NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1572047573|ref|NP_001355386|]
View 

Band 7 domain-containing protein [Caenorhabditis elegans]

Protein Classification

SPFH domain-containing protein( domain architecture ID 10362500)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
SPFH_like super family cl19107
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
146-263 4.59e-63

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


The actual alignment was detected with superfamily member cd13436:

Pssm-ID: 473137 [Multi-domain]  Cd Length: 131  Bit Score: 199.93  E-value: 4.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 146 GRAQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVCGVQDRNASVRTLANTM 225
Cdd:cd13436     1 GRLQKPRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1572047573 226 LYRYISKKRICD-------------DELGSFTCQFGVEITDVEISDVKIVK 263
Cdd:cd13436    81 LTNSLSKKTVREiqsdrrkineelkDELNKMTTAWGLEVTRVELSDVKVLK 131
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
357-439 2.60e-16

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


:

Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 74.17  E-value: 2.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 357 IGRVFQINCKDIEPI--CIDLKHGSGSAYKGTSLNPDVVFETSLEVFGKILTKEVSPVTVYMNGNLKVKGSIQDAMQLKH 434
Cdd:COG3255    20 WDGVVQFVITGEGGGayYLVIDDGKCTVSEGDDDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLAMKLMS 99

                  ....*
gi 1572047573 435 LVERM 439
Cdd:COG3255   100 LFKAL 104
 
Name Accession Description Interval E-value
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
146-263 4.59e-63

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: 199.93  E-value: 4.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 146 GRAQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVCGVQDRNASVRTLANTM 225
Cdd:cd13436     1 GRLQKPRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1572047573 226 LYRYISKKRICD-------------DELGSFTCQFGVEITDVEISDVKIVK 263
Cdd:cd13436    81 LTNSLSKKTVREiqsdrrkineelkDELNKMTTAWGLEVTRVELSDVKVLK 131
PHB smart00244
prohibitin homologues; prohibitin homologues
129-264 1.51e-31

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 118.15  E-value: 1.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573  129 FALKFISTSEKLVVLRLGRAQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAV 208
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAV 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1572047573  209 CGVQD-RNASVRTLANTMLYRYISKKRICD--------------DELGSFTCQFGVEITDVEISDVKIVKE 264
Cdd:smart00244  81 YRVLDaDYAVIEQLAQTTLRSVIGKRTLDElltdqrekisenirEELNEAAEAWGIKVEDVEIKDIRLPEE 151
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
109-259 5.32e-20

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 89.51  E-value: 5.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 109 LLIFCVSFLFVVMTmplsLLFALKFISTSEKLVVLRLGRAQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDR 188
Cdd:COG0330     3 LILLLILLVLVLVL----LFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 189 GLVELGATVFLKIRDPIAAVCGVQDRNASVRTLANTMLYRYISKKRICD--------------DELGSFTCQFGVEITDV 254
Cdd:COG0330    79 NIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEvlstgrdeinaeirEELQEALDPYGIEVVDV 158

                  ....*
gi 1572047573 255 EISDV 259
Cdd:COG0330   159 EIKDI 163
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
357-439 2.60e-16

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 74.17  E-value: 2.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 357 IGRVFQINCKDIEPI--CIDLKHGSGSAYKGTSLNPDVVFETSLEVFGKILTKEVSPVTVYMNGNLKVKGSIQDAMQLKH 434
Cdd:COG3255    20 WDGVVQFVITGEGGGayYLVIDDGKCTVSEGDDDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLAMKLMS 99

                  ....*
gi 1572047573 435 LVERM 439
Cdd:COG3255   100 LFKAL 104
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
338-437 9.03e-16

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 72.67  E-value: 9.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 338 IDHLISVASLAMDEhLVRLIGRVFQINCKDIE-PICIDLKHGSGSAYKGTSLNPDVVFETSLEVFGKILTKEVSPVTVYM 416
Cdd:pfam02036   1 LNQLLARDPAAREL-LKKLNGKVIRFDLTDLGlSLTLDLKDGGGRVLAGDEGKADVTLSASDSDLLALATGKLNPQKAFM 79
                          90       100
                  ....*....|....*....|.
gi 1572047573 417 NGNLKVKGSIQDAMQLKHLVE 437
Cdd:pfam02036  80 QGKLKIEGDMELAQKLEGLLK 100
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
134-264 1.81e-12

