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Conserved domains on  [gi|1273927483|gb|PIF40443|]
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SPFH domain-containing protein [Burkholderiales bacterium 23]

Protein Classification

slipin family protein( domain architecture ID 10194185)

slipin family protein (SLP or stomatin-like protein) is an uncharacterized SPFH domain-containing protein

CATH:  3.30.479.30
Gene Ontology:  GO:0016020
PubMed:  17766116|10542406|18267007
SCOP:  4003722

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 153-367 1.12e-102

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: 302.15  E-value: 1.12e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 153 VPAGQCALLTIDGKVDRLLQAGSHAFWKFGRSIAVELVDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFAQL 232
Cdd:cd13438     1 VPPGERGLLYRDGKLVRTLEPGRYAFWKFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 233 QKPAEHLYRELQFALRAAVGTRTLDELLENKTVIDDVVTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQVVQAEKQ 312
Cdd:cd13438    81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1273927483 313 AQANVIRRREETAATRSLLNTAKVMEDNPVALRMKELETLERVAERIDKISVFGG 367
Cdd:cd13438   161 AQANLIRAREETAATRSLLNAAKLMEENPALLRLRELEALEKIAEKVGHISVSGG 215
 
Name Accession Description Interval E-value
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 153-367 1.12e-102

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: 302.15  E-value: 1.12e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 153 VPAGQCALLTIDGKVDRLLQAGSHAFWKFGRSIAVELVDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFAQL 232
Cdd:cd13438     1 VPPGERGLLYRDGKLVRTLEPGRYAFWKFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 233 QKPAEHLYRELQFALRAAVGTRTLDELLENKTVIDDVVTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQVVQAEKQ 312
Cdd:cd13438    81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1273927483 313 AQANVIRRREETAATRSLLNTAKVMEDNPVALRMKELETLERVAERIDKISVFGG 367
Cdd:cd13438   161 AQANLIRAREETAATRSLLNAAKLMEENPALLRLRELEALEKIAEKVGHISVSGG 215
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 151-323 8.22e-27

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: 105.10  E-value: 8.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 151 VQVPAGQCALLTIDGKVDRLLQAGSHAFWKFGRSiaVELVDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYR--HTDVLRA 228
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQR--VVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRvnPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 229 FAQLQKPAEH---LYRELQFALRAAVGTRTLDELLENKTVIDDVVTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQ 305
Cdd:pfam01145  79 VQNVFGSDDLqelLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 1273927483 306 VVQAEKQAQANVIRRREE 323
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 151-364 3.28e-23

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 97.60  E-value: 3.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 151 VQVPAGQCALLTIDGKVDRLLQAGSHAFWKFGRSiaVELVDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFA 230
Cdd:COG0330    22 YIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDR--VRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLY 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 231 QLQKPAEHLYRELQFALRAAVGTRTLDELL-ENKTVIDDVVTAHMAAKLQPFGMVVESVGVKDIVLPGE--------MKA 301
Cdd:COG0330   100 NVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEvqdamedrMKA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 302 -------ILT------------------QVVQAEKQAQANVIRRREETAATRSLlntAKVMEDNPVALRMKELETLERVA 356
Cdd:COG0330   180 erereaaILEaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIV---AEAYSAAPFVLFYRSLEALEEVL 256


                  ....*...
gi 1273927483 357 ERIDKISV 364
Cdd:COG0330   257 SPNSKVIV 264
PHB smart00244
prohibitin homologues; prohibitin homologues
 153-307 2.13e-14

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 70.38  E-value: 2.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483  153 VPAGQCALLTIDGKVDRLLQAGSHAFWKFgrSIAVELVDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFAQL 232
Cdd:smart00244   6 VGEGERGVVERLGRVLRVLGPGLHFLIPF--IDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRV 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1273927483  233 QKPAEH-LYRELQFALRAAVGTRTLDELLE-NKTVIDDVVTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQVV 307
Cdd:smart00244  84 LDADYAvIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
PRK10930 PRK10930
FtsH protease activity modulator HflK;
165-374 9.14e-04

