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Conserved domains on  [gi|392926027|ref|NP_001257023|]
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Stomatin-2 [Caenorhabditis elegans]

Protein Classification

SPFH domain-containing protein( domain architecture ID 139628)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_like super family cl19107
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 113-313 1.47e-125

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


The actual alignment was detected with superfamily member cd03403:

Pssm-ID: 473137 [Multi-domain]  Cd Length: 202  Bit Score: 357.25  E-value: 1.47e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 113 GGAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQTTLRN 192
Cdd:cd03403    2 GGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 193 MLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQRAMAAEAEATREARAKVIAAEGEQKASRA 272
Cdd:cd03403   82 VLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392926027 273 LRDAASVIAQSPAALQLRYLQTLNSVAAEKNSTIIFPLPME 313
Cdd:cd03403  162 LKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
 
Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 113-313 1.47e-125

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: 357.25  E-value: 1.47e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 113 GGAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQTTLRN 192
Cdd:cd03403    2 GGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 193 MLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQRAMAAEAEATREARAKVIAAEGEQKASRA 272
Cdd:cd03403   82 VLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392926027 273 LRDAASVIAQSPAALQLRYLQTLNSVAAEKNSTIIFPLPME 313
Cdd:cd03403  162 LKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 87-309 2.35e-46

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 158.08  E-value: 2.35e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  87 VSIYFCMKVVQEYERAVIFRLGRLIGggAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRIS 166
Cdd:COG0330   15 VLLFSSVYIVPQGERGVVLRFGKYVR--TLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRIT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 167 NATVSVANVENAHHSTRLLAQTTLRNMLGTRSLSEILS-DRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQ-- 243
Cdd:COG0330   93 DPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQda 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 244 --------------------RAMAAEAEATREARAKVIAAEGEQKA--SRALRDA------ASVIAQSPAALQLRYLQTL 295
Cdd:COG0330  173 medrmkaerereaaileaegYREAAIIRAEGEAQRAIIEAEAYREAqiLRAEGEAeafrivAEAYSAAPFVLFYRSLEAL 252

                        250
                 ....*....|....
gi 392926027 296 NSVAAEKNSTIIFP 309
Cdd:COG0330  253 EEVLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 91-243 6.39e-44

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 147.81  E-value: 6.39e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027    91 FCMKVVQEYERAVIFRLGRLIGggAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATV 170
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR--VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926027   171 SVANVENAH-HSTRLLAQTTLRNMLGTRSLSEILSD-RETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQ 243
Cdd:smart00244  79 AVYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK 153
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 94-239 1.00e-29

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: 111.26  E-value: 1.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027   94 KVVQEYERAVIFRLGRLigGGAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATV--- 170
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKL--SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPpkl 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926027  171 --SVANVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLP 239
Cdd:pfam01145  79 vqNVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPP 149
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 95-243 1.63e-12

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: 66.27  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027   95 VVQEYERAVIFRLGRLIGggAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVAN 174
Cdd:TIGR01933   3 TIGEAERGVVLRFGKYHR--TVDPGLNWKPPFIEEVYPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPYKYLFS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926027  175 VENAHHSTRLLAQTTLRNMLGTRSLSEILSD-RETLAASMQTILDEATESW--GIKVERVEIKDVRLPIQLQ 243
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVK 152
PRK11029 PRK11029
protease modulator HflC;
74-167 2.78e-06

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 48.20  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  74 MGLSWIMVISTFPVSIYFCMKVVQEYERAVIFRLGRLIGGGAK-----GPGIFFVLPCIESYTKVDLRTVSFSVPPQEIL 148
Cdd:PRK11029   1 MRKSVIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADRFV 80

                         90
                 ....*....|....*....
gi 392926027 149 TKDSVTTSVDAVIYYRISN 167
Cdd:PRK11029  81 TKEKKDLIVDSYIKWRISD 99
 
Name Accession Description Interval E-value
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 113-313 1.47e-125

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: 357.25  E-value: 1.47e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 113 GGAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQTTLRN 192
Cdd:cd03403    2 GGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 193 MLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQRAMAAEAEATREARAKVIAAEGEQKASRA 272
Cdd:cd03403   82 VLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 392926027 273 LRDAASVIAQSPAALQLRYLQTLNSVAAEKNSTIIFPLPME 313
Cdd:cd03403  162 LKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 113-315 8.81e-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: 322.80  E-value: 8.81e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 113 GGAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQTTLRN 192
Cdd:cd13435    2 GGARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 193 MLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQRAMAAEAEATREARAKVIAAEGEQKASRA 272
Cdd:cd13435   82 VLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 392926027 273 LRDAASVIAQSPAALQLRYLQTLNSVAAEKNSTIIFPLPMELV 315
Cdd:cd13435  162 LKEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELL 204
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 90-311 1.87e-80

