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Conserved domains on  [gi|392886723|ref|NP_001251106|]
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Stomatin-like protein stl-1 [Caenorhabditis elegans]

Protein Classification

SPFH domain-containing protein( domain architecture ID 11417211)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein similar to Homo sapiens mitochondrial stomatin-like protein 2, and Escherichia coli protein QmcA

CATH:  3.30.479.30
Gene Ontology:  GO:0016020
PubMed:  16101677|17766116|10542406|21501885|24782879
TCDB:  8.A.21

Graphical summary

 Zoom to residue level

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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 ...
 41-298 4.64e-71

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 221.64  E-value: 4.64e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  41 VPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVD 120
Cdd:COG0330   24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 121 DPEFAVTQLAQTTMRSEVGKINLDTVFKE-RELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVEAERK 199
Cdd:COG0330  103 NAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAERE 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 200 KRAAILESEGIREAAINRAEGDKKSAILaseavqaerinVAKGEAEAVILKAESRAKAIERIALALEKdgganaAGLTVA 279
Cdd:COG0330  183 REAAILEAEGYREAAIIRAEGEAQRAII-----------EAEAYREAQILRAEGEAEAFRIVAEAYSA------APFVLF 245

                        250
                 ....*....|....*....
gi 392886723 280 EQYVGAFGNLAKESNTVVL 298
Cdd:COG0330  246 YRSLEALEEVLSPNSKVIV 264
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 41-298 4.64e-71

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 221.64  E-value: 4.64e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  41 VPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVD 120
Cdd:COG0330   24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 121 DPEFAVTQLAQTTMRSEVGKINLDTVFKE-RELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVEAERK 199
Cdd:COG0330  103 NAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAERE 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 200 KRAAILESEGIREAAINRAEGDKKSAILaseavqaerinVAKGEAEAVILKAESRAKAIERIALALEKdgganaAGLTVA 279
Cdd:COG0330  183 REAAILEAEGYREAAIIRAEGEAQRAII-----------EAEAYREAQILRAEGEAEAFRIVAEAYSA------APFVLF 245

                        250
                 ....*....|....*....
gi 392886723 280 EQYVGAFGNLAKESNTVVL 298
Cdd:COG0330  246 YRSLEALEEVLSPNSKVIV 264
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 75-184 1.29e-55

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: 176.13  E-value: 1.29e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  75 FVQNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVDDPEFAVTQLAQTTMRSEVGKINLDTVFKERELLN 154
Cdd:cd08829    2 YKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEIN 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 392886723 155 ENIVFAINKASAPWGIQCMRYEIRDMQMPS 184
Cdd:cd08829   82 AKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 38-194 1.81e-49

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 162.44  E-value: 1.81e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723    38 INFVPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASY 117
Cdd:smart00244   3 IKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKV-DLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVY 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392886723   118 GVDDPEFAVT-QLAQTTMRSEVGKINLDTVF-KERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQV 194
Cdd:smart00244  82 RVLDADYAVIeQLAQTTLRSVIGKRTLDELLtDQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 41-209 1.42e-31

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: 116.27  E-value: 1.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723   41 VPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRV--FDPYKASYG 118
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLVQN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  119 VDDPEFA---VTQLAQTTMRSEVGKINLDTVFKERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVE 195
Cdd:pfam01145  82 VFGSDDLqelLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQT 161

                         170
                  ....*....|....
gi 392886723  196 AERKKRAAILESEG 209
Cdd:pfam01145 162 AEQEAEAEIARAEA 175
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 41-266 4.56e-22

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: 93.24  E-value: 4.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723   41 VPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKFVqNLREIAiEIPEQGA-ITIDNVQLRLDGVLYLRVFDPYKASYGV 119
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPV-NVTAVR-NLRKQGLmLTGDENIVNVEMNVQYRITDPYKYLFSV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  120 DDPEFAVTQLAQTTMRSEVGKINLDTVFKE-RELLNENIVFAINKASAPW--GIQCMRYEIRDMQMPSKIQEAMQMQVEA 196
Cdd:TIGR01933  82 ENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDVIIA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392886723  197 ERKKRAAILESEGIREAAINRAEGDKKSAILASEAVQAERINVAKGEAE--AVILKAESRAKAIERIALALE 266
Cdd:TIGR01933 162 REDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGDVArfTKLLAEYKKAPDVTRERLYLE 233
PRK10930 PRK10930
FtsH protease activity modulator HflK;
41-266 1.08e-08

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 55.99  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  41 VPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKF--VQNLREIAieipEQGA-ITIDNVQLRLDGVLYLRVFDPYKASY 117
Cdd:PRK10930 100 IKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPvnVEAVRELA----ASGVmLTSDENVVRVEMNVQYRVTDPEKYLF 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 118 GVDDPEFAVTQLAQTTMRSEVGKINLDTVFKE-RELLNENIVFAINKASAPW--GIQCMRYEIRDMQMPSKIQEAMQMQV 194
Cdd:PRK10930 176 SVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYdmGITLLDVNFQAARPPEEVKAAFDDAI 255

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392886723 195 EAERKKRAAILESEGIREAAINRAEGDKKSAILASEAVQAERINVAKGEAE--AVILKAESRAKAIERIALALE 266
Cdd:PRK10930 256 AARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGEVArfAKLLPEYKAAPEITRERLYIE 329
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 41-298 4.64e-71

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 221.64  E-value: 4.64e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  41 VPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVD 120
Cdd:COG0330   24 VPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVRKV-DVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 121 DPEFAVTQLAQTTMRSEVGKINLDTVFKE-RELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVEAERK 199
Cdd:COG0330  103 NAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAERE 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 200 KRAAILESEGIREAAINRAEGDKKSAILaseavqaerinVAKGEAEAVILKAESRAKAIERIALALEKdgganaAGLTVA 279
Cdd:COG0330  183 REAAILEAEGYREAAIIRAEGEAQRAII-----------EAEAYREAQILRAEGEAEAFRIVAEAYSA------APFVLF 245

                        250
                 ....*....|....*....
gi 392886723 280 EQYVGAFGNLAKESNTVVL 298
Cdd:COG0330  246 YRSLEALEEVLSPNSKVIV 264
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 75-184 1.29e-55

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: 176.13  E-value: 1.29e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  75 FVQNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVDDPEFAVTQLAQTTMRSEVGKINLDTVFKERELLN 154
Cdd:cd08829    2 YKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEIN 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 392886723 155 ENIVFAINKASAPWGIQCMRYEIRDMQMPS 184
Cdd:cd08829   82 AKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 38-194 1.81e-49

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 162.44  E-value: 1.81e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723    38 INFVPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASY 117
Cdd:smart00244   3 IKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDVKKV-DLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVY 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392886723   118 GVDDPEFAVT-QLAQTTMRSEVGKINLDTVF-KERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQV 194
Cdd:smart00244  82 RVLDADYAVIeQLAQTTLRSVIGKRTLDELLtDQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 68-230 7.10e-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: 151.13  E-value: 7.10e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  68 PIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVDDPEFAVTQLAQTTMRSEVGKINLDTVF 147
Cdd:cd08826    1 PFIDRMVRV-DLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 148 KERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVEAERKKRAAILESEGIREAAINRAEGdkkSAIL 227
Cdd:cd08826   80 SEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEA---AEIL 156


                 ...
gi 392886723 228 ASE 230
Cdd:cd08826  157 AKS 159
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 41-231 3.31e-40

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: 140.44  E-value: 3.31e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  41 VPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVD 120
Cdd:cd13437    9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKIIQV-DMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 121 DPEFAVTQLAQTTMRSEVGKINLDTVFKERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVEAERkk 200
Cdd:cd13437   88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKR-- 165

                        170       180       190
                 ....*....|....*....|....*....|.
gi 392886723 201 raailesegIREAAINRAEGDKKSAILASEA 231
Cdd:cd13437  166 ---------IGESKIISAKADVESAKLMREA 187
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 61-231 1.73e-34

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: 125.19  E-value: 1.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  61 PGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVDDPEFAVTQLAQTTMRSEVGK 140
Cdd:cd13435    7 PGVFFVLPCIDNYCKV-DLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 141 INLDTVFKERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVEAERKKRAAILEsegireaainrAEG 220
Cdd:cd13435   86 RNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIA-----------AEG 154

                        170
                 ....*....|.
gi 392886723 221 DKKSAILASEA 231
Cdd:cd13435  155 EMKSSRALKEA 165
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 41-209 1.42e-31

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: 116.27  E-value: 1.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723   41 VPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRV--FDPYKASYG 118
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLVQN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  119 VDDPEFA---VTQLAQTTMRSEVGKINLDTVFKERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVE 195
Cdd:pfam01145  82 VFGSDDLqelLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQT 161

                         170
                  ....*....|....
gi 392886723  196 AERKKRAAILESEG 209
Cdd:pfam01145 162 AEQEAEAEIARAEA 175
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 61-231 1.32e-29

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: 111.87  E-value: 1.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  61 PGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVDDPEFAVTQLAQTTMRSEVGK 140
Cdd:cd03403    7 PGLFFILPCIDSYRKV-DLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 141 INLDTVFKERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVEAERKKRAAILESEGIREAAinRAEG 220
Cdd:cd03403   86 KNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNAS--RALK 163

                        170
                 ....*....|.
gi 392886723 221 DKKSAILASEA 231
Cdd:cd03403  164 EAADVISESPA 174
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 61-209 2.25e-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: 2.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  61 PGLNFLLPIIDKikFVQ-NLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVDDPEFAVTQLAQTTMRSEVG 139
Cdd:cd08828    3 PGLILVLPCTDT--FIKvDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 140 KINLDTVFKERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVEAERKKRAAILESEG 209
Cdd:cd08828   81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEG 150
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 41-308 9.63e-27

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: 106.13  E-value: 9.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  41 VPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKFVQNLREIAIEIPEQgAITIDNVQLRLDGVLYLRVFDP--YKASYG 118
Cdd:cd03407    2 VSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDVRVE-TKTKDNVFVTLVVSVQYRVVPEkvYDAFYK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 119 VDDPEFAVTQLAQTTMRSEVGKINLDTVFKERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVEAER 198
Cdd:cd03407   81 LTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 199 KKRAAILESEGIREAAINRAEGDKKSAILASEAVQAERINVAKGEAEAVilkaESRAKAIERIalalekdGGANAAGLTV 278
Cdd:cd03407  161 LREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVDGLRESI----EDFQEAVPGV-------SSKEVMDLLL 229

                        250       260       270
                 ....*....|....*....|....*....|..
gi 392886723 279 AEQYVGAFGNLAK--ESNTVVLPanlSDPGSM 308
Cdd:cd03407  230 ITQYFDTLKEVGKssKSSTVFLP---HGPGGV 258
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 79-214 2.06e-26

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: 102.70  E-value: 2.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  79 LREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVDDPEFAVTQLAQTTMRSEVGKINLDTVFKERELLNENIV 158
Cdd:cd13775    3 QRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQ 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 392886723 159 FAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVEAERKKRAAILESEGIREAA 214
Cdd:cd13775   83 DIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIA 138
Band_7_C pfam16200
C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal ...
 259-321 7.06e-26

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: 97.55  E-value: 7.06e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392886723  259 ERIALALEKDGGANAAGLTVAEQYVGAFGNLAKESNTVVLPANLSDPGSMVSQALAVYDSLSN 321
Cdd:pfam16200   1 EKVAEAIKKPGGQEAVSLRVAEQYVEAFGKLAKESNTVILPANLGDVSSMVAQAMSIYKKVNK 63
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 79-183 8.91e-26

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: 98.80  E-value: 8.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  79 LREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVDDPEFAVTQLAQTTMRSEVGKINLDTVFKERELLNENIV 158
Cdd:cd13434    3 LRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQ 82

                         90       100
                 ....*....|....*....|....*
gi 392886723 159 FAINKASAPWGIQCMRYEIRDMQMP 183
Cdd:cd13434   83 EILDEATDPWGIKVERVEIKDIILP 107
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 41-266 1.19e-22

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: 94.89  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  41 VPQQEAWVVERMGKFYKILEPGLNFLLP-IIDKIKFVQ----NLREIAIEIPEQGA-ITID----NVQLRldgVLYlRVF 110
Cdd:cd03404   18 VDPGERGVVLRFGKYVRTVGPGLHWKLPfPIEVVEKVNvtqvRSVEIGFRVPEESLmLTGDenivDVDFV---VQY-RIS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 111 DPYKASYGVDDPEFAVTQLAQTTMRSEVGKINLDTVFKE-RELLNENIVFAINKASAPW--GIQCMRYEIRDMQMPSKIQ 187
Cdd:cd03404   94 DPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEILDRYdlGIEIVQVQLQDADPPEEVQ 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 188 EAMQMQVEAERKKRAAILESEGIREAAINRAEGDKKSAILASEAVQAERINVAKGEAE--AVILKAESRAKAIERIALAL 265
Cdd:cd03404  174 DAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGDAArfLALLAEYRKAPEVTRERLYL 253


                 .
gi 392886723 266 E 266
Cdd:cd03404  254 E 254
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 41-266 4.56e-22

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: 93.24  E-value: 4.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723   41 VPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKFVqNLREIAiEIPEQGA-ITIDNVQLRLDGVLYLRVFDPYKASYGV 119
Cdd:TIGR01933   4 IGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEVYPV-NVTAVR-NLRKQGLmLTGDENIVNVEMNVQYRITDPYKYLFSV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  120 DDPEFAVTQLAQTTMRSEVGKINLDTVFKE-RELLNENIVFAINKASAPW--GIQCMRYEIRDMQMPSKIQEAMQMQVEA 196
Cdd:TIGR01933  82 ENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDVIIA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392886723  197 ERKKRAAILESEGIREAAINRAEGDKKSAILASEAVQAERINVAKGEAE--AVILKAESRAKAIERIALALE 266
Cdd:TIGR01933 162 REDEERYINEAEAYANEVVPKARGDAQRIIEEARGYKERRINRAKGDVArfTKLLAEYKKAPDVTRERLYLE 233
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 41-204 1.21e-19

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: 85.66  E-value: 1.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  41 VPQQEAWVVERMGKFYKILEPGLN-FLLPIIDKIKFVQNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGV 119
Cdd:cd13438    1 VPPGERGLLYRDGKLVRTLEPGRYaFWKFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 120 DDPEFAVTQLAQTTMRSEVGKINLDTVFKERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVEAERK 199
Cdd:cd13438   81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKR 160


                 ....*
gi 392886723 200 KRAAI 204
Cdd:cd13438  161 AQANL 165
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 41-268 4.87e-17

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: 79.07  E-value: 4.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  41 VPQQEAWVVERMGKFYK-ILEPGLNFLLPIIDKIKFVQNlREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDP---YKAs 116
Cdd:cd03405    5 VDETEQAVVLQFGKPVRvITEPGLHFKLPFIQNVRKFDK-RILTLDGPPEEVLTKDKKRLIVDSYARWRITDPlrfYQS- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 117 ygVDDPEFAVTQLAQ---TTMRSEVGKINL-DTVFKERELLNENIVFAINKASAPWGIqcmryEIRDMQM-----PSKIQ 187
Cdd:cd03405   83 --VGGEEGAESRLDDivdSALRNEIGKRTLaEVVSGGRDELMEEILEQANEEAKEYGI-----EVVDVRIkridlPEEVS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 188 EAMQMQVEAERKkraailesegiREAAINRAEGDKKSAILASEAVQAERINVAKGEAEAVILKAESRAKAIERIALALEK 267
Cdd:cd03405  156 ESVYERMRAERE-----------RIAAEYRAEGEEEAEKIRAEADRERTVILAEAYREAEEIRGEGDAEAARIYAEAYGK 224


                 .
gi 392886723 268 D 268
Cdd:cd03405  225 D 225
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 38-214 1.48e-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: 74.54  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  38 INFVPQQEAWVVERMGKFY--KILEPGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKA 115
Cdd:cd08827    4 VKVVREYERAVIFRLGHLLqgRARGPGLFFYLPCLDVCHKV-DIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 116 SYGVDDPEFAVTQLAQTTMRSEVGKINLDTVFKERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQMQVE 195
Cdd:cd08827   83 LSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                        170
                 ....*....|....*....
gi 392886723 196 AERKKRAAILESEGIREAA 214
Cdd:cd08827  163 AQRQAKVKVIAAEGEKAAS 181
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 53-181 2.48e-14

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: 68.58  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  53 GKFYKILEPGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKASYGVDDPEFAVTQLAQT 132
Cdd:cd13436    1 GRLQKPRGPGIVLILPCIDNFTRV-DMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 392886723 133 TMRSEVGKINLDTVFKERELLNENIVFAINKASAPWGIQCMRYEIRDMQ 181
Cdd:cd13436   80 SLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVK 128
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 41-225 1.49e-11

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: 62.53  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  41 VPQQEAWVVERMGKF--YKILEPGLNFLLPIIDKIKFVqNLREIAIEIPEQgAITIDNVQLRLD-GVLYlRVfDPYKA-- 115
Cdd:cd03401    4 VDAGEVGVVFRRGKGvkDEVLGEGLHFKIPWIQVVIIY-DVRTQPREITLT-VLSKDGQTVNIDlSVLY-RP-DPEKLpe 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 116 ---SYGVDDPEFAVTQLAQTTMRSEVGKINLDTVFKERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEAMQM 192
Cdd:cd03401   80 lyqNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEA 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 392886723 193 ----QVEAERKK-RAAILESEgiREAAINRAEGDKKSA 225
Cdd:cd03401  160 kqvaEQEAERAKfELEKAEQE--AERKVIEAEGEAEAQ 195
PRK10930 PRK10930
FtsH protease activity modulator HflK;
41-266 1.08e-08

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 55.99  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  41 VPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKF--VQNLREIAieipEQGA-ITIDNVQLRLDGVLYLRVFDPYKASY 117
Cdd:PRK10930 100 IKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEVKPvnVEAVRELA----ASGVmLTSDENVVRVEMNVQYRVTDPEKYLF 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 118 GVDDPEFAVTQLAQTTMRSEVGKINLDTVFKE-RELLNENIVFAINKASAPW--GIQCMRYEIRDMQMPSKIQEAMQMQV 194
Cdd:PRK10930 176 SVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYdmGITLLDVNFQAARPPEEVKAAFDDAI 255

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392886723 195 EAERKKRAAILESEGIREAAINRAEGDKKSAILASEAVQAERINVAKGEAE--AVILKAESRAKAIERIALALE 266
Cdd:PRK10930 256 AARENEQQYIREAEAYTNEVQPRANGQAQRILEEARAYKAQTILEAQGEVArfAKLLPEYKAAPEITRERLYIE 329
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
41-257 1.01e-07

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 52.95  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  41 VPQQEAWVVERMGKFYKILEPGLNFLLPIIDKIKFVqNLREIAIEI-PEQGAITIDNVQLRLDGVLYLRVFDPYKA---- 115
Cdd:COG2268   31 VPPNEALVITGRGGGYKVVTGGGAFVLPVLHRAERM-SLSTMTIEVeRTEGLITKDGIRVDVDAVFYVKVNSDPEDiana 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 116 --SYGVDDPEfAVTQLAQTT----MRSEVGKINLDTVFKERELLNENIVFAINKASAPWGIQCMRYEIRDMQMPSKIQEA 189
Cdd:COG2268  110 aeRFLGRDPE-EIEELAEEKlegaLRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDA 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392886723 190 MQMQVEAERKKRAAILESEGIREAAINRAEGDKKSAILASEAVQA-ERINVAKGEAEAVILKAESRAKA 257
Cdd:COG2268  189 LGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREiETARIAEAEAELAKKKAEERREA 257
PRK11029 PRK11029
protease modulator HflC;
40-253 1.82e-05

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 45.89  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  40 FVPQQ-EAWVVERMGKFYK-------ILEPGLNFLLPIIDKIKFVqNLREIAIEIPEQGAITIDNVQLRLDGVLYLRVFD 111
Cdd:PRK11029  21 FVVKEgERGIVLRFGKVLRdddnkplVYAPGLHFKIPFIETVKML-DARIQTMDNQADRFVTKEKKDLIVDSYIKWRISD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 112 ---PYKASYG--VDDPEFAVTQLAQTTMRSEVGKINL-DTVFKERELLNENIVFAINKAS-------------------- 165
Cdd:PRK11029 100 fsrYYLATGGgdISQAEVLLKRKFSDRLRSEIGRLDVkDIVTDSRGRLTLDVRDALNSGSagtedevatpaaddaiasaa 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723 166 -------------------APWGIQCMRYEIRDMQMPSKIQEAMQMQVEAERKKRAAILESEGIREAAINRAEGDKKSAI 226
Cdd:PRK11029 180 erveaetkgkvpvinpnsmAALGIEVVDVRIKQINLPTEVSDAIYNRMRAEREAVARRHRSQGQEEAEKLRATADYEVTR 259

                        250       260
                 ....*....|....*....|....*..
gi 392886723 227 LASEAVQAERINVAKGEAEAVILKAES 253
Cdd:PRK11029 260 TLAEAERQGRIMRGEGDAEAAKLFADA 286
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 80-183 6.24e-05

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: 41.58  E-value: 6.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886723  80 REIAIEIPEQGAITIDNVQLRLDGVLYLRVFDPYKA-----SYGVDDPEFAVTQLAQTTMRSEVGKINLDTVFKERELLN 154
Cdd:cd02106    1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                         90       100
                 ....*....|....*....|....*....
gi 392886723 155 ENIVFAINKASAPWGIQCMRYEIRDMQMP 183
Cdd:cd02106   81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
 
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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