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 40.97  E-value: 9.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 165 GKVDRLLQAGSHafWKfgRSIAVELVDLRLQAV-EVSGQDIM-TRDKVSLRLNLSAAYRHTDVLRAFAQLQKPAEHLYRE 242
Cdd:PRK10930  112 GKFSHLVEPGLN--WK--PTFIDEVKPVNVEAVrELAASGVMlTSDENVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQA 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 243 LQFALRAAVGTRTLDELL-ENKTVIDDVVTAHMAAKLQPF--GMVVESVGVKDIVLPGEMKAILTQVVQA---------E 310
Cdd:PRK10930  188 TDSALRGVIGKYTMDRILtEGRTVIRSDTQRELEETIRPYdmGITLLDVNFQAARPPEEVKAAFDDAIAAreneqqyirE 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 311 KQAQANVIRRR---------EETAA--TRSLLNT-------AKVMEDNPVALRMKE----LETLERVAERIDKISVFGG- 367
Cdd:PRK10930  268 AEAYTNEVQPRangqaqrilEEARAykAQTILEAqgevarfAKLLPEYKAAPEITRerlyIETMEKVLGHTRKVLVNDKg 347

                         250
                  ....*....|....
gi 1273927483 368 -------LDQVLNG 374
Cdd:PRK10930  348 gnlmvlpLDQMLKG 361
 
Name Accession Description Interval E-value
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 153-367 1.12e-102

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: 302.15  E-value: 1.12e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 153 VPAGQCALLTIDGKVDRLLQAGSHAFWKFGRSIAVELVDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFAQL 232
Cdd:cd13438     1 VPPGERGLLYRDGKLVRTLEPGRYAFWKFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 233 QKPAEHLYRELQFALRAAVGTRTLDELLENKTVIDDVVTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQVVQAEKQ 312
Cdd:cd13438    81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1273927483 313 AQANVIRRREETAATRSLLNTAKVMEDNPVALRMKELETLERVAERIDKISVFGG 367
Cdd:cd13438   161 AQANLIRAREETAATRSLLNAAKLMEENPALLRLRELEALEKIAEKVGHISVSGG 215
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 151-323 8.22e-27

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: 105.10  E-value: 8.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 151 VQVPAGQCALLTIDGKVDRLLQAGSHAFWKFGRSiaVELVDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYR--HTDVLRA 228
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQR--VVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRvnPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 229 FAQLQKPAEH---LYRELQFALRAAVGTRTLDELLENKTVIDDVVTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQ 305
Cdd:pfam01145  79 VQNVFGSDDLqelLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 1273927483 306 VVQAEKQAQANVIRRREE 323
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 190-296 1.41e-26

Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, podocin, and other members of the stomatin-like protein family (SLPs or slipins). The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome. Bacterial and archaebacterial SLPs and many of the eukaryotic family members remain uncharacterized.


Pssm-ID: 259812 [Multi-domain]  Cd Length: 108  Bit Score: 101.89  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 190 VDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFAQLQKPAEHLYRELQFALRAAVGTRTLDELLENKTVIDDV 269
Cdd:cd13434     1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                          90       100
                  ....*....|....*....|....*..
gi 1273927483 270 VTAHMAAKLQPFGMVVESVGVKDIVLP 296
Cdd:cd13434    81 LQEILDEATDPWGIKVERVEIKDIILP 107
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 190-365 5.82e-24

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: 98.22  E-value: 5.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 190 VDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFAQLQKPAEHLYRELQFALRAAVGTRTLDELLENKTVIDDV 269
Cdd:cd13435    22 VDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGTRNLSELLTERETISHS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 270 VTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQVVQAEKQAQANVIRRREETAATRSLLNTAKVMEDNPVALRMKEL 349
Cdd:cd13435   102 MQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRALKEASDIISASPSALQLRYL 181

                         170
                  ....*....|....*.
gi 1273927483 350 ETLERVAERIDKISVF 365
Cdd:cd13435   182 QTLSSISGEKNSTIIF 197
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 190-356 5.89e-24

