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Conserved domains on  [gi|1992576671|gb|QRY97853|]
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SPFH/Band 7/PHB domain protein [Sphingomonas paucimobilis]

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 ...
 19-290 5.85e-85

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 257.46  E-value: 5.85e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  19 MSIKIVRQGYQYTIEHFGRYTGTAVPGFNFYPAFFYRVgRRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKA 98
Cdd:COG0330    19 SSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  99 AYEVSDLYVALLNLVTTNLRTVMGSMDLDETLS-KRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQM 177
Cdd:COG0330    98 LYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRM 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 178 KAEREKRANILEAEGSRASEILRAEGQKQARILEAEGRRESAFRdsearerAAEAEAKATRVVSDAIaqggtQAINYFVA 257
Cdd:COG0330   178 KAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQIL-------RAEGEAEAFRIVAEAY-----SAAPFVLF 245

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1992576671 258 QKYVEAVGKFAtSPNAKTILFPVEATQLIGTLG 290
Cdd:COG0330   246 YRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLL 277
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 19-290 5.85e-85

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 257.46  E-value: 5.85e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  19 MSIKIVRQGYQYTIEHFGRYTGTAVPGFNFYPAFFYRVgRRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKA 98
Cdd:COG0330    19 SSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  99 AYEVSDLYVALLNLVTTNLRTVMGSMDLDETLS-KRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQM 177
Cdd:COG0330    98 LYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRM 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 178 KAEREKRANILEAEGSRASEILRAEGQKQARILEAEGRRESAFRdsearerAAEAEAKATRVVSDAIaqggtQAINYFVA 257
Cdd:COG0330   178 KAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQIL-------RAEGEAEAFRIVAEAY-----SAAPFVLF 245

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1992576671 258 QKYVEAVGKFAtSPNAKTILFPVEATQLIGTLG 290
Cdd:COG0330   246 YRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLL 277
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 59-166 2.45e-58

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: 183.44  E-value: 2.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  59 RVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKAAYEVSDLYVALLNLVTTNLRTVMGSMDLDETLSKRDEINA 138
Cdd:cd08829     3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                          90       100
                  ....*....|....*....|....*...
gi 1992576671 139 RLLNVVDHATTPWGVKITRVEIKDIRPP 166
Cdd:cd08829    83 KLLEALDEATDPWGVKVTRVEIKDITPP 110
PHB smart00244
prohibitin homologues; prohibitin homologues
 19-177 4.24e-39

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 135.48  E-value: 4.24e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671   19 MSIKIVRQGYQYTIEHFGRYTGTAVPGFNFYPAFFYRVgRRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKA 98
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671   99 AYEVSDL-YVALLNLVTTNLRTVMGSMDLDETLS-KRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQ 176
Cdd:smart00244  80 VYRVLDAdYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159


                   .
gi 1992576671  177 M 177
Cdd:smart00244 160 Q 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 22-192 2.98e-32

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: 118.19  E-value: 2.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  22 KIVRQGYQYTIEHFGRYTGTAVPGFNFYPAFFYRVgRRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVL--DAPKAA 99
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 100 YEV--SDLYVALL-NLVTTNLRTVMGSMDLDETLSKRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQ 176
Cdd:pfam01145  80 QNVfgSDDLQELLrRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*.
gi 1992576671 177 MKAEREKRANILEAEG 192
Cdd:pfam01145 160 QTAEQEAEAEIARAEA 175
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 35-218 3.05e-11

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: 62.80  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  35 FGRYTGTAVPGFNFYPAFFYRVgRRVNMmEQVIDIPGQ-EIITKDNAMISTDGVVFFQVLDAPKAAYEVSDLYVALLNLV 113
Cdd:TIGR01933  15 FGKYHRTVDPGLNWKPPFIEEV-YPVNV-TAVRNLRKQgLMLTGDENIVNVEMNVQYRITDPYKYLFSVENPEDSLRQAT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 114 TTNLRTVMGSMDLDETLSK-----RDEINARLLNVVDHATTpwGVKITRVEIKDIRPPVDIVNAMARQMKAEREKRANIL 188
Cdd:TIGR01933  93 DSALRGVIGDSTMDDILTEgrsqiREDTKERLNEIIDNYDL--GITVTDVNFQSARPPEEVKEAFDDVIIAREDEERYIN 170

                         170       180       190
                  ....*....|....*....|....*....|
gi 1992576671 189 EAEGSRASEILRAEGQKQARILEAEGRRES 218
Cdd:TIGR01933 171 EAEAYANEVVPKARGDAQRIIEEARGYKER 200
PRK11029 PRK11029
protease modulator HflC;
128-219 8.98e-07

