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Conserved domains on  [gi|1526745419|emb|VAY52618|]
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Band 7 domain-containing protein [Caenorhabditis elegans]

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 ...
 93-294 3.46e-131

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


:

Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 376.12  E-value: 3.46e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  93 PGGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLR 172
Cdd:cd03403     1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 173 NILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAAEAEAAREARAKVIVAEGEQKASR 252
Cdd:cd03403    81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1526745419 253 ALKEAAEVIAESPSALQLRYLQTLNSISAEKNSTIIFPFPID 294
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 ...
 93-294 3.46e-131

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


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 376.12  E-value: 3.46e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  93 PGGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLR 172
Cdd:cd03403     1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 173 NILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAAEAEAAREARAKVIVAEGEQKASR 252
Cdd:cd03403    81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1526745419 253 ALKEAAEVIAESPSALQLRYLQTLNSISAEKNSTIIFPFPID 294
Cdd:cd03403   161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
PHB smart00244
prohibitin homologues; prohibitin homologues
 72-224 3.02e-49

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 164.76  E-value: 3.02e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419   72 MCIKVVQEYERAVIFRLGRLMpgGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATI 151
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1526745419  152 SVTNVEDAA-RSTKLLAQTTLRNILGTKTLAEMLSD-REAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQ 224
Cdd:smart00244  79 AVYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK 153
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 51-290 1.53e-48

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 166.94  E-value: 1.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  51 GWILTILSYLLIFFTLPisacMCIKVVQEYERAVIFRLGRLMpgGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILS 130
Cdd:COG0330     2 KLILLLILLVLVLVLLF----SSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 131 KDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLRNILGTKTLAEMLS-DREAISHQMQTTLDEATEPWGVKV 209
Cdd:COG0330    76 KDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 210 ERVEVKDVRLPVQLQ----------------------RAMAAEAEAAREARAKVIVAEGEQKA----SRALKEAAEVIAE 263
Cdd:COG0330   156 VDVEIKDIDPPEEVQdamedrmkaerereaaileaegYREAAIIRAEGEAQRAIIEAEAYREAqilrAEGEAEAFRIVAE 235

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1526745419 264 S----PSALQLRYLQTLNSISAEKNSTIIFP 290
Cdd:COG0330   236 AysaaPFVLFYRSLEALEEVLSPNSKVIVLP 266
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 75-247 3.72e-31

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 117.42  E-value: 3.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  75 KVVQEYERAVIFRLGRLmpGGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRI--SNATIS 152
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKL--SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 153 VTNVEDAARSTKLL---AQTTLRNILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAA 229
Cdd:pfam01145  79 VQNVFGSDDLQELLrrvLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 1526745419 230 EAEAAREARAKVIVAEGE 247
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
PRK11029 PRK11029
protease modulator HflC;
53-148 8.88e-05

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 44.35  E-value: 8.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  53 ILTILSYLLIFFtlpisaCMCIKVVQEYERAVIFRLGRLMPGGAK-----GPGIFFIVPCIDTYRKVDLRVLSFEVPPQE 127
Cdd:PRK11029    5 VIAIIIIVLVVL------YMSVFVVKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADR 78

                          90       100
                  ....*....|....*....|.
gi 1526745419 128 ILSKDSVTVAVDAVVYFRISN 148
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 ...
 93-294 3.46e-131

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


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 376.12  E-value: 3.46e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  93 PGGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLR 172
Cdd:cd03403     1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 173 NILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAAEAEAAREARAKVIVAEGEQKASR 252
Cdd:cd03403    81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1526745419 253 ALKEAAEVIAESPSALQLRYLQTLNSISAEKNSTIIFPFPID 294
Cdd:cd03403   161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 94-300 1.21e-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: 324.34  E-value: 1.21e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  94 GGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLRN 173
Cdd:cd13435     2 GGARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 174 ILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAAEAEAAREARAKVIVAEGEQKASRA 253
Cdd:cd13435    82 VLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1526745419 254 LKEAAEVIAESPSALQLRYLQTLNSISAEKNSTIIFPFPIDLLSAFL 300
Cdd:cd13435   162 LKEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLTPLL 208
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 73-292 2.72e-76