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria 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: 97.20  E-value: 5.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 190 VDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFAQLQkpaEHLYRELQFA---LRAAVGTRTLDELLEN---- 262
Cdd:cd08826     9 VDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVE---DYRYATSQLAqttLRSVVGQVELDELLSEreei 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 263 ----KTVIDDVVTahmaaklqPFGMVVESVGVKDIVLPGEMKAILTQVVQAEKQAQANVIRRREETAATRSLLNTAKVME 338
Cdd:cd08826    86 nkriQEIIDEQTE--------PWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILA 157

                         170
                  ....*....|....*...
gi 1273927483 339 DNPVALRMKELETLERVA 356
Cdd:cd08826   158 KSPGALQLRYLQTLSEIA 175
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 151-364 3.28e-23

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 97.60  E-value: 3.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 151 VQVPAGQCALLTIDGKVDRLLQAGSHAFWKFGRSiaVELVDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFA 230
Cdd:COG0330    22 YIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDR--VRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLY 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 231 QLQKPAEHLYRELQFALRAAVGTRTLDELL-ENKTVIDDVVTAHMAAKLQPFGMVVESVGVKDIVLPGE--------MKA 301
Cdd:COG0330   100 NVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEvqdamedrMKA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 302 -------ILT------------------QVVQAEKQAQANVIRRREETAATRSLlntAKVMEDNPVALRMKELETLERVA 356
Cdd:COG0330   180 erereaaILEaegyreaaiiraegeaqrAIIEAEAYREAQILRAEGEAEAFRIV---AEAYSAAPFVLFYRSLEALEEVL 256


                  ....*...
gi 1273927483 357 ERIDKISV 364
Cdd:COG0330   257 SPNSKVIV 264
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 151-357 3.18e-22

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: 93.83  E-value: 3.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 151 VQVPAGQCALLTIDGKVDRLLQAGSHAFWKFGRSIavELVDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFA 230
Cdd:cd13437     7 KQVKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKI--IQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 231 QLQKpAEHLYREL-QFALRAAVGTRTLDELLENKTVIDDVVTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQVVQA 309
Cdd:cd13437    85 RIDN-VKQALIERtQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKA 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1273927483 310 EKQAQANVIRRREETAATRsLLNTAKVMEDNPVALRMKELETLERVAE 357
Cdd:cd13437   164 KRIGESKIISAKADVESAK-LMREAADILDSKAAMQIRYLETLQAIAK 210
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 190-365 1.34e-18

Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; Stomatin (or band 7) is widely expressed and, highly expressed in red blood cells. It localizes predominantly to the plasma membrane and to intracellular vesicles of the endocytic pathway, where it is present in higher order homo-oligomeric complexes (of between 9 and 12 monomers). Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and, is implicated in trafficking of Glut1 glucose transporters. This subgroup found in animals, also contains proteins similar to Caenorhabditis elegans MEC-2. MEC-2 interacts with MEC-4, which is part of the degenerin channel complex required for response to gentle body touch.


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 82.98  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 190 VDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFAQLQKpAEHLYREL-QFALRAAVGTRTLDELLENKTVIDD 268
Cdd:cd03403    22 VDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVEN-ADRSTRLLaQTTLRNVLGTKNLSEILSDRETISH 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 269 VVTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQVVQAEKQAQANVIRRREETAATRSLLNTAKVMEDNPVALRMKE 348
Cdd:cd03403   101 QMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRALKEAADVISESPAALQLRY 180

                         170
                  ....*....|....*..
gi 1273927483 349 LETLERVAERIDKISVF 365
Cdd:cd03403   181 LQTLNTISAEKNSTIIF 197
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 190-347 4.30e-17

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: 78.05  E-value: 4.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 190 VDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFAQLQKPAEHLYRELQFALRAAVGTRTLDELLENKTVIDDV 269
Cdd:cd13775     1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1273927483 270 VTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQVVQAEKQAQANVIRRREETAATRSLLNTAKVMEDNPVALRMK 347
Cdd:cd13775    81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLR 158
PHB smart00244
prohibitin homologues; prohibitin homologues
 153-307 2.13e-14

