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Conserved domains on  [gi|659113223|ref|XP_008456463|]
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hypersensitive-induced response protein 1 [Cucumis melo]

Protein Classification

SPFH domain-containing protein( domain architecture ID 10130471)

uncharacterized stomatin, prohibitin, flotillin, HflK/C (SPFH) domain-containing protein similar to Streptococcus pneumoniae SPFH domain/Band 7 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 10-278 1.18e-166

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: 462.44  E-value: 1.18e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  10 VDQSTVAIRETFGKFDDVLQPGCHCLPWClGSQIAGHLSLRLQQLDVRCETKTKDNVFVTVVASIQYRALADKASDAFYK 89
Cdd:cd03407    2 VSQSTVAIVERFGKFSRIAEPGLHFIIPP-IESVAGRVSLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  90 LSNTREQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRAMNEINAAAR 169
Cdd:cd03407   81 LTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223 170 LRVAATEKAEAEKILQIKRAEGDAESKYLAGLGIARQRQAIVDGLRDSVLAFAENVPGTTSKDVMDMVLVTQYFDTMKEI 249
Cdd:cd03407  161 LREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLRESIEDFQEAVPGVSSKEVMDLLLITQYFDTLKEV 240

                        250       260
                 ....*....|....*....|....*....
gi 659113223 250 GASSKSNSVFIPHGPGAVKDIASQIRDGL 278
Cdd:cd03407  241 GKSSKSSTVFLPHGPGGVSDISAQIRAGM 269
 
Name Accession Description Interval E-value
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 10-278 1.18e-166

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: 462.44  E-value: 1.18e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  10 VDQSTVAIRETFGKFDDVLQPGCHCLPWClGSQIAGHLSLRLQQLDVRCETKTKDNVFVTVVASIQYRALADKASDAFYK 89
Cdd:cd03407    2 VSQSTVAIVERFGKFSRIAEPGLHFIIPP-IESVAGRVSLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  90 LSNTREQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRAMNEINAAAR 169
Cdd:cd03407   81 LTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223 170 LRVAATEKAEAEKILQIKRAEGDAESKYLAGLGIARQRQAIVDGLRDSVLAFAENVPGTTSKDVMDMVLVTQYFDTMKEI 249
Cdd:cd03407  161 LREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLRESIEDFQEAVPGVSSKEVMDLLLITQYFDTLKEV 240

                        250       260
                 ....*....|....*....|....*....
gi 659113223 250 GASSKSNSVFIPHGPGAVKDIASQIRDGL 278
Cdd:cd03407  241 GKSSKSSTVFLPHGPGGVSDISAQIRAGM 269
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-273 5.67e-42

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 145.37  E-value: 5.67e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223   4 ALGCIQVDQSTVAIRETFGKFDDVLQPGCH-CLPWClgsQIAGHLSLRLQQLDVR-CETKTKDNVFVTVVASIQYRaLAD 81
Cdd:COG0330   18 FSSVYIVPQGERGVVLRFGKYVRTLEPGLHfKIPFI---DRVRKVDVREQVLDVPpQEVLTKDNNIVDVDAVVQYR-ITD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  82 kASDAFYKLSNTREQIQAYVFDVIRASVPKLDLDSTF-EQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRA 160
Cdd:COG0330   94 -PAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223 161 MNEINAAARLRVAATEKAEAEKILQIKRAEGDAESKYLAGLGIARQRQAIVDGLRDSVLAFAENVpgttskDVMDMVLVT 240
Cdd:COG0330  173 MEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAY------SAAPFVLFY 246

                        250       260       270
                 ....*....|....*....|....*....|....
gi 659113223 241 QYFDTMKEIgASSKSNSVFIPH-GPGAVKDIASQ 273
Cdd:COG0330  247 RSLEALEEV-LSPNSKVIVLPPdGNGFLKYLLKS 279
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 8-182 4.98e-27

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 103.56  E-value: 4.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223    8 IQVDQSTVAIRETFGKFDDVLQPGCHC-LPWCLGSQIaghLSLRLQQLDV-RCETKTKDNVFVTVVASIQYRALADKASD 85
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFiIPFIQRVVT---VDVRVQTLEVsVQTVLTKDGVPVNVDVTVIYRVNPDDPPK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223   86 AFYKL---SNTREQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRAMN 162
Cdd:pfam01145  78 LVQNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIE 157

