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Conserved domains on  [gi|281361631|ref|NP_731667|]
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uncharacterized protein Dmel_CG14736, isoform D [Drosophila melanogaster]

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 ...
 100-305 3.15e-89

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 cd13435:

Pssm-ID: 473137 [Multi-domain]  Cd Length: 208  Bit Score: 270.41  E-value: 3.15e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 100 GLRGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSIIQVDDAKQATQLISQVTLRNI 179
Cdd:cd13435    3 GARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 180 VGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLASEAEAVREARAKIILAEGELKASKAL 259
Cdd:cd13435   83 LGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRAL 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 281361631 260 KEASDVMSENKITLQLRHLQILSSIASERRVRIIYPIPLEIMEPFM 305
Cdd:cd13435  163 KEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLTPLL 208
 
Name Accession Description Interval E-value
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 100-305 3.15e-89

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: 270.41  E-value: 3.15e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 100 GLRGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSIIQVDDAKQATQLISQVTLRNI 179
Cdd:cd13435    3 GARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 180 VGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLASEAEAVREARAKIILAEGELKASKAL 259
Cdd:cd13435   83 LGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRAL 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 281361631 260 KEASDVMSENKITLQLRHLQILSSIASERRVRIIYPIPLEIMEPFM 305
Cdd:cd13435  163 KEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLTPLL 208
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 58-252 2.50e-38

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 140.36  E-value: 2.50e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  58 KVAIGICWFLVIITFPFSmccCLTIVPEYSRMIILRLGRLRKGLrGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKD 137
Cdd:COG0330    2 KLILLLILLVLVLVLLFS---SVYIVPQGERGVVLRFGKYVRTL-EPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 138 SVTITVNAVVYYCIYSPIDSIIQVDDAKQATQLISQVTLRNIVGSKTLN-VLLTSRQQLSREIQQAVAGITYRWGVRVER 216
Cdd:COG0330   78 NNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDeVLSTGRDEINAEIREELQEALDPYGIEVVD 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 281361631 217 VDVMDITLPTSLERSLASEAEAVREARAKIILAEGE 252
Cdd:COG0330  158 VEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGY 193
PHB smart00244
prohibitin homologues; prohibitin homologues
 78-225 1.68e-31

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 118.15  E-value: 1.68e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631    78 CCLTIVPEYSRMIILRLGRLRKgLRGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDS 157
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281361631   158 IIQVDDA--KQATQLIsQVTLRNIVGSKTLNVLLTS-RQQLSREIQQAVAGITYRWGVRVERVDVMDITLP 225
Cdd:smart00244  80 VYRVLDAdyAVIEQLA-QTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLP 149
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 81-252 1.29e-28

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: 110.87  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631   81 TIVPEYSRMIILRLGRLRkGLRGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCI--YSPIDSI 158
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLS-RVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  159 IQVDDAKQATQLISQV---TLRNIVGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLASE 235
Cdd:pfam01145  80 QNVFGSDDLQELLRRVlesALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*..
gi 281361631  236 AEAVREARAKIILAEGE 252
Cdd:pfam01145 160 QTAEQEAEAEIARAEAE 176
 
Name Accession Description Interval E-value
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 100-305 3.15e-89

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: 270.41  E-value: 3.15e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 100 GLRGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSIIQVDDAKQATQLISQVTLRNI 179
Cdd:cd13435    3 GARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 180 VGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLASEAEAVREARAKIILAEGELKASKAL 259
Cdd:cd13435   83 LGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRAL 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 281361631 260 KEASDVMSENKITLQLRHLQILSSIASERRVRIIYPIPLEIMEPFM 305
Cdd:cd13435  163 KEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLTPLL 208
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 100-299 1.93e-77

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: 239.76  E-value: 1.93e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 100 GLRGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSIIQVDDAKQATQLISQVTLRNI 179
Cdd:cd03403    3 GAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 180 VGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLASEAEAVREARAKIILAEGELKASKAL 259
Cdd:cd03403   83 LGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRAL 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 281361631 260 KEASDVMSENKITLQLRHLQILSSIASERRVRIIYPIPLE 299
Cdd:cd03403  163 KEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 111-288 1.15e-64

