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Conserved domains on  [gi|23346603|ref|NP_694796|]
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stomatin-like protein 3 [Mus musculus]

Protein Classification

SPFH domain-containing protein( domain architecture ID 139628)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_like super family cl19107
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 69-267 2.30e-106

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.


The actual alignment was detected with superfamily member cd03403:

Pssm-ID: 473137 [Multi-domain]  Cd Length: 202  Bit Score: 307.56  E-value: 2.30e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  69 AKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANVNDVHQATFLLAQTTLRNVL 148
Cdd:cd03403   4 AKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 149 GTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAAEAEATREARAKVLAAEGEMNASKSLK 228
Cdd:cd03403  84 GTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRALK 163

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 23346603 229 SASMVLAESPVALQLRYLQTLTTVATEKNSTIVFPLPMN 267
Cdd:cd03403 164 EAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
 
Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 69-267 2.30e-106

Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; Stomatin (or band 7) is widely expressed and, highly expressed in red blood cells. It localizes predominantly to the plasma membrane and to intracellular vesicles of the endocytic pathway, where it is present in higher order homo-oligomeric complexes (of between 9 and 12 monomers). Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and, is implicated in trafficking of Glut1 glucose transporters. This subgroup found in animals, also contains proteins similar to Caenorhabditis elegans MEC-2. MEC-2 interacts with MEC-4, which is part of the degenerin channel complex required for response to gentle body touch.


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 307.56  E-value: 2.30e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  69 AKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANVNDVHQATFLLAQTTLRNVL 148
Cdd:cd03403   4 AKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 149 GTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAAEAEATREARAKVLAAEGEMNASKSLK 228
Cdd:cd03403  84 GTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRALK 163

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 23346603 229 SASMVLAESPVALQLRYLQTLTTVATEKNSTIVFPLPMN 267
Cdd:cd03403 164 EAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 41-263 2.35e-43

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 149.22  E-value: 2.35e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  41 ISVWMCLKIIKEYERAVVFRLGRIQadKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIY 120
Cdd:COG0330  15 VLLFSSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRIT 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 121 SAVSAVANVNDVHQATFLLAQTTLRNVLGTQTLSQILS-GREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRS 199
Cdd:COG0330  93 DPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDA 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 200 MA-----------AEAEATREARAKVLAAEGEMNA-------------------SKSLKSASMVLAESPVALQLRYLQTL 249
Cdd:COG0330 173 MEdrmkaerereaAILEAEGYREAAIIRAEGEAQRaiieaeayreaqilraegeAEAFRIVAEAYSAAPFVLFYRSLEAL 252

                       250
                ....*....|....
gi 23346603 250 TTVATEKNSTIVFP 263
Cdd:COG0330 253 EEVLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 45-200 1.79e-42

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 143.18  E-value: 1.79e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603     45 MCLKIIKEYERAVVFRLGRIQadKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVS 124
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23346603    125 AVANVNDVHQA-TFLLAQTTLRNVLGTQTLSQILSG-REEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSM 200
Cdd:smart00244  79 AVYRVLDADYAvIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 48-220 5.86e-29

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: 108.56  E-value: 5.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603    48 KIIKEYERAVVFRLGRIQadKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRI-----YSA 122
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLS--RVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpddpPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603   123 VSAVANVNDVHQATFLLAQTTLRNVLGTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAA 202
Cdd:pfam01145  79 VQNVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 23346603   203 EAEATREARAKVLAAEGE 220
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 49-197 2.50e-11

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: 62.42  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603    49 IIKEYERAVVFRLGriQADKAKGPGLILVLPCIDVFVKVDLRTVTcNIPPQ-EILTRDSVTTQVDGVVYYRI---YSAVS 124
Cdd:TIGR01933   3 TIGEAERGVVLRFG--KYHRTVDPGLNWKPPFIEEVYPVNVTAVR-NLRKQgLMLTGDENIVNVEMNVQYRItdpYKYLF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23346603   125 AVANVNDV-HQATfllaQTTLRNVLGTQTLSQIL-SGREEIAHSIQTLLD---DATELwGIRVARVEIKDVRIPVQLQ 197
Cdd:TIGR01933  80 SVENPEDSlRQAT----DSALRGVIGDSTMDDILtEGRSQIREDTKERLNeiiDNYDL-GITVTDVNFQSARPPEEVK 152
PRK10930 PRK10930
FtsH protease activity modulator HflK;
50-193 1.29e-04

