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Conserved domains on  [gi|62484448|ref|NP_729016|]
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uncharacterized protein Dmel_CG42540, isoform B [Drosophila melanogaster]

Protein Classification

stomatin family protein( domain architecture ID 10130453)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 110-311 5.00e-129

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


:

Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 369.19  E-value: 5.00e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 110 QGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLR 189
Cdd:cd03403   1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 190 NTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASR 269
Cdd:cd03403  81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 62484448 270 ALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLPID 311
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 ...
 110-311 5.00e-129

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


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 369.19  E-value: 5.00e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 110 QGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLR 189
Cdd:cd03403   1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 190 NTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASR 269
Cdd:cd03403  81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 62484448 270 ALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLPID 311
Cdd:cd03403 161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 69-307 2.50e-49

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 168.09  E-value: 2.50e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448  69 KLLIFLSVALVIMtlpFSLFVCFKVVQEYERAVIFRLGRLMqgGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTK 148
Cdd:COG0330   2 KLILLLILLVLVL---VLLFSSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 149 DSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILSE-RMTISGTMQVQLDEATDAWGIKVE 227
Cdd:COG0330  77 DNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVV 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 228 RVEIKDVRLPVQLQ----------------------RAMAAEAEAAREARAKVIAAEGEQKA--------SRALREASEV 277
Cdd:COG0330 157 DVEIKDIDPPEEVQdamedrmkaerereaaileaegYREAAIIRAEGEAQRAIIEAEAYREAqilraegeAEAFRIVAEA 236

                       250       260       270
                ....*....|....*....|....*....|
gi 62484448 278 IGDSPAALQLRYLQTLNTISAEKNSTIVFP 307
Cdd:COG0330 237 YSAAPFVLFYRSLEALEEVLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 90-241 2.99e-42

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 145.50  E-value: 2.99e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448     90 CFKVVQEYERAVIFRLGRLMQggAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVS 169
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVLR--VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62484448    170 IANVENAH-HSTRLLAQTTLRNTMGTRHLHEILS-ERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQ 241
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 ...
 92-264 1.62e-26

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 104.33  E-value: 1.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448    92 KVVQEYERAVIFRLGRLmqGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRV--SNATVS 169
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKL--SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448   170 IANV---ENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAA 246
Cdd:pfam01145  79 VQNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 62484448   247 EAEAAREARAKVIAAEGE 264
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 91-241 2.45e-11

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


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 63.57  E-value: 2.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448    91 FKVVQEYERAVIFRLGRLMQggAKGPGIFFILPCIDSYARVDL-RTRTYDVPPQeVLTKDSVTVSVDAVVYYRVSNATVS 169
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHR--TVDPGLNWKPPFIEEVYPVNVtAVRNLRKQGL-MLTGDENIVNVEMNVQYRITDPYKY 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62484448   170 IANVENAHHSTRLLAQTTLRNTMGTRHLHEILSE-RMTISGTMQVQLDEATDAW--GIKVERVEIKDVRLPVQLQ 241
Cdd:TIGR01933  78 LFSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVK 152
PRK11029 PRK11029
protease modulator HflC;
70-165 3.04e-07

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 51.67  E-value: 3.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448   70 LLIFLSVALVImtLPFSLFVcfkvVQEYERAVIFRLGRLMQGGAK-----GPGIFFILPCIDSYARVDLRTRTYDVPPQE 144
Cdd:PRK11029   5 VIAIIIIVLVV--LYMSVFV----VKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADR 78

                         90       100
                 ....*....|....*....|.
gi 62484448  145 VLTKDSVTVSVDAVVYYRVSN 165
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 ...
 110-311 5.00e-129

