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Conserved domains on  [gi|2196662558|ref|XP_046659153|]
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band 7 protein AGAP004871 [Homalodisca vitripennis]

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 ...
 199-400 2.07e-130

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: 373.42  E-value: 2.07e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 199 SGGAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISVANVANAHHSTRLLAQTTLR 278
Cdd:cd03403     1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 279 NVLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASR 358
Cdd:cd03403    81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2196662558 359 ALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLPID 400
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 ...
 199-400 2.07e-130

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: 373.42  E-value: 2.07e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 199 SGGAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISVANVANAHHSTRLLAQTTLR 278
Cdd:cd03403     1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 279 NVLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASR 358
Cdd:cd03403    81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2196662558 359 ALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLPID 400
Cdd:cd03403   161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 162-396 4.46e-55

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 183.50  E-value: 4.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 162 ALSWVVVVCTLPFSLFVCFKVVQEYERAVIFRLGRLVsgGAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVT 241
Cdd:COG0330     3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 242 VSVDAVVYYRVSNATISVANVANAHHSTRLLAQTTLRNVLGTRPLHEILS-DREAISNTMQTSLDDATEAWGIKVERVEI 320
Cdd:COG0330    81 VDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 321 KDVRLPVQLQ----------------------RAMAAEAEAAREARAKVIAAEGEQKA--------SRALREASEVIGDS 370
Cdd:COG0330   161 KDIDPPEEVQdamedrmkaerereaaileaegYREAAIIRAEGEAQRAIIEAEAYREAqilraegeAEAFRIVAEAYSAA 240

                         250       260
                  ....*....|....*....|....*.
gi 2196662558 371 PAALQLRYLQTLNTISAEKNSTIVFP 396
Cdd:COG0330   241 PFVLFYRSLEALEEVLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 179-330 1.13e-49

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 165.53  E-value: 1.13e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558  179 CFKVVQEYERAVIFRLGRLVsgGAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATIS 258
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2196662558  259 VANVANAH-HSTRLLAQTTLRNVLGTRPLHEILSD-REAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQ 330
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 ...
 181-330 3.18e-32

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 120.12  E-value: 3.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 181 KVVQEYERAVIFRLGRLVsgGAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRV--SNATIS 258
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLS--RVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2196662558 259 VANVANAHHSTRLL---AQTTLRNVLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQ 330
Cdd:pfam01145  79 VQNVFGSDDLQELLrrvLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIA 153
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 180-330 1.63e-13

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: 70.12  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 180 FKVVQEYERAVIFRLGRLVSggAKGPGIFFILPCIDnyarvdlrtRTYDVPPQEV---------LTKDSVTVSVDAVVYY 250
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHR--TVDPGLNWKPPFIE---------EVYPVNVTAVrnlrkqglmLTGDENIVNVEMNVQY 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 251 RVSNATISVANVANAHHSTRLLAQTTLRNVLGTRPLHEILSD-REAISNTMQTSLDDATEAW--GIKVERVEIKDVRLPV 327
Cdd:TIGR01933  70 RITDPYKYLFSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPE 149


                  ...
gi 2196662558 328 QLQ 330
Cdd:TIGR01933 150 EVK 152
PRK11029 PRK11029
protease modulator HflC;
166-328 8.18e-07

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 50.51  E-value: 8.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 166 VVVVCTLPFSLFVcfkvVQEYERAVIFRLGRLVSGGAK-----GPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSV 240
Cdd:PRK11029   10 IIVLVVLYMSVFV----VKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADRFVTKEKK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 241 TVSVDAVVYYRVSN------AT----ISVANVanahhstrLLAQT---TLRNVLGTRPLHEILSD---------REAIsN 298
Cdd:PRK11029   86 DLIVDSYIKWRISDfsryylATgggdISQAEV--------LLKRKfsdRLRSEIGRLDVKDIVTDsrgrltldvRDAL-N 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2196662558 299 TMQTSLDDATE--------------------------------AWGIKVERVEIKDVRLPVQ 328
Cdd:PRK11029  157 SGSAGTEDEVAtpaaddaiasaaerveaetkgkvpvinpnsmaALGIEVVDVRIKQINLPTE 218
 
Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 199-400 2.07e-130

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: 373.42  E-value: 2.07e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 199 SGGAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISVANVANAHHSTRLLAQTTLR 278
Cdd:cd03403     1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 279 NVLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASR 358
Cdd:cd03403    81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2196662558 359 ALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLPID 400
Cdd:cd03403   161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 199-406 1.82e-112

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: 328.19  E-value: 1.82e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 199 SGGAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISVANVANAHHSTRLLAQTTLR 278
Cdd:cd13435     1 SGGARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 279 NVLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASR 358
Cdd:cd13435    81 NVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2196662558 359 ALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLPIDLLTYFV 406
Cdd:cd13435   161 ALKEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLTPLL 208
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 179-398 8.85e-79

Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Podocin is expressed in the kidney and mutations in the gene have been linked to familial idiopathic nephrotic syndrome. Podocin interacts with the TRP ion channel TRPV-6 and may function as a scaffolding protein in the organization of lipid-protein domains.


Pssm-ID: 259809 [Multi-domain]  Cd Length: 223  Bit Score: 242.87  E-value: 8.85e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 179 CFKVVQEYERAVIFRLGRLVSGGAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATIS 258
Cdd:cd08827     3 CVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 259 VANVANAHHSTRLLAQTTLRNVLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQRAMAAEAE 338
Cdd:cd08827    83 LSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 339 AAREARAKVIAAEGEQKASRALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLP 398
Cdd:cd08827   163 AQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLP 222
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 212-389 3.92e-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: 3.92e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 212 PCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISVANVANAHHSTRLLAQTTLRNVLGTRPLHEILS 291
Cdd:cd08826     1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 292 DREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASRALREASEVIGDSP 371
Cdd:cd08826    81 EREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSP 160

                         170
                  ....*....|....*...
gi 2196662558 372 AALQLRYLQTLNTISAEK 389
Cdd:cd08826   161 GALQLRYLQTLSEIASEK 178
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 203-356 9.03e-66

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: 206.81  E-value: 9.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 203 KGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISVANVANAHHSTRLLAQTTLRNVLG 282
Cdd:cd08828     1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2196662558 283 TRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKA 356
Cdd:cd08828    81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 220-326 2.58e-58

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: 185.86  E-value: 2.58e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 220 VDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISVANVANAHHSTRLLAQTTLRNVLGTRPLHEILSDREAISNT 299
Cdd:cd13434     1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                          90       100
                  ....*....|....*....|....*..
gi 2196662558 300 MQTSLDDATEAWGIKVERVEIKDVRLP 326
Cdd:cd13434    81 LQEILDEATDPWGIKVERVEIKDIILP 107
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 180-400 6.35e-57

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: 186.28  E-value: 6.35e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 180 FKVVQEYERAVIFRLGRLVSggAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISV 259
Cdd:cd13437     6 YKQVKQGSVGLVERFGKFYK--TVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 260 ANVANAHHSTRLLAQTTLRNVLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQRAMAAEAEA 339
Cdd:cd13437    84 YRIDNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKA 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2196662558 340 AREARAKVIAAEGEQKASRALREASEVIgDSPAALQLRYLQTLNTISAEKNSTIVFpLPID 400
Cdd:cd13437   164 KRIGESKIISAKADVESAKLMREAADIL-DSKAAMQIRYLETLQAIAKSANSKVIF-LPLD 222
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 162-396 4.46e-55

