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Conserved domains on  [gi|559098453|ref|NP_001273962|]
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stomatin-like protein 2, mitochondrial isoform d [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 ...
 16-254 5.69e-64

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 203.15  E-value: 5.69e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  16 GLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKL 95
Cdd:COG0330   45 GLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKM 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  96 SLDKVFRE-RESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEG 174
Cdd:COG0330  124 TLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEG 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453 175 KKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAAALTqhngdaAASLTVAEQYVSAFSKLAKDSNTILLPS 254
Cdd:COG0330  204 EAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLFYRSLEALEEVLSPNSKVIVLP 266
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 16-254 5.69e-64

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 203.15  E-value: 5.69e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  16 GLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKL 95
Cdd:COG0330   45 GLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKM 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  96 SLDKVFRE-RESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEG 174
Cdd:COG0330  124 TLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEG 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453 175 KKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAAALTqhngdaAASLTVAEQYVSAFSKLAKDSNTILLPS 254
Cdd:COG0330  204 EAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLFYRSLEALEEVLSPNSKVIVLP 266
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 28-138 1.75e-61

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: 190.76  E-value: 1.75e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  28 RYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESL 107
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 559098453 108 NASIVDAINQAADCWGIRCLRYEIKDIHVPP 138
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 16-148 3.93e-34

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 122.00  E-value: 3.93e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453    16 GLNILIPVLDRIrYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVT-QLAQTTMRSELGK 94
Cdd:smart00244  27 GLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRVLDADYAVIeQLAQTTLRSVIGK 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 559098453    95 LSLDKVFR-ERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQV 148
Cdd:smart00244 106 RTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
Band_7_C pfam16200
C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal ...
 213-275 7.37e-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: 94.86  E-value: 7.37e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559098453  213 RILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTILLPSNPGDVTSMVAQAMGVYGALTK 275
Cdd:pfam16200   1 EKVAEAIKKPGGQEAVSLRVAEQYVEAFGKLAKESNTVILPANLGDVSSMVAQAMSIYKKVNK 63
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 16-254 5.69e-64

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 203.15  E-value: 5.69e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  16 GLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKL 95
Cdd:COG0330   45 GLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKM 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  96 SLDKVFRE-RESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEG 174
Cdd:COG0330  124 TLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEG 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453 175 KKQAQILASEAEKAEQINQAAGEasavlakakakAEAIRILAAALTqhngdaAASLTVAEQYVSAFSKLAKDSNTILLPS 254
Cdd:COG0330  204 EAQRAIIEAEAYREAQILRAEGE-----------AEAFRIVAEAYS------AAPFVLFYRSLEALEEVLSPNSKVIVLP 266
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 28-138 1.75e-61

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: 190.76  E-value: 1.75e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  28 RYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESL 107
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 559098453 108 NASIVDAINQAADCWGIRCLRYEIKDIHVPP 138
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 22-184 2.03e-45

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: 151.90  E-value: 2.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  22 PVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVF 101
Cdd:cd08826    1 PFIDRMVRV-DLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453 102 RERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEGkkqAQIL 181
Cdd:cd08826   80 SEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEA---AEIL 156


                 ...
gi 559098453 182 ASE 184
Cdd:cd08826  157 AKS 159
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 16-191 1.11e-34

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: 125.42  E-value: 1.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  16 GLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKL 95
Cdd:cd13437   30 GLHKVNPCTEKIIQV-DMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRIDNVKQALIERTQTTLRSVIGER 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  96 SLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAinvAEGK 175
Cdd:cd13437  109 TLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIGESKIISAKADVESA---KLMR 185

                        170
                 ....*....|....*.
gi 559098453 176 KQAQILASEAekAEQI 191
Cdd:cd13437  186 EAADILDSKA--AMQI 199
PHB smart00244
prohibitin homologues; prohibitin homologues
 16-148 3.93e-34

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 122.00  E-value: 3.93e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453    16 GLNILIPVLDRIrYVQSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVT-QLAQTTMRSELGK 94
Cdd:smart00244  27 GLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRVLDADYAVIeQLAQTTLRSVIGK 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 559098453    95 LSLDKVFR-ERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQV 148
Cdd:smart00244 106 RTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 6-191 3.79e-32

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: 118.64  E-value: 3.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453   6 ARGTGALLLrglnilIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQ 85
Cdd:cd13435    4 ARGPGVFFV------LPCIDNYCKV-DLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  86 TTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTR 165
Cdd:cd13435   77 TTLRNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEM 156