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


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 369.19  E-value: 5.00e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 110 QGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLR 189
Cdd:cd03403   1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 190 NTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASR 269
Cdd:cd03403  81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 62484448 270 ALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLPID 311
Cdd:cd03403 161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 111-317 3.75e-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: 321.64  E-value: 3.75e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 111 GGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRN 190
Cdd:cd13435   2 GGARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 191 TMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASRA 270
Cdd:cd13435  82 VLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRA 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 62484448 271 LREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLPIDLITYFL 317
Cdd:cd13435 162 LKEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLTPLL 208
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 90-309 1.94e-78

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


Pssm-ID: 259809 [Multi-domain]  Cd Length: 223  Bit Score: 241.33  E-value: 1.94e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448  90 CFKVVQEYERAVIFRLGRLMQGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVS 169
Cdd:cd08827   3 CVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 170 IANVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAE 249
Cdd:cd08827  83 LSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 250 AAREARAKVIAAEGEQKASRALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVFPLP 309
Cdd:cd08827 163 AQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLP 222
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 123-300 5.50e-68

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized. This subgroup contains PH1511 from the hyperthermophilic archaeon Pyrococcus horikoshi.


Pssm-ID: 259808 [Multi-domain]  Cd Length: 178  Bit Score: 212.76  E-value: 5.50e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 123 PCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILS 202
Cdd:cd08826   1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 203 ERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASRALREASEVIGDSP 282
Cdd:cd08826  81 EREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSP 160

                       170
                ....*....|....*...
gi 62484448 283 AALQLRYLQTLNTISAEK 300
Cdd:cd08826 161 GALQLRYLQTLSEIASEK 178
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 114-267 1.24e-59

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: 190.63  E-value: 1.24e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 114 KGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMG 193
Cdd:cd08828   1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62484448 194 TRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKA 267
Cdd:cd08828  81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 131-237 8.92e-54

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


Pssm-ID: 259812 [Multi-domain]  Cd Length: 108  Bit Score: 173.53  E-value: 8.92e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 131 VDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGT 210
Cdd:cd13434   1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                        90       100
                ....*....|....*....|....*..
gi 62484448 211 MQVQLDEATDAWGIKVERVEIKDVRLP 237
Cdd:cd13434  81 LQEILDEATDPWGIKVERVEIKDIILP 107
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 91-311 1.03e-52

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


Pssm-ID: 259815 [Multi-domain]  Cd Length: 222  Bit Score: 175.11  E-value: 1.03e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448  91 FKVVQEYERAVIFRLGRLMQggAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSI 170
Cdd:cd13437   6 YKQVKQGSVGLVERFGKFYK--TVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 171 ANVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEA 250
Cdd:cd13437  84 YRIDNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKA 163

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62484448 251 AREARAKVIAAEGEQKASRALREASEVIgDSPAALQLRYLQTLNTISAEKNSTIVFpLPID 311
Cdd:cd13437 164 KRIGESKIISAKADVESAKLMREAADIL-DSKAAMQIRYLETLQAIAKSANSKVIF-LPLD 222
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 69-307 2.50e-49

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 168.09  E-value: 2.50e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448  69 KLLIFLSVALVIMtlpFSLFVCFKVVQEYERAVIFRLGRLMqgGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTK 148
Cdd:COG0330   2 KLILLLILLVLVL---VLLFSSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 149 DSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILSE-RMTISGTMQVQLDEATDAWGIKVE 227
Cdd:COG0330  77 DNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVV 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 228 RVEIKDVRLPVQLQ----------------------RAMAAEAEAAREARAKVIAAEGEQKA--------SRALREASEV 277
Cdd:COG0330 157 DVEIKDIDPPEEVQdamedrmkaerereaaileaegYREAAIIRAEGEAQRAIIEAEAYREAqilraegeAEAFRIVAEA 236

                       250       260       270
                ....*....|....*....|....*....|
gi 62484448 278 IGDSPAALQLRYLQTLNTISAEKNSTIVFP 307
Cdd:COG0330 237 YSAAPFVLFYRSLEALEEVLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 90-241 2.99e-42