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: 243.64  E-value: 1.87e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  90 YFCMKVVQEYERAVIFRLGRLIGGGAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNAT 169
Cdd:cd08827    1 WFCVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 170 VSVANVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQRAMAAE 249
Cdd:cd08827   81 VCLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926027 250 AEATREARAKVIAAEGEQKASRALRDAASVIAQSPAALQLRYLQTLNSVAAEKNSTIIFPLP 311
Cdd:cd08827  161 AEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLP 222
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 116-269 2.70e-71

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: 217.98  E-value: 2.70e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 116 KGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQTTLRNMLG 195
Cdd:cd08828    1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926027 196 TRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQRAMAAEAEATREARAKVIAAEGEQKA 269
Cdd:cd08828   81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 125-302 2.35e-69

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


Pssm-ID: 259808 [Multi-domain]  Cd Length: 178  Bit Score: 213.53  E-value: 2.35e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 125 PCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQTTLRNMLGTRSLSEILS 204
Cdd:cd08826    1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 205 DRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQRAMAAEAEATREARAKVIAAEGEQKASRALRDAASVIAQSP 284
Cdd:cd08826   81 EREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSP 160

                        170
                 ....*....|....*...
gi 392926027 285 AALQLRYLQTLNSVAAEK 302
Cdd:cd08826  161 GALQLRYLQTLSEIASEK 178
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 133-239 1.84e-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: 183.16  E-value: 1.84e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 133 VDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAAS 212
Cdd:cd13434    1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                         90       100
                 ....*....|....*....|....*..
gi 392926027 213 MQTILDEATESWGIKVERVEIKDVRLP 239
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDIILP 107
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 93-313 6.88e-55

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: 178.19  E-value: 6.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  93 MKVVQEYERAVIFRLGRLIGggAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSV 172
Cdd:cd13437    6 YKQVKQGSVGLVERFGKFYK--TVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 173 ANVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQRAMAAEAEA 252
Cdd:cd13437   84 YRIDNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKA 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926027 253 TREARAKVIAAEGEQKASRALRDAASVIAqSPAALQLRYLQTLNSVAAEKNSTIIFpLPME 313
Cdd:cd13437  164 KRIGESKIISAKADVESAKLMREAADILD-SKAAMQIRYLETLQAIAKSANSKVIF-LPLD 222
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 87-309 2.35e-46

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 158.08  E-value: 2.35e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  87 VSIYFCMKVVQEYERAVIFRLGRLIGggAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRIS 166
Cdd:COG0330   15 VLLFSSVYIVPQGERGVVLRFGKYVR--TLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRIT 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 167 NATVSVANVENAHHSTRLLAQTTLRNMLGTRSLSEILS-DRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQ-- 243
Cdd:COG0330   93 DPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQda 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 244 --------------------RAMAAEAEATREARAKVIAAEGEQKA--SRALRDA------ASVIAQSPAALQLRYLQTL 295
Cdd:COG0330  173 medrmkaerereaaileaegYREAAIIRAEGEAQRAIIEAEAYREAqiLRAEGEAeafrivAEAYSAAPFVLFYRSLEAL 252

                        250
                 ....*....|....
gi 392926027 296 NSVAAEKNSTIIFP 309
Cdd:COG0330  253 EEVLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
 91-243 6.39e-44

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 147.81  E-value: 6.39e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027    91 FCMKVVQEYERAVIFRLGRLIGggAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATV 170
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR--VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926027   171 SVANVENAH-HSTRLLAQTTLRNMLGTRSLSEILSD-RETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQ 243
Cdd:smart00244  79 AVYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK 153
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 132-239 8.27e-40

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


Pssm-ID: 259811 [Multi-domain]  Cd Length: 111  Bit Score: 135.68  E-value: 8.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 132 KVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAA 211
Cdd:cd08829    3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                         90       100
                 ....*....|....*....|....*...
gi 392926027 212 SMQTILDEATESWGIKVERVEIKDVRLP 239
Cdd:cd08829   83 KLLEALDEATDPWGVKVTRVEIKDITPP 110
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 108-238 1.04e-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: 135.99  E-value: 1.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 108 GRLIGggAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQ 187
Cdd:cd13436    1 GRLQK--PRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQ 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392926027 188 TTLRNMLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRL 238
Cdd:cd13436   79 TSLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 133-309 4.80e-39