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 49.74  E-value: 8.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 128 ETLSKRDEINARLLNVVdhattpwGVKITRVEIKDIRPPVDIVNAMARQMKAEREKRANILEAEGSRASEILRA------ 201
Cdd:PRK11029  185 ETKGKVPVINPNSMAAL-------GIEVVDVRIKQINLPTEVSDAIYNRMRAEREAVARRHRSQGQEEAEKLRAtadyev 257

                          90       100
                  ....*....|....*....|...
gi 1992576671 202 -----EGQKQARILEAEGRRESA 219
Cdd:PRK11029  258 trtlaEAERQGRIMRGEGDAEAA 280
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 19-290 5.85e-85

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 257.46  E-value: 5.85e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  19 MSIKIVRQGYQYTIEHFGRYTGTAVPGFNFYPAFFYRVgRRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKA 98
Cdd:COG0330    19 SSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  99 AYEVSDLYVALLNLVTTNLRTVMGSMDLDETLS-KRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQM 177
Cdd:COG0330    98 LYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRM 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 178 KAEREKRANILEAEGSRASEILRAEGQKQARILEAEGRRESAFRdsearerAAEAEAKATRVVSDAIaqggtQAINYFVA 257
Cdd:COG0330   178 KAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQIL-------RAEGEAEAFRIVAEAY-----SAAPFVLF 245

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1992576671 258 QKYVEAVGKFAtSPNAKTILFPVEATQLIGTLG 290
Cdd:COG0330   246 YRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLL 277
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 59-166 2.45e-58

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: 183.44  E-value: 2.45e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  59 RVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKAAYEVSDLYVALLNLVTTNLRTVMGSMDLDETLSKRDEINA 138
Cdd:cd08829     3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                          90       100
                  ....*....|....*....|....*...
gi 1992576671 139 RLLNVVDHATTPWGVKITRVEIKDIRPP 166
Cdd:cd08829    83 KLLEALDEATDPWGVKVTRVEIKDITPP 110
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 58-213 2.10e-52

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: 170.39  E-value: 2.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  58 RRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKAAYEVSDLYVALLNLVTTNLRTVMGSMDLDETLSKRDEIN 137
Cdd:cd08826     7 VRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLSEREEIN 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1992576671 138 ARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQMKAEREKRANILEAEGSR-ASEILRAegqkQARILEAE 213
Cdd:cd08826    87 KRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELqAAEKLAE----AAEILAKS 159
PHB smart00244
prohibitin homologues; prohibitin homologues
 19-177 4.24e-39

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 135.48  E-value: 4.24e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671   19 MSIKIVRQGYQYTIEHFGRYTGTAVPGFNFYPAFFYRVgRRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKA 98
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671   99 AYEVSDL-YVALLNLVTTNLRTVMGSMDLDETLS-KRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQ 176
Cdd:smart00244  80 VYRVLDAdYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159


                   .
gi 1992576671  177 M 177
Cdd:smart00244 160 Q 160
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 24-212 3.85e-38

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: 135.05  E-value: 3.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  24 VRQGYQYTIEHFGRYTGTAVPGFNFYPAFFYRVgRRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKAAYEVS 103
Cdd:cd13437     9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKI-IQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 104 DLYVALLNLVTTNLRTVMGSMDLDETLSKRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQMKAEREK 183
Cdd:cd13437    88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIG 167

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1992576671 184 RANILEAEGS--------RASEILRAEGQKQARILEA 212
Cdd:cd13437   168 ESKIISAKADvesaklmrEAADILDSKAAMQIRYLET 204
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 60-166 2.89e-37

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: 128.85  E-value: 2.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  60 VNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKAAYEVSDLYVALLNLVTTNLRTVMGSMDLDETLSKRDEINAR 139
Cdd:cd13434     1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                          90       100
                  ....*....|....*....|....*..
gi 1992576671 140 LLNVVDHATTPWGVKITRVEIKDIRPP 166
Cdd:cd13434    81 LQEILDEATDPWGIKVERVEIKDIILP 107
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 58-200 1.30e-34

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: 125.36  E-value: 1.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  58 RRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKAAYEVSDLYVALLNLVTTNLRTVMGSMDLDETLSKRDEIN 137
Cdd:cd03403    20 RKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGTKNLSEILSDRETIS 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1992576671 138 ARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQMKAEREKRANILEAEGS-RASEILR 200
Cdd:cd03403   100 HQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEqNASRALK 163
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 58-196 4.91e-33