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 145.50  E-value: 2.99e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448     90 CFKVVQEYERAVIFRLGRLMQggAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVS 169
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVLR--VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62484448    170 IANVENAH-HSTRLLAQTTLRNTMGTRHLHEILS-ERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQ 241
Cdd:smart00244  80 VYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK 153
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 130-237 1.83e-39

Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in all three kingdoms of life. The conserved domain common to these families has also been referred to as the Band 7 domain. Individual proteins of the SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This subgroup of the SLPs remains largely uncharacterized. It includes human SLP-2 which is upregulated and involved in the progression and development in several types of cancer, including esophageal squamous cell carcinoma, endometrial adenocarcinoma, breast cancer, and glioma.


Pssm-ID: 259811 [Multi-domain]  Cd Length: 111  Bit Score: 136.45  E-value: 1.83e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 130 RVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISG 209
Cdd:cd08829   3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                        90       100
                ....*....|....*....|....*...
gi 62484448 210 TMQVQLDEATDAWGIKVERVEIKDVRLP 237
Cdd:cd08829  83 KLLEALDEATDPWGVKVTRVEIKDITPP 110
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 106-236 8.93e-39

Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in animals. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. The family contains human SLP-1, which has been found to be expressed in the brain, and Caenorhabditis elegans UNC-24, which is a lipid raft-associated protein required for normal locomotion. It may mediate the correct localization of UNC-1. Mutations in the unc-24 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259814 [Multi-domain]  Cd Length: 131  Bit Score: 135.61  E-value: 8.93e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 106 GRLMQggAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQ 185
Cdd:cd13436   1 GRLQK--PRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQ 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 62484448 186 TTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRL 236
Cdd:cd13436  79 TSLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 131-307 1.56e-38

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


Pssm-ID: 259817 [Multi-domain]  Cd Length: 177  Bit Score: 136.60  E-value: 1.56e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 131 VDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGT 210
Cdd:cd13775   1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 211 MQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQKASRALREASEVIGDSPAALQLRYL 290
Cdd:cd13775  81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAM 160

                       170
                ....*....|....*..
gi 62484448 291 QTLNTISAEKNSTIVFP 307
Cdd:cd13775 161 NMLYEGLKEKGSMVVVP 177
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 94-306 2.49e-31

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


Pssm-ID: 259816 [Multi-domain]  Cd Length: 215  Bit Score: 118.41  E-value: 2.49e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448  94 VQEYERAVIFRLGRLMQggAKGPGI-FFILPCID-SYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIA 171
Cdd:cd13438   1 VPPGERGLLYRDGKLVR--TLEPGRyAFWKFGRKvQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 172 NVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAAEAEAA 251
Cdd:cd13438  79 TVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAE 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62484448 252 REARAKVIAAEGEQKASRALREASEVIGDSPAALQLRYLQTLNTISAEKNSTIVF 306
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 ...
 92-264 1.62e-26

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 104.33  E-value: 1.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448    92 KVVQEYERAVIFRLGRLmqGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRV--SNATVS 169
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKL--SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448   170 IANV---ENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQRAMAA 246
Cdd:pfam01145  79 VQNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 62484448   247 EAEAAREARAKVIAAEGE 264
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 90-237 3.42e-24

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


Pssm-ID: 259803 [Multi-domain]  Cd Length: 249  Bit Score: 99.87  E-value: 3.42e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448  90 CFKVVQEYERAVIFRLGRLmQGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATV- 168
Cdd:cd03405   1 SVFIVDETEQAVVLQFGKP-VRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRf 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62484448 169 --SIANVENAHhstRLLAQ---TTLRNTMGTRHLHEILS-ERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLP 237
Cdd:cd03405  80 yqSVGGEEGAE---SRLDDivdSALRNEIGKRTLAEVVSgGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLP 151
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 91-241 4.96e-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: 78.71  E-value: 4.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448  91 FKVVQEYERAVIFRLGRLMQGGAKGPGIFFILPCIDSYARVDLRTRTYDVPPqEVLTKDSVTVSVDAVVYYRVSNATVSI 170
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRPDPEKLPE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 171 ------ANVENahhstRLL---AQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQ 241
Cdd:cd03401  80 lyqnlgPDYEE-----RVLppiVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYE 154
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 87-241 8.20e-15

