAQFDAGELI-TQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGRE 178
Cdd:cd03405  75 DPL-RFYQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEE 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24585145 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 3.53e-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  Cd Length: 178  Bit Score: 57.52  E-value: 3.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  59 PWVQRPIIFDIRSQPRNVP---VITgsKDlqnvNITLRI---LYRPIPDQLPKIYTIlgQDYDERVLpSIAPEVLKAVVA 132
Cdd:cd08826   1 PFIDRMVRVDLRTVTLDVPpqeVIT--KD----NVTVKVnavVYFRVVDPEKAVLAV--EDYRYATS-QLAQTTLRSVVG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145 133 QFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLthltfgREFTLAVEMKQVAQQEAEkarfvvekAEQQKLASII 212
Cdd:cd08826  72 QVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEI------KDVDLPESMQRAMARQAE--------AERERRAKII 137
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24585145 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 3.22e-09

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


Pssm-ID: 259813  Cd Length: 208  Bit Score: 55.47  E-value: 3.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  51 GEGTHFFIPWVQRPIIFDIRSQPRNVP---VITgsKDLQNVNITLRILYRpIPDQLPKIYTILGQDYDERVLpsiAPEVL 127
Cdd:cd13435   6 GPGVFFVLPCIDNYCKVDLRTVSFDVPpqeVLT--KDSVTVTVDAVVYYR-ISDPLNAVIQVANYSHSTRLL---AATTL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145 128 KAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLthltfgREFTLAVEMKQVAQQEAEKARfvvekaeqQK 207
Cdd:cd13435  80 RNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEI------KDVSLPDSLQRAMAAEAEAAR--------EA 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24585145 208 LASIISAEGDAEAAGLL--AKSFGEAGDGLVELRRIEAAEDIA 248
Cdd:cd13435 146 RAKVIAAEGEMKSSRALkeASDIISASPSALQLRYLQTLSSIS 188
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) familyfamily; belonging to the ...
28-224 3.29e-08

Alloslipin, a subgroup of the stomatin-like proteins (slipins) familyfamily; 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  Cd Length: 222  Bit Score: 52.62  E-value: 3.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  28 YNVEGGHRAVI--FDRFtgikENVVGEGTHFFIPWVQRPIIFDIRSQPRNVP---VITgsKDLQNVNITLRILYRpIPDQ 102
Cdd:cd13437   7 KQVKQGSVGLVerFGKF----YKTVDPGLHKVNPCTEKIIQVDMKTQVIDLPrqsVMT--KDNVSVTIDSVVYYR-IIDP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145 103 LPKIYTIlgQDYDERVLpSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFtla 182
Cdd:cd13437  80 YKAIYRI--DNVKQALI-ERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDL--- 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 24585145 183 vemkqvaQQEAEKArfvvekAEQQKLAS--IISAEGDAEAAGLL 224
Cdd:cd13437 154 -------QQSLSSA------AKAKRIGEskIISAKADVESAKLM 184
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  Cd Length: 269  Bit Score: 51.05  E-value: 1.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  36 AVIFDRFtGIKENVVGEGTHFFIPWVQRpiIFD---IRSQPRNVPVITGSKDLQNVNITLRILYRPIPDQLPKIYTILgq 112
Cdd:cd03407   7 VAIVERF-GKFSRIAEPGLHFIIPPIES--VAGrvsLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYKL-- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145 113 DYDERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAVEMKQVAQQE 192
Cdd:cd03407  82 TNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRL 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24585145 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 2.77e-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  Cd Length: 110  Bit Score: 48.13  E-value: 2.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  70 RSQPRNVPVIT-GSKDLQNVNITLRILYRPIPDQ-LPKIYTILGQDYDERVLPSIAPEVLKAVVAQFDAGELITQREMVS 147
Cdd:cd02106   1 RPQFDDVRVEPvGTADGVPVAVDLVVQFRITDYNaLPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIA 80
                        90       100
                ....*....|....*....|....*.
gi 24585145 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 6.42e-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  Cd Length: 266  Bit Score: 46.35  E-value: 6.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  12 MGLGVAVLGGVVnSALYNVEGGHRAVIFdRFtGIKENVVGEGTHFFIPWVQRPIIFDIRSQPRNVPVITG--------SK 83
Cdd:cd03404   1 LILLLLLLVWLL-SGFYTVDPGERGVVL-RF-GKYVRTVGPGLHWKLPFPIEVVEKVNVTQVRSVEIGFRvpeeslmlTG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  84 DLQNVNITLRILYRpIPDqlPKIYTILGQDYDErVLPSIAPEVLKAVVAQFDAGELIT-QREMVSQRVSQELTVrakqfg 162
Cdd:cd03404  78 DENIVDVDFVVQYR-ISD--PVAYLFNVRDPEE-TLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQE------ 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145 163 fILDD----ISLThltfgreftlAVEMKQVAQQEAEKARFV-VEKAEQQKLASIisAEGDAEAAGLLAKSFGEAgdglve 237
Cdd:cd03404 148 -ILDRydlgIEIV----------QVQLQDADPPEEVQDAFDdVNAARQDKERLI--NEAQAYANEVIPRARGEA------ 208
                       250
                ....*....|....*.
gi 24585145 238 LRRIEAAEdiAYQLSR 253
Cdd:cd03404 209 ARIIQEAE--AYKAEV 222
PRK11029 PRK11029
FtsH protease regulator HflC; Provisional
190-245 4.28e-05