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 42.89  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603   50 IKEYERAVVFRLGRIqaDKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVS---AV 126
Cdd:PRK10930 100 IKEAERGVVTRFGKF--SHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTDPEKylfSV 177

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23346603  127 ANVND-VHQATfllaQTTLRNVLGTQTLSQILS-GREEIAHSIQTLLDDATELW--GIRVARVEIKDVRIP 193
Cdd:PRK10930 178 TSPDDsLRQAT----DSALRGVIGKYTMDRILTeGRTVIRSDTQRELEETIRPYdmGITLLDVNFQAARPP 244
 
Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 69-267 2.30e-106

Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; Stomatin (or band 7) is widely expressed and, highly expressed in red blood cells. It localizes predominantly to the plasma membrane and to intracellular vesicles of the endocytic pathway, where it is present in higher order homo-oligomeric complexes (of between 9 and 12 monomers). Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and, is implicated in trafficking of Glut1 glucose transporters. This subgroup found in animals, also contains proteins similar to Caenorhabditis elegans MEC-2. MEC-2 interacts with MEC-4, which is part of the degenerin channel complex required for response to gentle body touch.


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 307.56  E-value: 2.30e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  69 AKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANVNDVHQATFLLAQTTLRNVL 148
Cdd:cd03403   4 AKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 149 GTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAAEAEATREARAKVLAAEGEMNASKSLK 228
Cdd:cd03403  84 GTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRALK 163

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 23346603 229 SASMVLAESPVALQLRYLQTLTTVATEKNSTIVFPLPMN 267
Cdd:cd03403 164 EAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 70-223 9.22e-97

Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this slipin subgroup remain uncharacterized, except for Caenorhabditis elegans UNC-1. Mutations in the unc-1 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259810 [Multi-domain]  Cd Length: 154  Bit Score: 281.15  E-value: 9.22e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  70 KGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANVNDVHQATFLLAQTTLRNVLG 149
Cdd:cd08828   1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23346603 150 TQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAAEAEATREARAKVLAAEGEMNA 223
Cdd:cd08828  81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 69-269 1.05e-95

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: 280.81  E-value: 1.05e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  69 AKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANVNDVHQATFLLAQTTLRNVL 148
Cdd:cd13435   4 ARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 149 GTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAAEAEATREARAKVLAAEGEMNASKSLK 228
Cdd:cd13435  84 GTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRALK 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 23346603 229 SASMVLAESPVALQLRYLQTLTTVATEKNSTIVFPLPMNIL 269
Cdd:cd13435 164 EASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELL 204
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 44-265 5.47e-72

Podocin, 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 vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Podocin is expressed in the kidney and mutations in the gene have been linked to familial idiopathic nephrotic syndrome. Podocin interacts with the TRP ion channel TRPV-6 and may function as a scaffolding protein in the organization of lipid-protein domains.


Pssm-ID: 259809 [Multi-domain]  Cd Length: 223  Bit Score: 220.92  E-value: 5.47e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  44 WMCLKIIKEYERAVVFRLGRIQADKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSA- 122
Cdd:cd08827   1 WFCVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAs 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 123 --VSAVANVNDVHQAtflLAQTTLRNVLGTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSM 200
Cdd:cd08827  81 vcLSSFASISDAMQA---LVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSF 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23346603 201 AAEAEATREARAKVLAAEGEMNASKSLKSASMVLAESPVALQLRYLQTLTTVATEKNSTIVFPLP 265
Cdd:cd08827 158 AVEAEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLP 222
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 79-256 7.13e-69

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: 211.22  E-value: 7.13e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  79 PCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANVNDVHQATFLLAQTTLRNVLGTQTLSQILS 158
Cdd:cd08826   1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 159 GREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAAEAEATREARAKVLAAEGEMNASKSLKSASMVLAESP 238
Cdd:cd08826  81 EREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSP 160

