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Conserved domains on  [gi|665409888|ref|NP_001286936|]
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uncharacterized protein Dmel_CG42540, isoform K [Drosophila melanogaster]

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 ...
 117-318 2.15e-129

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: 2.15e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 117 QGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLR 196
Cdd:cd03403    1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 197 NTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASR 276
Cdd:cd03403   81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 665409888 277 ALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLPID 318
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 ...
 117-318 2.15e-129

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: 2.15e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 117 QGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLR 196
Cdd:cd03403    1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 197 NTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASR 276
Cdd:cd03403   81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 665409888 277 ALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLPID 318
Cdd:cd03403  161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 76-314 2.13e-49

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 168.48  E-value: 2.13e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  76 KLLIFLSVALVIMtlpFSLFVCFKVVQEYERAVIFRLGRLMqgGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTK 155
Cdd:COG0330    2 KLILLLILLVLVL---VLLFSSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 156 DSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILSE-RMTISGTMQVQLDEATDAWGIKVE 234
Cdd:COG0330   77 DNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 235 RVEIKDVRLPVQLQ----------------------RAMAAEAEAAREARAKVIAAEGEQKA--------SRALREASEV 284
Cdd:COG0330  157 DVEIKDIDPPEEVQdamedrmkaerereaaileaegYREAAIIRAEGEAQRAIIEAEAYREAqilraegeAEAFRIVAEA 236

                        250       260       270
                 ....*....|....*....|....*....|
gi 665409888 285 IGDSPAALQLRYLQTLNTISAEKNSTIVFP 314
Cdd:COG0330  237 YSAAPFVLFYRSLEALEEVLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 97-248 4.25e-42

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 145.50  E-value: 4.25e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888    97 CFKVVQEYERAVIFRLGRLMQggAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVS 176
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVLR--VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665409888   177 IANVENAH-HSTRLLAQTTLRNTMGTRHLHEILS-ERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQ 248
Cdd:smart00244  80 VYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK 153
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 99-271 2.49e-26

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 103.94  E-value: 2.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888   99 KVVQEYERAVIFRLGRLmqGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRV--SNATVS 176
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKL--SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  177 IANV---ENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAA 253
Cdd:pfam01145  79 VQNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 665409888  254 EAEAAREARAKVIAAEGE 271
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 98-248 3.71e-11

HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 63.19  E-value: 3.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888   98 FKVVQEYERAVIFRLGRLMQggAKGPGIFFILPCIDSYARVDL-RTRTYDVPPQeVLTKDSVTVSVDAVVYYRVSNATVS 176
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHR--TVDPGLNWKPPFIEEVYPVNVtAVRNLRKQGL-MLTGDENIVNVEMNVQYRITDPYKY 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665409888  177 IANVENAHHSTRLLAQTTLRNTMGTRHLHEILSE-RMTISGTMQVQLDEATDAW--GIKVERVEIKDVRLPVQLQ 248
Cdd:TIGR01933  78 LFSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVK 152
PRK11029 PRK11029
protease modulator HflC;
77-172 2.79e-07

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 52.05  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  77 LLIFLSVALVImtLPFSLFVcfkvVQEYERAVIFRLGRLMQGGAK-----GPGIFFILPCIDSYARVDLRTRTYDVPPQE 151
Cdd:PRK11029   5 VIAIIIIVLVV--LYMSVFV----VKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADR 78

                         90       100
                 ....*....|....*....|.
gi 665409888 152 VLTKDSVTVSVDAVVYYRVSN 172
Cdd:PRK11029  79 FVTKEKKDLIVDSYIKWRISD 99
 
Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 117-318 2.15e-129

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: 2.15e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 117 QGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLR 196
Cdd:cd03403    1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 197 NTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASR 276
Cdd:cd03403   81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 665409888 277 ALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLPID 318
Cdd:cd03403  161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 118-324 1.74e-110

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: 322.80  E-value: 1.74e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 118 GGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRN 197
Cdd:cd13435    2 GGARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 198 TMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASRA 277
Cdd:cd13435   82 VLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 665409888 278 LREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLPIDLITYFL 324
Cdd:cd13435  162 LKEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLTPLL 208
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 97-316 3.40e-78

