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Conserved domains on  [gi|991820199|ref|NP_001307002|]
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stomatin isoform 1 [Danio rerio]

Protein Classification

stomatin family protein( domain architecture ID 10130453)

stomatin family protein similar to Homo sapiens erythrocyte band 7 integral membrane protein that regulates ion channel activity and transmembrane ion transport

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 85-286 4.12e-131

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: 370.34  E-value: 4.12e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  85 RGGAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANITNADAATRLLAQTTLR 164
Cdd:cd03403    1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 165 NVLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQRAMAAEAEASREARAKVIAAEGEMNASR 244
Cdd:cd03403   81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 991820199 245 ALKEASLVIAESPSALQLRYLQTLNTIAAEKNSTIIFPLPID 286
Cdd:cd03403  161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
 
Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 85-286 4.12e-131

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: 370.34  E-value: 4.12e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  85 RGGAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANITNADAATRLLAQTTLR 164
Cdd:cd03403    1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 165 NVLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQRAMAAEAEASREARAKVIAAEGEMNASR 244
Cdd:cd03403   81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 991820199 245 ALKEASLVIAESPSALQLRYLQTLNTIAAEKNSTIIFPLPID 286
Cdd:cd03403  161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 62-282 7.28e-49

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 163.47  E-value: 7.28e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  62 IWMCIKIVKEYERAIIFRLGRILRggAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNA 141
Cdd:COG0330   17 LFSSVYIVPQGERGVVLRFGKYVR--TLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 142 TLAVANITNADAATRLLAQTTLRNVLGTKNLAEILS-DREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQL----- 215
Cdd:COG0330   95 AKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVqdame 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 216 ------QRAMAAEAEASREARAKVIAAEGE----MNASRALKEASLVIAE---------------SPSALQLRYLQTLNT 270
Cdd:COG0330  175 drmkaeREREAAILEAEGYREAAIIRAEGEaqraIIEAEAYREAQILRAEgeaeafrivaeaysaAPFVLFYRSLEALEE 254

                        250
                 ....*....|..
gi 991820199 271 IAAEKNSTIIFP 282
Cdd:COG0330  255 VLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 64-216 2.80e-48

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 158.21  E-value: 2.80e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199    64 MCIKIVKEYERAIIFRLGRILRggAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATL 143
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR--VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 991820199   144 AVANITNAD-AATRLLAQTTLRNVLGTKNLAEILSD-REEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQ 216
Cdd:smart00244  79 AVYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK 153
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 67-239 3.31e-32

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: 117.42  E-value: 3.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199   67 KIVKEYERAIIFRLGRIlrGGAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQ--NATLA 144
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKL--SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  145 VANITNADAATRLL---AQTTLRNVLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQRAMAA 221
Cdd:pfam01145  79 VQNVFGSDDLQELLrrvLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 991820199  222 EAEASREARAKVIAAEGE 239
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 66-216 1.79e-12

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: 65.89  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199   66 IKIVKEYERAIIFRLGRILRggAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAV 145
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHR--TVDPGLNWKPPFIEEVYPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPYKYL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 991820199  146 ANITNADAATRLLAQTTLRNVLGTKNLAEILSD-REEIAHSMQSTLDDATD--DWGIKVERVEIKDVKLPLQLQ 216
Cdd:TIGR01933  79 FSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDnyDLGITVTDVNFQSARPPEEVK 152
PRK11029 PRK11029
protease modulator HflC;
68-178 2.59e-05

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 45.12  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  68 IVKEYERAIIFRLGRILRGGAK-----GPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNAT 142
Cdd:PRK11029  22 VVKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADRFVTKEKKDLIVDSYIKWRISDFS 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 991820199 143 ---LAV--ANITNADAATRLLAQTTLRNVLGTKNLAEILSD 178
Cdd:PRK11029 102 ryyLATggGDISQAEVLLKRKFSDRLRSEIGRLDVKDIVTD 142
 
Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 85-286 4.12e-131

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: 370.34  E-value: 4.12e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  85 RGGAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANITNADAATRLLAQTTLR 164
Cdd:cd03403    1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 165 NVLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQRAMAAEAEASREARAKVIAAEGEMNASR 244
Cdd:cd03403   81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 991820199 245 ALKEASLVIAESPSALQLRYLQTLNTIAAEKNSTIIFPLPID 286
Cdd:cd03403  161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 86-292 1.80e-109