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 70.38  E-value: 2.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483  153 VPAGQCALLTIDGKVDRLLQAGSHAFWKFgrSIAVELVDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFAQL 232
Cdd:smart00244   6 VGEGERGVVERLGRVLRVLGPGLHFLIPF--IDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRV 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1273927483  233 QKPAEH-LYRELQFALRAAVGTRTLDELLE-NKTVIDDVVTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQVV 307
Cdd:smart00244  84 LDADYAvIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 190-353 1.01e-12

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: 66.84  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 190 VDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDV---LRAFAQLQKPAEHLyreLQFALRAAVGTRTL-DELLENKTV 265
Cdd:cd08827    44 VDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAsvcLSSFASISDAMQAL---VQTTVKRLLAHRAFtDILLERKSI 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 266 IDDVVTAHMAAKLQpFGMVVESVGVKDIVLPGEMKAILTQVVQAEKQAQANVIRRREETAATRSLLNTAKVMEDNPVALR 345
Cdd:cd08827   121 AQEIKVALDSGTCR-WGIKVERAEIKDVNLPPELQHSFAVEAEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQ 199


                  ....*...
gi 1273927483 346 MKELETLE 353
Cdd:cd08827   200 LRYLHTLQ 207
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 190-296 1.87e-10

Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in all three kingdoms of life. The conserved domain common to these families has also been referred to as the Band 7 domain. Individual proteins of the SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This subgroup of the SLPs remains largely uncharacterized. It includes human SLP-2 which is upregulated and involved in the progression and development in several types of cancer, including esophageal squamous cell carcinoma, endometrial adenocarcinoma, breast cancer, and glioma.


Pssm-ID: 259811 [Multi-domain]  Cd Length: 111  Bit Score: 57.48  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 190 VDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFAQLQKPAEHLYRELQFALRAAVGTRTLDELLENKTVIDDV 269
Cdd:cd08829     4 VDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAK 83

                          90       100
                  ....*....|....*....|....*..
gi 1273927483 270 VTAHMAAKLQPFGMVVESVGVKDIVLP 296
Cdd:cd08829    84 LLEALDEATDPWGVKVTRVEIKDITPP 110
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 190-326 2.24e-10

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: 58.51  E-value: 2.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 190 VDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFAQLQKPAEHLYRELQFALRAAVGTRTLDELLENKTVIDDV 269
Cdd:cd08828    18 VDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGTQTLAQILAGREEIAHS 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1273927483 270 VTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQVVQAEKQAQANVIRRREETAA 326
Cdd:cd08828    98 IQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 151-328 9.99e-10

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: 58.27  E-value: 9.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 151 VQVPAGQCALLTIDGKVDR-LLQAGSHAFWKFGRSiaVELVDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLR-- 227
Cdd:cd03405     3 FIVDETEQAVVLQFGKPVRvITEPGLHFKLPFIQN--VRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRfy 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 228 ------AFAQLQkpaehLYRELQFALRAAVGTRTLDELLENK-TVIDDVVTAHMAAKLQPFGMVVESVGVKDIVLPGEMK 300
Cdd:cd03405    81 qsvggeEGAESR-----LDDIVDSALRNEIGKRTLAEVVSGGrDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVS 155

                         170       180
                  ....*....|....*....|....*...
gi 1273927483 301 AILTQVVQAEKQAQANVIRRREETAATR 328
Cdd:cd03405   156 ESVYERMRAERERIAAEYRAEGEEEAEK 183
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 151-328 2.09e-09