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: 121.34  E-value: 4.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  58 RRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKAAYEVSDLYVALLNLVTTNLRTVMGSMDLDETLSKRDEIN 137
Cdd:cd13435    20 CKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGTRNLSELLTERETIS 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1992576671 138 ARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQMKAEREKRANILEAEGSRAS 196
Cdd:cd13435   100 HSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKS 158
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 59-192 1.74e-32

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: 118.21  E-value: 1.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  59 RVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKAAYEVSDLYVALLNLVTTNLRTVMGSMDLDETLSKRDEINA 138
Cdd:cd08828    17 KVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGTQTLAQILAGREEIAH 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1992576671 139 RLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQMKAEREKRANILEAEG 192
Cdd:cd08828    97 SIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEG 150
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 22-192 2.98e-32

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: 118.19  E-value: 2.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  22 KIVRQGYQYTIEHFGRYTGTAVPGFNFYPAFFYRVgRRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVL--DAPKAA 99
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNpdDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 100 YEV--SDLYVALL-NLVTTNLRTVMGSMDLDETLSKRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQ 176
Cdd:pfam01145  80 QNVfgSDDLQELLrRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*.
gi 1992576671 177 MKAEREKRANILEAEG 192
Cdd:pfam01145 160 QTAEQEAEAEIARAEA 175
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 60-191 1.51e-28

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: 108.48  E-value: 1.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  60 VNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKAAYEVSDLYVALLNLVTTNLRTVMGSMDLDETLSKRDEINAR 139
Cdd:cd13775     1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1992576671 140 LLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQMKAEREKRANILEAE 191
Cdd:cd13775    81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAE 132
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 18-217 5.63e-26

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: 104.13  E-value: 5.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  18 MMSIKIVRQGYQYTIEHFGRYTGTAVPGFNFYPAFFYRVGRRVNMME-QVIDIPGQ-----EIITKDNAMISTDGVVFFQ 91
Cdd:cd03404    12 LSGFYTVDPGERGVVLRFGKYVRTVGPGLHWKLPFPIEVVEKVNVTQvRSVEIGFRvpeesLMLTGDENIVDVDFVVQYR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  92 VLDAPKAAYEVSDLYVALLNLVTTNLRTVMGSMDLDETLS-KRDEINARLL----NVVDHATTpwGVKITRVEIKDIRPP 166
Cdd:cd03404    92 ISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRellqEILDRYDL--GIEIVQVQLQDADPP 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1992576671 167 VDIVNAMARQMKAEREKRANILEAEGSRASEILRAEGQKQARILEAEGRRE 217
Cdd:cd03404   170 EEVQDAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKA 220
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 20-219 5.89e-23

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: 95.25  E-value: 5.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  20 SIKIVRQGYQYTIEHFGRYTGTAV-PGFNFYPAFFYRVgRRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKA 98
Cdd:cd03405     1 SVFIVDETEQAVVLQFGKPVRVITePGLHFKLPFIQNV-RKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  99 AYEVSDLYVA---LLNLVTTNLRTVMGSMDLDETLS-KRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMA 174
Cdd:cd03405    80 YQSVGGEEGAesrLDDIVDSALRNEIGKRTLAEVVSgGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESVY 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1992576671 175 RQMKAEREKRANILEAEGSRASEILRAEGQKQARILEAEGRRESA 219
Cdd:cd03405   160 ERMRAERERIAAEYRAEGEEEAEKIRAEADRERTVILAEAYREAE 204
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 36-190 6.88e-23

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: 94.52  E-value: 6.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  36 GRYTGTAVPGFNFYPAFFYRVGR-RVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKAAYEVSDLYVALLNLVT 114
Cdd:cd13438    13 GKLVRTLEPGRYAFWKFGRKVQVeLVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETVDDPEEQLYLALQ 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1992576671 115 TNLRTVMGSMDLDETLSKRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQMKAEREKRANILEA 190
Cdd:cd13438    93 LALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKRAQANLIRA 168
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 23-279 2.17e-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: 88.80  E-value: 2.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  23 IVRQGYQYTIEHFGRYTGTAVPGFNFYPAFFYRVGRRVNMMEQVIDIPgQEIITKDNAMISTDGVVFFQVLD--APKAAY 100
Cdd:cd03407     1 CVSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDVR-VETKTKDNVFVTLVVSVQYRVVPekVYDAFY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 101 EVSDLYVALLNLVTTNLRTVMGSMDLDETLSKRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQMKAE 180
Cdd:cd03407    80 KLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 181 REKRANILEAEGSRASEILRAEGQKQARILEAEG----RRESA--FRDSEARERAAeaeakatrvVSDAIAQggtQAINY 254
Cdd:cd03407   160 RLREAAEEKAEAEKILQVKAAEAEAEAKRLQGVGiaeqRKAIVdgLRESIEDFQEA---------VPGVSSK---EVMDL 227