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


Pssm-ID: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 73.70  E-value: 8.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448  87 LFVCFKVVQEYERAVIFRLGRLMqgGAKGPGIFFILPC-IDSYARVDL-RTRTYDVP---PQE--VLTKDSVTVSVDAVV 159
Cdd:cd03404  11 LLSGFYTVDPGERGVVLRFGKYV--RTVGPGLHWKLPFpIEVVEKVNVtQVRSVEIGfrvPEEslMLTGDENIVDVDFVV 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 160 YYRVSNATVSIANVENAHHSTRLLAQTTLRNTMGTRHLHEILSE-RMTISGTMQVQLDEATDAW--GIKVERVEIKDVRL 236
Cdd:cd03404  89 QYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEILDRYdlGIEIVQVQLQDADP 168


                ....*
gi 62484448 237 PVQLQ 241
Cdd:cd03404 169 PEEVQ 173
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 91-241 2.45e-11

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


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 63.57  E-value: 2.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448    91 FKVVQEYERAVIFRLGRLMQggAKGPGIFFILPCIDSYARVDL-RTRTYDVPPQeVLTKDSVTVSVDAVVYYRVSNATVS 169
Cdd:TIGR01933   1 IYTIGEAERGVVLRFGKYHR--TVDPGLNWKPPFIEEVYPVNVtAVRNLRKQGL-MLTGDENIVNVEMNVQYRITDPYKY 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62484448   170 IANVENAHHSTRLLAQTTLRNTMGTRHLHEILSE-RMTISGTMQVQLDEATDAW--GIKVERVEIKDVRLPVQLQ 241
Cdd:TIGR01933  78 LFSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVK 152
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 83-233 1.48e-10

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


Pssm-ID: 259800  Cd Length: 231  Bit Score: 60.64  E-value: 1.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448  83 LPFSLFVCFKVVQEYERAVIFRLGRLMqGGAKGPGIFFILPCIdSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYR 162
Cdd:cd03402   2 VGIILLGGFFVVQPNEAAVLTLFGRYR-GTVRRPGLRWVNPFY-RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWR 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62484448 163 VSNATVSIANVENAHHSTRLLAQTTLRNTMGTR----HLHEILSERM---TISGTMQVQLDEATDAWGIKVERVEIKD 233
Cdd:cd03402  80 VVDTAKAVFDVDDYEEFVSIQSEAALRRVASRYpydsFEDGEPSLRGnsdEVSEELRRELQERLAVAGVEVIEARITH 157
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 120-235 5.87e-10

Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; The flotillin (reggie) like proteins are lipid raft-associated. Individual proteins of this SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. In addition, microdomains formed from flotillin proteins may be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and interact with a variety of proteins. They may play a role in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and in cancer invasion, and metastasis.


Pssm-ID: 259798 [Multi-domain]  Cd Length: 145  Bit Score: 57.13  E-value: 5.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 120 FILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSIAN-VENA-----HHSTRLLAQT---TLRN 190
Cdd:cd03399   1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAaAERFlgkstEEIRELVKETlegHLRA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 62484448 191 TMGTRHLHEILSERMTISgtMQVQLDEATD--AWGIKVERVEIKDVR 235
Cdd:cd03399  81 IVGTMTVEEIYQDREKFA--EQVQEVAEPDlaKMGLEIDSFNIKDIS 125
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 93-306 2.00e-09

