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Conserved domains on  [gi|489185372|ref|WP_003094795|]
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MULTISPECIES: slipin family protein [Pseudomonas]

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 1.85e-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: 301.76  E-value: 1.85e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 153 VPAFQVGVLKVDGALAGLLQAGQYGFWRYNRQVSVELVDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRL 232
Cdd:cd13438    1 VPPGERGLLYRDGKLVRTLEPGRYAFWKFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 233 SKPLEYLYRELQFGLRAAVGTRTLDELLENKQSIDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEKA 312
Cdd:cd13438   81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKR 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489185372 313 AQANVIRRREETSATRSLLNTAKVMEENPTALRLKELETLERVAERIDRISVFGG 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 1.85e-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: 301.76  E-value: 1.85e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 153 VPAFQVGVLKVDGALAGLLQAGQYGFWRYNRQVSVELVDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRL 232
Cdd:cd13438    1 VPPGERGLLYRDGKLVRTLEPGRYAFWKFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 233 SKPLEYLYRELQFGLRAAVGTRTLDELLENKQSIDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEKA 312
Cdd:cd13438   81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKR 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489185372 313 AQANVIRRREETSATRSLLNTAKVMEENPTALRLKELETLERVAERIDRISVFGG 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 2.06e-24

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: 98.55  E-value: 2.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372  151 VQVPAFQVGVLKVDGALAGLLQAGQYGFWRYNRqvSVELVDTRIQALEVSGQEILTRDKVSLRLNLAANWR--YNDVLTA 228
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQ--RVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRvnPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372  229 FSRLSKP---LEYLYRELQFGLRAAVGTRTLDELLENKQSIDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQ 305
Cdd:pfam01145  79 VQNVFGSddlQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 489185372  306 VVEAEKAAQANVIRRREE 323
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 186-319 4.47e-18

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 83.35  E-value: 4.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 186 SVELVDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRLSKPLEYLYRELQFGLRAAVGTRTLDELL-ENKQ 264
Cdd:COG0330   55 RVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLsTGRD 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489185372 265 SIDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEKAAQANVIR 319
Cdd:COG0330  135 EINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILE 189
PHB smart00244
prohibitin homologues; prohibitin homologues
 187-307 2.56e-14

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 70.00  E-value: 2.56e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372   187 VELVDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVL-TAFSRLSKPLEYLYRELQFGLRAAVGTRTLDELLE-NKQ 264
Cdd:smart00244  38 VKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLrAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDELLTdQRE 117

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 489185372   265 SIDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVV 307
Cdd:smart00244 118 KISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
 
Name Accession Description Interval E-value
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 153-367 1.85e-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: 301.76  E-value: 1.85e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 153 VPAFQVGVLKVDGALAGLLQAGQYGFWRYNRQVSVELVDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRL 232
Cdd:cd13438    1 VPPGERGLLYRDGKLVRTLEPGRYAFWKFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 233 SKPLEYLYRELQFGLRAAVGTRTLDELLENKQSIDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEKA 312
Cdd:cd13438   81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEKR 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489185372 313 AQANVIRRREETSATRSLLNTAKVMEENPTALRLKELETLERVAERIDRISVFGG 367
Cdd:cd13438  161 AQANLIRAREETAATRSLLNAAKLMEENPALLRLRELEALEKIAEKVGHISVSGG 215
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 489185372 190 VDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRLSKPLEYLYRELQFGLRAAVGTRTLDELLENKQSIDEA 269
Cdd:cd13434    1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80

                         90       100
                 ....*....|....*....|....*..
gi 489185372 270 VSAHLAAKLEDSGLEVSGLGVRDIILP 296
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDIILP 107
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 151-323 2.06e-24

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: 98.55  E-value: 2.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372  151 VQVPAFQVGVLKVDGALAGLLQAGQYGFWRYNRqvSVELVDTRIQALEVSGQEILTRDKVSLRLNLAANWR--YNDVLTA 228
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQ--RVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRvnPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372  229 FSRLSKP---LEYLYRELQFGLRAAVGTRTLDELLENKQSIDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQ 305
Cdd:pfam01145  79 VQNVFGSddlQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158

