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Conserved domains on  [gi|18395564|ref|NP_027545|]
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SPFH/Band 7/PHB domain-containing membrane-associated protein family [Arabidopsis thaliana]

Protein Classification

erlin( domain architecture ID 10130465)

erlin family protein similar to Homo sapiens erlin-1 and erlin-2, which forms the ERLIN1/ERLIN2 complex that mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 40-332 0e+00

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: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 573.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564  40 VMFPSSLVHQVPEGHVGAYWRGGALLNIITEPGFHLKLPFITNYEPVQVTLQTDQVRDIPCGTKGGVLITFEKIEVVNRL 119
Cdd:cd03406   1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 120 RKDFVYDTLLNYGVNYDNTWIYDKIHHEINQFCSSHSLQQVYIDIFDQIDERMKDALQADCTRYAPGIEILSVRVTKPKI 199
Cdd:cd03406  81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 200 PESVRRNFEQMEEERTKVLIAIEKQRVAEKEAETKKIMAISEAEKNANVSKILMQQKLTEKDSSRREADIENQMYLDRQK 279
Cdd:cd03406 161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 18395564 280 SLADADYYRVLREAEANKLKLTPEFLELKFIDAIARNTKIFFGDKVPNMVLDQ 332
Cdd:cd03406 241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 40-332 0e+00

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: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 573.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564  40 VMFPSSLVHQVPEGHVGAYWRGGALLNIITEPGFHLKLPFITNYEPVQVTLQTDQVRDIPCGTKGGVLITFEKIEVVNRL 119
Cdd:cd03406   1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 120 RKDFVYDTLLNYGVNYDNTWIYDKIHHEINQFCSSHSLQQVYIDIFDQIDERMKDALQADCTRYAPGIEILSVRVTKPKI 199
Cdd:cd03406  81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 200 PESVRRNFEQMEEERTKVLIAIEKQRVAEKEAETKKIMAISEAEKNANVSKILMQQKLTEKDSSRREADIENQMYLDRQK 279
Cdd:cd03406 161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 18395564 280 SLADADYYRVLREAEANKLKLTPEFLELKFIDAIARNTKIFFGDKVPNMVLDQ 332
Cdd:cd03406 241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 49-231 8.73e-24

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: 96.24  E-value: 8.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564    49 QVPEGHVGAYWRGGALlNIITEPGFHLKLPFITNYEPVQVTLQTDQVRDIPCGTKGGVLITFEkIEVVNRLRKDFVYDTL 128
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVD-VTVIYRVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564   129 LNY-GVNYDNTWIYDKIHHEINQFCSSHSLQQVYIDiFDQIDERMKDALQADCTRYapGIEILSVRVTKPKIPESVRRNF 207
Cdd:pfam01145  80 QNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEELAKY--GVEIIDVQITDIDPPPEIAEAI 156

                         170       180
                  ....*....|....*....|....
gi 18395564   208 EQMEEERtkvLIAIEKQRVAEKEA 231
Cdd:pfam01145 157 EAKQTAE---QEAEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 28-323 2.75e-23

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 97.60  E-value: 2.75e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564  28 IAFGVFAAIAALVMFPSSlVHQVPEGHVGAYWRGGALLNIiTEPGFHLKLPFITNYEPVQVTLQTDQVRDIPCGTKGGVL 107
Cdd:COG0330   3 LILLLILLVLVLVLLFSS-VYIVPQGERGVVLRFGKYVRT-LEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 108 ITfekIEVVNRLRKDFVYDTLLNYGvNYDNTwIYDKIHHEINQFCSSHSLQQVYIDIFDQIDERMKDALQADCTRYapGI 187
Cdd:COG0330  81 VD---VDAVVQYRITDPAKFLYNVE-NAEEA-LRQLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDPY--GI 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 188 EILSVRVTKPKIPESVRRNFE-QMEEERTKVliaiEKQRVAEKEAETKKIMAISEAEKNANVSKIlmqqkltEKDSSRRE 266
Cdd:COG0330 154 EVVDVEIKDIDPPEEVQDAMEdRMKAERERE----AAILEAEGYREAAIIRAEGEAQRAIIEAEA-------YREAQILR 222

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395564 267 ADienqmyldrqkslADADYYRVLREAeankLKLTPEFLELKFIDAIAR----NTKIFFGD 323
Cdd:COG0330 223 AE-------------GEAEAFRIVAEA----YSAAPFVLFYRSLEALEEvlspNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 45-211 6.90e-21