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 183.50  E-value: 4.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 162 ALSWVVVVCTLPFSLFVCFKVVQEYERAVIFRLGRLVsgGAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVT 241
Cdd:COG0330     3 LILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 242 VSVDAVVYYRVSNATISVANVANAHHSTRLLAQTTLRNVLGTRPLHEILS-DREAISNTMQTSLDDATEAWGIKVERVEI 320
Cdd:COG0330    81 VDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 321 KDVRLPVQLQ----------------------RAMAAEAEAAREARAKVIAAEGEQKA--------SRALREASEVIGDS 370
Cdd:COG0330   161 KDIDPPEEVQdamedrmkaerereaaileaegYREAAIIRAEGEAQRAIIEAEAYREAqilraegeAEAFRIVAEAYSAA 240

                         250       260
                  ....*....|....*....|....*.
gi 2196662558 371 PAALQLRYLQTLNTISAEKNSTIVFP 396
Cdd:COG0330   241 PFVLFYRSLEALEEVLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 179-330 1.13e-49

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 165.53  E-value: 1.13e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558  179 CFKVVQEYERAVIFRLGRLVsgGAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATIS 258
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2196662558  259 VANVANAH-HSTRLLAQTTLRNVLGTRPLHEILSD-REAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQ 330
Cdd:smart00244  80 VYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK 153
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 219-326 1.69e-42

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: 144.92  E-value: 1.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 219 RVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISVANVANAHHSTRLLAQTTLRNVLGTRPLHEILSDREAISN 298
Cdd:cd08829     3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                          90       100
                  ....*....|....*....|....*...
gi 2196662558 299 TMQTSLDDATEAWGIKVERVEIKDVRLP 326
Cdd:cd08829    83 KLLEALDEATDPWGVKVTRVEIKDITPP 110
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 220-396 1.87e-41

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: 144.69  E-value: 1.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 220 VDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISVANVANAHHSTRLLAQTTLRNVLGTRPLHEILSDREAISNT 299
Cdd:cd13775     1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 300 MQTSLDDATEAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASRALREASEVIGDSPAALQLRYL 379
Cdd:cd13775    81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAM 160

                         170
                  ....*....|....*..
gi 2196662558 380 QTLNTISAEKNSTIVFP 396
Cdd:cd13775   161 NMLYEGLKEKGSMVVVP 177
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 195-325 1.24e-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: 141.00  E-value: 1.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 195 GRLVSggAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISVANVANAHHSTRLLAQ 274
Cdd:cd13436     1 GRLQK--PRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2196662558 275 TTLRNVLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRL 325
Cdd:cd13436    79 TSLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 183-395 5.51e-36

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: 131.50  E-value: 5.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 183 VQEYERAVIFRLGRLVsgGAKGPGI-FFILPCID-NYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISVA 260
Cdd:cd13438     1 VPPGERGLLYRDGKLV--RTLEPGRyAFWKFGRKvQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 261 NVANAHHSTRLLAQTTLRNVLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQRAMAAEAEAA 340
Cdd:cd13438    79 TVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2196662558 341 REARAKVIAAEGEQKASRALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVF 395
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 ...
 181-330 3.18e-32

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 120.12  E-value: 3.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 181 KVVQEYERAVIFRLGRLVsgGAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRV--SNATIS 258
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLS--RVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKL 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2196662558 259 VANVANAHHSTRLL---AQTTLRNVLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQ 330
Cdd:pfam01145  79 VQNVFGSDDLQELLrrvLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIA 153
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 179-326 5.88e-31

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: 118.74  E-value: 5.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 179 CFKVVQEYERAVIFRLGRLVsGGAKGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNAT-- 256
Cdd:cd03405     1 SVFIVDETEQAVVLQFGKPV-RVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLrf 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2196662558 257 -ISVANVANAHhstRLLAQ---TTLRNVLGTRPLHEILSD-REAISNTMQTSLDDATEAWGIKVERVEIKDVRLP 326
Cdd:cd03405    80 yQSVGGEEGAE---SRLDDivdSALRNEIGKRTLAEVVSGgRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLP 151
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 180-330 3.69e-22