                         250       260
                  ....*....|....*....|....*
gi 1992576671 255 FVAQKYVEAVGKFATSPNAKTILFP 279
Cdd:cd03407   228 LLITQYFDTLKEVGKSSKSSTVFLP 252
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 21-205 1.45e-18

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: 83.01  E-value: 1.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  21 IKIVRQGYQYTIEHFGR-YTGTAV-PGFNFYPAFFyRVGRRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKA 98
Cdd:cd08827     4 VKVVREYERAVIFRLGHlLQGRARgPGLFFYLPCL-DVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  99 AYEVSDLYVALLNLVTTNLRTVMGSMDLDETLSKRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQMK 178
Cdd:cd08827    83 LSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                         170       180
                  ....*....|....*....|....*...
gi 1992576671 179 AEREKRANILEAEGSR-ASEILRAEGQK 205
Cdd:cd08827   163 AQRQAKVKVIAAEGEKaASEALKAAAES 190
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 64-166 1.22e-15

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: 71.63  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  64 EQVIDIPGQEIITKDNAMISTDGVVFFQVLDaPKAAYEVSDLYV------ALLNLVTTNLRTVMGSMDLDETLSKRDEIN 137
Cdd:cd02106     2 PQFDDVRVEPVGTADGVPVAVDLVVQFRITD-YNALPAFYLVDFvkdikaDIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                          90       100
                  ....*....|....*....|....*....
gi 1992576671 138 ARLLNVVDHATTPWGVKITRVEIKDIRPP 166
Cdd:cd02106    81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 59-164 5.28e-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: 67.81  E-value: 5.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  59 RVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPKAAYEVSDLYVALLNLVTTNLRTVMGSMDLDETLSKRDEINA 138
Cdd:cd13436    23 RVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTSLTNSLSKKTVREIQSDRRKINE 102

                          90       100
                  ....*....|....*....|....*.
gi 1992576671 139 RLLNVVDHATTPWGVKITRVEIKDIR 164
Cdd:cd13436   103 ELKDELNKMTTAWGLEVTRVELSDVK 128
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 21-219 4.36e-13

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: 66.77  E-value: 4.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  21 IKIVRQGYQYTIEHFGRYTGTAV--PGFNFYPAFFYRVgRRVNMMEQVIDIPgQEIITKDNAMISTDGVVFFQVlDAPKA 98
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKDEVlgEGLHFKIPWIQVV-IIYDVRTQPREIT-LTVLSKDGQTVNIDLSVLYRP-DPEKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  99 AY---EVSDLYVA--LLNLVTTNLRTVMGSMDLDETLSKRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAM 173
Cdd:cd03401    78 PElyqNLGPDYEErvLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1992576671 174 ARQMKAERE-KRANIleaegsrasEILRAEGQKQARILEAEGRRESA 219
Cdd:cd03401   158 EAKQVAEQEaERAKF---------ELEKAEQEAERKVIEAEGEAEAQ 195
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 35-218 3.05e-11

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: 62.80  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  35 FGRYTGTAVPGFNFYPAFFYRVgRRVNMmEQVIDIPGQ-EIITKDNAMISTDGVVFFQVLDAPKAAYEVSDLYVALLNLV 113
Cdd:TIGR01933  15 FGKYHRTVDPGLNWKPPFIEEV-YPVNV-TAVRNLRKQgLMLTGDENIVNVEMNVQYRITDPYKYLFSVENPEDSLRQAT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 114 TTNLRTVMGSMDLDETLSK-----RDEINARLLNVVDHATTpwGVKITRVEIKDIRPPVDIVNAMARQMKAEREKRANIL 188
Cdd:TIGR01933  93 DSALRGVIGDSTMDDILTEgrsqiREDTKERLNEIIDNYDL--GITVTDVNFQSARPPEEVKEAFDDVIIAREDEERYIN 170

                         170       180       190
                  ....*....|....*....|....*....|
gi 1992576671 189 EAEGSRASEILRAEGQKQARILEAEGRRES 218
Cdd:TIGR01933 171 EAEAYANEVVPKARGDAQRIIEEARGYKER 200
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
59-221 3.47e-10