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 88.10  E-value: 6.90e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564     45 SLVHQVPEGHVGAYWRGGALLNIItEPGFHLKLPFITNYEPVQVTLQTDQVRDIPCGTKGGVLITFE---KIEVVNRLRk 121
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVL-GPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDavvYYRVLDPLR- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564    122 dFVYDTLlnygvNYDNTWIYDKIHHEINQFCSSHSLQQVYIDIFDQIDERMKDALQADCTRYapGIEILSVRVTKPKIPE 201
Cdd:smart00244  79 -AVYRVL-----DADYAVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAEAW--GIKVEDVEIKDIRLPE 150

                          170
                   ....*....|
gi 18395564    202 SVRRNFEQME 211
Cdd:smart00244 151 EIKEAMEAQQ 160
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 65-324 2.23e-07

HflK 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.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 51.25  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564    65 LNIITEPGFHLKLPFITNYEPVQVTlqtdQVRDIpcgTKGGVLITFE----KIEVVNRLRKDFVYDTLlnYGVNYDNTWI 140
Cdd:TIGR01933  18 YHRTVDPGLNWKPPFIEEVYPVNVT----AVRNL---RKQGLMLTGDenivNVEMNVQYRITDPYKYL--FSVENPEDSL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564   141 YDKIHHEINQFCSSHSLQQVYIDIFDQIDERMKDALQADCTRYAPGIEILSVRVTKPKIPESVRRNFEQmeeertkVLIA 220
Cdd:TIGR01933  89 RQATDSALRGVIGDSTMDDILTEGRSQIREDTKERLNEIIDNYDLGITVTDVNFQSARPPEEVKEAFDD-------VIIA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564   221 IE-KQRvaekeaetkkimAISEAEKNAN--VSKILMQ-QKLTEKDSSRREADIENqmyldrqkSLADADYY-RVLREAEA 295
Cdd:TIGR01933 162 REdEER------------YINEAEAYANevVPKARGDaQRIIEEARGYKERRINR--------AKGDVARFtKLLAEYKK 221

                         250       260       270
                  ....*....|....*....|....*....|
gi 18395564   296 NKlKLTPEFLELKFIDAIARNT-KIFFGDK 324
Cdd:TIGR01933 222 AP-DVTRERLYLETMEKVLSNTrKVLLDDK 250
PRK11029 PRK11029
protease modulator HflC;
32-92 8.38e-03

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 37.80  E-value: 8.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18395564   32 VFAAIAALVMFPSSLVhQVPEGHVGAYWRGGALLN------IITEPGFHLKLPFITNYEPVQVTLQT 92
Cdd:PRK11029   6 IAIIIIVLVVLYMSVF-VVKEGERGIVLRFGKVLRdddnkpLVYAPGLHFKIPFIETVKMLDARIQT 71
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 40-332 0e+00

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: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 573.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564  40 VMFPSSLVHQVPEGHVGAYWRGGALLNIITEPGFHLKLPFITNYEPVQVTLQTDQVRDIPCGTKGGVLITFEKIEVVNRL 119
Cdd:cd03406   1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 120 RKDFVYDTLLNYGVNYDNTWIYDKIHHEINQFCSSHSLQQVYIDIFDQIDERMKDALQADCTRYAPGIEILSVRVTKPKI 199
Cdd:cd03406  81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLFDQIDENLKDALQADLNKMAPGLEIIAVRVTKPKI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 200 PESVRRNFEQMEEERTKVLIAIEKQRVAEKEAETKKIMAISEAEKNANVSKILMQQKLTEKDSSRREADIENQMYLDRQK 279
Cdd:cd03406 161 PEAIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREK 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 18395564 280 SLADADYYRVLREAEANKLKLTPEFLELKFIDAIARNTKIFFGDKVPNMVLDQ 332
Cdd:cd03406 241 ARADAEYYRALREAEANKLKLTPEYLELKKYQAIANNTKIYFGNDIPNMFLDN 293
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 49-231 8.73e-24

