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Conserved domains on  [gi|1093634250|gb|OHY17474|]
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paraslipin [Mannheimia haemolytica]

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 ...
 7-288 2.00e-90

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 270.56  E-value: 2.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250   7 IVSIAFVVLVLVALSSTIKIVPQGYHWTVERFGRYTKTLSPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVA 86
Cdd:COG0330     4 ILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNIVD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  87 IDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGSMDLDDMLS-QRDLINGRLLSIVDEATNIWGVKVTRIEIRD 165
Cdd:COG0330    83 VDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 166 VRPPKELVAAMNAQMKAERNKRADILEAEGIRQAEILRAEGEKQSRILKAEGERQEAFLQaeareraAEAEAKATQMVSE 245
Cdd:COG0330   163 IDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILR-------AEGEAEAFRIVAE 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1093634250 246 AIakgdtTAINYFIAQKYTEALKEIGSSDNSKVVLMPLEAGNL 288
Cdd:COG0330   236 AY-----SAAPFVLFYRSLEALEEVLSPNSKVIVLPPDGNGFL 273
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 7-288 2.00e-90

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 270.56  E-value: 2.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250   7 IVSIAFVVLVLVALSSTIKIVPQGYHWTVERFGRYTKTLSPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVA 86
Cdd:COG0330     4 ILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNIVD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  87 IDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGSMDLDDMLS-QRDLINGRLLSIVDEATNIWGVKVTRIEIRD 165
Cdd:COG0330    83 VDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 166 VRPPKELVAAMNAQMKAERNKRADILEAEGIRQAEILRAEGEKQSRILKAEGERQEAFLQaeareraAEAEAKATQMVSE 245
Cdd:COG0330   163 IDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILR-------AEGEAEAFRIVAE 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1093634250 246 AIakgdtTAINYFIAQKYTEALKEIGSSDNSKVVLMPLEAGNL 288
Cdd:COG0330   236 AY-----SAAPFVLFYRSLEALEEVLSPNSKVIVLPPDGNGFL 273
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 62-170 1.44e-51

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: 165.34  E-value: 1.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  62 KMNMMEQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGSMDLDDMLSQRDLING 141
Cdd:cd08829     3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                          90       100
                  ....*....|....*....|....*....
gi 1093634250 142 RLLSIVDEATNIWGVKVTRIEIRDVRPPK 170
Cdd:cd08829    83 KLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 24-180 3.85e-38

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 132.40  E-value: 3.85e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250   24 IKIVPQGYHWTVERFGRYTKTLSPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAY 103
Cdd:smart00244   3 IKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVY 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093634250  104 EVNHLEQA-IVNLTMTNMRTVLGSMDLDDMLS-QRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQM 180
Cdd:smart00244  82 RVLDADYAvIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 25-195 1.46e-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: 118.58  E-value: 1.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  25 KIVPQGYHWTVERFGRYTKTLSPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVCF--VQTVDARRAA 102
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIyrVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 103 YEV---NHLEQAIVNLTMTNMRTVLGSMDLDDMLSQRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQ 179
Cdd:pfam01145  80 QNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*.
gi 1093634250 180 MKAERNKRADILEAEG 195
Cdd:pfam01145 160 QTAEQEAEAEIARAEA 175
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 35-221 1.20e-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: 77.83  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  35 VERFGRYTKTLSPGLNIVVPFIDRIgrKMNMMEQVLDIPSQ-EVISRDNASVAIDAVCFVQTVDARRAAYEVNHLEQAIV 113
Cdd:TIGR01933  12 VLRFGKYHRTVDPGLNWKPPFIEEV--YPVNVTAVRNLRKQgLMLTGDENIVNVEMNVQYRITDPYKYLFSVENPEDSLR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 114 NLTMTNMRTVLGSMDLDDMLSQ-RDLINGRLLSIVDEATNIW--GVKVTRIEIRDVRPPKELVAAMNAQMKAERNKRADI 190
Cdd:TIGR01933  90 QATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDVIIAREDEERYI 169

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1093634250 191 LEAEGIRQAEILRAEGEKQSRILKAEGERQE 221
Cdd:TIGR01933 170 NEAEAYANEVVPKARGDAQRIIEEARGYKER 200
PRK11029 PRK11029
protease modulator HflC;
10-224 1.03e-09