                       170
                ....*....|....*...
gi 23346603 239 VALQLRYLQTLTTVATEK 256
Cdd:cd08826 161 GALQLRYLQTLSEIASEK 178
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 87-193 1.36e-53

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: 169.68  E-value: 1.36e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  87 VDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANVNDVHQATFLLAQTTLRNVLGTQTLSQILSGREEIAHS 166
Cdd:cd13434   1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                        90       100
                ....*....|....*....|....*..
gi 23346603 167 IQTLLDDATELWGIRVARVEIKDVRIP 193
Cdd:cd13434  81 LQEILDEATDPWGIKVERVEIKDIILP 107
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 50-267 4.83e-52

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: 169.72  E-value: 4.83e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  50 IKEYERAVVFRLGRIQadKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANV 129
Cdd:cd13437   9 VKQGSVGLVERFGKFY--KTVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 130 NDVHQATFLLAQTTLRNVLGTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAAEAEATRE 209
Cdd:cd13437  87 DNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRI 166

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23346603 210 ARAKVLAAEGEMNASKSLKSASMVLAeSPVALQLRYLQTLTTVATEKNSTIVFpLPMN 267
Cdd:cd13437 167 GESKIISAKADVESAKLMREAADILD-SKAAMQIRYLETLQAIAKSANSKVIF-LPLD 222
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 41-263 2.35e-43

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 149.22  E-value: 2.35e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  41 ISVWMCLKIIKEYERAVVFRLGRIQadKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIY 120
Cdd:COG0330  15 VLLFSSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRIT 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 121 SAVSAVANVNDVHQATFLLAQTTLRNVLGTQTLSQILS-GREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRS 199
Cdd:COG0330  93 DPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDA 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 200 MA-----------AEAEATREARAKVLAAEGEMNA-------------------SKSLKSASMVLAESPVALQLRYLQTL 249
Cdd:COG0330 173 MEdrmkaerereaAILEAEGYREAAIIRAEGEAQRaiieaeayreaqilraegeAEAFRIVAEAYSAAPFVLFYRSLEAL 252

                       250
                ....*....|....
gi 23346603 250 TTVATEKNSTIVFP 263
Cdd:COG0330 253 EEVLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 45-200 1.79e-42

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 143.18  E-value: 1.79e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603     45 MCLKIIKEYERAVVFRLGRIQadKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVS 124
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23346603    125 AVANVNDVHQA-TFLLAQTTLRNVLGTQTLSQILSG-REEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSM 200
Cdd:smart00244  79 AVYRVLDADYAvIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAM 156
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 87-263 4.70e-40

Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of the SPFH family (stomatin, prohibitin, flotillin, and HflK/C); This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized.


Pssm-ID: 259817 [Multi-domain]  Cd Length: 177  Bit Score: 137.37  E-value: 4.70e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  87 VDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANVNDVHQATFLLAQTTLRNVLGTQTLSQILSGREEIAHS 166
Cdd:cd13775   1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 167 IQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAAEAEATREARAKVLAAEGEMNASKSLKSASMVLAESPVALQLRYL 246
Cdd:cd13775  81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAM 160

                       170
                ....*....|....*..
gi 23346603 247 QTLTTVATEKNSTIVFP 263
Cdd:cd13775 161 NMLYEGLKEKGSMVVVP 177
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 86-193 1.24e-38

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: 131.44  E-value: 1.24e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  86 KVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANVNDVHQATFLLAQTTLRNVLGTQTLSQILSGREEIAH 165
Cdd:cd08829   3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                        90       100
                ....*....|....*....|....*...
gi 23346603 166 SIQTLLDDATELWGIRVARVEIKDVRIP 193
Cdd:cd08829  83 KLLEALDEATDPWGVKVTRVEIKDITPP 110
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 62-192 6.31e-36