                         170
                  ....*....|....*...
gi 489185372  306 VVEAEKAAQANVIRRREE 323
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAE 176
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 190-356 1.24e-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 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: 96.43  E-value: 1.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 190 VDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRLSkplEYLYRELQFG---LRAAVGTRTLDELLENKQSI 266
Cdd:cd08826    9 VDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVE---DYRYATSQLAqttLRSVVGQVELDELLSEREEI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 267 DEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEKAAQANVIRRREETSATRSLLNTAKVMEENPTALRL 346
Cdd:cd08826   86 NKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSPGALQL 165

                        170
                 ....*....|
gi 489185372 347 KELETLERVA 356
Cdd:cd08826  166 RYLQTLSEIA 175
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 190-365 4.55e-22

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: 92.83  E-value: 4.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 190 VDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRLSKPLEYLYRELQFGLRAAVGTRTLDELLENKQSIDEA 269
Cdd:cd13435   22 VDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGTRNLSELLTERETISHS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 270 VSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEKAAQANVIRRREETSATRSLLNTAKVMEENPTALRLKEL 349
Cdd:cd13435  102 MQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRALKEASDIISASPSALQLRYL 181

                        170
                 ....*....|....*.
gi 489185372 350 ETLERVAERIDRISVF 365
Cdd:cd13435  182 QTLSSISGEKNSTIIF 197
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 190-365 8.93e-19

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: 83.75  E-value: 8.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 190 VDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRLSKPLEYLYRELQFGLRAAVGTRTLDELLENKQSIDEA 269
Cdd:cd03403   22 VDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGTKNLSEILSDRETISHQ 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 270 VSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEKAAQANVIRRREETSATRSLLNTAKVMEENPTALRLKEL 349
Cdd:cd03403  102 MQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRALKEAADVISESPAALQLRYL 181

                        170
                 ....*....|....*.
gi 489185372 350 ETLERVAERIDRISVF 365
Cdd:cd03403  182 QTLNTISAEKNSTIIF 197
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 190-347 2.95e-18

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: 81.52  E-value: 2.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 190 VDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRLSKPLEYLYRELQFGLRAAVGTRTLDELLENKQSIDEA 269
Cdd:cd13775    1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489185372 270 VSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEKAAQANVIRRREETSATRSLLNTAKVMEENPTALRLK 347
Cdd:cd13775   81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLR 158
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 186-319 4.47e-18

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 83.35  E-value: 4.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 186 SVELVDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRLSKPLEYLYRELQFGLRAAVGTRTLDELL-ENKQ 264
Cdd:COG0330   55 RVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLsTGRD 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489185372 265 SIDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEKAAQANVIR 319
Cdd:COG0330  135 EINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILE 189
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 169-357 3.35e-17

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: 79.58  E-value: 3.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 169 GLLQAgqygFWRYNRQV------------SVELVDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRLSKpL 236
Cdd:cd13437   15 GLVER----FGKFYKTVdpglhkvnpcteKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRIDN-V 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 237 EYLYREL-QFGLRAAVGTRTLDELLENKQSIDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEKAAQA 315
Cdd:cd13437   90 KQALIERtQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIGES 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489185372 316 NVIRRREETSATRsLLNTAKVMEENPTALRLKELETLERVAE 357
Cdd:cd13437  170 KIISAKADVESAK-LMREAADILDSKAAMQIRYLETLQAIAK 210
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 190-353 1.07e-14

Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Podocin is expressed in the kidney and mutations in the gene have been linked to familial idiopathic nephrotic syndrome. Podocin interacts with the TRP ion channel TRPV-6 and may function as a scaffolding protein in the organization of lipid-protein domains.


Pssm-ID: 259809 [Multi-domain]  Cd Length: 223  Bit Score: 72.61  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 190 VDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDV---LTAFSRLSKPLEYLyreLQFGLRAAVGTRTLDELLENKQSI 266
Cdd:cd08827   44 VDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAsvcLSSFASISDAMQAL---VQTTVKRLLAHRAFTDILLERKSI 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 267 DEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEKAAQANVIRRREETSATRSLLNTAKVMEENPTALRL 346
Cdd:cd08827  121 AQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQL 200


                 ....*..
gi 489185372 347 KELETLE 353
Cdd:cd08827  201 RYLHTLQ 207
PHB smart00244
prohibitin homologues; prohibitin homologues
 187-307 2.56e-14

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 70.00  E-value: 2.56e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372   187 VELVDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVL-TAFSRLSKPLEYLYRELQFGLRAAVGTRTLDELLE-NKQ 264
Cdd:smart00244  38 VKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLrAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDELLTdQRE 117