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: 240.95  E-value: 3.40e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  97 CFKVVQEYERAVIFRLGRLMQGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVS 176
Cdd:cd08827    3 CVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 177 IANVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAE 256
Cdd:cd08827   83 LSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 257 AAREARAKVIAAEGEQKASRALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLP 316
Cdd:cd08827  163 AQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLP 222
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 130-307 3.48e-68

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: 213.53  E-value: 3.48e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 130 PCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILS 209
Cdd:cd08826    1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 210 ERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASRALREASEVIGDSP 289
Cdd:cd08826   81 EREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSP 160

                        170
                 ....*....|....*...
gi 665409888 290 AALQLRYLQTLNTISAEK 307
Cdd:cd08826  161 GALQLRYLQTLSEIASEK 178
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 121-274 4.96e-60

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: 191.78  E-value: 4.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 121 KGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMG 200
Cdd:cd08828    1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665409888 201 TRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKA 274
Cdd:cd08828   81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 138-244 1.38e-53

Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, podocin, and other members of the stomatin-like protein family (SLPs or slipins). The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome. Bacterial and archaebacterial SLPs and many of the eukaryotic family members remain uncharacterized.


Pssm-ID: 259812 [Multi-domain]  Cd Length: 108  Bit Score: 173.53  E-value: 1.38e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 138 VDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGT 217
Cdd:cd13434    1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                         90       100
                 ....*....|....*....|....*..
gi 665409888 218 MQVQLDEATDAWGIKVERVEIKDVRLP 244
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDIILP 107
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 98-318 1.04e-52

Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in some eukaryotes and viruses. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This diverse subgroup of the SLPs remains largely uncharacterized.


Pssm-ID: 259815 [Multi-domain]  Cd Length: 222  Bit Score: 175.11  E-value: 1.04e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  98 FKVVQEYERAVIFRLGRLMQggAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSI 177
Cdd:cd13437    6 YKQVKQGSVGLVERFGKFYK--TVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 178 ANVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEA 257
Cdd:cd13437   84 YRIDNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKA 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665409888 258 AREARAKVIAAEGEQKASRALREASEVIgDSPAALQLRYLQTLNTISAEKNSTIVFpLPID 318
Cdd:cd13437  164 KRIGESKIISAKADVESAKLMREAADIL-DSKAAMQIRYLETLQAIAKSANSKVIF-LPLD 222
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 76-314 2.13e-49

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 168.48  E-value: 2.13e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  76 KLLIFLSVALVIMtlpFSLFVCFKVVQEYERAVIFRLGRLMqgGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTK 155
Cdd:COG0330    2 KLILLLILLVLVL---VLLFSSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 156 DSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILSE-RMTISGTMQVQLDEATDAWGIKVE 234
Cdd:COG0330   77 DNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 235 RVEIKDVRLPVQLQ----------------------RAMAAEAEAAREARAKVIAAEGEQKA--------SRALREASEV 284
Cdd:COG0330  157 DVEIKDIDPPEEVQdamedrmkaerereaaileaegYREAAIIRAEGEAQRAIIEAEAYREAqilraegeAEAFRIVAEA 236

                        250       260       270
                 ....*....|....*....|....*....|
gi 665409888 285 IGDSPAALQLRYLQTLNTISAEKNSTIVFP 314
Cdd:COG0330  237 YSAAPFVLFYRSLEALEEVLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 97-248 4.25e-42

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 145.50  E-value: 4.25e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888    97 CFKVVQEYERAVIFRLGRLMQggAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVS 176
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVLR--VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665409888   177 IANVENAH-HSTRLLAQTTLRNTMGTRHLHEILS-ERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQ 248
Cdd:smart00244  80 VYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK 153
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 137-244 2.68e-39

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: 136.45  E-value: 2.68e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 137 RVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISG 216
Cdd:cd08829    3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                         90       100
                 ....*....|....*....|....*...
gi 665409888 217 TMQVQLDEATDAWGIKVERVEIKDVRLP 244
Cdd:cd08829   83 KLLEALDEATDPWGVKVTRVEIKDITPP 110
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 113-243 4.85e-39

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: 136.38  E-value: 4.85e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 113 GRLMQggAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQ 192
Cdd:cd13436    1 GRLQK--PRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQ 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 665409888 193 TTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRL 243
Cdd:cd13436   79 TSLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 138-314 1.18e-38