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: 93.35  E-value: 3.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 180 FKVVQEYERAVIFRLGRLVSGGAKGPGIFFILPCIDNYARVDLRTRTYDVPPqEVLTKDSVTVSVDAVVYYRvsnatISV 259
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYR-----PDP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 260 ANVANAHHS------TRLL---AQTTLRNVLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQ 330
Cdd:cd03401    75 EKLPELYQNlgpdyeERVLppiVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYE 154
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 176-330 2.45e-19

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: 87.18  E-value: 2.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 176 LFVCFKVVQEYERAVIFRLGRLVSggAKGPGIFFILPC-IDNYARVDL-RTRTYDVP---PQE--VLTKDSVTVSVDAVV 248
Cdd:cd03404    11 LLSGFYTVDPGERGVVLRFGKYVR--TVGPGLHWKLPFpIEVVEKVNVtQVRSVEIGfrvPEEslMLTGDENIVDVDFVV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 249 YYRVSNATISVANVANAHHSTRLLAQTTLRNVLGTRPLHEILS-DREAISNT----MQTSLD--DAteawGIKVERVEIK 321
Cdd:cd03404    89 QYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADvrelLQEILDryDL----GIEIVQVQLQ 164


                  ....*....
gi 2196662558 322 DVRLPVQLQ 330
Cdd:cd03404   165 DADPPEEVQ 173
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 209-324 2.52e-14

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: 69.84  E-value: 2.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 209 FILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATISVANVA------NAHHSTRLLAQT---TLRN 279
Cdd:cd03399     1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAerflgkSTEEIRELVKETlegHLRA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2196662558 280 VLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVR 324
Cdd:cd03399    81 IVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDIS 125
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 172-322 9.06e-14

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: 70.27  E-value: 9.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 172 LPFSLFVCFKVVQEYERAVIFRLGRLVsGGAKGPGIFFILPCIdNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYR 251
Cdd:cd03402     2 VGIILLGGFFVVQPNEAAVLTLFGRYR-GTVRRPGLRWVNPFY-RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2196662558 252 VSNATISVANVANAHHSTRLLAQTTLRNVLGTRPL-----HEI--LSDREAISNTMQTSLDDATEAWGIKVERVEIKD 322
Cdd:cd03402    80 VVDTAKAVFDVDDYEEFVSIQSEAALRRVASRYPYdsfedGEPslRGNSDEVSEELRRELQERLAVAGVEVIEARITH 157
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 180-330 1.63e-13

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: 70.12  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 180 FKVVQEYERAVIFRLGRLVSggAKGPGIFFILPCIDnyarvdlrtRTYDVPPQEV---------LTKDSVTVSVDAVVYY 250
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHR--TVDPGLNWKPPFIE---------EVYPVNVTAVrnlrkqglmLTGDENIVNVEMNVQY 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 251 RVSNATISVANVANAHHSTRLLAQTTLRNVLGTRPLHEILSD-REAISNTMQTSLDDATEAW--GIKVERVEIKDVRLPV 327
Cdd:TIGR01933  70 RITDPYKYLFSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPE 149


                  ...
gi 2196662558 328 QLQ 330
Cdd:TIGR01933 150 EVK 152
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
166-324 1.04e-12

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 69.13  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 166 VVVVCTLPFSLFVCFKVVQEyERAVIF--RLG--RLVSGGAKgpgifFILPCIDNYARVDLRTRTYDVPPQE-VLTKDSV 240
Cdd:COG2268    14 VVVLLLLLIILARFYRKVPP-NEALVItgRGGgyKVVTGGGA-----FVLPVLHRAERMSLSTMTIEVERTEgLITKDGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 241 TVSVDAVVYYRVSNATISVANVAnahhsTRLLAQTT--------------LRNVLGTRPLHEILSDREAISNTMQTSLDD 306
Cdd:COG2268    88 RVDVDAVFYVKVNSDPEDIANAA-----ERFLGRDPeeieelaeeklegaLRAVAAQMTVEELNEDREKFAEKVQEVAGT 162