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 58.60  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  10 IAFVVLVLVALSSTIKIVPQGYHWTVERFGRY-----TKTL--SPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDN 82
Cdd:PRK11029    6 IAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVlrdddNKPLvyAPGLHFKIPFIETV-KMLDARIQTMDNQADRFVTKEK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  83 ASVAIDAVCFVQTVD------------------------ARRAAYEVNHLE-QAIV----NLTMTNMRTVL--GSMDLDD 131
Cdd:PRK11029   85 KDLIVDSYIKWRISDfsryylatgggdisqaevllkrkfSDRLRSEIGRLDvKDIVtdsrGRLTLDVRDALnsGSAGTED 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 132 MLSQR---DLI-----------NGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQMKAERNKRADILEAEGIR 197
Cdd:PRK11029  165 EVATPaadDAIasaaerveaetKGKVPVINPNSMAALGIEVVDVRIKQINLPTEVSDAIYNRMRAEREAVARRHRSQGQE 244

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1093634250 198 QAEILRA-----------EGEKQSRILKAEGERQEAFL 224
Cdd:PRK11029  245 EAEKLRAtadyevtrtlaEAERQGRIMRGEGDAEAAKL 282
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 7-288 2.00e-90

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 270.56  E-value: 2.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250   7 IVSIAFVVLVLVALSSTIKIVPQGYHWTVERFGRYTKTLSPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVA 86
Cdd:COG0330     4 ILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNNIVD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  87 IDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGSMDLDDMLS-QRDLINGRLLSIVDEATNIWGVKVTRIEIRD 165
Cdd:COG0330    83 VDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 166 VRPPKELVAAMNAQMKAERNKRADILEAEGIRQAEILRAEGEKQSRILKAEGERQEAFLQaeareraAEAEAKATQMVSE 245
Cdd:COG0330   163 IDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILR-------AEGEAEAFRIVAE 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1093634250 246 AIakgdtTAINYFIAQKYTEALKEIGSSDNSKVVLMPLEAGNL 288
Cdd:COG0330   236 AY-----SAAPFVLFYRSLEALEEVLSPNSKVIVLPPDGNGFL 273
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 62-170 1.44e-51

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: 165.34  E-value: 1.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  62 KMNMMEQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGSMDLDDMLSQRDLING 141
Cdd:cd08829     3 KVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINA 82

                          90       100
                  ....*....|....*....|....*....
gi 1093634250 142 RLLSIVDEATNIWGVKVTRIEIRDVRPPK 170
Cdd:cd08829    83 KLLEALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 54-204 5.99e-45

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized. This subgroup contains PH1511 from the hyperthermophilic archaeon Pyrococcus horikoshi.


Pssm-ID: 259808 [Multi-domain]  Cd Length: 178  Bit Score: 150.74  E-value: 5.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  54 PFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGSMDLDDML 133
Cdd:cd08826     1 PFIDRM-VRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093634250 134 SQRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQMKAERNKRADILEAEGIRQA-EILRA 204
Cdd:cd08826    80 SEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAaEKLAE 151
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 27-284 8.35e-45

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: 151.61  E-value: 8.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  27 VPQGYHWTVERFGRYTKTLSPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAYEVN 106
Cdd:cd13437     9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKI-IQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 107 HLEQAIVNLTMTNMRTVLGSMDLDDMLSQRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQMKAERnk 186
Cdd:cd13437    88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKR-- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 187 radileaegirQAEilraegekqSRILKAEGERQEAFLQAeareraaeaeaKATQMVSEAIAkgdtTAINYFiaqkytEA 266
Cdd:cd13437   166 -----------IGE---------SKIISAKADVESAKLMR-----------EAADILDSKAA----MQIRYL------ET 204

                         250
                  ....*....|....*...
gi 1093634250 267 LKEIGSSDNSKVVLMPLE 284
Cdd:cd13437   205 LQAIAKSANSKVIFLPLD 222
PHB smart00244
prohibitin homologues; prohibitin homologues
 24-180 3.85e-38

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 132.40  E-value: 3.85e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250   24 IKIVPQGYHWTVERFGRYTKTLSPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAY 103
Cdd:smart00244   3 IKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVY 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093634250  104 EVNHLEQA-IVNLTMTNMRTVLGSMDLDDMLS-QRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQM 180
Cdd:smart00244  82 RVLDADYAvIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 47-225 6.08e-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: 123.04  E-value: 6.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  47 PGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGS 126
Cdd:cd03403     7 PGLFFILPCIDSY-RKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 127 MDLDDMLSQRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQMKAERNKRADILEAEGIRQAEilRAEG 206
Cdd:cd03403    86 KNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNAS--RALK 163

