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Conserved domains on  [gi|224908506|gb|ACN67101|]
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nephrosis 2-like protein [Mus musculus]

Protein Classification

SPFH domain-containing protein; flotillin family protein( domain architecture ID 10172174)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein| flotillin family protein may act as a scaffolding protein within caveolar membranes, functionally participating in the formation of caveolae or caveolae-like vesicles

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
134-356 3.48e-149

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: 421.22  E-value: 3.48e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 134 WFCIKVVQEYERVIIFRLGHLLPGRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENAS 213
Cdd:cd08827    1 WFCVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 214 LLLSSLAHVSKAIQFLVQTTMKRLLAHRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLAVE 293
Cdd:cd08827   81 VCLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224908506 294 AEAQRQAKVRVIAAEGEKAASESLRMAAEILSGTPAAVQLRYLHTLQSLSTEKPATVVLPLPF 356
Cdd:cd08827  161 AEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLPF 223
 
Name Accession Description Interval E-value
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
134-356 3.48e-149

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: 421.22  E-value: 3.48e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 134 WFCIKVVQEYERVIIFRLGHLLPGRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENAS 213
Cdd:cd08827    1 WFCVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 214 LLLSSLAHVSKAIQFLVQTTMKRLLAHRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLAVE 293
Cdd:cd08827   81 VCLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224908506 294 AEAQRQAKVRVIAAEGEKAASESLRMAAEILSGTPAAVQLRYLHTLQSLSTEKPATVVLPLPF 356
Cdd:cd08827  161 AEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLPF 223
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
116-353 1.92e-41

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 147.29  E-value: 1.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 116 LLVLASLIFIIMTfpfsIWFCIKVVQEYERVIIFRLGHLLpgRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKD 195
Cdd:COG0330    4 ILLLILLVLVLVL----LFSSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 196 MFIMEIDAVCYYRMENASLLLSSLAHVSKAIQFLVQTTMKRLLAHRSLTEILLE-RKSIAQDVKVALDAVTCIWGIKVER 274
Cdd:COG0330   78 NNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 275 TEIKDVRLPAGLQHSLA-------------VEAEAQRQAKV---------RVIAAEGEKAA--------SESLRMAAEIL 324
Cdd:COG0330  158 VEIKDIDPPEEVQDAMEdrmkaerereaaiLEAEGYREAAIiraegeaqrAIIEAEAYREAqilraegeAEAFRIVAEAY 237
                        250       260
                 ....*....|....*....|....*....
gi 224908506 325 SGTPAAVQLRYLHTLQSLSTEKPATVVLP 353
Cdd:COG0330  238 SAAPFVLFYRSLEALEEVLSPNSKVIVLP 266
PHB smart00244
prohibitin homologues; prohibitin homologues
135-299 1.23e-30

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 115.07  E-value: 1.23e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506   135 FCIKVVQEYERVIIFRLGHLLpgRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENAsl 214
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDP-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506   215 lLSSLAHVS----KAIQFLVQTTMKRLLAHRSLTEIL-LERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQhs 289
Cdd:smart00244  77 -LRAVYRVLdadyAVIEQLAQTTLRSVIGKRTLDELLtDQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK-- 153
                          170
                   ....*....|
gi 224908506   290 lavEAEAQRQ 299
Cdd:smart00244 154 ---EAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
138-311 2.27e-29

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: 112.03  E-value: 2.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506  138 KVVQEYERVIIFRLGhlLPGRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRM--ENASLL 215
Cdd:pfam01145   1 IIVPPGEVGVVTRFG--KLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506  216 LSSLAHVSKAIQFL---VQTTMKRLLAHRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLAV 292
Cdd:pfam01145  79 VQNVFGSDDLQELLrrvLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158
                         170
                  ....*....|....*....
gi 224908506  293 EAEAQRQAKVRVIAAEGEK 311
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAEA 177
PRK11029 PRK11029
protease modulator HflC;
121-322 1.75e-06