FtsH protease regulator HflC; Provisional


Pssm-ID: 182913  Cd Length: 334  Bit Score: 43.96  E-value: 4.28e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24585145  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 6.15e-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  Cd Length: 215  Bit Score: 42.91  E-value: 6.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  30 VEGGHRAVIFdrFTGIKENVVGEGTHFFipW-VQRPI---IFDIRSQprnVPVITG----SKDLQNVNITLRILYRpIPD 101
Cdd:cd13438   1 VPPGERGLLY--RDGKLVRTLEPGRYAF--WkFGRKVqveLVDLREQ---LLEVSGqeilTADKVALRVNLVATYR-VVD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145 102 qlPKIYTILGQDYDErVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQELTVRAKQFGFILDDISLthltfgREFTL 181
Cdd:cd13438  73 --PVKAVETVDDPEE-QLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGV------KDIIL 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24585145 182 AVEMKQVAQQEAEkarfvvekAEQQKLASIISAEG-------DAEAAGLLaksfgEAGDGLVELRRIEAAEDIA 248
Cdd:cd13438 144 PGEIREILNQVLE--------AEKRAQANLIRAREetaatrsLLNAAKLM-----EENPALLRLRELEALEKIA 204
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
18-247 2.63e-04

HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]


Pssm-ID: 273883  Cd Length: 317  Bit Score: 41.69  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145    18 VLGGVVNSALYNVEGGHRAVIFdRFTGI------KENVVGEGTHFFIPWVQRPIIFDIR-----SQPRNVPvitgSKDLQ 86
Cdd:TIGR01932  11 LLIVVLFQPFFIIKEGERGIIT-RFGKIlkdnnhHVLVYEPGLHFKIPFIEHVKIFDAKiqtmdGRPDRIP----TKEKK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145    87 NVNITLRILYRpIPDqLPKIYTILGQD---YDERVLPSIAPEVLKAVVAQFDAGELITQ--------------------- 142
Cdd:TIGR01932  86 DIIIDTYIRWR-IED-FKKYYLSTGGGtisAAEVLIKRKIDDRLRSEIGVLGLKEIVRSsndqldtlvsklalnrggkin 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145   143 ---------REMVSQRVSQELTVRAKQFGFILDDISLTHLTFGREFTLAV------EMKQVAQQ-------EAEKARFVV 200
Cdd:TIGR01932 164 kiamtitkgREILAREISQIANSQLKDIGIEVVDVRIKKINYSDELSESIynrmrsEREQIARMhrsqgeeKAEEILGKA 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24585145   201 EK------AEQQKLASIISAEGDAEAAGLLAKSFGEAGDGLVELRRIEAAEDI 247
Cdd:TIGR01932 244 EYevrkilSEAYRTARIIKGEGDAEAAKIYSDAYGKDPEFYSFWRSLEAYEKS 296
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
13-220 6.34e-03

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


Pssm-ID: 225177  Cd Length: 548  Bit Score: 37.50  E-value: 6.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  13 GLGVAVLGGVV----NSALYNVEGGHRAVI-FDRFTGIKEN------VVGEGTHFFIPWVQRPIIFDIRSQPRNVPVITG 81
Cdd:COG2268  16 IVVVVILVILVliffGKRFYIIARPNEALIrTGSKLGSKDEagggqkVVRGGGAIVMPIFQTIERMSLTTIKLEVEIDNV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585145  82 -SKDlqNVNITLRIL-YRPIPDQLPKIYTI---LGQDYD----ERVLPSIAPEVLKAVVAQFDAGELITQREMVSQRVSQ 152
Cdd:COG2268  96 yTKD--GMPLNVEAVaYVKIGDTFQDIATAaerFGGKGSredlEQLAEDTLEGALRAVLAQMTVEELNEDRLGFAQVVQE 173
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24585145 153 ELTVRAKQFGFILDDISLTHLTFGREFTL----AVEMKQVAQQEAEKARFVVEKAEQQKLASIISAEGDAEA 220
Cdd:COG2268 174 VVGDDLSKMGLVLDSLAINDINDTSKENQdpnnYLDALGRRRIAQVLQDAEIAENEAEKETEIAIAEANRDA 245
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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