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: 205.83  E-value: 1.15e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 111 PCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSIIQVDDAKQATQLISQVTLRNIVGSKTLNVLLT 190
Cdd:cd08826    1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 191 SRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLASEAEAVREARAKIILAEGELKASKALKEASDVMSENK 270
Cdd:cd08826   81 EREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSP 160

                        170
                 ....*....|....*...
gi 281361631 271 ITLQLRHLQILSSIASER 288
Cdd:cd08826  161 GALQLRYLQTLSEIASEK 178
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 102-255 2.08e-55

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: 181.38  E-value: 2.08e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 102 RGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSIIQVDDAKQATQLISQVTLRNIVG 181
Cdd:cd08828    1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281361631 182 SKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLASEAEAVREARAKIILAEGELKA 255
Cdd:cd08828   81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 83-285 4.78e-54

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: 180.12  E-value: 4.78e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  83 VPEYSRMIILRLGRLRKGLRgPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSIIQVD 162
Cdd:cd13437    9 VKQGSVGLVERFGKFYKTVD-PGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 163 DAKQATQLISQVTLRNIVGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLASEAEAVREA 242
Cdd:cd13437   88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIG 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 281361631 243 RAKIILAEGELKASKALKEASDVMSeNKITLQLRHLQILSSIA 285
Cdd:cd13437  168 ESKIISAKADVESAKLMREAADILD-SKAAMQIRYLETLQAIA 209
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 79-297 1.46e-53

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: 178.93  E-value: 1.46e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  79 CLTIVPEYSRMIILRLGRLRKG-LRGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDS 157
Cdd:cd08827    3 CVKVVREYERAVIFRLGHLLQGrARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 158 IIQVDDAKQATQLISQVTLRNIVGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLASEAE 237
Cdd:cd08827   83 LSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 238 AVREARAKIILAEGELKASKALKEASDVMSENKITLQLRHLQILSSIASERRVRIIYPIP 297
Cdd:cd08827  163 AQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLP 222
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 119-225 1.87e-41

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: 143.10  E-value: 1.87e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 119 VDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSIIQVDDAKQATQLISQVTLRNIVGSKTLNVLLTSRQQLSRE 198
Cdd:cd13434    1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                         90       100
                 ....*....|....*....|....*..
gi 281361631 199 IQQAVAGITYRWGVRVERVDVMDITLP 225
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDIILP 107
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 119-295 3.72e-39

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: 139.30  E-value: 3.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 119 VDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSIIQVDDAKQATQLISQVTLRNIVGSKTLNVLLTSRQQLSRE 198
Cdd:cd13775    1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 199 IQQAVAGITYRWGVRVERVDVMDITLPTSLERSLASEAEAVREARAKIILAEGELKASKALKEASDVMSENKITLQLRHL 278
Cdd:cd13775   81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAM 160

                        170
                 ....*....|....*..
gi 281361631 279 QILSSIASERRVRIIYP 295
Cdd:cd13775  161 NMLYEGLKEKGSMVVVP 177
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 58-252 2.50e-38

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 140.36  E-value: 2.50e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  58 KVAIGICWFLVIITFPFSmccCLTIVPEYSRMIILRLGRLRKGLrGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKD 137
Cdd:COG0330    2 KLILLLILLVLVLVLLFS---SVYIVPQGERGVVLRFGKYVRTL-EPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 138 SVTITVNAVVYYCIYSPIDSIIQVDDAKQATQLISQVTLRNIVGSKTLN-VLLTSRQQLSREIQQAVAGITYRWGVRVER 216
Cdd:COG0330   78 NNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDeVLSTGRDEINAEIREELQEALDPYGIEVVD 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 281361631 217 VDVMDITLPTSLERSLASEAEAVREARAKIILAEGE 252
Cdd:COG0330  158 VEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGY 193
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 83-286 3.61e-34

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: 127.27  E-value: 3.61e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  83 VPEYSRMIILRLGRLRKGLrGPGL-VFILPCID-ETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSIIQ 160
Cdd:cd13438    1 VPPGERGLLYRDGKLVRTL-EPGRyAFWKFGRKvQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVET 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 161 VDDAKQATQLISQVTLRNIVGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLASEAEAVR 240
Cdd:cd13438   80 VDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 281361631 241 EARAKIILAEGELKASKALKEASDVMSENKITLQLRHLQILSSIAS 286
Cdd:cd13438  160 RAQANLIRAREETAATRSLLNAAKLMEENPALLRLRELEALEKIAE 205
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 95-221 4.26e-33