                         170       180
                  ....*....|....*....|
gi 659113223  163 EINAAARLRVAATEKAEAEK 182
Cdd:pfam01145 158 AKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 10-165 2.45e-25

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 98.50  E-value: 2.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223    10 VDQSTVAIRETFGKFDDVLQPGCHCL-PWCLGSQIaghLSLRLQQLDVRC-ETKTKDNVFVTVVASIQYRaLADKASDAF 87
Cdd:smart00244   6 VGEGERGVVERLGRVLRVLGPGLHFLiPFIDDVKK---VDLRAQTDDVPPqETITKDNVKVSVDAVVYYR-VLDPLRAVY 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 659113223    88 YKLSNTREQIQAYVFDVIRASVPKLDLDSTFE-QKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRAMNEIN 165
Cdd:smart00244  82 RVLDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 10-254 1.04e-08

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: 54.72  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223   10 VDQSTVAIRETFGKFDDVLQPGCHCLPWCLGSQIAGHLSlRLQQLDVRCETKTKDNVFVTVVASIQYRaLADKAsDAFYK 89
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNVT-AVRNLRKQGLMLTGDENIVNVEMNVQYR-ITDPY-KYLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223   90 LSNTREQIQAYVFDVIRASVPKLDLDSTF-EQKNDIAKAVEDELEKAMSAY--GYEIVQTLIVDIEPDEHVKRAMNEINA 166
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDILtEGRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDVII 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  167 AARLRVAATEKAEAEKILQIKRAEGDAESKYLAGLGIARQR--QAIVDGLR-DSVLAFAENVPGTTSKDVmdmvlvtqYF 243
Cdd:TIGR01933 161 AREDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRinRAKGDVARfTKLLAEYKKAPDVTRERL--------YL 232

                         250
                  ....*....|.
gi 659113223  244 DTMKEIGASSK 254
Cdd:TIGR01933 233 ETMEKVLSNTR 243
 
Name Accession Description Interval E-value
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 10-278 1.18e-166

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: 462.44  E-value: 1.18e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  10 VDQSTVAIRETFGKFDDVLQPGCHCLPWClGSQIAGHLSLRLQQLDVRCETKTKDNVFVTVVASIQYRALADKASDAFYK 89
Cdd:cd03407    2 VSQSTVAIVERFGKFSRIAEPGLHFIIPP-IESVAGRVSLRVQQLDVRVETKTKDNVFVTLVVSVQYRVVPEKVYDAFYK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  90 LSNTREQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRAMNEINAAAR 169
Cdd:cd03407   81 LTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223 170 LRVAATEKAEAEKILQIKRAEGDAESKYLAGLGIARQRQAIVDGLRDSVLAFAENVPGTTSKDVMDMVLVTQYFDTMKEI 249
Cdd:cd03407  161 LREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLRESIEDFQEAVPGVSSKEVMDLLLITQYFDTLKEV 240

                        250       260
                 ....*....|....*....|....*....
gi 659113223 250 GASSKSNSVFIPHGPGAVKDIASQIRDGL 278
Cdd:cd03407  241 GKSSKSSTVFLPHGPGGVSDISAQIRAGM 269
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-273 5.67e-42

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 145.37  E-value: 5.67e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223   4 ALGCIQVDQSTVAIRETFGKFDDVLQPGCH-CLPWClgsQIAGHLSLRLQQLDVR-CETKTKDNVFVTVVASIQYRaLAD 81
Cdd:COG0330   18 FSSVYIVPQGERGVVLRFGKYVRTLEPGLHfKIPFI---DRVRKVDVREQVLDVPpQEVLTKDNNIVDVDAVVQYR-ITD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  82 kASDAFYKLSNTREQIQAYVFDVIRASVPKLDLDSTF-EQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRA 160
Cdd:COG0330   94 -PAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223 161 MNEINAAARLRVAATEKAEAEKILQIKRAEGDAESKYLAGLGIARQRQAIVDGLRDSVLAFAENVpgttskDVMDMVLVT 240
Cdd:COG0330  173 MEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAY------SAAPFVLFY 246

                        250       260       270
                 ....*....|....*....|....*....|....
gi 659113223 241 QYFDTMKEIgASSKSNSVFIPH-GPGAVKDIASQ 273
Cdd:COG0330  247 RSLEALEEV-LSPNSKVIVLPPdGNGFLKYLLKS 279
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 8-182 4.98e-27