                         170
                  ....*....|....*....
gi 1093634250 207 EKQSRILKAEGERQEAFLQ 225
Cdd:cd03403   164 EAADVISESPAALQLRYLQ 182
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 67-170 1.43e-32

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: 116.14  E-value: 1.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  67 EQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGSMDLDDMLSQRDLINGRLLSI 146
Cdd:cd13434     5 TQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQEI 84

                          90       100
                  ....*....|....*....|....
gi 1093634250 147 VDEATNIWGVKVTRIEIRDVRPPK 170
Cdd:cd13434    85 LDEATDPWGIKVERVEIKDIILPQ 108
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 25-195 1.46e-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: 118.58  E-value: 1.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  25 KIVPQGYHWTVERFGRYTKTLSPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVCF--VQTVDARRAA 102
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIyrVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 103 YEV---NHLEQAIVNLTMTNMRTVLGSMDLDDMLSQRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQ 179
Cdd:pfam01145  80 QNVfgsDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*.
gi 1093634250 180 MKAERNKRADILEAEG 195
Cdd:pfam01145 160 QTAEQEAEAEIARAEA 175
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 47-225 2.26e-32

Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in arthropods. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this divergent slipin subgroup remain largely uncharacterized. It contains Drosophila Mec2, the gene for which was identified in a screen for genes required for nephrocyte function; it may function together with Sns in maintaining nephrocyte diaphragm.


Pssm-ID: 259813 [Multi-domain]  Cd Length: 208  Bit Score: 119.03  E-value: 2.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  47 PGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGS 126
Cdd:cd13435     7 PGVFFVLPCIDNY-CKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 127 MDLDDMLSQRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQMKAERNKRADILEAEGIRQAEilRAEG 206
Cdd:cd13435    86 RNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSS--RALK 163

                         170
                  ....*....|....*....
gi 1093634250 207 EKQSRILKAEGERQEAFLQ 225
Cdd:cd13435   164 EASDIISASPSALQLRYLQ 182
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 47-195 1.04e-28

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: 107.81  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  47 PGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGS 126
Cdd:cd08828     3 PGLILVLPCTDTF-IKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGT 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093634250 127 MDLDDMLSQRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQMKAERNKRADILEAEG 195
Cdd:cd08828    82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEG 150
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 10-221 1.08e-27

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: 107.98  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  10 IAFVVLVLVALSSTIKIVPQGYHWTVERFGRYTKTLSPGLNIVVPFIDRIGRKMNMMEqvldIPSQEVISRDNAS----- 84
Cdd:cd03404     1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGKYVRTVGPGLHWKLPFPIEVVEKVNVTQ----VRSVEIGFRVPEEslmlt 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  85 -----VAIDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGSMDLDDMLS-QRDLINGRLLSIVDEATNIW--GV 156
Cdd:cd03404    77 gdeniVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTeGRAEIAADVRELLQEILDRYdlGI 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1093634250 157 KVTRIEIRDVRPPKELVAAMNAQMKAERNKRADILEAEGIRQAEILRAEGEKQSRILKAEGERQE 221
Cdd:cd03404   157 EIVQVQLQDADPPEEVQDAFDDVNAARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAE 221
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 68-205 2.62e-27

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: 104.63  E-value: 2.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  68 QVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGSMDLDDMLSQRDLINGRLLSIV 147
Cdd:cd13775     6 RTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDII 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1093634250 148 DEATNIWGVKVTRIEIRDVRPPKELVAAMNAQMKAERNKRADILEAEgirqAEILRAE 205
Cdd:cd13775    86 DEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAE----AEKEIAE 139
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 26-220 2.32e-24