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: 315.86  E-value: 1.80e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  86 GGAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANITNADAATRLLAQTTLRN 165
Cdd:cd13435    2 GGARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 166 VLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQRAMAAEAEASREARAKVIAAEGEMNASRA 245
Cdd:cd13435   82 VLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 991820199 246 LKEASLVIAESPSALQLRYLQTLNTIAAEKNSTIIFPLPIDMMQSFL 292
Cdd:cd13435  162 LKEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLTPLL 208
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 63-284 6.44e-79

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: 238.63  E-value: 6.44e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  63 WMCIKIVKEYERAIIFRLGRILRGGAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNAT 142
Cdd:cd08827    1 WFCVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 143 LAVANITNADAATRLLAQTTLRNVLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQRAMAAE 222
Cdd:cd08827   81 VCLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 991820199 223 AEASREARAKVIAAEGEMNASRALKEASLVIAESPSALQLRYLQTLNTIAAEKNSTIIFPLP 284
Cdd:cd08827  161 AEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLP 222
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 89-242 2.28e-75

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: 227.22  E-value: 2.28e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  89 KGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANITNADAATRLLAQTTLRNVLG 168
Cdd:cd08828    1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 991820199 169 TKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQRAMAAEAEASREARAKVIAAEGEMNA 242
Cdd:cd08828   81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 98-275 5.10e-67

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: 206.60  E-value: 5.10e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  98 PCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANITNADAATRLLAQTTLRNVLGTKNLAEILS 177
Cdd:cd08826    1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 178 DREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQRAMAAEAEASREARAKVIAAEGEMNASRALKEASLVIAESP 257
Cdd:cd08826   81 EREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSP 160

                        170
                 ....*....|....*...
gi 991820199 258 SALQLRYLQTLNTIAAEK 275
Cdd:cd08826  161 GALQLRYLQTLSEIASEK 178
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 69-286 7.47e-58

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: 184.74  E-value: 7.47e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  69 VKEYERAIIFRLGRILRggAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANI 148
Cdd:cd13437    9 VKQGSVGLVERFGKFYK--TVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 149 TNADAATRLLAQTTLRNVLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQRAMAAEAEASRE 228
Cdd:cd13437   87 DNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRI 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 991820199 229 ARAKVIAAEGEMNASRALKEASLVIAeSPSALQLRYLQTLNTIAAEKNSTIIFpLPID 286
Cdd:cd13437  167 GESKIISAKADVESAKLMREAADILD-SKAAMQIRYLETLQAIAKSANSKVIF-LPLD 222
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 106-212 2.32e-56

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: 177.00  E-value: 2.32e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 106 VDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANITNADAATRLLAQTTLRNVLGTKNLAEILSDREEIAHS 185
Cdd:cd13434    1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                         90       100
                 ....*....|....*....|....*..
gi 991820199 186 MQSTLDDATDDWGIKVERVEIKDVKLP 212
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDIILP 107
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 62-282 7.28e-49

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 163.47  E-value: 7.28e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  62 IWMCIKIVKEYERAIIFRLGRILRggAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNA 141
Cdd:COG0330   17 LFSSVYIVPQGERGVVLRFGKYVR--TLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 142 TLAVANITNADAATRLLAQTTLRNVLGTKNLAEILS-DREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQL----- 215
Cdd:COG0330   95 AKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVqdame 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 216 ------QRAMAAEAEASREARAKVIAAEGE----MNASRALKEASLVIAE---------------SPSALQLRYLQTLNT 270
Cdd:COG0330  175 drmkaeREREAAILEAEGYREAAIIRAEGEaqraIIEAEAYREAQILRAEgeaeafrivaeaysaAPFVLFYRSLEALEE 254

                        250
                 ....*....|..
gi 991820199 271 IAAEKNSTIIFP 282
Cdd:COG0330  255 VLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 64-216 2.80e-48

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 158.21  E-value: 2.80e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199    64 MCIKIVKEYERAIIFRLGRILRggAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATL 143
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR--VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 991820199   144 AVANITNAD-AATRLLAQTTLRNVLGTKNLAEILSD-REEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQ 216
Cdd:smart00244  79 AVYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK 153
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 106-212 3.16e-43

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: 143.38  E-value: 3.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 106 VDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANITNADAATRLLAQTTLRNVLGTKNLAEILSDREEIAHS 185
Cdd:cd08829    4 VDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAK 83

                         90       100
                 ....*....|....*....|....*..
gi 991820199 186 MQSTLDDATDDWGIKVERVEIKDVKLP 212
Cdd:cd08829   84 LLEALDEATDPWGVKVTRVEIKDITPP 110
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 106-282 6.54e-42