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: 65.42  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 134 ISTSEKLVVLRLGRAQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKI--RDP---IAAV 208
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPpklVQNV 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1572047573 209 CGVQDRNASVRTLANTMLYRYISKKRICD-------------DELGSFTCQFGVEITDVEISDVKIVKE 264
Cdd:pfam01145  83 FGSDDLQELLRRVLESALREIIARYTLEEllsnreelaeeikNALQEELAKYGVEIIDVQITDIDPPPE 151
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
134-242 3.45e-07

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: 51.25  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 134 ISTSEKLVVLRLGRAQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVCGVQD 213
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPYKYLFSVEN 83
                          90       100
                  ....*....|....*....|....*....
gi 1572047573 214 RNASVRTLANTMLYRYISKKRIcDDELGS 242
Cdd:TIGR01933  84 PEDSLRQATDSALRGVIGDSTM-DDILTE 111
 
Name Accession Description Interval E-value
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
146-263 4.59e-63

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: 199.93  E-value: 4.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 146 GRAQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVCGVQDRNASVRTLANTM 225
Cdd:cd13436     1 GRLQKPRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1572047573 226 LYRYISKKRICD-------------DELGSFTCQFGVEITDVEISDVKIVK 263
Cdd:cd13436    81 LTNSLSKKTVREiqsdrrkineelkDELNKMTTAWGLEVTRVELSDVKVLK 131
PHB smart00244
prohibitin homologues; prohibitin homologues
129-264 1.51e-31

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 118.15  E-value: 1.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573  129 FALKFISTSEKLVVLRLGRAQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAV 208
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAV 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1572047573  209 CGVQD-RNASVRTLANTMLYRYISKKRICD--------------DELGSFTCQFGVEITDVEISDVKIVKE 264
Cdd:smart00244  81 YRVLDaDYAVIEQLAQTTLRSVIGKRTLDElltdqrekisenirEELNEAAEAWGIKVEDVEIKDIRLPEE 151
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
152-324 2.72e-20

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: 88.59  E-value: 2.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 152 RGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVCGVQDRNASVRTLANTMLYRYIS 231
Cdd:cd13435     5 RGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 232 KKR----ICDDELGSFTCQ---------FGVEITDVEISDVKIvKEGENMGMSALSSVAKsdagqqlwqvigpvfEDFAK 298
Cdd:cd13435    85 TRNlselLTERETISHSMQvtldeatdpWGVQVERVEIKDVSL-PDSLQRAMAAEAEAAR---------------EARAK 148
                         170       180
                  ....*....|....*....|....*.
gi 1572047573 299 ECAAEEKAKENAPLVDLSDVPSTSAA 324
Cdd:cd13435   149 VIAAEGEMKSSRALKEASDIISASPS 174
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
109-259 5.32e-20

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 89.51  E-value: 5.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 109 LLIFCVSFLFVVMTmplsLLFALKFISTSEKLVVLRLGRAQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDR 188
Cdd:COG0330     3 LILLLILLVLVLVL----LFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 189 GLVELGATVFLKIRDPIAAVCGVQDRNASVRTLANTMLYRYISKKRICD--------------DELGSFTCQFGVEITDV 254
Cdd:COG0330    79 NIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEvlstgrdeinaeirEELQEALDPYGIEVVDV 158

                  ....*
gi 1572047573 255 EISDV 259
Cdd:COG0330   159 EIKDI 163
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
152-324 1.96e-18

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: 83.37  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 152 RGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVCGVQDRNASVRTLANTMLYRYIS 231
Cdd:cd03403     5 KGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 232 KKR----ICDDELGSFTCQ---------FGVEITDVEISDVKIVKEGENmGMSALSSVAKsdagqqlwqvigpvfEDFAK 298
Cdd:cd03403    85 TKNlseiLSDRETISHQMQstldeatdpWGVKVERVEIKDVRLPVQLQR-AMAAEAEAAR---------------EARAK 148
                         170       180
                  ....*....|....*....|....*.
gi 1572047573 299 ECAAEEKAKENAPLVDLSDVPSTSAA 324
Cdd:cd03403   149 VIAAEGEQNASRALKEAADVISESPA 174
SCP2 COG3255
Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];
357-439 2.60e-16