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


Pssm-ID: 259817 [Multi-domain]  Cd Length: 177  Bit Score: 135.83  E-value: 4.80e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 133 VDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAAS 212
Cdd:cd13775    1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 213 MQTILDEATESWGIKVERVEIKDVRLPIQLQRAMAAEAEATREARAKVIAAEGEQKASRALRDAASVIAQSPAALQLRYL 292
Cdd:cd13775   81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAM 160

                        170
                 ....*....|....*..
gi 392926027 293 QTLNSVAAEKNSTIIFP 309
Cdd:cd13775  161 NMLYEGLKEKGSMVVVP 177
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 96-308 3.95e-34

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


Pssm-ID: 259816 [Multi-domain]  Cd Length: 215  Bit Score: 124.18  E-value: 3.95e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  96 VQEYERAVIFRLGRLIGggAKGPGI--FFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVA 173
Cdd:cd13438    1 VPPGERGLLYRDGKLVR--TLEPGRyaFWKFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 174 NVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQRAMAAEAEAT 253
Cdd:cd13438   79 TVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392926027 254 REARAKVIAAEGEQKASRALRDAASVIAQSPAALQLRYLQTLNSVAAEKNSTIIF 308
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 ...
 94-239 1.00e-29

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: 111.26  E-value: 1.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027   94 KVVQEYERAVIFRLGRLigGGAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATV--- 170
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKL--SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPpkl 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392926027  171 --SVANVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLP 239
Cdd:pfam01145  79 vqNVFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPP 149
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 92-239 1.84e-25

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: 102.18  E-value: 1.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  92 CMKVVQEYERAVIFRLGRlIGGGAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATV- 170
Cdd:cd03405    1 SVFIVDETEQAVVLQFGK-PVRVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRf 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392926027 171 --SVANVENAHhstRLLAQ---TTLRNMLGTRSLSEILSD-RETLAASMQTILDEATESWGIKVERVEIKDVRLP 239
Cdd:cd03405   80 yqSVGGEEGAE---SRLDDivdSALRNEIGKRTLAEVVSGgRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLP 151
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 65-243 8.06e-17

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: 78.71  E-value: 8.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  65 GLGFCGWFLMGlswimvistfpvsIYfcmkVVQEYERAVIFRLGRLIGggAKGPGIFFVLPC-IESYTKVDLRTV----- 138
Cdd:cd03404    4 LLLLLVWLLSG-------------FY----TVDPGERGVVLRFGKYVR--TVGPGLHWKLPFpIEVVEKVNVTQVrsvei 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 139 SFSVPPQ-EILTKDSVTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQTTLRNMLGTRSLSEILS-DRETLAAS---- 212
Cdd:cd03404   65 GFRVPEEsLMLTGDENIVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADvrel 144

                        170       180       190
                 ....*....|....*....|....*....|.
gi 392926027 213 MQTILDEAtESwGIKVERVEIKDVRLPIQLQ 243
Cdd:cd03404  145 LQEILDRY-DL-GIEIVQVQLQDADPPEEVQ 173
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 95-239 5.18e-16

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


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 74.86  E-value: 5.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  95 VVQEYERAVIFRLGRLIGGGAKGPGIFFVLPCIESYTKVDLRTVSFSVPPqEILTKDSVTTSVDAVIYYRISNATVSV-- 172
Cdd:cd03401    3 TVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRPDPEKLPEly 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926027 173 ----ANVENahhstRLL---AQTTLRNMLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLP 239
Cdd:cd03401   82 qnlgPDYEE-----RVLppiVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFP 150
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 122-237 1.85e-13

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


Pssm-ID: 259798 [Multi-domain]  Cd Length: 145  Bit Score: 66.76  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 122 FVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVAN-VENA-----HHSTRLLAQT---TLRN 192
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAaAERFlgkstEEIRELVKETlegHLRA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 392926027 193 MLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVR 237
Cdd:cd03399   81 IVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDIS 125
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 95-243 1.63e-12

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: 66.27  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027   95 VVQEYERAVIFRLGRLIGggAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVAN 174
Cdd:TIGR01933   3 TIGEAERGVVLRFGKYHR--TVDPGLNWKPPFIEEVYPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPYKYLFS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926027  175 VENAHHSTRLLAQTTLRNMLGTRSLSEILSD-RETLAASMQTILDEATESW--GIKVERVEIKDVRLPIQLQ 243
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVK 152
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 139-239 2.43e-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: 59.68  E-value: 2.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 139 SFSVPPQEILTKDSVTTSVDAVIYYRISN-----ATVSVANVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAASM 213
Cdd:cd02106    4 FDDVRVEPVGTADGVPVAVDLVVQFRITDynalpAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAV 83