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 49.35  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 121 SLIFIIMTFPFSIWFCIKVVQEYERVIIFRLGHLLPGRAK-----GPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKD 195
Cdd:PRK11029   4 SVIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADRFVTKE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 196 MFIMEIDAVCYYRMENASL--LLSSLAHVSKAiqflvQTTMKRLLAHRSLTEI-LLERKSIAQD--------VKVALDAV 264
Cdd:PRK11029  84 KKDLIVDSYIKWRISDFSRyyLATGGGDISQA-----EVLLKRKFSDRLRSEIgRLDVKDIVTDsrgrltldVRDALNSG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 265 T--------------------------------CI-------WGIKVERTEIKDVRLPAGLQHSLAVEAEAQRQAKVRVI 305
Cdd:PRK11029 159 SagtedevatpaaddaiasaaerveaetkgkvpVInpnsmaaLGIEVVDVRIKQINLPTEVSDAIYNRMRAEREAVARRH 238
                        250
                 ....*....|....*..
gi 224908506 306 AAEGEKAAsESLRMAAE 322
Cdd:PRK11029 239 RSQGQEEA-EKLRATAD 254
 
Name Accession Description Interval E-value
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
134-356 3.48e-149

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: 421.22  E-value: 3.48e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 134 WFCIKVVQEYERVIIFRLGHLLPGRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENAS 213
Cdd:cd08827    1 WFCVKVVREYERAVIFRLGHLLQGRARGPGLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 214 LLLSSLAHVSKAIQFLVQTTMKRLLAHRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLAVE 293
Cdd:cd08827   81 VCLSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224908506 294 AEAQRQAKVRVIAAEGEKAASESLRMAAEILSGTPAAVQLRYLHTLQSLSTEKPATVVLPLPF 356
Cdd:cd08827  161 AEAQRQAKVKVIAAEGEKAASEALKAAAESLSGSPLAMQLRYLHTLQSLRSEKPSTVVLPLPF 223
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
156-357 2.71e-77

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: 237.45  E-value: 2.71e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 156 PGRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENASLLLSSLAHVSKAIQFLVQTTMK 235
Cdd:cd03403    1 PGGAKGPGLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 236 RLLAHRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLAVEAEAQRQAKVRVIAAEGEKAASE 315
Cdd:cd03403   81 NVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASR 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 224908506 316 SLRMAAEILSGTPAAVQLRYLHTLQSLSTEKPATVVLPLPFD 357
Cdd:cd03403  161 ALKEAADVISESPAALQLRYLQTLNTISAEKNSTIIFPLPID 202
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
157-360 1.74e-75

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: 233.04  E-value: 1.74e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 157 GRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENASLLLSSLAHVSKAIQFLVQTTMKR 236
Cdd:cd13435    2 GGARGPGVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 237 LLAHRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLAVEAEAQRQAKVRVIAAEGEKAASES 316
Cdd:cd13435   82 VLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRA 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 224908506 317 LRMAAEILSGTPAAVQLRYLHTLQSLSTEKPATVVLPLPFDMLS 360
Cdd:cd13435  162 LKEASDIISASPSALQLRYLQTLSSISGEKNSTIIFPLPMELLT 205
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
169-346 4.78e-51

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: 169.23  E-value: 4.78e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 169 PCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENASLLLSSLAHVSKAIQFLVQTTMKRLLAHRSLTEILL 248
Cdd:cd08826    1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 249 ERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLAVEAEAQRQAKVRVIAAEGEKAASESLRMAAEILSGTP 328
Cdd:cd08826   81 EREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLAEAAEILAKSP 160
                        170
                 ....*....|....*...
gi 224908506 329 AAVQLRYLHTLQSLSTEK 346
Cdd:cd08826  161 GALQLRYLQTLSEIASEK 178
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
160-313 1.66e-48