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


Pssm-ID: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 57.98  E-value: 2.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448  93 VVQEYERAVIFRLGRLMqgGAKGPGIFFILPCIDSYA-RVDLRTRTYDVPpQEVLTKDSVTVSVDAVVYYRVSNATVSIA 171
Cdd:cd03407   1 CVSQSTVAIVERFGKFS--RIAEPGLHFIIPPIESVAgRVSLRVQQLDVR-VETKTKDNVFVTLVVSVQYRVVPEKVYDA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 172 --NVENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTISGTMQVQLDEATDAWGIKVERVEIKDVRLPVQLQ-------- 241
Cdd:cd03407  78 fyKLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKaamneina 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 242 ---RAMAAEAEAAREARAKVIAAEGEQKASRA---------------LRE-----ASEVIGDSPA-ALQL----RYLQTL 293
Cdd:cd03407 158 aqrLREAAEEKAEAEKILQVKAAEAEAEAKRLqgvgiaeqrkaivdgLREsiedfQEAVPGVSSKeVMDLllitQYFDTL 237

                       250
                ....*....|...
gi 62484448 294 NTISAEKNSTIVF 306
Cdd:cd03407 238 KEVGKSSKSSTVF 250
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 134-237 5.83e-08

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


Pssm-ID: 259797 [Multi-domain]  Cd Length: 110  Bit Score: 50.44  E-value: 5.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448 134 RTRTYDVPPQEVLTKDSVTVSVDAVVYYRVS--NATVSIANV---ENAHHSTRLLAQTTLRNTMGTRHLHEILSERMTIS 208
Cdd:cd02106   1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITdyNALPAFYLVdfvKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                        90       100
                ....*....|....*....|....*....
gi 62484448 209 GTMQVQLDEATDAWGIKVERVEIKDVRLP 237
Cdd:cd02106  81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
PRK11029 PRK11029
protease modulator HflC;
70-165 3.04e-07

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 51.67  E-value: 3.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448   70 LLIFLSVALVImtLPFSLFVcfkvVQEYERAVIFRLGRLMQGGAK-----GPGIFFILPCIDSYARVDLRTRTYDVPPQE 144
Cdd:PRK11029   5 VIAIIIIVLVV--LYMSVFV----VKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADR 78

                         90       100
                 ....*....|....*....|.
gi 62484448  145 VLTKDSVTVSVDAVVYYRVSN 165
Cdd:PRK11029  79 FVTKEKKDLIVDSYIKWRISD 99
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
70-217 1.59e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 49.87  E-value: 1.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448  70 LLIFLSVALVIMTLPFSLFVCFKVVQEYERAVI---FRLGRLMQGGAKgpgifFILPCIDSYARVDLRTRTYDVPPQE-V 145
Cdd:COG2268   7 LIIIGVIVVVLLLLLIILARFYRKVPPNEALVItgrGGGYKVVTGGGA-----FVLPVLHRAERMSLSTMTIEVERTEgL 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62484448 146 LTKDSVTVSVDAVVYYRVSNATVSIANVenahhSTRLLAQT--TLRNTmgtrhLHEILSERM-TISGTMQV-QLDE 217
Cdd:COG2268  82 ITKDGIRVDVDAVFYVKVNSDPEDIANA-----AERFLGRDpeEIEEL-----AEEKLEGALrAVAAQMTVeELNE 147
PRK10930 PRK10930
FtsH protease activity modulator HflK;
91-237 2.51e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 45.97  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448   91 FKVVQEYERAVIFRLGRLMQggAKGPGIFFILPCIDSYARVDLRTRTYDVPPQEVLTKDSVTVSVDAVVYYRVSNATVSI 170
Cdd:PRK10930  97 FYTIKEAERGVVTRFGKFSH--LVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTDPEKYL 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62484448  171 ANVENAHHSTRLLAQTTLRNTMGTRHLHEILSE-RMTISGTMQVQLDEATDAW--GIKVERVEIKDVRLP 237
Cdd:PRK10930 175 FSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYdmGITLLDVNFQAARPP 244
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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