Putative sterol carrier protein, contains SCP2 domain [Lipid transport and metabolism];


Pssm-ID: 442486 [Multi-domain]  Cd Length: 104  Bit Score: 74.17  E-value: 2.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 357 IGRVFQINCKDIEPI--CIDLKHGSGSAYKGTSLNPDVVFETSLEVFGKILTKEVSPVTVYMNGNLKVKGSIQDAMQLKH 434
Cdd:COG3255    20 WDGVVQFVITGEGGGayYLVIDDGKCTVSEGDDDDADVTLTASYEDWKKLLTGELDPMTAFMTGKLKVEGDMGLAMKLMS 99

                  ....*
gi 1572047573 435 LVERM 439
Cdd:COG3255   100 LFKAL 104
SCP2 pfam02036
SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the ...
338-437 9.03e-16

SCP-2 sterol transfer family; This domain is involved in binding sterols. It is found in the SCP2 protein as well as the C terminus of the enzyme estradiol 17 beta-dehydrogenase EC:1.1.1.62. The UNC-24 protein contains an SPFH domain pfam01145.


Pssm-ID: 460423 [Multi-domain]  Cd Length: 100  Bit Score: 72.67  E-value: 9.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 338 IDHLISVASLAMDEhLVRLIGRVFQINCKDIE-PICIDLKHGSGSAYKGTSLNPDVVFETSLEVFGKILTKEVSPVTVYM 416
Cdd:pfam02036   1 LNQLLARDPAAREL-LKKLNGKVIRFDLTDLGlSLTLDLKDGGGRVLAGDEGKADVTLSASDSDLLALATGKLNPQKAFM 79
                          90       100
                  ....*....|....*....|.
gi 1572047573 417 NGNLKVKGSIQDAMQLKHLVE 437
Cdd:pfam02036  80 QGKLKIEGDMELAQKLEGLLK 100
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
129-264 1.23e-15

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: 75.69  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 129 FALKFISTSEKLVVLRLGR--AQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIA 206
Cdd:cd08827     2 FCVKVVREYERAVIFRLGHllQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASV 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1572047573 207 AVCGVQDRNASVRTLANTMLYRYIS----------KKRICDD---ELGSFTCQFGVEITDVEISDVKIVKE 264
Cdd:cd08827    82 CLSSFASISDAMQALVQTTVKRLLAhraftdilleRKSIAQEikvALDSGTCRWGIKVERAEIKDVNLPPE 152
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
152-261 2.73e-15

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: 73.14  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 152 RGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVCGVQDRNASVRTLANTMLYRYIS 231
Cdd:cd08828     1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1572047573 232 KKRICD-----DE--------LGSFTCQFGVEITDVEISDVKI 261
Cdd:cd08828    81 TQTLAQilagrEEiahsiqsiLDHATEKWGIKVARVEIKDVRI 123
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
175-261 9.11e-14

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: 67.22  E-value: 9.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 175 AFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVCGVQDRNASVRTLANTMLYRYISKKRICD-------------DELG 241
Cdd:cd13434     7 SVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDEllsereeisqqlqEILD 86
                          90       100
                  ....*....|....*....|
gi 1572047573 242 SFTCQFGVEITDVEISDVKI 261
Cdd:cd13434    87 EATDPWGIKVERVEIKDIIL 106
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
134-264 1.81e-12

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: 65.42  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 134 ISTSEKLVVLRLGRAQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKI--RDP---IAAV 208
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPpklVQNV 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1572047573 209 CGVQDRNASVRTLANTMLYRYISKKRICD-------------DELGSFTCQFGVEITDVEISDVKIVKE 264
Cdd:pfam01145  83 FGSDDLQELLRRVLESALREIIARYTLEEllsnreelaeeikNALQEELAKYGVEIIDVQITDIDPPPE 151
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
134-279 1.50e-11

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: 63.79  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 134 ISTSEKLVVLRLGRAQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVCGVQD 213
Cdd:cd13437     9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRIDN 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1572047573 214 RNASVRTLANTMLYRYISKKRICD---------DELGSF----TCQFGVEITDVEISDVKIVKEgenmGMSALSSVAKS 279
Cdd:cd13437    89 VKQALIERTQTTLRSVIGERTLQDllekreeiaDEIEEIveevAKEWGVYVESILIKDIVLSKD----LQQSLSSAAKA 163
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
166-261 4.22e-10