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: 136.99  E-value: 1.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 138 VDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGT 217
Cdd:cd13775    1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 218 MQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASRALREASEVIGDSPAALQLRYL 297
Cdd:cd13775   81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAM 160

                        170
                 ....*....|....*..
gi 665409888 298 QTLNTISAEKNSTIVFP 314
Cdd:cd13775  161 NMLYEGLKEKGSMVVVP 177
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 101-313 2.65e-31

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


Pssm-ID: 259816 [Multi-domain]  Cd Length: 215  Bit Score: 118.41  E-value: 2.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 101 VQEYERAVIFRLGRLMQggAKGPGI-FFILPCID-SYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIA 178
Cdd:cd13438    1 VPPGERGLLYRDGKLVR--TLEPGRyAFWKFGRKvQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 179 NVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAA 258
Cdd:cd13438   79 TVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665409888 259 REARAKVIAAEGEQKASRALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVF 313
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 ...
 99-271 2.49e-26

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 103.94  E-value: 2.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888   99 KVVQEYERAVIFRLGRLmqGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRV--SNATVS 176
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKL--SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  177 IANV---ENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAA 253
Cdd:pfam01145  79 VQNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 665409888  254 EAEAAREARAKVIAAEGE 271
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 97-244 3.24e-24

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: 100.26  E-value: 3.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  97 CFKVVQEYERAVIFRLGRLmQGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATV- 175
Cdd:cd03405    1 SVFIVDETEQAVVLQFGKP-VRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRf 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665409888 176 --SIANVENAHhstRLLAQ---TTLRNTMGTRHLHEILS-ERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLP 244
Cdd:cd03405   80 yqSVGGEEGAE---SRLDDivdSALRNEIGKRTLAEVVSgGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLP 151
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 98-248 8.55e-17

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


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 77.94  E-value: 8.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  98 FKVVQEYERAVIFRLGRLMQGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPqEVLTKDSVTVSVDAVVYYRVSNATVSI 177
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRPDPEKLPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 178 ------ANVENahhstRLL---AQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQ 248
Cdd:cd03401   80 lyqnlgPDYEE-----RVLppiVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYE 154
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 94-248 7.64e-15

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: 74.09  E-value: 7.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  94 LFVCFKVVQEYERAVIFRLGRLMqgGAKGPGIFFILPC-IDSYARVDL-RTRTYDVP---PQE--VLTKDSVTVSVDAVV 166
Cdd:cd03404   11 LLSGFYTVDPGERGVVLRFGKYV--RTVGPGLHWKLPFpIEVVEKVNVtQVRSVEIGfrvPEEslMLTGDENIVDVDFVV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 167 YYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILSE-RMTISGTMQVQLDEATDAW--GIKVERVEIKDVRL 243
Cdd:cd03404   89 QYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEILDRYdlGIEIVQVQLQDADP 168


                 ....*
gi 665409888 244 PVQLQ 248
Cdd:cd03404  169 PEEVQ 173
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 98-248 3.71e-11

HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 63.19  E-value: 3.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888   98 FKVVQEYERAVIFRLGRLMQggAKGPGIFFILPCIDSYARVDL-RTRTYDVPPQeVLTKDSVTVSVDAVVYYRVSNATVS 176
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHR--TVDPGLNWKPPFIEEVYPVNVtAVRNLRKQGL-MLTGDENIVNVEMNVQYRITDPYKY 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665409888  177 IANVENAHHSTRLLAQTTLRNTMGTRHLHEILSE-RMTISGTMQVQLDEATDAW--GIKVERVEIKDVRLPVQLQ 248
Cdd:TIGR01933  78 LFSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVK 152
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 90-240 1.06e-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: 259800  Cd Length: 231  Bit Score: 61.41  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  90 LPFSLFVCFKVVQEYERAVIFRLGRLMqGGAKGPGIFFILPCIdSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYR 169
Cdd:cd03402    2 VGIILLGGFFVVQPNEAAVLTLFGRYR-GTVRRPGLRWVNPFY-RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWR 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665409888 170 VSNATVSIANVENAHHSTRLLAQTTLRNTMGTR----HLHEILSERM---TISGTMQVQLDEATDAWGIKVERVEIKD 240
Cdd:cd03402   80 VVDTAKAVFDVDDYEEFVSIQSEAALRRVASRYpydsFEDGEPSLRGnsdEVSEELRRELQERLAVAGVEVIEARITH 157
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 127-242 6.31e-10

