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Conserved domains on  [gi|559098406|ref|NP_001273960|]
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stomatin-like protein 2, mitochondrial isoform b [Homo sapiens]

Protein Classification

SPFH domain-containing protein( domain architecture ID 11417211)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein similar to Escherichia coli protein QmcA that has been identified as a multi-copy suppressor of an FtsH/HtpX protease double disruption mutant and may play a role in the quality control of integral membrane proteins

Gene Ontology:  GO:0016020
PubMed:  17766116|10542406

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 41-255 1.31e-53

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 176.57  E-value: 1.31e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVE 120
Cdd:COG0330   24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 121 DPEYAVTQLAQTTMRSELGKLSLDKVF----------------------------------------------RVEAERR 154
Cdd:COG0330  103 NAEEALRQLAESALREVIGKMTLDEVLstgrdeinaeireelqealdpygievvdveikdidppeevqdamedRMKAERE 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 155 KRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAAALTqhngdaAASLTVA 234
Cdd:COG0330  183 REAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLF 245

                        250       260
                 ....*....|....*....|.
gi 559098406 235 EQYVSAFSKLAKDSNTILLPS 255
Cdd:COG0330  246 YRSLEALEEVLSPNSKVIVLP 266
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 41-255 1.31e-53

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 176.57  E-value: 1.31e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVE 120
Cdd:COG0330   24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 121 DPEYAVTQLAQTTMRSELGKLSLDKVF----------------------------------------------RVEAERR 154
Cdd:COG0330  103 NAEEALRQLAESALREVIGKMTLDEVLstgrdeinaeireelqealdpygievvdveikdidppeevqdamedRMKAERE 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 155 KRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAAALTqhngdaAASLTVA 234
Cdd:COG0330  183 REAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLF 245

                        250       260
                 ....*....|....*....|.
gi 559098406 235 EQYVSAFSKLAKDSNTILLPS 255
Cdd:COG0330  246 YRSLEALEEVLSPNSKVIVLP 266
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 74-147 1.04e-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: 137.61  E-value: 1.04e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 559098406  74 RYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVF 147
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETL 74
PHB smart00244
prohibitin homologues; prohibitin homologues
 40-163 1.15e-31

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 115.84  E-value: 1.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406    40 FVPQQEAWVVERMGRFHRILEPGLNILIPVLDRIrYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:smart00244   5 VVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRV 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 559098406   120 EDPEYAVT-QLAQTTMRSELGKLSLDKVFRVeaERRKRATVLESE 163
Cdd:smart00244  84 LDADYAVIeQLAQTTLRSVIGKRTLDELLTD--QREKISENIREE 126
Band_7_C pfam16200
C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal ...
 214-276 3.71e-25

C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal extension of the Band_7 family, pfam01145. It is found in proteins fro bacteria to fungi, plants and mammals.


Pssm-ID: 465062  Cd Length: 63  Bit Score: 95.63  E-value: 3.71e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559098406  214 RILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTILLPSNPGDVTSMVAQAMGVYGALTK 276
Cdd:pfam16200   1 EKVAEAIKKPGGQEAVSLRVAEQYVEAFGKLAKESNTVILPANLGDVSSMVAQAMSIYKKVNK 63
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 41-146 1.68e-13

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


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 68.97  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406   41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQSlkEIVINVPEQSAV-TLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNV--TAVRNLRKQGLMlTGDENIVNVEMNVQYRITDPYKYLFSV 81

                          90       100
                  ....*....|....*....|....*..
gi 559098406  120 EDPEYAVTQLAQTTMRSELGKLSLDKV 146
Cdd:TIGR01933  82 ENPEDSLRQATDSALRGVIGDSTMDDI 108
PRK10930 PRK10930
FtsH protease activity modulator HflK;
41-167 9.35e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 43.66  E-value: 9.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQslkeiVINVPEQSA----VTLDNVTLQIDGVLYLRIMDPYKAS 116
Cdd:PRK10930 100 IKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVN-----VEAVRELAAsgvmLTSDENVVRVEMNVQYRVTDPEKYL 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 559098406 117 YGVEDPEYAVTQLAQTTMRSELGKLSLDKVFrveAERRkraTVLESEGTRE 167
Cdd:PRK10930 175 FSVTSPDDSLRQATDSALRGVIGKYTMDRIL---TEGR---TVIRSDTQRE 219
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 41-255 1.31e-53