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: 56.75  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 151 VQVPAGQCALLTIDGKV--DRLLQAGSHAFWKFGRSiaVELVDLRLQAVEVSgQDIMTRDKVSLRLNLSAAYRhtdvLRA 228
Cdd:cd03401     2 YTVDAGEVGVVFRRGKGvkDEVLGEGLHFKIPWIQV--VIIYDVRTQPREIT-LTVLSKDGQTVNIDLSVLYR----PDP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 229 faqlqKPAEHLYREL-------------QFALRAAVGTRTLDELLENKTVIDDVVTAHMAAKLQPFGMVVESVGVKDIVL 295
Cdd:cd03401    75 -----EKLPELYQNLgpdyeervlppivREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDF 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1273927483 296 PGEMKAILTQVVQAEKQAQ-ANVIRRREETAATR 328
Cdd:cd03401   150 PDEYEKAIEAKQVAEQEAErAKFELEKAEQEAER 183
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 165-320 2.74e-08

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: 54.51  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 165 GKVDRLLQAGSHAFWKFGRSIAvELVDLRLQAVEVSgQDIMTRDKVSLRLNLSAAYR--HTDVLRAFAQLQKPAEHLYRE 242
Cdd:cd03407    14 GKFSRIAEPGLHFIIPPIESVA-GRVSLRVQQLDVR-VETKTKDNVFVTLVVSVQYRvvPEKVYDAFYKLTNPEQQIQSY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 243 LQFALRAAVGTRTLDELLENKTVIDDVVTAHMAAKLQPFGMVVESVGVKDIVLPGEMKAILTQV-------VQAEKQAQA 315
Cdd:cd03407    92 VFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEInaaqrlrEAAEEKAEA 171


                  ....*
gi 1273927483 316 NVIRR 320
Cdd:cd03407   172 EKILQ 176
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 193-296 2.21e-07

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: 48.90  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 193 RLQAVEVSGQDIMTRDKVSLRLNLSAAYRHTDVLRAFA----QLQKPAE-HLYRELQFALRAAVGTRTLDELLENKTVID 267
Cdd:cd02106     1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAfylvDFVKDIKaDIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                          90       100
                  ....*....|....*....|....*....
gi 1273927483 268 DVVTAHMAAKLQPFGMVVESVGVKDIVLP 296
Cdd:cd02106    81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
PRK10930 PRK10930
FtsH protease activity modulator HflK;
165-374 9.14e-04

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 40.97  E-value: 9.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 165 GKVDRLLQAGSHafWKfgRSIAVELVDLRLQAV-EVSGQDIM-TRDKVSLRLNLSAAYRHTDVLRAFAQLQKPAEHLYRE 242
Cdd:PRK10930  112 GKFSHLVEPGLN--WK--PTFIDEVKPVNVEAVrELAASGVMlTSDENVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQA 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 243 LQFALRAAVGTRTLDELL-ENKTVIDDVVTAHMAAKLQPF--GMVVESVGVKDIVLPGEMKAILTQVVQA---------E 310
Cdd:PRK10930  188 TDSALRGVIGKYTMDRILtEGRTVIRSDTQRELEETIRPYdmGITLLDVNFQAARPPEEVKAAFDDAIAAreneqqyirE 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 311 KQAQANVIRRR---------EETAA--TRSLLNT-------AKVMEDNPVALRMKE----LETLERVAERIDKISVFGG- 367
Cdd:PRK10930  268 AEAYTNEVQPRangqaqrilEEARAykAQTILEAqgevarfAKLLPEYKAAPEITRerlyIETMEKVLGHTRKVLVNDKg 347

                         250
                  ....*....|....
gi 1273927483 368 -------LDQVLNG 374
Cdd:PRK10930  348 gnlmvlpLDQMLKG 361
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 187-293 1.59e-03

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: 38.64  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1273927483 187 VELVDLRLQAVEVSGQDIMTRDKVSLRLNLSAAYR----HTDVLRAFAQ-LQKPAEHLYRE----LQFALRAAVGTRTLD 257
Cdd:cd03399     9 VQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKvgsdPEEIAAAAERfLGKSTEEIRELvketLEGHLRAIVGTMTVE 88

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1273927483 258 ELLENKTVIDDVVTAHMAAKLQPFGMVVESVGVKDI 293
Cdd:cd03399    89 EIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDI 124
 
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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