                         90       100
                 ....*....|....*....|....*.
gi 392926027 214 QTILDEATESWGIKVERVEIKDVRLP 239
Cdd:cd02106   84 KEDLEEDLENFGVVISDVDITSIEPP 109
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
111-237 2.01e-09

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 58.35  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 111 IGGGAkgpgifFVLPCIESYTKVDLRTVSFSVPPQE-ILTKDSVTTSVDAVIYYRISNATVSVANVenahhSTRLLAQTT 189
Cdd:COG2268   50 TGGGA------FVLPVLHRAERMSLSTMTIEVERTEgLITKDGIRVDVDAVFYVKVNSDPEDIANA-----AERFLGRDP 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392926027 190 --------------LRNMLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVR 237
Cdd:COG2268  119 eeieelaeeklegaLRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLE 180
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 94-238 6.31e-08

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: 52.55  E-value: 6.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  94 KVVQEYERAVIFRLGRLIGGgAKGPGIFFVLPCIeSYTKVDLRTVSFSVPPQEILTKDSVTTSVDAVIYYRISNATVSVA 173
Cdd:cd03402   11 FVVQPNEAAVLTLFGRYRGT-VRRPGLRWVNPFY-RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWRVVDTAKAVF 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392926027 174 NVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAASMQTILDEATESWGIKVER--VEIKDVRL 238
Cdd:cd03402   89 DVDDYEEFVSIQSEAALRRVASRYPYDSFEDGEPSLRGNSDEVSEELRRELQERLAVagVEVIEARI 155
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 95-308 1.86e-07

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: 51.43  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  95 VVQEYERAVIFRLGRLigGGAKGPGIFFVLPCIESYT-KVDLRT--VSFSVppqEILTKDSVTTSVDAVIYYRISNATVS 171
Cdd:cd03407    1 CVSQSTVAIVERFGKF--SRIAEPGLHFIIPPIESVAgRVSLRVqqLDVRV---ETKTKDNVFVTLVVSVQYRVVPEKVY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 172 VA--NVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAASMQTILDEATESWGIKVERVEIKDVRLPIQLQ------ 243
Cdd:cd03407   76 DAfyKLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKaamnei 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 244 -----RAMAAEAEATREARAKVIAAEGEQKASRA---------------LRD--------AASVIAQSPAALQL--RYLQ 293
Cdd:cd03407  156 naaqrLREAAEEKAEAEKILQVKAAEAEAEAKRLqgvgiaeqrkaivdgLREsiedfqeaVPGVSSKEVMDLLLitQYFD 235

                        250
                 ....*....|....*
gi 392926027 294 TLNSVAAEKNSTIIF 308
Cdd:cd03407  236 TLKEVGKSSKSSTVF 250
PRK11029 PRK11029
protease modulator HflC;
74-167 2.78e-06

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 48.20  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  74 MGLSWIMVISTFPVSIYFCMKVVQEYERAVIFRLGRLIGGGAK-----GPGIFFVLPCIESYTKVDLRTVSFSVPPQEIL 148
Cdd:PRK11029   1 MRKSVIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADRFV 80

                         90
                 ....*....|....*....
gi 392926027 149 TKDSVTTSVDAVIYYRISN 167
Cdd:PRK11029  81 TKEKKDLIVDSYIKWRISD 99
PRK10930 PRK10930
FtsH protease activity modulator HflK;
73-239 2.00e-04

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 42.89  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027  73 LMGLSWIMVISTFPVSIYFCMKvvqEYERAVIFRLGRLigGGAKGPGIFFVLPCIESYTKVDLRTVSFSVPPQEILTKDS 152
Cdd:PRK10930  80 VVGIAAAAVVIIWAASGFYTIK---EAERGVVTRFGKF--SHLVEPGLNWKPTFIDEVKPVNVEAVRELAASGVMLTSDE 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926027 153 VTTSVDAVIYYRISNATVSVANVENAHHSTRLLAQTTLRNMLGTRSLSEILSDRETLAAS-MQTILDEATESW--GIKVE 229
Cdd:PRK10930 155 NVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEGRTVIRSdTQRELEETIRPYdmGITLL 234

                        170
                 ....*....|
gi 392926027 230 RVEIKDVRLP 239
Cdd:PRK10930 235 DVNFQAARPP 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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