                        170       180
                 ....*....|....*....|....*.
gi 559098453 166 ESainvAEGKKQAQILASEAEKAEQI 191
Cdd:cd13435  157 KS----SRALKEASDIISASPSALQL 178
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 33-137 3.58e-31

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: 112.67  E-value: 3.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  33 LKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIV 112
Cdd:cd13434    3 LRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQ 82

                         90       100
                 ....*....|....*....|....*
gi 559098453 113 DAINQAADCWGIRCLRYEIKDIHVP 137
Cdd:cd13434   83 EILDEATDPWGIKVERVEIKDIILP 107
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 16-191 3.27e-28

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: 108.02  E-value: 3.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  16 GLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKL 95
Cdd:cd03403    8 GLFFILPCIDSYRKV-DLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGTK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  96 SLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTResaiNVAEGK 175
Cdd:cd03403   87 NLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQ----NASRAL 162

                        170
                 ....*....|....*.
gi 559098453 176 KQAQILASEAEKAEQI 191
Cdd:cd03403  163 KEAADVISESPAALQL 178
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 16-163 1.69e-27

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: 104.73  E-value: 1.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  16 GLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKL 95
Cdd:cd08828    4 GLILVLPCTDTFIKV-DLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGTQ 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 559098453  96 SLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEG 163
Cdd:cd08828   83 TLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEG 150
Band_7_C pfam16200
C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal ...
 213-275 7.37e-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: 94.86  E-value: 7.37e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559098453  213 RILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDSNTILLPSNPGDVTSMVAQAMGVYGALTK 275
Cdd:pfam16200   1 EKVAEAIKKPGGQEAVSLRVAEQYVEAFGKLAKESNTVILPANLGDVSSMVAQAMSIYKKVNK 63
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 16-163 1.26e-24

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: 97.78  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453   16 GLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIM--DPYKASYGVEDPEYA---VTQLAQTTMRS 90
Cdd:pfam01145  24 GLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLVQNVFGSDDLqelLRRVLESALRE 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 559098453   91 ELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEG 163
Cdd:pfam01145 103 IIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQTAEQEAEAEIARAEA 175
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 43-168 2.87e-22

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: 91.53  E-value: 2.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  43 QSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCW 122
Cdd:cd13775   13 EQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPW 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 559098453 123 GIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESA 168
Cdd:cd13775   93 GITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIA 138
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 1-165 7.59e-17

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: 78.01  E-value: 7.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453   1 MLARAARGTGalllrgLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAV 80
Cdd:cd08827   21 LLQGRARGPG------LFFYLPCLDVCHKV-DIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVCLSSFASISDAM 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  81 TQLAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLE 160
Cdd:cd08827   94 QALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAEAQRQAKVKVIA 173


                 ....*
gi 559098453 161 SEGTR 165
Cdd:cd08827  174 AEGEK 178
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 33-156 1.22e-16

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: 77.19  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  33 LKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASIV 112
Cdd:cd13438   40 LREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLL 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 559098453 113 DAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRA 156
Cdd:cd13438  120 AAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKRAQA 163
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 16-265 2.05e-16

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: 77.63  E-value: 2.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  16 GLNILIPVLDRIRYVQSLKEIVINVPEQSAvTLDNVTLQIDGVLYLRIMDP--YKASYGVEDPEYAVTQLAQTTMRSELG 93
Cdd:cd03407   23 GLHFIIPPIESVAGRVSLRVQQLDVRVETK-TKDNVFVTLVVSVQYRVVPEkvYDAFYKLTNPEQQIQSYVFDVVRASVP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  94 KLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLEsegtresainvAE 173
Cdd:cd03407  102 KLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRLREAAEEK-----------AE 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453 174 GKKQAQILASEAEKAEQINQAAGEASAVLAKAKAKAEAIRILAAALTQHNGDAAASLTVAEQYVSAFSKLAKDS--NTIL 251
Cdd:cd03407  171 AEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLRESIEDFQEAVPGVSSKEVMDLLLITQYFDTLKEVGKSSksSTVF 250

                        250
                 ....*....|....
gi 559098453 252 LPSNPGDVTSMVAQ 265
Cdd:cd03407  251 LPHGPGGVSDISAQ 264
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 54-197 3.38e-16