Stomatin-like protein 1 (SLP-1), 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 animals. 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. The family contains human SLP-1, which has been found to be expressed in the brain, and Caenorhabditis elegans UNC-24, which is a lipid raft-associated protein required for normal locomotion. It may mediate the correct localization of UNC-1. Mutations in the unc-24 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259814 [Multi-domain]  Cd Length: 131  Bit Score: 125.20  E-value: 6.31e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  62 GRIQadKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVANVNDVHQATFLLAQ 141
Cdd:cd13436   1 GRLQ--KPRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQ 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 23346603 142 TTLRNVLGTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRI 192
Cdd:cd13436  79 TSLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 50-262 4.20e-32

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: 118.02  E-value: 4.20e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  50 IKEYERAVVFRLGRIQadKAKGPGLILV-LPCIDVFV-KVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVA 127
Cdd:cd13438   1 VPPGERGLLYRDGKLV--RTLEPGRYAFwKFGRKVQVeLVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 128 NVNDVHQATFLLAQTTLRNVLGTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAAEAEAT 207
Cdd:cd13438  79 TVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAE 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23346603 208 REARAKVLAAEGEMNASKSLKSASMVLAESPVALQLRYLQTLTTVATEKNSTIVF 262
Cdd:cd13438 159 KRAQANLIRAREETAATRSLLNAAKLMEENPALLRLRELEALEKIAEKVGHISVS 213
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 48-220 5.86e-29

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: 108.56  E-value: 5.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603    48 KIIKEYERAVVFRLGRIQadKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRI-----YSA 122
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLS--RVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpddpPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603   123 VSAVANVNDVHQATFLLAQTTLRNVLGTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQRSMAA 202
Cdd:pfam01145  79 VQNVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 23346603   203 EAEATREARAKVLAAEGE 220
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 46-192 1.41e-20

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: 88.31  E-value: 1.41e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  46 CLKIIKEYERAVVFRLGRIQADKaKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSA 125
Cdd:cd03405   1 SVFIVDETEQAVVLQFGKPVRVI-TEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRF 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23346603 126 VANVNDVHQATFLLAQ---TTLRNVLGTQTLSQILSG-REEIAHSIQTLLDDATELWGIrvarvEIKDVRI 192
Cdd:cd03405  80 YQSVGGEEGAESRLDDivdSALRNEIGKRTLAEVVSGgRDELMEEILEQANEEAKEYGI-----EVVDVRI 145
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 49-197 6.65e-16

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: 75.63  E-value: 6.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  49 IIKEYERAVVFRLGRIQADKakGPGLILVLPC-IDVFVKVDLRTV----TCNIPPQE--ILTRDSVTTQVDGVVYYRIYS 121
Cdd:cd03404  17 TVDPGERGVVLRFGKYVRTV--GPGLHWKLPFpIEVVEKVNVTQVrsveIGFRVPEEslMLTGDENIVDVDFVVQYRISD 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 122 AVSAVANVNDVHQATFLLAQTTLRNVLGTQTLSQILS-GREEIAHSIQTLLD---DATELwGIRVARVEIKDVRIPVQLQ 197
Cdd:cd03404  95 PVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQeilDRYDL-GIEIVQVQLQDADPPEEVQ 173
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 47-199 1.96e-15

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: 72.93  E-value: 1.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  47 LKIIKEYERAVVFRLGRIQADKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPqEILTRDSVTTQVDGVVYYRIYsavsaV 126
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRPD-----P 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 127 ANVNDVHQ-------ATFL--LAQTTLRNVLGTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQ 197
Cdd:cd03401  75 EKLPELYQnlgpdyeERVLppIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYE 154


                ..
gi 23346603 198 RS 199
Cdd:cd03401 155 KA 156
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 95-193 3.12e-14

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: 67.39  E-value: 3.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  95 NIPPQEILTRDSVTTQVDGVVYYRI--YSAVSAVANVNDVHQA-TFLL--AQTTLRNVLGTQTLSQILSGREEIAHSIQT 169
Cdd:cd02106   6 DVRVEPVGTADGVPVAVDLVVQFRItdYNALPAFYLVDFVKDIkADIRrkIADVLRAAIGRMTLDQIISGRDEIAKAVKE 85