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: 96.24  E-value: 8.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564    49 QVPEGHVGAYWRGGALlNIITEPGFHLKLPFITNYEPVQVTLQTDQVRDIPCGTKGGVLITFEkIEVVNRLRKDFVYDTL 128
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVD-VTVIYRVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564   129 LNY-GVNYDNTWIYDKIHHEINQFCSSHSLQQVYIDiFDQIDERMKDALQADCTRYapGIEILSVRVTKPKIPESVRRNF 207
Cdd:pfam01145  80 QNVfGSDDLQELLRRVLESALREIIARYTLEELLSN-REELAEEIKNALQEELAKY--GVEIIDVQITDIDPPPEIAEAI 156

                         170       180
                  ....*....|....*....|....
gi 18395564   208 EQMEEERtkvLIAIEKQRVAEKEA 231
Cdd:pfam01145 157 EAKQTAE---QEAEAEIARAEAEA 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 28-323 2.75e-23

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 97.60  E-value: 2.75e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564  28 IAFGVFAAIAALVMFPSSlVHQVPEGHVGAYWRGGALLNIiTEPGFHLKLPFITNYEPVQVTLQTDQVRDIPCGTKGGVL 107
Cdd:COG0330   3 LILLLILLVLVLVLLFSS-VYIVPQGERGVVLRFGKYVRT-LEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 108 ITfekIEVVNRLRKDFVYDTLLNYGvNYDNTwIYDKIHHEINQFCSSHSLQQVYIDIFDQIDERMKDALQADCTRYapGI 187
Cdd:COG0330  81 VD---VDAVVQYRITDPAKFLYNVE-NAEEA-LRQLAESALREVIGKMTLDEVLSTGRDEINAEIREELQEALDPY--GI 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 188 EILSVRVTKPKIPESVRRNFE-QMEEERTKVliaiEKQRVAEKEAETKKIMAISEAEKNANVSKIlmqqkltEKDSSRRE 266
Cdd:COG0330 154 EVVDVEIKDIDPPEEVQDAMEdRMKAERERE----AAILEAEGYREAAIIRAEGEAQRAIIEAEA-------YREAQILR 222

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395564 267 ADienqmyldrqkslADADYYRVLREAeankLKLTPEFLELKFIDAIAR----NTKIFFGD 323
Cdd:COG0330 223 AE-------------GEAEAFRIVAEA----YSAAPFVLFYRSLEALEEvlspNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 45-211 6.90e-21

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 88.10  E-value: 6.90e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564     45 SLVHQVPEGHVGAYWRGGALLNIItEPGFHLKLPFITNYEPVQVTLQTDQVRDIPCGTKGGVLITFE---KIEVVNRLRk 121
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVL-GPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDavvYYRVLDPLR- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564    122 dFVYDTLlnygvNYDNTWIYDKIHHEINQFCSSHSLQQVYIDIFDQIDERMKDALQADCTRYapGIEILSVRVTKPKIPE 201
Cdd:smart00244  79 -AVYRVL-----DADYAVIEQLAQTTLRSVIGKRTLDELLTDQREKISENIREELNEAAEAW--GIKVEDVEIKDIRLPE 150

                          170
                   ....*....|
gi 18395564    202 SVRRNFEQME 211
Cdd:smart00244 151 EIKEAMEAQQ 160
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 47-245 5.08e-17

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: 78.32  E-value: 5.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564  47 VHQVPEGHVG-AYWRGGALLNIITEPGFHLKLPFITNYEPVQVTLQTDQVrDIPCGTKGGVLITFEkIEVVNRLRKDFVY 125
Cdd:cd03401   1 FYTVDAGEVGvVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREI-TLTVLSKDGQTVNID-LSVLYRPDPEKLP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 126 DTLLNYGVNYDNTWIYDKIHHEINQFCSSHSLQQVYI---DIFDQIDERMKDALQADctryapGIEILSVRVTKPKIPES 202
Cdd:cd03401  79 ELYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTkreEVSAEIREALTERLAPF------GIIVDDVLITNIDFPDE 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 18395564 203 VRRNFEQMEEERTKVLIAIEKQRVAEKEAETKKIMAISEAEKN 245
Cdd:cd03401 153 YEKAIEAKQVAEQEAERAKFELEKAEQEAERKVIEAEGEAEAQ 195
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 89-201 4.14e-13

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: 65.08  E-value: 4.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564  89 TLQTDQVRDIPCGTKGGVLITFEKIEVVNRLRKDFVYDTLLNYGVNYDNTWIYDKIHHEINQFCSSHSLQQVyIDIFDQI 168
Cdd:cd02106   1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQI-ISGRDEI 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 18395564 169 DERMKDALQADCTRYapGIEILSVRVTKPKIPE 201
Cdd:cd02106  80 AKAVKEDLEEDLENF--GVVISDVDITSIEPPD 110
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 33-250 4.08e-10