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: 142.38  E-value: 6.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 106 VDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANITNADAATRLLAQTTLRNVLGTKNLAEILSDREEIAHS 185
Cdd:cd13775    1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 186 MQSTLDDATDDWGIKVERVEIKDVKLPLQLQRAMAAEAEASREARAKVIAAEGEMNASRALKEASLVIAESPSALQLRYL 265
Cdd:cd13775   81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAM 160

                        170
                 ....*....|....*..
gi 991820199 266 QTLNTIAAEKNSTIIFP 282
Cdd:cd13775  161 NMLYEGLKEKGSMVVVP 177
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 81-211 5.30e-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: 125.59  E-value: 5.30e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  81 GRILRggAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANITNADAATRLLAQ 160
Cdd:cd13436    1 GRLQK--PRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQ 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 991820199 161 TTLRNVLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKL 211
Cdd:cd13436   79 TSLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 69-281 1.97e-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: 119.18  E-value: 1.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  69 VKEYERAIIFRLGRILRggAKGPGL--FFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVA 146
Cdd:cd13438    1 VPPGERGLLYRDGKLVR--TLEPGRyaFWKFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 147 NITNADAATRLLAQTTLRNVLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQRAMAAEAEAS 226
Cdd:cd13438   79 TVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 991820199 227 REARAKVIAAEGEMNASRALKEASLVIAESPSALQLRYLQTLNTIAAEKNSTIIF 281
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 ...
 67-239 3.31e-32

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: 117.42  E-value: 3.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199   67 KIVKEYERAIIFRLGRIlrGGAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQ--NATLA 144
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKL--SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  145 VANITNADAATRLL---AQTTLRNVLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQRAMAA 221
Cdd:pfam01145  79 VQNVFGSDDLQELLrrvLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 991820199  222 EAEASREARAKVIAAEGE 239
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 65-212 1.96e-26

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: 104.11  E-value: 1.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  65 CIKIVKEYERAIIFRLGRILRGgAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLA 144
Cdd:cd03405    1 SVFIVDETEQAVVLQFGKPVRV-ITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 991820199 145 VANITNADAATRLLAQ---TTLRNVLGTKNLAEILSD-REEIAHSMQSTLDDATDDWGIKVERVEIKDVKLP 212
Cdd:cd03405   80 YQSVGGEEGAESRLDDivdSALRNEIGKRTLAEVVSGgRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLP 151
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 66-212 3.27e-19

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: 83.33  E-value: 3.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  66 IKIVKEYERAIIFRLGRILRGGAKGPGLFFILPCTDSFINVDMRTITFDIPPqEVLTKDSVTVSVDGVVYYRVQNATLA- 144
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRPDPEKLPe 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 991820199 145 VANITNADAATRLL---AQTTLRNVLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLP 212
Cdd:cd03401   80 LYQNLGPDYEERVLppiVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFP 150
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 62-216 8.96e-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: 75.24  E-value: 8.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  62 IWMC--IKIVKEYERAIIFRLGRILRggAKGPGLFFILPC-TDSFINVDM---RTITFDIPPQE---VLTKDSVTVSVDG 132
Cdd:cd03404    9 VWLLsgFYTVDPGERGVVLRFGKYVR--TVGPGLHWKLPFpIEVVEKVNVtqvRSVEIGFRVPEeslMLTGDENIVDVDF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 133 VVYYRVQNATLAVANITNADAATRLLAQTTLRNVLGTKNLAEILS-DREEIA----HSMQSTLDDAtdDWGIKVERVEIK 207
Cdd:cd03404   87 VVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAadvrELLQEILDRY--DLGIEIVQVQLQ 164


                 ....*....
gi 991820199 208 DVKLPLQLQ 216
Cdd:cd03404  165 DADPPEEVQ 173
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 66-216 1.79e-12

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: 65.89  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199   66 IKIVKEYERAIIFRLGRILRggAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAV 145
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHR--TVDPGLNWKPPFIEEVYPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPYKYL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 991820199  146 ANITNADAATRLLAQTTLRNVLGTKNLAEILSD-REEIAHSMQSTLDDATD--DWGIKVERVEIKDVKLPLQLQ 216
Cdd:TIGR01933  79 FSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDnyDLGITVTDVNFQSARPPEEVK 152
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 112-212 2.51e-12

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: 62.38  E-value: 2.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 112 TFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVA-----NITNADAATRLLAQTTLRNVLGTKNLAEILSDREEIAHSM 186
Cdd:cd02106    4 FDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAfylvdFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAV 83