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 103.56  E-value: 4.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223    8 IQVDQSTVAIRETFGKFDDVLQPGCHC-LPWCLGSQIaghLSLRLQQLDV-RCETKTKDNVFVTVVASIQYRALADKASD 85
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFiIPFIQRVVT---VDVRVQTLEVsVQTVLTKDGVPVNVDVTVIYRVNPDDPPK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223   86 AFYKL---SNTREQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRAMN 162
Cdd:pfam01145  78 LVQNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIE 157

                         170       180
                  ....*....|....*....|
gi 659113223  163 EINAAARLRVAATEKAEAEK 182
Cdd:pfam01145 158 AKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 10-165 2.45e-25

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 98.50  E-value: 2.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223    10 VDQSTVAIRETFGKFDDVLQPGCHCL-PWCLGSQIaghLSLRLQQLDVRC-ETKTKDNVFVTVVASIQYRaLADKASDAF 87
Cdd:smart00244   6 VGEGERGVVERLGRVLRVLGPGLHFLiPFIDDVKK---VDLRAQTDDVPPqETITKDNVKVSVDAVVYYR-VLDPLRAVY 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 659113223    88 YKLSNTREQIQAYVFDVIRASVPKLDLDSTFE-QKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRAMNEIN 165
Cdd:smart00244  82 RVLDADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 7-195 2.75e-16

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: 75.24  E-value: 2.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223   7 CIQVDQSTVAIRETFGKF--DDVLQPGCH-CLPWclgSQIAGHLSLRLQQLDVRCETKTKDNVFVTVVASIQYRALADKA 83
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGvkDEVLGEGLHfKIPW---IQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  84 SDAF--YKLSNTREQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRAM 161
Cdd:cd03401   78 PELYqnLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAI 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 659113223 162 NEINAA------ARLRVaatEKAEAEKILQIKRAEGDAES 195
Cdd:cd03401  158 EAKQVAeqeaerAKFEL---EKAEQEAERKVIEAEGEAEA 194
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 8-261 8.07e-16

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: 74.57  E-value: 8.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223   8 IQVDQSTVAIRETFGKFDDVLQPGCHCLPWCLGSQIagHLSLRLQQLDV-RCETKTKDNVFVTVVASIQYRALADKasDA 86
Cdd:cd13437    7 KQVKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKII--QVDMKTQVIDLpRQSVMTKDNVSVTIDSVVYYRIIDPY--KA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  87 FYKLSNTREQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRAMNeina 166
Cdd:cd13437   83 IYRIDNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLS---- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223 167 aarlrVAATEKAEAE-KILQikrAEGDAESKYLaglgiarQRQA--IVDglrdsvlafaenvpgttSKDVMDMvlvtQYF 243
Cdd:cd13437  159 -----SAAKAKRIGEsKIIS---AKADVESAKL-------MREAadILD-----------------SKAAMQI----RYL 202

                        250
                 ....*....|....*...
gi 659113223 244 DTMKEIGASSKSNSVFIP 261
Cdd:cd13437  203 ETLQAIAKSANSKVIFLP 220
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 50-155 8.09e-15

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: 68.93  E-value: 8.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  50 RLQQLDVRCET-KTKDNVFVTVVASIQYRALADKASDAFYKLS---NTREQIQAYVFDVIRASVPKLDLDSTFEQKNDIA 125
Cdd:cd02106    1 RPQFDDVRVEPvGTADGVPVAVDLVVQFRITDYNALPAFYLVDfvkDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 659113223 126 KAVEDELEKAMSAYGYEIVQTLIVDIEPDE 155
Cdd:cd02106   81 KAVKEDLEEDLENFGVVISDVDITSIEPPD 110
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 9-207 9.19e-13

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: 66.77  E-value: 9.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223   9 QVDQSTVAIRETFGKFDDVLQPGCHC-LPWCLGSQIAGHLSlRLQQLDVRCETK------TKDNVFVTVVASIQYRaLAD 81
Cdd:cd03404   17 TVDPGERGVVLRFGKYVRTVGPGLHWkLPFPIEVVEKVNVT-QVRSVEIGFRVPeeslmlTGDENIVDVDFVVQYR-ISD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  82 kASDAFYKLSNTREQIQAYVFDVIRASVPKLDLDSTF-EQKNDIAKAVEDELEKAMSAY--GYEIVQTLIVDIEPDEHVK 158
Cdd:cd03404   95 -PVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLtEGRAEIAADVRELLQEILDRYdlGIEIVQVQLQDADPPEEVQ 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 659113223 159 RAMNEINAA----ARLRVAATEKA---------EAEKILQ---------IKRAEGDAE------SKYLAGLGIARQR 207
Cdd:cd03404  174 DAFDDVNAArqdkERLINEAQAYAneviprargEAARIIQeaeaykaevVARAEGDAArflallAEYRKAPEVTRER 250
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 22-181 9.96e-12