                         170
                  ....*....|....*...
gi 2196662558 307 ATEAWGIKVERVEIKDVR 324
Cdd:COG2268   163 DLAKNGLELESVAITDLE 180
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 223-326 2.47e-11

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


Pssm-ID: 259797 [Multi-domain]  Cd Length: 110  Bit Score: 60.07  E-value: 2.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 223 RTRTYDVPPQEVLTKDSVTVSVDAVVYYRVS--NATISVANVANAHHSTRLL---AQTTLRNVLGTRPLHEILSDREAIS 297
Cdd:cd02106     1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITdyNALPAFYLVDFVKDIKADIrrkIADVLRAAIGRMTLDQIISGRDEIA 80

                          90       100
                  ....*....|....*....|....*....
gi 2196662558 298 NTMQTSLDDATEAWGIKVERVEIKDVRLP 326
Cdd:cd02106    81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 182-395 1.58e-10

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


Pssm-ID: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 61.45  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 182 VVQEYERAVIFRLGRLVsgGAKGPGIFFILPCIDNYA-RVDLRTRTYDVPpQEVLTKDSVTVSVDAVVYYRVSNATISVA 260
Cdd:cd03407     1 CVSQSTVAIVERFGKFS--RIAEPGLHFIIPPIESVAgRVSLRVQQLDVR-VETKTKDNVFVTLVVSVQYRVVPEKVYDA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 261 --NVANAHHSTRLLAQTTLRNVLGTRPLHEILSDREAISNTMQTSLDDATEAWGIKVERVEIKDVRLPVQLQ-------- 330
Cdd:cd03407    78 fyKLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKaamneina 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 331 ---RAMAAEAEAAREARAKVIAAEGEQKASRA---------------LRE-----ASEVIGDSPA-ALQL----RYLQTL 382
Cdd:cd03407   158 aqrLREAAEEKAEAEKILQVKAAEAEAEAKRLqgvgiaeqrkaivdgLREsiedfQEAVPGVSSKeVMDLllitQYFDTL 237

                         250
                  ....*....|...
gi 2196662558 383 NTISAEKNSTIVF 395
Cdd:cd03407   238 KEVGKSSKSSTVF 250
PRK11029 PRK11029
protease modulator HflC;
166-328 8.18e-07

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 50.51  E-value: 8.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 166 VVVVCTLPFSLFVcfkvVQEYERAVIFRLGRLVSGGAK-----GPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSV 240
Cdd:PRK11029   10 IIVLVVLYMSVFV----VKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADRFVTKEKK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 241 TVSVDAVVYYRVSN------AT----ISVANVanahhstrLLAQT---TLRNVLGTRPLHEILSD---------REAIsN 298
Cdd:PRK11029   86 DLIVDSYIKWRISDfsryylATgggdISQAEV--------LLKRKfsdRLRSEIGRLDVKDIVTDsrgrltldvRDAL-N 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2196662558 299 TMQTSLDDATE--------------------------------AWGIKVERVEIKDVRLPVQ 328
Cdd:PRK11029  157 SGSAGTEDEVAtpaaddaiasaaerveaetkgkvpvinpnsmaALGIEVVDVRIKQINLPTE 218
PRK10930 PRK10930
FtsH protease activity modulator HflK;
180-326 3.03e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 45.97  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2196662558 180 FKVVQEYERAVIFRLGR---LVsggakGPGIFFILPCIDNYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNAT 256
Cdd:PRK10930   97 FYTIKEAERGVVTRFGKfshLV-----EPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTDPE 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2196662558 257 ISVANVANAHHSTRLLAQTTLRNVLGTRPLHEILSD-REAISNTMQTSLDDATEAW--GIKVERVEIKDVRLP 326
Cdd:PRK10930  172 KYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYdmGITLLDVNFQAARPP 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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