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: 59.83  E-value: 4.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564  33 FAAIAALVMFPSSLVHQVPEGHVGAYWRGGALLNIiTEPGFHLKLPF-ITNYEPVQVTlQTDQVRDIPCGTKGGVLIT-- 109
Cdd:cd03404   1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGKYVRT-VGPGLHWKLPFpIEVVEKVNVT-QVRSVEIGFRVPEESLMLTgd 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 110 --FEKIEVVNRLR----KDFVYDTllnygVNYDNTwIYDKIHHEINQFCSSHSLQQVYIDIFDQIDERMKDALQADCTRY 183
Cdd:cd03404  79 enIVDVDFVVQYRisdpVAYLFNV-----RDPEET-LRQAAESALREVVGSRTLDDVLTEGRAEIAADVRELLQEILDRY 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18395564 184 APGIEILSVRVTKPKIPESVRRNFE-----QMEEERtkvLIAIEK----QRVAEKEAETKKIMAISEAEKNANVSK 250
Cdd:cd03404 153 DLGIEIVQVQLQDADPPEEVQDAFDdvnaaRQDKER---LINEAQayanEVIPRARGEAARIIQEAEAYKAEVVAR 225
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 49-295 1.12e-08

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: 55.19  E-value: 1.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564  49 QVPEGHVGAYWRGGALLNIITEPGFHLKLPFITNYEPVQVTLQT--DQVRDIPCGTKGGVLI-TFEKIEVVNRLRkdFvY 125
Cdd:cd03405   4 IVDETEQAVVLQFGKPVRVITEPGLHFKLPFIQNVRKFDKRILTldGPPEEVLTKDKKRLIVdSYARWRITDPLR--F-Y 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 126 DTLLNYGVNYD--NTWIYDKIHHEInqfcSSHSLQQVYIDIFDQIDERMKDALQADCTRYapGIEILSVRVTKPKIPESV 203
Cdd:cd03405  81 QSVGGEEGAESrlDDIVDSALRNEI----GKRTLAEVVSGGRDELMEEILEQANEEAKEY--GIEVVDVRIKRIDLPEEV 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 204 RRN-FEQMEEERTKvliaIEKQRVAEKEAETKKIMA---------ISEAEKNAnvskilmqQKLtekdssRREAD----- 268
Cdd:cd03405 155 SESvYERMRAERER----IAAEYRAEGEEEAEKIRAeadrertviLAEAYREA--------EEI------RGEGDaeaar 216

                       250       260
                ....*....|....*....|....*..
gi 18395564 269 IENQMYldrqksLADADYYRVLREAEA 295
Cdd:cd03405 217 IYAEAY------GKDPEFYSFYRSLEA 237
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 65-324 2.23e-07

HflK 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.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 51.25  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564    65 LNIITEPGFHLKLPFITNYEPVQVTlqtdQVRDIpcgTKGGVLITFE----KIEVVNRLRKDFVYDTLlnYGVNYDNTWI 140
Cdd:TIGR01933  18 YHRTVDPGLNWKPPFIEEVYPVNVT----AVRNL---RKQGLMLTGDenivNVEMNVQYRITDPYKYL--FSVENPEDSL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564   141 YDKIHHEINQFCSSHSLQQVYIDIFDQIDERMKDALQADCTRYAPGIEILSVRVTKPKIPESVRRNFEQmeeertkVLIA 220
Cdd:TIGR01933  89 RQATDSALRGVIGDSTMDDILTEGRSQIREDTKERLNEIIDNYDLGITVTDVNFQSARPPEEVKEAFDD-------VIIA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564   221 IE-KQRvaekeaetkkimAISEAEKNAN--VSKILMQ-QKLTEKDSSRREADIENqmyldrqkSLADADYY-RVLREAEA 295
Cdd:TIGR01933 162 REdEER------------YINEAEAYANevVPKARGDaQRIIEEARGYKERRINR--------AKGDVARFtKLLAEYKK 221

                         250       260       270
                  ....*....|....*....|....*....|
gi 18395564   296 NKlKLTPEFLELKFIDAIARNT-KIFFGDK 324
Cdd:TIGR01933 222 AP-DVTRERLYLETMEKVLSNTrKVLLDDK 250
MRP-S26 pfam14943
Mitochondrial ribosome subunit S26; This family of proteins corresponds to mitochondrial ...
 201-306 1.85e-05