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: 98.71  E-value: 2.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  26 IVPQGYHWTVERFGRYTKTLS-PGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVC---------FVQT 95
Cdd:cd03405     4 IVDETEQAVVLQFGKPVRVITePGLHFKLPFIQNV-RKFDKRILTLDGPPEEVLTKDKKRLIVDSYArwritdplrFYQS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  96 V-DARRAAyevNHLEQAIVNltmtNMRTVLGSMDLDDMLS-QRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELV 173
Cdd:cd03405    83 VgGEEGAE---SRLDDIVDS----ALRNEIGKRTLAEVVSgGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1093634250 174 AAMNAQMKAERNKRADILEAEGIRQAEILRAEGEKQSRILKAEGERQ 220
Cdd:cd03405   156 ESVYERMRAERERIAAEYRAEGEEEAEKIRAEADRERTVILAEAYRE 202
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 39-214 1.45e-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: 95.68  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  39 GRYTKTLSPGL--------NIVVPFIDrigrkmnMMEQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAYEVNHLEQ 110
Cdd:cd13438    13 GKLVRTLEPGRyafwkfgrKVQVELVD-------LREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETVDDPEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 111 AIVNLTMTNMRTVLGSMDLDDMLSQRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQMKAErnKRAdi 190
Cdd:cd13438    86 QLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAE--KRA-- 161

                         170       180
                  ....*....|....*....|....*
gi 1093634250 191 leaegirQAEILRAEGEKQS-RILK 214
Cdd:cd13438   162 -------QANLIRAREETAAtRSLL 179
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 35-282 2.20e-22

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: 93.80  E-value: 2.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  35 VERFGRYTKTLSPGLNIVVPFIDRIGRKMNMMEQVLDIpSQEVISRDNASVAIDAVCFVQTVD--ARRAAYEVNHLEQAI 112
Cdd:cd03407    10 VERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDV-RVETKTKDNVFVTLVVSVQYRVVPekVYDAFYKLTNPEQQI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 113 VNLTMTNMRTVLGSMDLDDMLSQRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQMKAERNKRADILE 192
Cdd:cd03407    89 QSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRLREAAEEK 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 193 AEGIRQAEILRAEGEKQSRILKAEG---ERQeAFLQaeareraaeAEAKATQMVSEAIAkgDTTA---INYFIAQKYTEA 266
Cdd:cd03407   169 AEAEKILQVKAAEAEAEAKRLQGVGiaeQRK-AIVD---------GLRESIEDFQEAVP--GVSSkevMDLLLITQYFDT 236

                         250
                  ....*....|....*.
gi 1093634250 267 LKEIGSSDNSKVVLMP 282
Cdd:cd03407   237 LKEVGKSSKSSTVFLP 252
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 24-210 3.48e-22

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: 92.26  E-value: 3.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  24 IKIVPQGYHWTVERFGRYT--KTLSPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRA 101
Cdd:cd08827     4 VKVVREYERAVIFRLGHLLqgRARGPGLFFYLPCLDVC-HKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 102 AYEVNHLEQAIVNLTMTNMRTVLGSMDLDDMLSQRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQMK 181
Cdd:cd08827    83 LSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1093634250 182 AERNKRADILEAEGIRQA-EILRAEGEKQS 210
Cdd:cd08827   163 AQRQAKVKVIAAEGEKAAsEALKAAAESLS 192
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 24-220 6.16e-17

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: 77.17  E-value: 6.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  24 IKIVPQGYHWTVERFGRYTK--TLSPGLNIVVPFIDRIgRKMNMMEQVLDIPSqEVISRDNASVAIDAVCFVQtVDARRA 101
Cdd:cd03401     1 FYTVDAGEVGVVFRRGKGVKdeVLGEGLHFKIPWIQVV-IIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYR-PDPEKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 102 A-----YEVNHLEQAIVNLTMTNMRTVLGSMDLDDMLSQRDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAM 176
Cdd:cd03401    78 PelyqnLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1093634250 177 NAQMKAE-RNKRAdileaegirQAEILRAEGEKQSRILKAEGERQ 220
Cdd:cd03401   158 EAKQVAEqEAERA---------KFELEKAEQEAERKVIEAEGEAE 193
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 35-221 1.20e-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: 77.83  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  35 VERFGRYTKTLSPGLNIVVPFIDRIgrKMNMMEQVLDIPSQ-EVISRDNASVAIDAVCFVQTVDARRAAYEVNHLEQAIV 113
Cdd:TIGR01933  12 VLRFGKYHRTVDPGLNWKPPFIEEV--YPVNVTAVRNLRKQgLMLTGDENIVNVEMNVQYRITDPYKYLFSVENPEDSLR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 114 NLTMTNMRTVLGSMDLDDMLSQ-RDLINGRLLSIVDEATNIW--GVKVTRIEIRDVRPPKELVAAMNAQMKAERNKRADI 190
Cdd:TIGR01933  90 QATDSALRGVIGDSTMDDILTEgRSQIREDTKERLNEIIDNYdlGITVTDVNFQSARPPEEVKEAFDDVIIAREDEERYI 169

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1093634250 191 LEAEGIRQAEILRAEGEKQSRILKAEGERQE 221
Cdd:TIGR01933 170 NEAEAYANEVVPKARGDAQRIIEEARGYKER 200
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 39-167 2.33e-14

Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in animals. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. The family contains human SLP-1, which has been found to be expressed in the brain, and Caenorhabditis elegans UNC-24, which is a lipid raft-associated protein required for normal locomotion. It may mediate the correct localization of UNC-1. Mutations in the unc-24 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259814 [Multi-domain]  Cd Length: 131  Bit Score: 68.58  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  39 GRYTKTLSPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRAAYEVNHLEQAIVNLTMT 118
Cdd:cd13436     1 GRLQKPRGPGIVLILPCIDNF-TRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1093634250 119 NMRTVLGSMDLDDMLSQRDLINGRLLSIVDEATNIWGVKVTRIEIRDVR 167
Cdd:cd13436    80 SLTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVK 128
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 67-170 1.36e-11

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: 60.46  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  67 EQVLDIPSQEVISRDNASVAIDAVCFVQTVDARRA-----AYEVNHLEQAIVNLTMTNMRTVLGSMDLDDMLSQRDLING 141
Cdd:cd02106     2 PQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAK 81

                          90       100
                  ....*....|....*....|....*....
gi 1093634250 142 RLLSIVDEATNIWGVKVTRIEIRDVRPPK 170
Cdd:cd02106    82 AVKEDLEEDLENFGVVISDVDITSIEPPD 110
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 7-222 2.70e-11

HflC 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. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]


Pssm-ID: 273883 [Multi-domain]  Cd Length: 317  Bit Score: 63.26  E-value: 2.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250   7 IVSIAFVVLVLVALSSTIKIVPQGYHWTVERFGRYTKT-------LSPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVIS 79
Cdd:TIGR01932   3 KIGIVVIVLLIVVLFQPFFIIKEGERGIITRFGKILKDnnhhvlvYEPGLHFKIPFIEHV-KIFDAKIQTMDGRPDRIPT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  80 RDNASVAIDAVC---------FVQTVDARRAAYEVNHLEQAIVNltmtNMRTVLGSMDLDDMLSQ--------------- 135
Cdd:TIGR01932  82 KEKKDIIIDTYIrwriedfkkYYLSTGGGTISAAEVLIKRKIDD----RLRSEIGVLGLKEIVRSsndqldtlvsklaln 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 136 ---------------RDLINGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQMKAERNKRADILEAEGIRQAE 200
Cdd:TIGR01932 158 rggkinkiamtitkgREILAREISQIANSQLKDIGIEVVDVRIKKINYSDELSESIYNRMRSEREQIARMHRSQGEEKAE 237

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1093634250 201 ILR-----------AEGEKQSRILKAEGERQEA 222
Cdd:TIGR01932 238 EILgkaeyevrkilSEAYRTARIIKGEGDAEAA 270
PRK11029 PRK11029
protease modulator HflC;
10-224 1.03e-09

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 58.60  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  10 IAFVVLVLVALSSTIKIVPQGYHWTVERFGRY-----TKTL--SPGLNIVVPFIDRIgRKMNMMEQVLDIPSQEVISRDN 82
Cdd:PRK11029    6 IAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVlrdddNKPLvyAPGLHFKIPFIETV-KMLDARIQTMDNQADRFVTKEK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  83 ASVAIDAVCFVQTVD------------------------ARRAAYEVNHLE-QAIV----NLTMTNMRTVL--GSMDLDD 131
Cdd:PRK11029   85 KDLIVDSYIKWRISDfsryylatgggdisqaevllkrkfSDRLRSEIGRLDvKDIVtdsrGRLTLDVRDALnsGSAGTED 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250 132 MLSQR---DLI-----------NGRLLSIVDEATNIWGVKVTRIEIRDVRPPKELVAAMNAQMKAERNKRADILEAEGIR 197
Cdd:PRK11029  165 EVATPaadDAIasaaerveaetKGKVPVINPNSMAALGIEVVDVRIKQINLPTEVSDAIYNRMRAEREAVARRHRSQGQE 244

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1093634250 198 QAEILRA-----------EGEKQSRILKAEGERQEAFL 224
Cdd:PRK11029  245 EAEKLRAtadyevtrtlaEAERQGRIMRGEGDAEAAKL 282
PRK10930 PRK10930
FtsH protease activity modulator HflK;
7-214 1.47e-09

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 58.30  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250   7 IVSIAFVVLVLVALSS---TIKIVPQGyhwTVERFGRYTKTLSPGLNIVVPFIDRIgRKMNmMEQVLDIPSQEV-ISRDN 82
Cdd:PRK10930   80 VVGIAAAAVVIIWAASgfyTIKEAERG---VVTRFGKFSHLVEPGLNWKPTFIDEV-KPVN-VEAVRELAASGVmLTSDE 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  83 ASVAIDAVCFVQTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGSMDLDDMLSQ-RDLINGRLLSIVDEATNIWGVKVTRI 161
Cdd:PRK10930  155 NVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgRTVIRSDTQRELEETIRPYDMGITLL 234

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1093634250 162 EI--RDVRPPKELVAAMNAQMKAERNKRADILEAEGIRQAEILRAEGEKQsRILK 214
Cdd:PRK10930  235 DVnfQAARPPEEVKAAFDDAIAARENEQQYIREAEAYTNEVQPRANGQAQ-RILE 288
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
7-222 5.21e-08

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 53.72  E-value: 5.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250   7 IVSIAFVVLVLVALSSTIKIVPQGYHWTVERFGRYTKTLSPGLNIVVPFIDRIGRkMNMMEQVLDI-PSQEVISRDNASV 85
Cdd:COG2268    11 GVIVVVLLLLLIILARFYRKVPPNEALVITGRGGGYKVVTGGGAFVLPVLHRAER-MSLSTMTIEVeRTEGLITKDGIRV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  86 AIDAVCFVQ---TVDARRAAYE------VNHLEQAIVNLTMTNMRTVLGSMDLDDMLSQRDLINGRLLSIVDEATNIWGV 156
Cdd:COG2268    90 DVDAVFYVKvnsDPEDIANAAErflgrdPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGL 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1093634250 157 KVTRIEIRDVRPPkelvaamnaqmkaernkrADILEAEGIRQ-------AEILRAEGEKQSRILKAEGERQEA 222
Cdd:COG2268   170 ELESVAITDLEDE------------------NNYLDALGRRKiaeiirdARIAEAEAERETEIAIAQANREAE 224
Band_7_C pfam16200
C-terminal region of band_7; This domain is found on a subset of proteins as a C-terminal ...
 241-301 1.23e-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: 45.17  E-value: 1.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1093634250 241 QMVSEAIAK-GDTTAINYFIAQKYTEALKEIGSSDNSkvVLMPLEAGNLIGSVAGIAEILKS 301
Cdd:pfam16200   1 EKVAEAIKKpGGQEAVSLRVAEQYVEAFGKLAKESNT--VILPANLGDVSSMVAQAMSIYKK 60
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 51-137 8.72e-06

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: 44.80  E-value: 8.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  51 IVVPFIDRIgRKMNMMEQVLDIPSQEVISRDNASVAIDAVCFVQ---TVDARRAAYE------VNHLEQAIVNLTMTNMR 121
Cdd:cd03399     1 FVIPFLQRV-QRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKvgsDPEEIAAAAErflgksTEEIRELVKETLEGHLR 79

                          90
                  ....*....|....*.
gi 1093634250 122 TVLGSMDLDDMLSQRD 137
Cdd:cd03399    80 AIVGTMTVEEIYQDRE 95
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 15-176 1.21e-03

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: 39.46  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  15 LVLVALSSTIKIVPQGYHWTVERFGRYTKTL-SPGLNIVVPFIDRigRKMNMMEQVLDIPSQEVISRDNASVAIDAVCFV 93
Cdd:cd03402     1 VVGIILLGGFFVVQPNEAAVLTLFGRYRGTVrRPGLRWVNPFYRK--KRVSLRVRNFESEPLKVNDANGNPIEIAAVVVW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093634250  94 QTVDARRAAYEVNHLEQAIVNLTMTNMRTVLGSMDLDDM----LSQR---DLINGRLLSIVDEATNIWGVKVTRIEIRDV 166
Cdd:cd03402    79 RVVDTAKAVFDVDDYEEFVSIQSEAALRRVASRYPYDSFedgePSLRgnsDEVSEELRRELQERLAVAGVEVIEARITHL 158

                         170
                  ....*....|
gi 1093634250 167 RPPKELVAAM 176
Cdd:cd03402   159 AYAPEIAQAM 168
 
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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