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: 62.94  E-value: 9.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  22 GKFDDVLQPGCHcLPWCLGSQI-AGHLSLRLQQLDVRC-ETKTKDNVFVTVVASIQYRaLADkASDAFYKLSNTREQIQA 99
Cdd:cd13438   13 GKLVRTLEPGRY-AFWKFGRKVqVELVDLREQLLEVSGqEILTADKVALRVNLVATYR-VVD-PVKAVETVDDPEEQLYL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223 100 YVFDVIRASVPKLDLDSTFEQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIE-PDEhVKRAMNEINAAARLRVAATEKA 178
Cdd:cd13438   90 ALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIIlPGE-IREILNQVLEAEKRAQANLIRA 168


                 ...
gi 659113223 179 EAE 181
Cdd:cd13438  169 REE 171
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 44-155 2.18e-09

Paraslipin or slipin-2 (SLP-2, 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 all three kingdoms of life. The conserved domain common to these families has also been referred to as the Band 7 domain. Individual proteins of the SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This subgroup of the SLPs remains largely uncharacterized. It includes human SLP-2 which is upregulated and involved in the progression and development in several types of cancer, including esophageal squamous cell carcinoma, endometrial adenocarcinoma, breast cancer, and glioma.


Pssm-ID: 259811 [Multi-domain]  Cd Length: 111  Bit Score: 54.02  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  44 AGHLSLRLQQLDV-RCETKTKDNVFVTVVASIQYRALaDkASDAFYKLSNTREQIQAYVFDVIRASVPKLDLDSTFEQKN 122
Cdd:cd08829    1 AYKVDLREQVLDIpPQEVITKDNVTVTVDAVLYYRVV-D-PYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSRE 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 659113223 123 DIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDE 155
Cdd:cd08829   79 EINAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 10-254 1.04e-08

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: 54.72  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223   10 VDQSTVAIRETFGKFDDVLQPGCHCLPWCLGSQIAGHLSlRLQQLDVRCETKTKDNVFVTVVASIQYRaLADKAsDAFYK 89
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNVT-AVRNLRKQGLMLTGDENIVNVEMNVQYR-ITDPY-KYLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223   90 LSNTREQIQAYVFDVIRASVPKLDLDSTF-EQKNDIAKAVEDELEKAMSAY--GYEIVQTLIVDIEPDEHVKRAMNEINA 166
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDILtEGRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDVII 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  167 AARLRVAATEKAEAEKILQIKRAEGDAESKYLAGLGIARQR--QAIVDGLR-DSVLAFAENVPGTTSKDVmdmvlvtqYF 243
Cdd:TIGR01933 161 AREDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRinRAKGDVARfTKLLAEYKKAPDVTRERL--------YL 232

                         250
                  ....*....|.
gi 659113223  244 DTMKEIGASSK 254
Cdd:TIGR01933 233 ETMEKVLSNTR 243
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 49-151 2.08e-08

Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, podocin, and other members of the stomatin-like protein family (SLPs or slipins). 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. 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. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome. Bacterial and archaebacterial SLPs and many of the eukaryotic family members remain uncharacterized.


Pssm-ID: 259812 [Multi-domain]  Cd Length: 108  Bit Score: 51.04  E-value: 2.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  49 LRLQQLDV-RCETKTKDNVFVTVVASIQYRALadKASDAFYKLSNTREQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKA 127
Cdd:cd13434    3 LRTQSVDVpPQEILTKDNVTVSVDAVVYYRVV--DPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                         90       100
                 ....*....|....*....|....
gi 659113223 128 VEDELEKAMSAYGYEIVQTLIVDI 151
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDI 104
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 48-182 4.57e-07

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: 49.05  E-value: 4.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  48 SLRLQQLDV-RCETKTKDNVFVTVVASIQYRALAdkASDAFYKLSNTREQIQAYVFDVIRASVPKLDLDSTFEQKNDIAK 126
Cdd:cd08826   10 DLRTVTLDVpPQEVITKDNVTVKVNAVVYFRVVD--PEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLSEREEINK 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 659113223 127 AVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRAMNEINAAARLRVAATEKAEAEK 182
Cdd:cd08826   88 RIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGEL 143
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 9-194 8.27e-07