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: 57.13  E-value: 6.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 127 FILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIAN-VENA-----HHSTRLLAQT---TLRN 197
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAaAERFlgkstEEIRELVKETlegHLRA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 665409888 198 TMGTRHLHEILSERMTISgtMQVQLDEATD--AWGIKVERVEIKDVR 242
Cdd:cd03399   81 IVGTMTVEEIYQDREKFA--EQVQEVAEPDlaKMGLEIDSFNIKDIS 125
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 100-313 1.70e-09

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: 58.37  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 100 VVQEYERAVIFRLGRLMqgGAKGPGIFFILPCIDSYA-RVDLRTRTYDVPpQEVLTKDSVTVSVDAVVYYRVSNATVSIA 178
Cdd:cd03407    1 CVSQSTVAIVERFGKFS--RIAEPGLHFIIPPIESVAgRVSLRVQQLDVR-VETKTKDNVFVTLVVSVQYRVVPEKVYDA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 179 --NVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQ-------- 248
Cdd:cd03407   78 fyKLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKaamneina 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 249 ---RAMAAEAEAAREARAKVIAAEGEQKASRA---------------LRE-----ASEVIGDSPA-ALQL----RYLQTL 300
Cdd:cd03407  158 aqrLREAAEEKAEAEKILQVKAAEAEAEAKRLqgvgiaeqrkaivdgLREsiedfQEAVPGVSSKeVMDLllitQYFDTL 237

                        250
                 ....*....|...
gi 665409888 301 NTISAEKNSTIVF 313
Cdd:cd03407  238 KEVGKSSKSSTVF 250
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 141-244 6.37e-08

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: 50.44  E-value: 6.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 141 RTRTYDVPPQEVLTKDSVTVSVDAVVYYRVS--NATVSIANV---ENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTIS 215
Cdd:cd02106    1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITdyNALPAFYLVdfvKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                         90       100
                 ....*....|....*....|....*....
gi 665409888 216 GTMQVQLDEATDAWGIKVERVEIKDVRLP 244
Cdd:cd02106   81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
PRK11029 PRK11029
protease modulator HflC;
77-172 2.79e-07

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 52.05  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  77 LLIFLSVALVImtLPFSLFVcfkvVQEYERAVIFRLGRLMQGGAK-----GPGIFFILPCIDSYARVDLRTRTYDVPPQE 151
Cdd:PRK11029   5 VIAIIIIVLVV--LYMSVFV----VKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADR 78

                         90       100
                 ....*....|....*....|.
gi 665409888 152 VLTKDSVTVSVDAVVYYRVSN 172
Cdd:PRK11029  79 FVTKEKKDLIVDSYIKWRISD 99
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
77-224 1.43e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 50.26  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  77 LLIFLSVALVIMTLPFSLFVCFKVVQEYERAVI---FRLGRLMQGGAKgpgifFILPCIDSYARVDLRTRTYDVPPQE-V 152
Cdd:COG2268    7 LIIIGVIVVVLLLLLIILARFYRKVPPNEALVItgrGGGYKVVTGGGA-----FVLPVLHRAERMSLSTMTIEVERTEgL 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665409888 153 LTKDSVTVSVDAVVYYRVSNATVSIANVenahhSTRLLAQT--TLRNTmgtrhLHEILSERM-TISGTMQV-QLDE 224
Cdd:COG2268   82 ITKDGIRVDVDAVFYVKVNSDPEDIANA-----AERFLGRDpeEIEEL-----AEEKLEGALrAVAAQMTVeELNE 147
PRK10930 PRK10930
FtsH protease activity modulator HflK;
98-244 2.39e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 46.36  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888  98 FKVVQEYERAVIFRLGRLMQggAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSI 177
Cdd:PRK10930  97 FYTIKEAERGVVTRFGKFSH--LVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTDPEKYL 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665409888 178 ANVENAHHSTRLLAQTTLRNTMGTRHLHEILSE-RMTISGTMQVQLDEATDAW--GIKVERVEIKDVRLP 244
Cdd:PRK10930 175 FSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYdmGITLLDVNFQAARPP 244
 
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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