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: 237.09  E-value: 2.72e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  73 CIKVVQEYERAVIFRLGRLMPGGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATIS 152
Cdd:cd08827     3 CVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 153 VTNVEDAARSTKLLAQTTLRNILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAAEAE 232
Cdd:cd08827    83 LSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 233 AAREARAKVIVAEGEQKASRALKEAAEVIAESPSALQLRYLQTLNSISAEKNSTIIFPFP 292
Cdd:cd08827   163 AQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLP 222
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 106-283 5.74e-72

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: 223.93  E-value: 5.74e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 106 PCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLRNILGTKTLAEMLS 185
Cdd:cd08826     1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 186 DREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAAEAEAAREARAKVIVAEGEQKASRALKEAAEVIAESP 265
Cdd:cd08826    81 EREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSP 160

                         170
                  ....*....|....*...
gi 1526745419 266 SALQLRYLQTLNSISAEK 283
Cdd:cd08826   161 GALQLRYLQTLSEIASEK 178
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 97-250 5.19e-65

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: 205.65  E-value: 5.19e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  97 KGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLRNILG 176
Cdd:cd08828     1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1526745419 177 TKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAAEAEAAREARAKVIVAEGEQKA 250
Cdd:cd08828    81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 114-220 1.58e-55

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: 179.31  E-value: 1.58e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 114 VDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLRNILGTKTLAEMLSDREAISHQ 193
Cdd:cd13434     1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                          90       100
                  ....*....|....*....|....*..
gi 1526745419 194 MQTTLDEATEPWGVKVERVEVKDVRLP 220
Cdd:cd13434    81 LQEILDEATDPWGIKVERVEIKDIILP 107
PHB smart00244
prohibitin homologues; prohibitin homologues
 72-224 3.02e-49

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 164.76  E-value: 3.02e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419   72 MCIKVVQEYERAVIFRLGRLMpgGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATI 151
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1526745419  152 SVTNVEDAA-RSTKLLAQTTLRNILGTKTLAEMLSD-REAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQ 224
Cdd:smart00244  79 AVYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK 153
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 75-289 1.21e-48

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: 165.48  E-value: 1.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  75 KVVQEYERAVIFRLGRLMPggAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISN---ATI 151
Cdd:cd13437     7 KQVKQGSVGLVERFGKFYK--TVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDpykAIY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 152 SVTNVEDAARStklLAQTTLRNILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAAEA 231
Cdd:cd13437    85 RIDNVKQALIE---RTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1526745419 232 EAAREARAKVIVAEGEQKASRALKEAAEVIAeSPSALQLRYLQTLNSISAEKNSTIIF 289
Cdd:cd13437   162 KAKRIGESKIISAKADVESAKLMREAADILD-SKAAMQIRYLETLQAIAKSANSKVIF 218
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 51-290 1.53e-48

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 166.94  E-value: 1.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  51 GWILTILSYLLIFFTLPisacMCIKVVQEYERAVIFRLGRLMpgGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILS 130
Cdd:COG0330     2 KLILLLILLVLVLVLLF----SSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 131 KDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLRNILGTKTLAEMLS-DREAISHQMQTTLDEATEPWGVKV 209
Cdd:COG0330    76 KDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 210 ERVEVKDVRLPVQLQ----------------------RAMAAEAEAAREARAKVIVAEGEQKA----SRALKEAAEVIAE 263
Cdd:COG0330   156 VDVEIKDIDPPEEVQdamedrmkaerereaaileaegYREAAIIRAEGEAQRAIIEAEAYREAqilrAEGEAEAFRIVAE 235

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1526745419 264 S----PSALQLRYLQTLNSISAEKNSTIIFP 290
Cdd:COG0330   236 AysaaPFVLFYRSLEALEEVLSPNSKVIVLP 266
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 114-290 8.79e-44

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: 150.85  E-value: 8.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 114 VDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLRNILGTKTLAEMLSDREAISHQ 193
Cdd:cd13775     1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 194 MQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAAEAEAAREARAKVIVAEGEQKASRALKEAAEVIAESPSALQLRYL 273
Cdd:cd13775    81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAM 160

                         170
                  ....*....|....*..
gi 1526745419 274 QTLNSISAEKNSTIIFP 290
Cdd:cd13775   161 NMLYEGLKEKGSMVVVP 177
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 89-219 2.27e-40

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: 140.61  E-value: 2.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  89 GRLMPggAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQ 168
Cdd:cd13436     1 GRLQK--PRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1526745419 169 TTLRNILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRL 219
Cdd:cd13436    79 TSLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 113-220 3.93e-40