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: 56.71  E-value: 4.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 166 THKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVCGVQDRNASVRTLANTMLyRYISKKRICDD------- 238
Cdd:cd08829     1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTL-RSEIGKMELDEtlssree 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1572047573 239 -------ELGSFTCQFGVEITDVEISDVKI 261
Cdd:cd08829    80 inaklleALDEATDPWGVKVTRVEIKDITP 109
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
161-268 6.62e-10

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: 57.91  E-value: 6.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 161 PCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVCGVQDRNASVRTLANTMLyR------------ 228
Cdd:cd08826     1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTL-Rsvvgqveldell 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1572047573 229 ----YISKK--RICDDElgsfTCQFGVEITDVEISDVKIvkeGENM 268
Cdd:cd08826    80 sereEINKRiqEIIDEQ----TEPWGIKVTAVEIKDVDL---PESM 118
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
127-259 7.10e-10

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: 59.45  E-value: 7.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 127 LLFALKFISTSEKLVVLRLGRAQKTRGPGITLVIPCIDTTHKV-------TMSITAFNVPPLQIITTDRGLVELGATVFL 199
Cdd:cd03404    11 LLSGFYTVDPGERGVVLRFGKYVRTVGPGLHWKLPFPIEVVEKvnvtqvrSVEIGFRVPEESLMLTGDENIVDVDFVVQY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 200 KIRDPIAAVCGVQDRNASVRTLANTMLYRYISKKRICD---------------------DELGSftcqfGVEITDVEISD 258
Cdd:cd03404    91 RISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDvltegraeiaadvrellqeilDRYDL-----GIEIVQVQLQD 165

                  .
gi 1572047573 259 V 259
Cdd:cd03404   166 A 166
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
134-242 3.45e-07

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: 51.25  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 134 ISTSEKLVVLRLGRAQKTRGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVCGVQD 213
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPYKYLFSVEN 83
                          90       100
                  ....*....|....*....|....*....
gi 1572047573 214 RNASVRTLANTMLYRYISKKRIcDDELGS 242
Cdd:TIGR01933  84 PEDSLRQATDSALRGVIGDSTM-DDILTE 111
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
138-256 9.91e-07

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: 49.79  E-value: 9.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 138 EKLVVLRLGRAQKT-RGPGITLVIPCIDTTHKVTMSITAFNVPPLQIITTDRGLVELGATVFLKIRDP------IAAVCG 210
Cdd:cd03405     9 EQAVVLQFGKPVRViTEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPlrfyqsVGGEEG 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1572047573 211 VQDR-----NASVRT-LANTMLYRYISKKR--ICDD---ELGSFTCQFGVEITDVEI 256
Cdd:cd03405    89 AESRlddivDSALRNeIGKRTLAEVVSGGRdeLMEEileQANEEAKEYGIEVVDVRI 145
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
182-280 2.52e-04

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: 41.84  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 182 QIITTDRGLVELGATVFLKIRDPIAAVCGVQDRNASVRTLANTMLYRYISKKRICD-------------DELGSFTCQFG 248
Cdd:cd13775    14 QTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAEllsrreqideelqDIIDEKTTPWG 93
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1572047573 249 VEITDVEISDVKIVKEGENmgmsALSSVAKSD 280
Cdd:cd13775    94 ITVQSVEIRDIIIPKELQD----AMSREAQAE 121
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
138-259 2.68e-03

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: 39.06  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572047573 138 EKLVVLRLGRAQKTRGPGI--------TLVIPCIDTTHKVtmsitaFNVPPLQIITTDRGLVELGATVFLKIRDPIAAVC 209
Cdd:cd13438     5 ERGLLYRDGKLVRTLEPGRyafwkfgrKVQVELVDLREQL------LEVSGQEILTADKVALRVNLVATYRVVDPVKAVE 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1572047573 210 GVQDRNASVRTLANTMLYRYISKKRI-----CDDELGSF--------TCQFGVEITDVEISDV 259
Cdd:cd13438    79 TVDDPEEQLYLALQLALREAVAARTLdelleDREDLSEFllaavkeaAAELGVEVLSVGVKDI 141
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH