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Conserved domains on  [gi|1237881467|gb|PAJ75296|]
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paraslipin [Pseudoalteromonas sp. NBT06-2]

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 ...
 12-257 3.48e-73

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 227.42  E-value: 3.48e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  12 ILWITLVVLYTLKKGIYFVPQNRGYVIYTLGKYDKTLSAGLNFIIPFIQSVAaDRNLKEQSLDISSQSAITKDNISLELD 91
Cdd:COG0330     6 LLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVR-KVDVREQVLDVPPQEVLTKDNNIVDVD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  92 GILFMKVTDAAAATNNISDYKLSVTQLAMTTMRNAIGSMELDECF-QSRDTINATILSAMTEATAPWGVMVTRYEIRDIM 170
Cdd:COG0330    85 AVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDID 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 171 PPQSIREDMEKQMTAEREKRsviltaegvktAAITEAEGLKAARVLDAEASKAEQVLNAQADKEKQILEATGKAEAIRLV 250
Cdd:COG0330   165 PPEEVQDAMEDRMKAERERE-----------AAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIV 233


                  ....*..
gi 1237881467 251 ANAEAAA 257
Cdd:COG0330   234 AEAYSAA 240
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 12-257 3.48e-73

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 227.42  E-value: 3.48e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  12 ILWITLVVLYTLKKGIYFVPQNRGYVIYTLGKYDKTLSAGLNFIIPFIQSVAaDRNLKEQSLDISSQSAITKDNISLELD 91
Cdd:COG0330     6 LLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVR-KVDVREQVLDVPPQEVLTKDNNIVDVD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  92 GILFMKVTDAAAATNNISDYKLSVTQLAMTTMRNAIGSMELDECF-QSRDTINATILSAMTEATAPWGVMVTRYEIRDIM 170
Cdd:COG0330    85 AVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDID 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 171 PPQSIREDMEKQMTAEREKRsviltaegvktAAITEAEGLKAARVLDAEASKAEQVLNAQADKEKQILEATGKAEAIRLV 250
Cdd:COG0330   165 PPEEVQDAMEDRMKAERERE-----------AAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIV 233


                  ....*..
gi 1237881467 251 ANAEAAA 257
Cdd:COG0330   234 AEAYSAA 240
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 67-173 2.36e-54

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: 173.04  E-value: 2.36e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  67 NLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAATNNISDYKLSVTQLAMTTMRNAIGSMELDECFQSRDTINATI 146
Cdd:cd08829     5 DLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAKL 84

                          90       100
                  ....*....|....*....|....*..
gi 1237881467 147 LSAMTEATAPWGVMVTRYEIRDIMPPQ 173
Cdd:cd08829    85 LEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 25-183 2.97e-38

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 133.55  E-value: 2.97e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467   25 KGIYFVPQNRGYVIYTLGKYDKTLSAGLNFIIPFIQSVaaDR-NLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAA 103
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV--KKvDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  104 ATNNISDYK-LSVTQLAMTTMRNAIGSMELDECFQS-RDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDMEK 181
Cdd:smart00244  79 AVYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEA 158


                   ..
gi 1237881467  182 QM 183
Cdd:smart00244 159 QQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-198 1.81e-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: 1.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  30 VPQNRGYVIYTLGKYDKTLSAGLNFIIPFIQSVAADrNLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAAT---- 105
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKlvqn 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 106 -NNISDYKLSVTQLAMTTMRNAIGSMELDECFQSRDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDMEKQMT 184
Cdd:pfam01145  82 vFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQT 161

                         170
                  ....*....|....
gi 1237881467 185 AEREKRSVILTAEG 198
Cdd:pfam01145 162 AEQEAEAEIARAEA 175
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 27-235 1.31e-16

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: 78.21  E-value: 1.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  27 IYFV-PQNRGyVIYTLGKYDKTLSAGLNFIIPFIQSVAADRNLKEQSLDISSQsAITKDNISLELDGILFMKVTDAAAAT 105
Cdd:TIGR01933   1 IYTIgEAERG-VVLRFGKYHRTVDPGLNWKPPFIEEVYPVNVTAVRNLRKQGL-MLTGDENIVNVEMNVQYRITDPYKYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 106 NNISDYKLSVTQLAMTTMRNAIGSMELDECFQS-RDTINATILSAMTEATAPW--GVMVTRYEIRDIMPPQSIREDMEKQ 182
Cdd:TIGR01933  79 FSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDV 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1237881467 183 MTAEREKRSVILTAEGVKTAAITEAEGlKAARVL-DAEASKAEQVLNAQADKEK 235
Cdd:TIGR01933 159 IIAREDEERYINEAEAYANEVVPKARG-DAQRIIeEARGYKERRINRAKGDVAR 211
PRK11029 PRK11029
protease modulator HflC;
12-253 1.04e-05

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 46.66  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  12 ILWITLVVLYTlkkgIYFVPQ--NRGyVIYTLGKY-----DKTL--SAGLNFIIPFIQSVaadRNL--KEQSLDISSQSA 80
Cdd:PRK11029    8 IIIIVLVVLYM----SVFVVKegERG-IVLRFGKVlrdddNKPLvyAPGLHFKIPFIETV---KMLdaRIQTMDNQADRF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  81 ITKDNISLELDGILFMKVTD-----AAAATNNIS---------------------DYKLSVT----QLaMTTMRNAI--G 128
Cdd:PRK11029   80 VTKEKKDLIVDSYIKWRISDfsryyLATGGGDISqaevllkrkfsdrlrseigrlDVKDIVTdsrgRL-TLDVRDALnsG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 129 SMELDE---CFQSRDTINATILSAMTEAT-----------APWGVMVTRYEIRDIMPPQSIREDMEKQMTAEREKrsvil 194
Cdd:PRK11029  159 SAGTEDevaTPAADDAIASAAERVEAETKgkvpvinpnsmAALGIEVVDVRIKQINLPTEVSDAIYNRMRAEREA----- 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1237881467 195 TAEGVKTAAITEAEGLKAARvlDAEASKAEqvlnAQADKEKQILEATGKAEAIRLVANA 253
Cdd:PRK11029  234 VARRHRSQGQEEAEKLRATA--DYEVTRTL----AEAERQGRIMRGEGDAEAAKLFADA 286
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 12-257 3.48e-73

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 227.42  E-value: 3.48e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  12 ILWITLVVLYTLKKGIYFVPQNRGYVIYTLGKYDKTLSAGLNFIIPFIQSVAaDRNLKEQSLDISSQSAITKDNISLELD 91
Cdd:COG0330     6 LLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRVR-KVDVREQVLDVPPQEVLTKDNNIVDVD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  92 GILFMKVTDAAAATNNISDYKLSVTQLAMTTMRNAIGSMELDECF-QSRDTINATILSAMTEATAPWGVMVTRYEIRDIM 170
Cdd:COG0330    85 AVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDID 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 171 PPQSIREDMEKQMTAEREKRsviltaegvktAAITEAEGLKAARVLDAEASKAEQVLNAQADKEKQILEATGKAEAIRLV 250
Cdd:COG0330   165 PPEEVQDAMEDRMKAERERE-----------AAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIV 233


                  ....*..
gi 1237881467 251 ANAEAAA 257
Cdd:COG0330   234 AEAYSAA 240
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 67-173 2.36e-54

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: 173.04  E-value: 2.36e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  67 NLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAATNNISDYKLSVTQLAMTTMRNAIGSMELDECFQSRDTINATI 146
Cdd:cd08829     5 DLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAKL 84

                          90       100
                  ....*....|....*....|....*..
gi 1237881467 147 LSAMTEATAPWGVMVTRYEIRDIMPPQ 173
Cdd:cd08829    85 LEALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 57-219 7.91e-41

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: 140.73  E-value: 7.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  57 PFIQS-VAADrnLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAATNNISDYKLSVTQLAMTTMRNAIGSMELDEC 135
Cdd:cd08826     1 PFIDRmVRVD--LRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 136 FQSRDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDMEKQMTAEREKRSVILTAEGVKTAAITEAEglkAARV 215
Cdd:cd08826    79 LSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAE---AAEI 155


                  ....
gi 1237881467 216 LDAE 219
Cdd:cd08826   156 LAKS 159
PHB smart00244
prohibitin homologues; prohibitin homologues
 25-183 2.97e-38

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 133.55  E-value: 2.97e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467   25 KGIYFVPQNRGYVIYTLGKYDKTLSAGLNFIIPFIQSVaaDR-NLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAA 103
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV--KKvDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  104 ATNNISDYK-LSVTQLAMTTMRNAIGSMELDECFQS-RDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDMEK 181
Cdd:smart00244  79 AVYRVLDADyAVIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEA 158


                   ..
gi 1237881467  182 QM 183
Cdd:smart00244 159 QQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 30-198 1.81e-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: 1.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  30 VPQNRGYVIYTLGKYDKTLSAGLNFIIPFIQSVAADrNLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAAT---- 105
Cdd:pfam01145   3 VPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRVVTV-DVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKlvqn 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 106 -NNISDYKLSVTQLAMTTMRNAIGSMELDECFQSRDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDMEKQMT 184
Cdd:pfam01145  82 vFGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQT 161

                         170
                  ....*....|....
gi 1237881467 185 AEREKRSVILTAEG 198
Cdd:pfam01145 162 AEQEAEAEIARAEA 175
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 68-173 1.36e-30

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: 111.52  E-value: 1.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  68 LKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAATNNISDYKLSVTQLAMTTMRNAIGSMELDECFQSRDTINATIL 147
Cdd:cd13434     3 LRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQ 82

                          90       100
                  ....*....|....*....|....*.
gi 1237881467 148 SAMTEATAPWGVMVTRYEIRDIMPPQ 173
Cdd:cd13434    83 EILDEATDPWGIKVERVEIKDIILPQ 108
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 51-226 1.96e-29

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: 112.09  E-value: 1.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  51 GLNFIIPFIQSVAAdRNLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAATNNISDYKLSVTQLAMTTMRNAIGSM 130
Cdd:cd13435     8 GVFFVLPCIDNYCK-VDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGTR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 131 ELDECFQSRDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDMEKQMTAEREKRSVILTAEGVKTAaiteAEGL 210
Cdd:cd13435    87 NLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKS----SRAL 162

                         170
                  ....*....|....*.
gi 1237881467 211 KAARVLDAEASKAEQV 226
Cdd:cd13435   163 KEASDIISASPSALQL 178
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 30-220 1.18e-27

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: 107.31  E-value: 1.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  30 VPQnrGYV--IYTLGKYDKTLSAGLNFIIPF---IQSVaadrNLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAA 104
Cdd:cd13437     9 VKQ--GSVglVERFGKFYKTVDPGLHKVNPCtekIIQV----DMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 105 TNNISDYKLSVTQLAMTTMRNAIGSMELDECFQSRDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDMEKQMT 184
Cdd:cd13437    83 IYRIDNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAK 162

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1237881467 185 AEREKRSVILTAEG-VKTAAITEaeglKAARVLDAEA 220
Cdd:cd13437   163 AKRIGESKIISAKAdVESAKLMR----EAADILDSKA 195
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 51-226 3.06e-27

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: 105.71  E-value: 3.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  51 GLNFIIPFIQSVAaDRNLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAATNNISDYKLSVTQLAMTTMRNAIGSM 130
Cdd:cd03403     8 GLFFILPCIDSYR-KVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGTK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 131 ELDECFQSRDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDMEKQMTAEREKRSVILTAEGVKTAaiteAEGL 210
Cdd:cd03403    87 NLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNA----SRAL 162

                         170
                  ....*....|....*.
gi 1237881467 211 KAARVLDAEASKAEQV 226
Cdd:cd03403   163 KEAADVISESPAALQL 178
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 71-197 5.56e-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: 101.55  E-value: 5.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  71 QSLDISSQSAITKDNISLELDGILFMKVTDAAAATNNISDYKLSVTQLAMTTMRNAIGSMELDECFQSRDTINATILSAM 150
Cdd:cd13775     6 RTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDII 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1237881467 151 TEATAPWGVMVTRYEIRDIMPPQSIREDMEKQMTAEREKRSVILTAE 197
Cdd:cd13775    86 DEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAE 132
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 15-247 1.22e-25

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: 103.36  E-value: 1.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  15 ITLVVLYTLKkGIYFV-PQNRGyVIYTLGKYDKTLSAGLNFIIPFIQSVAADRNLKE-QSLDISSQSA-----ITKD-NI 86
Cdd:cd03404     4 LLLLLVWLLS-GFYTVdPGERG-VVLRFGKYVRTVGPGLHWKLPFPIEVVEKVNVTQvRSVEIGFRVPeeslmLTGDeNI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  87 sLELDGILFMKVTDAAAATNNISDYKLSVTQLAMTTMRNAIGSMELDECFQS-RDTINATILSAMTEATAPW--GVMVTR 163
Cdd:cd03404    82 -VDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEILDRYdlGIEIVQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 164 YEIRDIMPPQSIREDMEKQMTAEREKRSVILTAEGVKTAAITEAEGLKAARVLDAEASKAEQVLNAQADKEK--QILEAT 241
Cdd:cd03404   161 VQLQDADPPEEVQDAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGDAARflALLAEY 240


                  ....*.
gi 1237881467 242 GKAEAI 247
Cdd:cd03404   241 RKAPEV 246
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 42-218 6.50e-24

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: 97.22  E-value: 6.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  42 GKYDKTLSAGLNFIIPFIQSVAADR-NLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAATNNISDYKLSVTQLAM 120
Cdd:cd13438    13 GKLVRTLEPGRYAFWKFGRKVQVELvDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETVDDPEEQLYLALQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 121 TTMRNAIGSMELDECFQSRDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDMEKQMTAEREKRSVILTAEGvK 200
Cdd:cd13438    93 LALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKRAQANLIRARE-E 171

                         170
                  ....*....|....*...
gi 1237881467 201 TAAiTEAEgLKAARVLDA 218
Cdd:cd13438   172 TAA-TRSL-LNAAKLMEE 187
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 51-198 2.31e-21

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: 88.94  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  51 GLNFIIPFIqSVAADRNLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAATNNISDYKLSVTQLAMTTMRNAIGSM 130
Cdd:cd08828     4 GLILVLPCT-DTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGTQ 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237881467 131 ELDECFQSRDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDMEKQMTAEREKRSVILTAEG 198
Cdd:cd08828    83 TLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEG 150
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 27-253 2.47e-21

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: 91.01  E-value: 2.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  27 IYFVPQNRGYVIYTLGKYDKTLS-AGLNFIIPFIQSVAA-DRNLkeQSLDISSQSAITKDNISLELDGILFMKVTDAAA- 103
Cdd:cd03405     2 VFIVDETEQAVVLQFGKPVRVITePGLHFKLPFIQNVRKfDKRI--LTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRf 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 104 --ATNNISDYKLSVTQLAMTTMRNAIGSMELDECFQS-RDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDME 180
Cdd:cd03405    80 yqSVGGEEGAESRLDDIVDSALRNEIGKRTLAEVVSGgRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESVY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237881467 181 KQMTAEREKRsviltaegvktAAITEAEGLKAARVLDAEASKAEQVLNAQADKEKQILEATGKAEAIRLVANA 253
Cdd:cd03405   160 ERMRAERERI-----------AAEYRAEGEEEAEKIRAEADRERTVILAEAYREAEEIRGEGDAEAARIYAEA 221
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 30-252 1.34e-20

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: 89.57  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  30 VPQNRGYVIYTLGKYDKTLSAGLNFIIPFIQSVAADRNLKEQSLDISSQSAiTKDNISLELDGILFMKVTDAAAATnniS 109
Cdd:cd03407     2 VSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDVRVETK-TKDNVFVTLVVSVQYRVVPEKVYD---A 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 110 DYKLSVTQLAMT-----TMRNAIGSMELDECFQSRDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDMEKqmt 184
Cdd:cd03407    78 FYKLTNPEQQIQsyvfdVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNE--- 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237881467 185 aerekrsviltaegvktaaITEAEGLKAARVLDAEASKAEQVLNAQADKEKQILEATGKAEAIRLVAN 252
Cdd:cd03407   155 -------------------INAAQRLREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGIAEQRKAIVD 203
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 27-235 1.31e-16

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: 78.21  E-value: 1.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  27 IYFV-PQNRGyVIYTLGKYDKTLSAGLNFIIPFIQSVAADRNLKEQSLDISSQsAITKDNISLELDGILFMKVTDAAAAT 105
Cdd:TIGR01933   1 IYTIgEAERG-VVLRFGKYHRTVDPGLNWKPPFIEEVYPVNVTAVRNLRKQGL-MLTGDENIVNVEMNVQYRITDPYKYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 106 NNISDYKLSVTQLAMTTMRNAIGSMELDECFQS-RDTINATILSAMTEATAPW--GVMVTRYEIRDIMPPQSIREDMEKQ 182
Cdd:TIGR01933  79 FSVENPEDSLRQATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDV 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1237881467 183 MTAEREKRSVILTAEGVKTAAITEAEGlKAARVL-DAEASKAEQVLNAQADKEK 235
Cdd:TIGR01933 159 IIAREDEERYINEAEAYANEVVPKARG-DAQRIIeEARGYKERRINRAKGDVAR 211
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 27-246 2.97e-14

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: 70.23  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  27 IYFVPQ-NRGyVIYTLGKY--DKTLSAGLNFIIPFIQSVAaDRNLKEQSLDISSqSAITKDNISLELDGILFMKVTDAAA 103
Cdd:cd03401     1 FYTVDAgEVG-VVFRRGKGvkDEVLGEGLHFKIPWIQVVI-IYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRPDPEKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 104 AT--NNI-SDYKLSV-TQLAMTTMRNAIGSMELDECFQSRDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDM 179
Cdd:cd03401    78 PElyQNLgPDYEERVlPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237881467 180 EKQMTAERekrsviltaegvktaaiteaeglkaarvldaEASKAEQVLN-AQADKEKQILEATGKAEA 246
Cdd:cd03401   158 EAKQVAEQ-------------------------------EAERAKFELEkAEQEAERKVIEAEGEAEA 194
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 37-213 4.94e-14

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: 70.30  E-value: 4.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  37 VIYTLGKY--DKTLSAGLNFIIPFIqSVAADRNLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAATNNISDYKLS 114
Cdd:cd08827    14 VIFRLGHLlqGRARGPGLFFYLPCL-DVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVCLSSFASISDA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 115 VTQLAMTTMRNAIGSMELDECFQSRDTINATILSAMTEATAPWGVMVTRYEIRDIMPPQSIREDMEKQMTAEREKRSVIL 194
Cdd:cd08827    93 MQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAEAQRQAKVKVI 172

                         170
                  ....*....|....*....
gi 1237881467 195 TAEGVKTAaiteAEGLKAA 213
Cdd:cd08827   173 AAEGEKAA----SEALKAA 187
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 42-168 1.79e-10

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: 57.79  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  42 GKYDKTLSAGLNFIIPFI---QSVaadrNLKEQSLDISSQSAITKDNISLELDGILFMKVTDAAAATNNISDYKLSVTQL 118
Cdd:cd13436     1 GRLQKPRGPGIVLILPCIdnfTRV----DMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTT 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1237881467 119 AMTTMRNAIGSMELDECFQSRDTINATILSAMTEATAPWGVMVTRYEIRD 168
Cdd:cd13436    77 AQTSLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSD 126
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 70-173 2.63e-10

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: 56.99  E-value: 2.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  70 EQSLDISSQSAITKDNISLELDGILFMKVTDAAAA-----TNNISDYKLSVTQLAMTTMRNAIGSMELDECFQSRDTINA 144
Cdd:cd02106     2 PQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAK 81

                          90       100
                  ....*....|....*....|....*....
gi 1237881467 145 TILSAMTEATAPWGVMVTRYEIRDIMPPQ 173
Cdd:cd02106    82 AVKEDLEEDLENFGVVISDVDITSIEPPD 110
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1-257 2.90e-10

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 61.04  E-value: 2.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467   1 METFIPLLASPILWITLVVLY-TLKKGIYFVPQNRGYVIYTLGKYDKTLSAGLNFIIPFIQSVaaDR-NLKEQSLDIS-S 77
Cdd:COG2268     1 METLGILIIIGVIVVVLLLLLiILARFYRKVPPNEALVITGRGGGYKVVTGGGAFVLPVLHRA--ERmSLSTMTIEVErT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  78 QSAITKDNISLELDGILFMKVTD-----AAAATNNISDYKLSVTQLAMTT----MRNAIGSMELDECFQSRDTINATILS 148
Cdd:COG2268    79 EGLITKDGIRVDVDAVFYVKVNSdpediANAAERFLGRDPEEIEELAEEKlegaLRAVAAQMTVEELNEDREKFAEKVQE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 149 AMTEATAPWGVMVTRYEIRDIMPPQSIREDMEKQMTAEREKRSVILTAEGVKTAAITEAEGLKAARvlDAEASKAEQVLN 228
Cdd:COG2268   159 VAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAE--EAELEQEREIET 236

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1237881467 229 ---AQADKEKQILEATGKAEAIRLVANAEAAA 257
Cdd:COG2268   237 ariAEAEAELAKKKAEERREAETARAEAEAAY 268
PRK11029 PRK11029
protease modulator HflC;
12-253 1.04e-05

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 46.66  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  12 ILWITLVVLYTlkkgIYFVPQ--NRGyVIYTLGKY-----DKTL--SAGLNFIIPFIQSVaadRNL--KEQSLDISSQSA 80
Cdd:PRK11029    8 IIIIVLVVLYM----SVFVVKegERG-IVLRFGKVlrdddNKPLvyAPGLHFKIPFIETV---KMLdaRIQTMDNQADRF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  81 ITKDNISLELDGILFMKVTD-----AAAATNNIS---------------------DYKLSVT----QLaMTTMRNAI--G 128
Cdd:PRK11029   80 VTKEKKDLIVDSYIKWRISDfsryyLATGGGDISqaevllkrkfsdrlrseigrlDVKDIVTdsrgRL-TLDVRDALnsG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 129 SMELDE---CFQSRDTINATILSAMTEAT-----------APWGVMVTRYEIRDIMPPQSIREDMEKQMTAEREKrsvil 194
Cdd:PRK11029  159 SAGTEDevaTPAADDAIASAAERVEAETKgkvpvinpnsmAALGIEVVDVRIKQINLPTEVSDAIYNRMRAEREA----- 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1237881467 195 TAEGVKTAAITEAEGLKAARvlDAEASKAEqvlnAQADKEKQILEATGKAEAIRLVANA 253
Cdd:PRK11029  234 VARRHRSQGQEEAEKLRATA--DYEVTRTL----AEAERQGRIMRGEGDAEAAKLFADA 286
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 54-141 1.62e-05

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


Pssm-ID: 259798 [Multi-domain]  Cd Length: 145  Bit Score: 44.03  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  54 FIIPFIQSVaaDR-NLKEQSLDISSQSAITKDNISLELDGILFMKVTD-----AAAATNNISDYKLSVTQLAMTTM---- 123
Cdd:cd03399     1 FVIPFLQRV--QRlSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSdpeeiAAAAERFLGKSTEEIRELVKETLeghl 78

                          90
                  ....*....|....*...
gi 1237881467 124 RNAIGSMELDECFQSRDT 141
Cdd:cd03399    79 RAIVGTMTVEEIYQDREK 96
PRK10930 PRK10930
FtsH protease activity modulator HflK;
21-232 1.74e-03

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 39.81  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467  21 YTLKKGiyfvpqNRGyVIYTLGKYDKTLSAGLNFIIPFIQSVAAdRNLKEQSLDISSQSAITKDNISLELDGILFMKVTD 100
Cdd:PRK10930   98 YTIKEA------ERG-VVTRFGKFSHLVEPGLNWKPTFIDEVKP-VNVEAVRELAASGVMLTSDENVVRVEMNVQYRVTD 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881467 101 AAAATNNISDYKLSVTQLAMTTMRNAIGSMELDECF-QSRDTINATILSAMTEATAPWGVMVTRYEI--RDIMPPQSIRE 177
Cdd:PRK10930  170 PEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILtEGRTVIRSDTQRELEETIRPYDMGITLLDVnfQAARPPEEVKA 249

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1237881467 178 DMEKQMTAEREKRSVILTAEGVKTAAITEAEGlKAARVL-DAEASKAEQVLNAQAD 232
Cdd:PRK10930  250 AFDDAIAARENEQQYIREAEAYTNEVQPRANG-QAQRILeEARAYKAQTILEAQGE 304
 
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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