                         90       100
                 ....*....|....*....|....*.
gi 991820199 187 QSTLDDATDDWGIKVERVEIKDVKLP 212
Cdd:cd02106   84 KEDLEEDLENFGVVISDVDITSIEPP 109
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 95-210 1.80e-11

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: 60.98  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  95 FILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANitnadAATRLLAQTT------------ 162
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAA-----AAERFLGKSTeeirelvketle 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 991820199 163 --LRNVLGTKNLAEILSDREEIAHSMQstlDDATDD---WGIKVERVEIKDVK 210
Cdd:cd03399   76 ghLRAIVGTMTVEEIYQDREKFAEQVQ---EVAEPDlakMGLEIDSFNIKDIS 125
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
82-210 2.05e-09

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 57.96  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  82 RILRGGAKgpglfFILPCTDSFINVDMRTITFDIPPQE-VLTKDSVTVSVDGVVYYRVQNATLAVANitnadAATRLLAQ 160
Cdd:COG2268   47 KVVTGGGA-----FVLPVLHRAERMSLSTMTIEVERTEgLITKDGIRVDVDAVFYVKVNSDPEDIAN-----AAERFLGR 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 991820199 161 TT--------------LRNVLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVK 210
Cdd:COG2268  117 DPeeieelaeeklegaLRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLE 180
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 68-281 2.36e-08

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: 53.74  E-value: 2.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  68 IVKEYERAIIFRLGRILRggAKGPGLFFILPCTDS-FINVDMRT--ITFDIppqEVLTKDSVTVSVDGVVYYRV--QNAT 142
Cdd:cd03407    1 CVSQSTVAIVERFGKFSR--IAEPGLHFIIPPIESvAGRVSLRVqqLDVRV---ETKTKDNVFVTLVVSVQYRVvpEKVY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 143 LAVANITNADAATRLLAQTTLRNVLGTKNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKDVKLPLQLQ------ 216
Cdd:cd03407   76 DAFYKLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKaamnei 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199 217 -----RAMAAEAEASREARAKVIAAEGEMNASRA---------------LKEASL--------VIAESPSALQL--RYLQ 266
Cdd:cd03407  156 naaqrLREAAEEKAEAEKILQVKAAEAEAEAKRLqgvgiaeqrkaivdgLRESIEdfqeavpgVSSKEVMDLLLitQYFD 235

                        250
                 ....*....|....*
gi 991820199 267 TLNTIAAEKNSTIIF 281
Cdd:cd03407  236 TLKEVGKSSKSSTVF 250
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 67-208 2.69e-07

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259800  Cd Length: 231  Bit Score: 50.24  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  67 KIVKEYERAIIFRLGRiLRGGAKGPGLFFILPCTdSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVA 146
Cdd:cd03402   11 FVVQPNEAAVLTLFGR-YRGTVRRPGLRWVNPFY-RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWRVVDTAKAVF 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 991820199 147 NITNADAATRLLAQTTLRNVLGT-------KNLAEILSDREEIAHSMQSTLDDATDDWGIKVERVEIKD 208
Cdd:cd03402   89 DVDDYEEFVSIQSEAALRRVASRypydsfeDGEPSLRGNSDEVSEELRRELQERLAVAGVEVIEARITH 157
PRK11029 PRK11029
protease modulator HflC;
68-178 2.59e-05

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 45.12  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  68 IVKEYERAIIFRLGRILRGGAK-----GPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNAT 142
Cdd:PRK11029  22 VVKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADRFVTKEKKDLIVDSYIKWRISDFS 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 991820199 143 ---LAV--ANITNADAATRLLAQTTLRNVLGTKNLAEILSD 178
Cdd:PRK11029 102 ryyLATggGDISQAEVLLKRKFSDRLRSEIGRLDVKDIVTD 142
PRK10930 PRK10930
FtsH protease activity modulator HflK;
69-185 2.07e-04

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 42.51  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 991820199  69 VKEYERAIIFRLGRIlrGGAKGPGLFFILPCTDSFINVDMRTITFDIPPQEVLTKDSVTVSVDGVVYYRVQNATLAVANI 148
Cdd:PRK10930 100 IKEAERGVVTRFGKF--SHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTDPEKYLFSV 177

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 991820199 149 TNADAATRLLAQTTLRNVLGTKNLAEILSDREEIAHS 185
Cdd:PRK10930 178 TSPDDSLRQATDSALRGVIGKYTMDRILTEGRTVIRS 214
 
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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