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: 139.15  E-value: 3.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 113 KVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLRNILGTKTLAEMLSDREAISH 192
Cdd:cd08829     3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                          90       100
                  ....*....|....*....|....*...
gi 1526745419 193 QMQTTLDEATEPWGVKVERVEVKDVRLP 220
Cdd:cd08829    83 KLLEALDEATDPWGVKVTRVEIKDITPP 110
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 77-289 1.57e-35

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: 130.35  E-value: 1.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  77 VQEYERAVIFRLGRLMpgGAKGPGI-FFIVPCIDTYR-KVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNATISVT 154
Cdd:cd13438     1 VPPGERGLLYRDGKLV--RTLEPGRyAFWKFGRKVQVeLVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 155 NVEDAARSTKLLAQTTLRNILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAAEAEAA 234
Cdd:cd13438    79 TVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1526745419 235 REARAKVIVAEGEQKASRALKEAAEVIAESPSALQLRYLQTLNSISAEKNSTIIF 289
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 ...
 75-247 3.72e-31

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 117.42  E-value: 3.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  75 KVVQEYERAVIFRLGRLmpGGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRI--SNATIS 152
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKL--SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 153 VTNVEDAARSTKLL---AQTTLRNILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQRAMAA 229
Cdd:pfam01145  79 VQNVFGSDDLQELLrrvLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 1526745419 230 EAEAAREARAKVIVAEGE 247
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 73-263 4.43e-26

High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259803 [Multi-domain]  Cd Length: 249  Bit Score: 105.65  E-value: 4.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  73 CIKVVQEYERAVIFRLGRLMpGGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNAT-- 150
Cdd:cd03405     1 SVFIVDETEQAVVLQFGKPV-RVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLrf 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 151 -ISVTNVEDAARstkLLAQ---TTLRNILGTKTLAEMLSD-REAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQR 225
Cdd:cd03405    80 yQSVGGEEGAES---RLDDivdSALRNEIGKRTLAEVVSGgRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSE 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1526745419 226 AMAAEAEAAREARAKVIVAEGEQKA----SRALKEAAEVIAE 263
Cdd:cd03405   157 SVYERMRAERERIAAEYRAEGEEEAekirAEADRERTVILAE 198
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 74-224 4.58e-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: 79.09  E-value: 4.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  74 IKVVQEYERAVIFRLGRLMPGGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPqEILSKDSVTVAVDAVVYFRISNATIS- 152
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRPDPEKLPe 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1526745419 153 -VTNVEDAARSTKL--LAQTTLRNILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPVQLQ 224
Cdd:cd03401    80 lYQNLGPDYEERVLppIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYE 154
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 60-224 3.21e-14

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: 72.16  E-value: 3.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  60 LLIFFTLPISACMCIKVVQEYERAVIFRLGRlmPGGAKGPGIFFIVPC-IDTYRKVDL-RVLSFEVP---PQE--ILSKD 132
Cdd:cd03404     1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGK--YVRTVGPGLHWKLPFpIEVVEKVNVtQVRSVEIGfrvPEEslMLTGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 133 SVTVAVDAVVYFRISNATISVTNVEDAARSTKLLAQTTLRNILGTKTLAEMLS-DREAIS----HQMQTTLDE-ATepwG 206
Cdd:cd03404    79 ENIVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAadvrELLQEILDRyDL---G 155

                         170
                  ....*....|....*...
gi 1526745419 207 VKVERVEVKDVRLPVQLQ 224
Cdd:cd03404   156 IEIVQVQLQDADPPEEVQ 173
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 103-218 6.47e-13

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: 65.99  E-value: 6.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 103 FIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNatisvTNVEDAARSTKLLAQTT------------ 170
Cdd:cd03399     1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGS-----DPEEIAAAAERFLGKSTeeirelvketle 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1526745419 171 --LRNILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVR 218
Cdd:cd03399    76 ghLRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDIS 125
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 117-220 3.48e-12

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


Pssm-ID: 259797 [Multi-domain]  Cd Length: 110  Bit Score: 62.77  E-value: 3.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 117 RVLSFEVPPQEILSKDSVTVAVDAVVYFRISNA----TISVTN-VEDAARSTKLLAQTTLRNILGTKTLAEMLSDREAIS 191
Cdd:cd02106     1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYnalpAFYLVDfVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                          90       100
                  ....*....|....*....|....*....
gi 1526745419 192 HQMQTTLDEATEPWGVKVERVEVKDVRLP 220
Cdd:cd02106    81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 76-263 1.96e-11