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: 76.78  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  54 QIDGVLYLRIMDPYKASYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRE-RESLNASIVDAINQAADCW--GIRCLRYE 130
Cdd:cd03404   83 DVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEILDRYdlGIEIVQVQ 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 559098453 131 IKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESAINVAEGKKQAQILASEAEKAEQINQAAGE 197
Cdd:cd03404  163 LQDADPPEEVQDAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGD 229
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 16-221 5.65e-15

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: 72.91  E-value: 5.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  16 GLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDP---YKAsygVEDPEYAVTQLAQ---TTMR 89
Cdd:cd03405   27 GLHFKLPFIQNVRKF-DKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPlrfYQS---VGGEEGAESRLDDivdSALR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  90 SELGKLSLDKVFR-ERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKRATVLESEGTRESA 168
Cdd:cd03405  103 NEIGKRTLAEVVSgGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESVYERMRAERERIAAEYRAEGEEEAE 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 559098453 169 INVAEGKKQAQILASEAE-KAEQI-NQAAGEAsavlakakakaeaIRILAAALTQ 221
Cdd:cd03405  183 KIRAEADRERTVILAEAYrEAEEIrGEGDAEA-------------ARIYAEAYGK 224
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 3-136 1.85e-11

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: 60.49  E-value: 1.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453   3 ARAARGTGalllrgLNILIPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKASYGVEDPEYAVTQ 82
Cdd:cd13436    3 LQKPRGPG------IVLILPCIDNFTRV-DMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRT 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 559098453  83 LAQTTMRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHV 136
Cdd:cd13436   76 TAQTSLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 37-138 1.96e-07

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: 48.51  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  37 VINVPEQSAVTLDNVTLQIDGVLYLRIMDPYKA-----SYGVEDPEYAVTQLAQTTMRSELGKLSLDKVFRERESLNASI 111
Cdd:cd02106    4 FDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAV 83

                         90       100
                 ....*....|....*....|....*..
gi 559098453 112 VDAINQAADCWGIRCLRYEIKDIHVPP 138
Cdd:cd02106   84 KEDLEEDLENFGVVISDVDITSIEPPD 110
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 21-134 3.12e-05

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: 43.26  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  21 IPVLDRIRYVqSLKEIVINVPEQSAVTLDNVTLQIDGVLYLRIM-DPYKASYGVE----DPEYAVTQLAQTTM----RSE 91
Cdd:cd03399    3 IPFLQRVQRL-SLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGsDPEEIAAAAErflgKSTEEIRELVKETLeghlRAI 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 559098453  92 LGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDI 134
Cdd:cd03399   82 VGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDI 124
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
7-218 4.45e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.32  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453   7 RGTGAlllrglnILIPVLDRIRYVqSLKEIVINV-PEQSAVTLDNVTLQIDGVLYLRIMDPYKA------SYGVEDPEyA 79
Cdd:COG2268   50 TGGGA-------FVLPVLHRAERM-SLSTMTIEVeRTEGLITKDGIRVDVDAVFYVKVNSDPEDianaaeRFLGRDPE-E 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  80 VTQLAQTT----MRSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKESMQMQVEAERRKR 155
Cdd:COG2268  121 IEELAEEKlegaLRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRD 200

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 559098453 156 ATVLESEGTRESAINVAEGKKQAQI--LASEAEKAE-QINQAAGEASAVLAKAKAKAEAIRILAAA 218
Cdd:COG2268  201 ARIAEAEAERETEIAIAQANREAEEaeLEQEREIETaRIAEAEAELAKKKAEERREAETARAEAEA 266
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 16-197 6.90e-03

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: 37.11  E-value: 6.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  16 GLNILIPVLDR-IRYVQSLKEIVINVpeqSAVTLDNVTLQID-GVLYlRImDPYKA-----SYGVEDPEYAVTQLAQTTM 88
Cdd:cd03401   27 GLHFKIPWIQVvIIYDVRTQPREITL---TVLSKDGQTVNIDlSVLY-RP-DPEKLpelyqNLGPDYEERVLPPIVREVL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 559098453  89 RSELGKLSLDKVFRERESLNASIVDAINQAADCWGIRCLRYEIKDIHVPPRVKEsmqmqveaerrkratvlesegtresA 168
Cdd:cd03401  102 KAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEK-------------------------A 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 559098453 169 InvaEGKKQAQILASEA----EKAEQ-----INQAAGE 197
Cdd:cd03401  157 I---EAKQVAEQEAERAkfelEKAEQeaerkVIEAEGE 191
 
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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