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: 121.74  E-value: 4.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  95 GRLRKgLRGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSIIQVDDAKQATQLISQV 174
Cdd:cd13436    1 GRLQK-PRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 281361631 175 TLRNIVGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMD 221
Cdd:cd13436   80 SLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSD 126
PHB smart00244
prohibitin homologues; prohibitin homologues
 78-225 1.68e-31

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 118.15  E-value: 1.68e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631    78 CCLTIVPEYSRMIILRLGRLRKgLRGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDS 157
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281361631   158 IIQVDDA--KQATQLIsQVTLRNIVGSKTLNVLLTS-RQQLSREIQQAVAGITYRWGVRVERVDVMDITLP 225
Cdd:smart00244  80 VYRVLDAdyAVIEQLA-QTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLP 149
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 116-225 2.58e-30

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: 113.34  E-value: 2.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 116 THRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSIIQVDDAKQATQLISQVTLRNIVGSKTLNVLLTSRQQL 195
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 281361631 196 SREIQQAVAGITYRWGVRVERVDVMDITLP 225
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPP 110
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 81-252 1.29e-28

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: 110.87  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631   81 TIVPEYSRMIILRLGRLRkGLRGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCI--YSPIDSI 158
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLS-RVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  159 IQVDDAKQATQLISQV---TLRNIVGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLASE 235
Cdd:pfam01145  80 QNVFGSDDLQELLRRVlesALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*..
gi 281361631  236 AEAVREARAKIILAEGE 252
Cdd:pfam01145 160 QTAEQEAEAEIARAEAE 176
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 79-257 7.25e-21

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: 91.40  E-value: 7.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  79 CLTIVPEYSRMIILRLGRLRKGLRGPGLVFILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSI 158
Cdd:cd03405    1 SVFIVDETEQAVVLQFGKPVRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRFY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 159 IQVDDAKQATQLISQV---TLRNIVGSKTLN-VLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLAS 234
Cdd:cd03405   81 QSVGGEEGAESRLDDIvdsALRNEIGKRTLAeVVSGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESVYE 160

                        170       180
                 ....*....|....*....|...
gi 281361631 235 EAEAVREARAKIILAEGELKASK 257
Cdd:cd03405  161 RMRAERERIAAEYRAEGEEEAEK 183
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 82-262 1.41e-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: 79.48  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  82 IVPEYSRMIILRLGRLrKGLRGPGLVFILPCIDETHRVdmrTDVTNVRPQDV----------LTKDSVTITVNAVVYYCI 151
Cdd:cd03404   17 TVDPGERGVVLRFGKY-VRTVGPGLHWKLPFPIEVVEK---VNVTQVRSVEIgfrvpeeslmLTGDENIVDVDFVVQYRI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 152 YSPIDSIIQVDDAKQATQLISQVTLRNIVGSKTLNVLLTS-RQQLSREIQQAVAGI--TYRWGVRVERVDVMDITLPTSL 228
Cdd:cd03404   93 SDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEIldRYDLGIEIVQVQLQDADPPEEV 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 281361631 229 -------ERSLASEAEAVREARA---KII-LAEGElkASKALKEA 262
Cdd:cd03404  173 qdafddvNAARQDKERLINEAQAyanEVIpRARGE--AARIIQEA 215
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 80-255 9.71e-16

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


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 75.24  E-value: 9.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  80 LTIVPEYSRMIILRLGR-LRKGLRGPGLVFILPCIDETHRVDMRTdVTNVRPQDVLTKD--SVTITVnAVVYYCIYSPID 156
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKgVKDEVLGEGLHFKIPWIQVVIIYDVRT-QPREITLTVLSKDgqTVNIDL-SVLYRPDPEKLP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 157 SIIQ-VDDAKQATQLISQV--TLRNIVGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLP----TSLE 229
Cdd:cd03401   79 ELYQnLGPDYEERVLPPIVreVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPdeyeKAIE 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 281361631 230 RSLASEAEAVR----------EARAKIILAEGELKA 255
Cdd:cd03401  159 AKQVAEQEAERakfelekaeqEAERKVIEAEGEAEA 194
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 122-225 1.61e-11