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 60.66  E-value: 3.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  59 RVNMMEQVIDI-PGQEIITKDNAMISTDGVVFFQVLDAP----KAAYEVSDLYVALL-NLVTT----NLRTVMGSMDLDE 128
Cdd:COG2268    65 RMSLSTMTIEVeRTEGLITKDGIRVDVDAVFYVKVNSDPediaNAAERFLGRDPEEIeELAEEklegALRAVAAQMTVEE 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 129 TLSKRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMARQMKAEREKRANILEAEGSRASEILRAEGQKQAR 208
Cdd:COG2268   145 LNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAE 224

                         170
                  ....*....|...
gi 1992576671 209 ILEAEGRRESAFR 221
Cdd:COG2268   225 EAELEQEREIETA 237
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 52-175 4.25e-07

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: 48.65  E-value: 4.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  52 FFYRVgRRVNMMEQVIDIPGQEIITKDNAMISTDGVVFFQVLDAPK---AAYE------VSDLYVALLNLVTTNLRTVMG 122
Cdd:cd03399     5 FLQRV-QRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEeiaAAAErflgksTEEIRELVKETLEGHLRAIVG 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1992576671 123 SMDLDETLSKRDEINARLLNVVDHATTPWGVKITRVEIKDIRPPVDIVNAMAR 175
Cdd:cd03399    84 TMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGR 136
PRK11029 PRK11029
protease modulator HflC;
128-219 8.98e-07

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 49.74  E-value: 8.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 128 ETLSKRDEINARLLNVVdhattpwGVKITRVEIKDIRPPVDIVNAMARQMKAEREKRANILEAEGSRASEILRA------ 201
Cdd:PRK11029  185 ETKGKVPVINPNSMAAL-------GIEVVDVRIKQINLPTEVSDAIYNRMRAEREAVARRHRSQGQEEAEKLRAtadyev 257

                          90       100
                  ....*....|....*....|...
gi 1992576671 202 -----EGQKQARILEAEGRRESA 219
Cdd:PRK11029  258 trtlaEAERQGRIMRGEGDAEAA 280
Band_7_C pfam16200
C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal ...
 238-283 3.31e-06

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: 44.01  E-value: 3.31e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1992576671 238 RVVSDAIAQ-GGTQAINYFVAQKYVEAVGKFATSPNakTILFPVEAT 283
Cdd:pfam16200   1 EKVAEAIKKpGGQEAVSLRVAEQYVEAFGKLAKESN--TVILPANLG 45
PRK10930 PRK10930
FtsH protease activity modulator HflK;
30-211 5.42e-05

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 44.43  E-value: 5.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  30 YTIEH--------FGRYTGTAVPGFNFYPAFFYRVgRRVNmMEQVIDIPGQEI-ITKDNAMISTDGVVFFQVLDAPKAAY 100
Cdd:PRK10930   98 YTIKEaergvvtrFGKFSHLVEPGLNWKPTFIDEV-KPVN-VEAVRELAASGVmLTSDENVVRVEMNVQYRVTDPEKYLF 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671 101 EVSDLYVALLNLVTTNLRTVMGSMDLDETLSK-RDEINARLLNVVDHATTPWGVKIT--RVEIKDIRPPVDIVNAMARQM 177
Cdd:PRK10930  176 SVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYDMGITllDVNFQAARPPEEVKAAFDDAI 255

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1992576671 178 KAEREKRANILEAEgSRASEIL-RAEGQKQaRILE 211
Cdd:PRK10930  256 AARENEQQYIREAE-AYTNEVQpRANGQAQ-RILE 288
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 20-189 6.82e-04

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


Pssm-ID: 259800  Cd Length: 231  Bit Score: 40.23  E-value: 6.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  20 SIKIVRQGYQYTIEHFGRYTGT-AVPGFNFYPAFF--YRVGRRVNMME----QVIDIPGQEIitkdnaMISTdgVVFFQV 92
Cdd:cd03402     9 GFFVVQPNEAAVLTLFGRYRGTvRRPGLRWVNPFYrkKRVSLRVRNFEseplKVNDANGNPI------EIAA--VVVWRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1992576671  93 LDAPKAAYEVSDLYVALLNLVTTNLRTVMGSMDLD------ETLSK-RDEINARLLNVVDHATTPWGVKITRVEIKDIRP 165
Cdd:cd03402    81 VDTAKAVFDVDDYEEFVSIQSEAALRRVASRYPYDsfedgePSLRGnSDEVSEELRRELQERLAVAGVEVIEARITHLAY 160

                         170       180
                  ....*....|....*....|....*.
gi 1992576671 166 PVDIVNAMAR--QMKAEREKRANILE 189
Cdd:cd03402   161 APEIAQAMLQrqQASAIIAARQTIVE 186
 
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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