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 489185372   265 SIDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVV 307
Cdd:smart00244 118 KISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQQ 160
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 190-326 1.05e-12

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: 65.44  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 190 VDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRLSKPLEYLYRELQFGLRAAVGTRTLDELLENKQSIDEA 269
Cdd:cd08828   18 VDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGTQTLAQILAGREEIAHS 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489185372 270 VSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEKAAQANVIRRREETSA 326
Cdd:cd08828   98 IQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 190-296 6.61e-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: 55.94  E-value: 6.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 190 VDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLTAFSRLSKPLEYLYRELQFGLRAAVGTRTLDELLENKQSIDEA 269
Cdd:cd08829    4 VDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAK 83

                         90       100
                 ....*....|....*....|....*..
gi 489185372 270 VSAHLAAKLEDSGLEVSGLGVRDIILP 296
Cdd:cd08829   84 LLEALDEATDPWGVKVTRVEIKDITPP 110
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 186-328 2.91e-09

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: 57.11  E-value: 2.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 186 SVELVDTRIQALEVSGQEILTRDKVSLRLNLAANWRYNDVLT----------AFSRLSkplEYLYRElqfgLRAAVGTRT 255
Cdd:cd03405   37 NVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRfyqsvggeegAESRLD---DIVDSA----LRNEIGKRT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 256 LDELLENKQS-IDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGE--------MKTLLAQVVE---AEKAAQANVIRRREE 323
Cdd:cd03405  110 LAEVVSGGRDeLMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEvsesvyerMRAERERIAAeyrAEGEEEAEKIRAEAD 189


                 ....*
gi 489185372 324 TSATR 328
Cdd:cd03405  190 RERTV 194
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 193-296 4.64e-09

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: 53.52  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 193 RIQALEVSGQEILTRDKVSLRLNLAANWRYNDV--LTAFSRLSKPLEY---LYRELQFGLRAAVGTRTLDELLENKQSID 267
Cdd:cd02106    1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYnaLPAFYLVDFVKDIkadIRRKIADVLRAAIGRMTLDQIISGRDEIA 80

                         90       100
                 ....*....|....*....|....*....
gi 489185372 268 EAVSAHLAAKLEDSGLEVSGLGVRDIILP 296
Cdd:cd02106   81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 186-328 9.60e-06

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: 45.97  E-value: 9.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 186 SVELVDTRIQALEVSgQEILTRDKVSLRLNLAANWRYNDvltafsrlsKPLEYLYRElqFG---------------LRAA 250
Cdd:cd03401   37 VVIIYDVRTQPREIT-LTVLSKDGQTVNIDLSVLYRPDP---------EKLPELYQN--LGpdyeervlppivrevLKAV 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489185372 251 VGTRTLDELLENKQSIDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAE-KAAQANVIRRREETSATR 328
Cdd:cd03401  105 VAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAKQVAEqEAERAKFELEKAEQEAER 183
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 190-322 1.54e-05

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: 46.04  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 190 VDTRIQALEVSgQEILTRDKVSLRLNLAANWRYND--VLTAFSRLSKPLE----YLYRELqfglRAAVGTRTLDELLENK 263
Cdd:cd03407   38 VSLRVQQLDVR-VETKTKDNVFVTLVVSVQYRVVPekVYDAFYKLTNPEQqiqsYVFDVV----RASVPKLTLDEVFESK 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489185372 264 QSIDEAVSAHLAAKLEDSGLEVSGLGVRDIILPGEMKTLLAQVVEAEkaaqanviRRRE 322
Cdd:cd03407  113 DEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQ--------RLRE 163
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
187-326 5.39e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.70  E-value: 5.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489185372 187 VELVDTRIQALEVS-GQEILTRDKVSLRLNLAANWRYN----DVLTAFSR-LSKPLEYLYRELQ---FG-LRAAVGTRTL 256
Cdd:COG2268   63 AERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNsdpeDIANAAERfLGRDPEEIEELAEeklEGaLRAVAAQMTV 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489185372 257 DELLENKQSIDEAVSAHLAAKLEDSGLEVSGLGVRDI-----ILPGEMKTLLAQVVEAEKAAQANVIRRREETSA 326
Cdd:COG2268  143 EELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLedennYLDALGRRKIAEIIRDARIAEAEAERETEIAIA 217
 
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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