                        90       100
                ....*....|....*....|....
gi 23346603 170 LLDDATELWGIRVARVEIKDVRIP 193
Cdd:cd02106  86 DLEEDLENFGVVISDVDITSIEPP 109
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 49-197 2.50e-11

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: 62.42  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603    49 IIKEYERAVVFRLGriQADKAKGPGLILVLPCIDVFVKVDLRTVTcNIPPQ-EILTRDSVTTQVDGVVYYRI---YSAVS 124
Cdd:TIGR01933   3 TIGEAERGVVLRFG--KYHRTVDPGLNWKPPFIEEVYPVNVTAVR-NLRKQgLMLTGDENIVNVEMNVQYRItdpYKYLF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23346603   125 AVANVNDV-HQATfllaQTTLRNVLGTQTLSQIL-SGREEIAHSIQTLLD---DATELwGIRVARVEIKDVRIPVQLQ 197
Cdd:TIGR01933  80 SVENPEDSlRQAT----DSALRGVIGDSTMDDILtEGRSQIREDTKERLNeiiDNYDL-GITVTDVNFQSARPPEEVK 152
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 76-191 2.38e-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: 43.26  E-value: 2.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  76 LVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAVAN---------VNDVHQatfLLAQT---T 143
Cdd:cd03399   1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAaaerflgksTEEIRE---LVKETlegH 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 23346603 144 LRNVLGTQTLSQILSGREEIAHSIQTLLddATEL--WGIRVARVEIKDVR 191
Cdd:cd03399  78 LRAIVGTMTVEEIYQDREKFAEQVQEVA--EPDLakMGLEIDSFNIKDIS 125
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 49-236 3.73e-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: 44.11  E-value: 3.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  49 IIKEYERAVVFRLGRIqaDKAKGPGLILVLPCID-VFVKVDLRT----VTCnippqEILTRDSVTTQVDGVVYYR----- 118
Cdd:cd03407   1 CVSQSTVAIVERFGKF--SRIAEPGLHFIIPPIEsVAGRVSLRVqqldVRV-----ETKTKDNVFVTLVVSVQYRvvpek 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603 119 IYSAVSAVANVNDVHQAtflLAQTTLRNVLGTQTLSQILSGREEIAHSIQTLLDDATELWGIRVARVEIKDVRIPVQLQR 198
Cdd:cd03407  74 VYDAFYKLTNPEQQIQS---YVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKA 150

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23346603 199 SMaaeaeatrearakvlaaeGEMNASKSLKSASMVLAE 236
Cdd:cd03407 151 AM------------------NEINAAQRLREAAEEKAE 170
PRK10930 PRK10930
FtsH protease activity modulator HflK;
50-193 1.29e-04

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 42.89  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603   50 IKEYERAVVFRLGRIqaDKAKGPGLILVLPCIDVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVS---AV 126
Cdd:PRK10930 100 IKEAERGVVTRFGKF--SHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTDPEKylfSV 177

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23346603  127 ANVND-VHQATfllaQTTLRNVLGTQTLSQILS-GREEIAHSIQTLLDDATELW--GIRVARVEIKDVRIP 193
Cdd:PRK10930 178 TSPDDsLRQAT----DSALRGVIGKYTMDRILTeGRTVIRSDTQRELEETIRPYdmGITLLDVNFQAARPP 244
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 47-192 1.53e-03

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: 259800  Cd Length: 231  Bit Score: 39.07  E-value: 1.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346603  47 LKIIKEYERAVVFRLGRIqADKAKGPGLILVLPCIdVFVKVDLRTVTCNIPPQEILTRDSVTTQVDGVVYYRIYSAVSAV 126
Cdd:cd03402  10 FFVVQPNEAAVLTLFGRY-RGTVRRPGLRWVNPFY-RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWRVVDTAKAV 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23346603 127 ANVNDVHQATFLLAQTTLRNVL----------GTQTLSqilSGREEIAHSIQTLLDDATElwgirVARVEIKDVRI 192
Cdd:cd03402  88 FDVDDYEEFVSIQSEAALRRVAsrypydsfedGEPSLR---GNSDEVSEELRRELQERLA-----VAGVEVIEARI 155
 
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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