Mitochondrial ribosome subunit S26; This family of proteins corresponds to mitochondrial ribosomal subunit S26 in eukaryotes


Pssm-ID: 464391 [Multi-domain]  Cd Length: 168  Bit Score: 44.54  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564   201 ESVRRNFEQMEEERTKVLIAIEKQRVAEKEAETKKIMAISEAEkNANVSKILMQ--QKLTEKDSSRREADIENQmyLDRQ 278
Cdd:pfam14943  41 RSLRSFFREEVRKKYEEELGSESEEEAEEEEEHRELMAWNEEW-NAEIAKLREErlAKEAEEREEEILERIEEK--EEKE 117

                          90       100
                  ....*....|....*....|....*...
gi 18395564   279 KSLADADYYRVLREAEANKLKLTPEFLE 306
Cdd:pfam14943 118 EEKKERAEEEVRQEKEESKTFITRENLD 145
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 68-246 3.17e-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: 44.88  E-value: 3.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564  68 ITEPGFHLKLPFItnyEPV--QVTLQTDQVR-DIPCGTKGGVLITFEkIEVVNRLRKDFVYDTL--LNYGVNYDNTWIYD 142
Cdd:cd03407  19 IAEPGLHFIIPPI---ESVagRVSLRVQQLDvRVETKTKDNVFVTLV-VSVQYRVVPEKVYDAFykLTNPEQQIQSYVFD 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564 143 KIHHEInqfcSSHSLQQVYIDiFDQIDERMKDALQADCTRYapGIEILSVRVTKPKIPESVRrnfEQMEEertkvLIAIE 222
Cdd:cd03407  95 VVRASV----PKLTLDEVFES-KDEIAKAVKEELAKVMSEY--GYEIVKTLVTDIEPDASVK---AAMNE-----INAAQ 159

                       170       180
                ....*....|....*....|....*
gi 18395564 223 KQRVA-EKEAETKKIMAISEAEKNA 246
Cdd:cd03407 160 RLREAaEEKAEAEKILQVKAAEAEA 184
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 26-297 5.32e-03

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 [Multi-domain]  Cd Length: 317  Bit Score: 38.23  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564    26 ILIAFGVfaaIAALVMFPSSLVhqVPEGHVGAYWRGGALL------NIITEPGFHLKLPFITNYEPVQVTLQT--DQVRD 97
Cdd:TIGR01932   4 IGIVVIV---LLIVVLFQPFFI--IKEGERGIITRFGKILkdnnhhVLVYEPGLHFKIPFIEHVKIFDAKIQTmdGRPDR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564    98 IPCGTKGGVLITFE---KIEVVNRLrkdfvYDTLLNYGVNYDNTWIYDKIHHEINQFCSSHSLQQVYIDIFDQID----- 169
Cdd:TIGR01932  79 IPTKEKKDIIIDTYirwRIEDFKKY-----YLSTGGGTISAAEVLIKRKIDDRLRSEIGVLGLKEIVRSSNDQLDtlvsk 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18395564   170 ----------------ERMKDALQADCTRYAP------GIEILSVRVTKPKIPESVRRN-FEQMEEERTKvlIAIEKQRV 226
Cdd:TIGR01932 154 lalnrggkinkiamtiTKGREILAREISQIANsqlkdiGIEVVDVRIKKINYSDELSESiYNRMRSEREQ--IARMHRSQ 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18395564   227 AEKEAEtkKIMAISEAEKNANVSKILMQQKLTEKDSSRREADIENQMYLDrqkslaDADYYRVLREAEANK 297
Cdd:TIGR01932 232 GEEKAE--EILGKAEYEVRKILSEAYRTARIIKGEGDAEAAKIYSDAYGK------DPEFYSFWRSLEAYE 294
PRK11029 PRK11029
protease modulator HflC;
32-92 8.38e-03

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 37.80  E-value: 8.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18395564   32 VFAAIAALVMFPSSLVhQVPEGHVGAYWRGGALLN------IITEPGFHLKLPFITNYEPVQVTLQT 92
Cdd:PRK11029   6 IAIIIIVLVVLYMSVF-VVKEGERGIVLRFGKVLRdddnkpLVYAPGLHFKIPFIETVKMLDARIQT 71
 
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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