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: 49.02  E-value: 8.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223   9 QVDQSTVAIRETFGK-FDDVLQPGCH-CLPWclgSQIAGHLSLRLQQLDVRC-ETKTKDNVFVTVVASIQYRAladkaSD 85
Cdd:cd03405    4 IVDETEQAVVLQFGKpVRVITEPGLHfKLPF---IQNVRKFDKRILTLDGPPeEVLTKDKKRLIVDSYARWRI-----TD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  86 A--FYKLSNT----REQIQAYVFDVIRASVPKLDLDSTF-EQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIE-PDEhV 157
Cdd:cd03405   76 PlrFYQSVGGeegaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDlPEE-V 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 659113223 158 KRAMNEINAAARLRVAATEKAEAEKILQIKRAEGDAE 194
Cdd:cd03405  155 SESVYERMRAERERIAAEYRAEGEEEAEKIRAEADRE 191
SPFH_like_u1 cd03408
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 66-168 3.97e-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: 259806  Cd Length: 217  Bit Score: 43.70  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  66 VFVTVVASIQYRALADKASDAFyklsntREQIQAYVFDVI-RASVPKLDLDSTfEQKNDIAKAVEDELEKAMSAYGYEIV 144
Cdd:cd03408  117 LFLTEVVGTQGTFTTDEIEEQL------RSEIVQALKDAIaELSISGLDLALE-ANLDELSAALKEKLAPEFEKYGLELT 189

                         90       100
                 ....*....|....*....|....
gi 659113223 145 QTLIVDIEPDEHVKRAMNEINAAA 168
Cdd:cd03408  190 SFGIESISLPEEVQKRIDKRASMA 213
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 47-168 6.63e-05

Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; The flotillin (reggie) like proteins are lipid raft-associated. Individual proteins of this SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. In addition, microdomains formed from flotillin proteins may be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and interact with a variety of proteins. They may play a role 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.


Pssm-ID: 259798 [Multi-domain]  Cd Length: 145  Bit Score: 42.11  E-value: 6.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  47 LSLRLQQLDVRCETK-TKDNVFVTVVASIQYRALADKASDA-----FykLSNTREQIQAYVFDVI----RASVPKLDLDS 116
Cdd:cd03399   12 LSLETMTIDVKVEEVlTKDGIPVDVTAVAQVKVGSDPEEIAaaaerF--LGKSTEEIRELVKETLeghlRAIVGTMTVEE 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 659113223 117 TFEQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRAMNEINAAA 168
Cdd:cd03399   90 IYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAE 141
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
47-210 3.44e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.78  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  47 LSLRLQQLDVRCETK--TKDNVFVTVVASIQYRALAD-----KASDAFykLSNTREQIQAYVFDV----IRASVPKLDLD 115
Cdd:COG2268   66 MSLSTMTIEVERTEGliTKDGIRVDVDAVFYVKVNSDpediaNAAERF--LGRDPEEIEELAEEKlegaLRAVAAQMTVE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223 116 STFEQKNDIAKAVEDELEKAMSAYGYEIVQTLIVDIEPDEHV-----KRAMNEINAAARLRVAATEKAEAEKILQIKRAE 190
Cdd:COG2268  144 ELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYldalgRRKIAEIIRDARIAEAEAERETEIAIAQANREA 223

                        170       180
                 ....*....|....*....|...
gi 659113223 191 GDAESK---YLAGLGIARQRQAI 210
Cdd:COG2268  224 EEAELEqerEIETARIAEAEAEL 246
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 47-182 3.78e-04

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: 40.83  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659113223  47 LSLRLQQLDV-RCETKTKDNVFVTVVASIQYRaLADKASdAFYKLSNTREQIQAYVFDVIRASVPKLDLDSTFEQKNDIA 125
Cdd:cd13435   22 VDLRTVSFDVpPQEVLTKDSVTVTVDAVVYYR-ISDPLN-AVIQVANYSHSTRLLAATTLRNVLGTRNLSELLTERETIS 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 659113223 126 KAVEDELEKAMSAYGYEIVQTLIVDIEPDEHVKRAMNEINAAARLRVAATEKAEAEK 182
Cdd:cd13435  100 HSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEM 156
 
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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