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 176.57  E-value: 1.31e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVE 120
Cdd:COG0330   24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 121 DPEYAVTQLAQTTMRSELGKLSLDKVF----------------------------------------------RVEAERR 154
Cdd:COG0330  103 NAEEALRQLAESALREVIGKMTLDEVLstgrdeinaeireelqealdpygievvdveikdidppeevqdamedRMKAERE 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 155 KRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAAALTqhngdaAASLTVA 234
Cdd:COG0330  183 REAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLF 245

                        250       260
                 ....*....|....*....|.
gi 559098406 235 EQYVSAFSKLAKDSNTILLPS 255
Cdd:COG0330  246 YRSLEALEEVLSPNSKVIVLP 266
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 74-147 1.04e-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: 137.61  E-value: 1.04e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 559098406  74 RYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVF 147
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETL 74
PHB smart00244
prohibitin homologues; prohibitin homologues
 40-163 1.15e-31

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 115.84  E-value: 1.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406    40 FVPQQEAWVVERMGRFHRILEPGLNILIPVLDRIrYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:smart00244   5 VVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRV 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 559098406   120 EDPEYAVT-QLAQTTMRSELGKLSLDKVFRVeaERRKRATVLESE 163
Cdd:smart00244  84 LDADYAVIeQLAQTTLRSVIGKRTLDELLTD--QREKISENIREE 126
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 41-196 1.15e-26

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: 104.23  E-value: 1.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVE 120
Cdd:cd13437    9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKIIQV-DMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 121 DPEYAVTQLAQTTMRSELGKLSLDKVFR------------VEAERRKRATVLE---------SEGTRESAINVAEGKKQA 179
Cdd:cd13437   88 NVKQALIERTQTTLRSVIGERTLQDLLEkreeiadeieeiVEEVAKEWGVYVEsilikdivlSKDLQQSLSSAAKAKRIG 167

                        170       180
                 ....*....|....*....|.
gi 559098406 180 Q---ILA-SEAEKAEQINQAA 196
Cdd:cd13437  168 EskiISAkADVESAKLMREAA 188
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 68-185 2.11e-25

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: 99.90  E-value: 2.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  68 PVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLD--- 144
Cdd:cd08826    1 PFIDRMVRV-DLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDell 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 145 -----------------------KVFRV-------------------EAERRKRATVLESEGTRESAINVAEGkkqAQIL 182
Cdd:cd08826   80 sereeinkriqeiideqtepwgiKVTAVeikdvdlpesmqramarqaEAERERRAKIIKAEGELQAAEKLAEA---AEIL 156


                 ...
gi 559098406 183 ASE 185
Cdd:cd08826  157 AKS 159
Band_7_C pfam16200
C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal ...
 214-276 3.71e-25

C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal extension of the Band_7 family, pfam01145. It is found in proteins fro bacteria to fungi, plants and mammals.


Pssm-ID: 465062  Cd Length: 63  Bit Score: 95.63  E-value: 3.71e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559098406  214 RILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTILLPSNPGDVTSMVAQAMGVYGALTK 276
Cdd:pfam16200   1 EKVAEAIKKPGGQEAVSLRVAEQYVEAFGKLAKESNTVILPANLGDVSSMVAQAMSIYKKVNK 63
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 41-266 4.31e-18

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: 82.25  E-value: 4.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQSLKEIVINVPEQSAvTLDNVTLQIDGVLYLRIMDP--YKASYG 118
Cdd:cd03407    2 VSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDVRVETK-TKDNVFVTLVVSVQYRVVPEkvYDAFYK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 119 VEDPEYAVTQLAQTTMRSELGKLSLDKVFR--------VEAERRKR------------ATVLESEGTRESA---INVAEG 175
Cdd:cd03407   81 LTNPEQQIQSYVFDVVRASVPKLTLDEVFEskdeiakaVKEELAKVmseygyeivktlVTDIEPDASVKAAmneINAAQR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 176 KKQAQILASEAEKAEQINQAAGEASAVLAKAKAKAEAIRILAAALT------QHNGDAAASLTVAE-----QYVSAFSKL 244
Cdd:cd03407  161 LREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLResiedfQEAVPGVSSKEVMDlllitQYFDTLKEV 240

                        250       260
                 ....*....|....*....|....
gi 559098406 245 AKDS--NTILLPSNPGDVTSMVAQ 266
Cdd:cd03407  241 GKSSksSTVFLPHGPGGVSDISAQ 264
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 79-146 6.54e-18

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: 77.62  E-value: 6.54e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559098406  79 LKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKV 146
Cdd:cd13434    3 LRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDEL 70
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 41-158 4.50e-17

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: 77.36  E-value: 4.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406   41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIM--DPYKASYG 118
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLVQN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 559098406  119 VEDPEYA---VTQLAQTTMRSELGKLSLDKVFRVEAERRKRAT 158
Cdd:pfam01145  82 VFGSDDLqelLRRVLESALREIIARYTLEELLSNREELAEEIK 124
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 61-186 6.31e-14

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: 69.33  E-value: 6.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  61 PGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELG- 139
Cdd:cd13435    7 PGVFFVLPCIDNYCKV-DLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGt 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 140 -----------------KLSLD--------KVFRVEAE------RRKRATVLESEGTRESAINV--AEGKKQAQILASEA 186
Cdd:cd13435   86 rnlsellteretishsmQVTLDeatdpwgvQVERVEIKdvslpdSLQRAMAAEAEAAREARAKViaAEGEMKSSRALKEA 165
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 41-146 1.68e-13

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


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 68.97  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406   41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQSlkEIVINVPEQSAV-TLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNV--TAVRNLRKQGLMlTGDENIVNVEMNVQYRITDPYKYLFSV 81

                          90       100
                  ....*....|....*....|....*..
gi 559098406  120 EDPEYAVTQLAQTTMRSELGKLSLDKV 146
Cdd:TIGR01933  82 ENPEDSLRQATDSALRGVIGDSTMDDI 108
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 41-198 1.90e-13

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: 69.08  E-value: 1.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  41 VPQQEAWVVERMGRFHRILEPGLNILIP-VLDRIRYVQS----LKEIVINVPEQSAV-TLD-NVtLQIDGVLYLRIMDPY 113
Cdd:cd03404   18 VDPGERGVVLRFGKYVRTVGPGLHWKLPfPIEVVEKVNVtqvrSVEIGFRVPEESLMlTGDeNI-VDVDFVVQYRISDPV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 114 KASYGVEDPEYAVTQLAQTTMRSELGKLSLDKV----------------------------------------------F 147
Cdd:cd03404   97 AYLFNVRDPEETLRQAAESALREVVGSRTLDDVltegraeiaadvrellqeildrydlgieivqvqlqdadppeevqdaF 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 559098406 148 R--VEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 198
Cdd:cd03404  177 DdvNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGD 229
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 61-191 1.65e-12

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: 64.28  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  61 PGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGK 140
Cdd:cd08828    3 PGLILVLPCTDTFIKV-DLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGT 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 559098406 141 LSLDKVFRVEAERRKRATVLESEGTRESAINVAEGK--------KQAQILASEAEKAEQ 191
Cdd:cd08828   82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEikdvripvQMQRAMAAEAEATRE 140
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 61-186 2.31e-12

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: 64.88  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  61 PGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELG- 139
Cdd:cd03403    7 PGLFFILPCIDSYRKV-DLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGt 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 140 -----------------KLSLD--------KVFRVEAE------RRKRATVLESEGTRESAINV--AEGKKQAQILASEA 186
Cdd:cd03403   86 knlseilsdretishqmQSTLDeatdpwgvKVERVEIKdvrlpvQLQRAMAAEAEAAREARAKViaAEGEQNASRALKEA 165
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 41-192 8.87e-10

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: 58.27  E-value: 8.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  41 VPQQEAWVVERMGR-FHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDP---YKAs 116
Cdd:cd03405    5 VDETEQAVVLQFGKpVRVITEPGLHFKLPFIQNVRKF-DKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPlrfYQS- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 117 ygVEDPEYAVTQLAQ---TTMRSELGKLSL---------------------------------------------DKVF- 147
Cdd:cd03405   83 --VGGEEGAESRLDDivdSALRNEIGKRTLaevvsggrdelmeeileqaneeakeygievvdvrikridlpeevsESVYe 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 559098406 148 RVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAE-KAEQI 192
Cdd:cd03405  161 RMRAERERIAAEYRAEGEEEAEKIRAEADRERTVILAEAYrEAEEI 206
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 53-155 6.51e-08