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: 60.84  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 122 RTDVTNVRPQDVLTKDSVTITVNAVVYYCI--YSPIDSIIQVDDAKQATQLISQV---TLRNIVGSKTLNVLLTSRQQLS 196
Cdd:cd02106    1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRItdYNALPAFYLVDFVKDIKADIRRKiadVLRAAIGRMTLDQIISGRDEIA 80

                         90       100
                 ....*....|....*....|....*....
gi 281361631 197 REIQQAVAGITYRWGVRVERVDVMDITLP 225
Cdd:cd02106   81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 82-262 2.70e-10

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: 60.68  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  82 IVPEYSRMIILRLGRLRkGLRGPGLVFILPCIDET-HRVDMRTDVTNVRpQDVLTKDSVTITVNAVVYY-----CIYspi 155
Cdd:cd03407    1 CVSQSTVAIVERFGKFS-RIAEPGLHFIIPPIESVaGRVSLRVQQLDVR-VETKTKDNVFVTLVVSVQYrvvpeKVY--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 156 DSIIQVDDAKQatQLISQV--TLRNIVGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDITLPTSLERSLA 233
Cdd:cd03407   76 DAFYKLTNPEQ--QIQSYVfdVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMN 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 281361631 234 SEAEAVREARAKIILAEGE----LKASKALKEA 262
Cdd:cd03407  154 EINAAQRLREAAEEKAEAEkilqVKAAEAEAEA 186
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 108-223 3.08e-07

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: 49.42  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 108 FILPCIDETHRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCIYSPIDSII---------QVDDAKQATQLISQVTLRN 178
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAaaaerflgkSTEEIRELVKETLEGHLRA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 281361631 179 IVGSKTLNVLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDIT 223
Cdd:cd03399   81 IVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDIS 125
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
59-264 6.75e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 48.33  E-value: 6.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  59 VAIGICwFLVIITFPFSMCCCLTIVPeySRMIILRLGRLR--KGLRGpGLVFILPCIDETHRVDMRT---DVTnvRPQDV 133
Cdd:COG2268    8 IIIGVI-VVVLLLLLIILARFYRKVP--PNEALVITGRGGgyKVVTG-GGAFVLPVLHRAERMSLSTmtiEVE--RTEGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 134 LTKDSVTITVNAVVYYCIYSPIDSIIQV------DDAKQATQLISQV---TLRNIVGSKTLNVLLTSRQQLSREIQQAVA 204
Cdd:COG2268   82 ITKDGIRVDVDAVFYVKVNSDPEDIANAaerflgRDPEEIEELAEEKlegALRAVAAQMTVEELNEDREKFAEKVQEVAG 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281361631 205 GITYRWGVRVERVDVMDITLPT----SLERSLASEAEAVREARAKIILAEGELKASKALKEASD 264
Cdd:COG2268  162 TDLAKNGLELESVAITDLEDENnyldALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEE 225
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 72-246 1.23e-04

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: 43.31  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631  72 FPFSMCCCLTIVPEYSRMIILRLGRLRKGLRGPGLVFILPCIDEThRVDMRTDVTNVRPQDVLTKDSVTITVNAVVYYCI 151
Cdd:cd03402    2 VGIILLGGFFVVQPNEAAVLTLFGRYRGTVRRPGLRWVNPFYRKK-RVSLRVRNFESEPLKVNDANGNPIEIAAVVVWRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361631 152 YSPIDSIIQVDDAKQATQLISQVTLRNIVGS--------KTLNvLLTSRQQLSREIQQAVAGITYRWGVRVERVDVMDIt 223
Cdd:cd03402   81 VDTAKAVFDVDDYEEFVSIQSEAALRRVASRypydsfedGEPS-LRGNSDEVSEELRRELQERLAVAGVEVIEARITHL- 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 281361631 224 lptslerSLASE----------AEAVREARAKI 246
Cdd:cd03402  159 -------AYAPEiaqamlqrqqASAIIAARQTI 184
 
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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