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: 64.14  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  76 VVQEYERAVIFRLGRLMpgGAKGPGIFFIVPCIDTYR-KVDLRV--LSFEVppqEILSKDSVTVAVDAVVYFR-----IS 147
Cdd:cd03407     1 CVSQSTVAIVERFGKFS--RIAEPGLHFIIPPIESVAgRVSLRVqqLDVRV---ETKTKDNVFVTLVVSVQYRvvpekVY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 148 NATISVTNVEDAARStklLAQTTLRNILGTKTLAEMLSDREAISHQMQTTLDEATEPWGVKVERVEVKDVRLPvqlqram 227
Cdd:cd03407    76 DAFYKLTNPEQQIQS---YVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPD------- 145

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1526745419 228 aaeaeaarearAKVIVAEGEQKASRALKEAAEVIAE 263
Cdd:cd03407   146 -----------ASVKAAMNEINAAQRLREAAEEKAE 170
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 66-216 3.01e-11

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: 62.96  E-value: 3.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  66 LPISACMCIKVVQEYERAVIFRLGRLMpGGAKGPGIFFIVPCIDTyRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFR 145
Cdd:cd03402     2 VGIILLGGFFVVQPNEAAVLTLFGRYR-GTVRRPGLRWVNPFYRK-KRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 146 ISNATISVTNVEDAARSTKLLAQTTLRNIL----------GTKTLAemlSDREAISHQMQTTLDEATEPWGVKVERVEVK 215
Cdd:cd03402    80 VVDTAKAVFDVDDYEEFVSIQSEAALRRVAsrypydsfedGEPSLR---GNSDEVSEELRRELQERLAVAGVEVIEARIT 156


                  .
gi 1526745419 216 D 216
Cdd:cd03402   157 H 157
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
52-218 9.48e-08

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 54.11  E-value: 9.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  52 WILTILSYLLIFFTLPISACMCIKVVQEyeRAVIF--RLG--RLMPGGAKgpgifFIVPCIDTYRKVDLRVLSFEVPPQE 127
Cdd:COG2268     7 LIIIGVIVVVLLLLLIILARFYRKVPPN--EALVItgRGGgyKVVTGGGA-----FVLPVLHRAERMSLSTMTIEVERTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 128 -ILSKDSVTVAVDAVVYFRISNATISVTNvedAARStkLLAQTT--------------LRNILGTKTLAEMLSDREAISH 192
Cdd:COG2268    80 gLITKDGIRVDVDAVFYVKVNSDPEDIAN---AAER--FLGRDPeeieelaeeklegaLRAVAAQMTVEELNEDREKFAE 154

                         170       180
                  ....*....|....*....|....*.
gi 1526745419 193 QMQTTLDEATEPWGVKVERVEVKDVR 218
Cdd:COG2268   155 KVQEVAGTDLAKNGLELESVAITDLE 180
PRK11029 PRK11029
protease modulator HflC;
53-148 8.88e-05

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 44.35  E-value: 8.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  53 ILTILSYLLIFFtlpisaCMCIKVVQEYERAVIFRLGRLMPGGAK-----GPGIFFIVPCIDTYRKVDLRVLSFEVPPQE 127
Cdd:PRK11029    5 VIAIIIIVLVVL------YMSVFVVKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADR 78

                          90       100
                  ....*....|....*....|.
gi 1526745419 128 ILSKDSVTVAVDAVVYFRISN 148
Cdd:PRK11029   79 FVTKEKKDLIVDSYIKWRISD 99
PRK10930 PRK10930
FtsH protease activity modulator HflK;
77-220 1.91e-03

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 40.20  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419  77 VQEYERAVIFRLGRLmpGGAKGPGIFFIVPCIDTYRKVDLRVLSFEVPPQEILSKDSVTVAVDAVVYFRISNAT---ISV 153
Cdd:PRK10930  100 IKEAERGVVTRFGKF--SHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTDPEkylFSV 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526745419 154 TNVEDAARSTkllAQTTLRNILGTKTLAEMLSD-REAISHQMQTTLDEATEPW--GVKVERVEVKDVRLP 220
Cdd:PRK10930  178 TSPDDSLRQA---TDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYdmGITLLDVNFQAARPP 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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