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: 50.48  E-value: 6.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  53 GRFHRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQT 132
Cdd:cd13436    1 GRLQKPRGPGIVLILPCIDNFTRV-DMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQT 79

                         90       100
                 ....*....|....*....|...
gi 559098406 133 TMRSELGKLSLDKvfrVEAERRK 155
Cdd:cd13436   80 SLTNSLSKKTVRE---IQSDRRK 99
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 89-196 9.23e-08

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: 51.09  E-value: 9.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  89 QSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSL----------DKVFRVEAERRKRA- 157
Cdd:cd13775   13 EQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELaellsrreqiDEELQDIIDEKTTPw 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 559098406 158 --TVLeSEGTRESAI-----------NVAEGKKQAQILASEAEK--AEQINQAA 196
Cdd:cd13775   93 giTVQ-SVEIRDIIIpkelqdamsreAQAEREKNARVILAEAEKeiAEMFVEAA 145
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 41-146 1.09e-07

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: 51.38  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  41 VPQQEAWVVERMGRFHRILEPGL--------NILIPVLDriryvqsLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDP 112
Cdd:cd13438    1 VPPGERGLLYRDGKLVRTLEPGRyafwkfgrKVQVELVD-------LREQLLEVSGQEILTADKVALRVNLVATYRVVDP 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 559098406 113 YKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKV 146
Cdd:cd13438   74 VKAVETVDDPEEQLYLALQLALREAVAARTLDEL 107
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 38-196 7.28e-07

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: 49.12  E-value: 7.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  38 VLFVPQQEAWVVERMGRF--HRILEPGLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKA 115
Cdd:cd08827    4 VKVVREYERAVIFRLGHLlqGRARGPGLFFYLPCLDVCHKV-DIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406 116 SYGVEDPEYAVTQLAQTTMRSELG------------------KLSLDKV---FRVEAERRKRATVLESEGTRESAINVAE 174
Cdd:cd08827   83 LSSFASISDAMQALVQTTVKRLLAhraftdillerksiaqeiKVALDSGtcrWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                        170       180
                 ....*....|....*....|....*.
gi 559098406 175 GKKQAQI--LASEAEKA--EQINQAA 196
Cdd:cd08827  163 AQRQAKVkvIAAEGEKAasEALKAAA 188
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 41-135 5.69e-05

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: 43.70  E-value: 5.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  41 VPQQEAWVVERMGRFHR-ILEPGLNILIPVLDRIRYvqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGV 119
Cdd:cd03402   13 VQPNEAAVLTLFGRYRGtVRRPGLRWVNPFYRKKRV--SLRVRNFESEPLKVNDANGNPIEIAAVVVWRVVDTAKAVFDV 90

                         90
                 ....*....|....*.
gi 559098406 120 EDPEYAVTQLAQTTMR 135
Cdd:cd03402   91 DDYEEFVSIQSEAALR 106
PRK10930 PRK10930
FtsH protease activity modulator HflK;
41-167 9.35e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 43.66  E-value: 9.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098406  41 VPQQEAWVVERMGRFHRILEPGLNILIPVLDRIRYVQslkeiVINVPEQSA----VTLDNVTLQIDGVLYLRIMDPYKAS 116
Cdd:PRK10930 100 IKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPVN-----VEAVRELAAsgvmLTSDENVVRVEMNVQYRVTDPEKYL 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 559098406 117 YGVEDPEYAVTQLAQTTMRSELGKLSLDKVFrveAERRkraTVLESEGTRE 167
Cdd:PRK10930 175 FSVTSPDDSLRQATDSALRGVIGKYTMDRIL---TEGR---TVIRSDTQRE 219
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 83-144 5.48e-04

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: 38.88  E-value: 5.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 559098406  83 VINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKA-----SYGVEDPEYAVTQLAQTTMRSELGKLSLD 144
Cdd:cd02106    4 FDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLD 70
 
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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