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: 161.74  E-value: 1.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 160 KGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENASLLLSSLAHVSKAIQFLVQTTMKRLLA 239
Cdd:cd08828    1 KGPGLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224908506 240 HRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLAVEAEAQRQAKVRVIAAEGEKAA 313
Cdd:cd08828   81 TQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
158-357 3.10e-47

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: 160.47  E-value: 3.10e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 158 RAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENASLLLSSLAHVSKAIQFLVQTTMKRL 237
Cdd:cd13437   25 KTVDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRIDNVKQALIERTQTTLRSV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 238 LAHRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLAVEAEAQRQAKVRVIAAEGEKAASESL 317
Cdd:cd13437  105 IGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAKRIGESKIISAKADVESAKLM 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 224908506 318 RMAAEILSgTPAAVQLRYLHTLQSLSTEKPATVVLpLPFD 357
Cdd:cd13437  185 REAADILD-SKAAMQIRYLETLQAIAKSANSKVIF-LPLD 222
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
177-284 5.93e-45

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: 150.81  E-value: 5.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 177 VDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENASLLLSSLAHVSKAIQFLVQTTMKRLLAHRSLTEILLERKSIAQD 256
Cdd:cd13434    1 VDLRTQSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQ 80
                         90       100
                 ....*....|....*....|....*...
gi 224908506 257 VKVALDAVTCIWGIKVERTEIKDVRLPA 284
Cdd:cd13434   81 LQEILDEATDPWGIKVERVEIKDIILPQ 108
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
116-353 1.92e-41

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 147.29  E-value: 1.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 116 LLVLASLIFIIMTfpfsIWFCIKVVQEYERVIIFRLGHLLpgRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKD 195
Cdd:COG0330    4 ILLLILLVLVLVL----LFSSVYIVPQGERGVVLRFGKYV--RTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 196 MFIMEIDAVCYYRMENASLLLSSLAHVSKAIQFLVQTTMKRLLAHRSLTEILLE-RKSIAQDVKVALDAVTCIWGIKVER 274
Cdd:COG0330   78 NNIVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 275 TEIKDVRLPAGLQHSLA-------------VEAEAQRQAKV---------RVIAAEGEKAA--------SESLRMAAEIL 324
Cdd:COG0330  158 VEIKDIDPPEEVQDAMEdrmkaerereaaiLEAEGYREAAIiraegeaqrAIIEAEAYREAqilraegeAEAFRIVAEAY 237
                        250       260
                 ....*....|....*....|....*....
gi 224908506 325 SGTPAAVQLRYLHTLQSLSTEKPATVVLP 353
Cdd:COG0330  238 SAAPFVLFYRSLEALEEVLSPNSKVIVLP 266
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
177-353 5.05e-31

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: 116.57  E-value: 5.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 177 VDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENASLLLSSLAHVSKAIQFLVQTTMKRLLAHRSLTEILLERKSIAQD 256
Cdd:cd13775    1 VDQRIRTTPFSAEQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 257 VKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLAVEAEAQRQAKVRVIAAEGEKAASESLRMAAEILSGTPAAVQLRYL 336
Cdd:cd13775   81 LQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEIAEMFVEAAEVYENNPIALQLRAM 160
                        170
                 ....*....|....*..
gi 224908506 337 HTLQSLSTEKPATVVLP 353
Cdd:cd13775  161 NMLYEGLKEKGSMVVVP 177
PHB smart00244
prohibitin homologues; prohibitin homologues
135-299 1.23e-30

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 115.07  E-value: 1.23e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506   135 FCIKVVQEYERVIIFRLGHLLpgRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENAsl 214
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVL--RVLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDP-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506   215 lLSSLAHVS----KAIQFLVQTTMKRLLAHRSLTEIL-LERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQhs 289
Cdd:smart00244  77 -LRAVYRVLdadyAVIEQLAQTTLRSVIGKRTLDELLtDQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIK-- 153
                          170
                   ....*....|
gi 224908506   290 lavEAEAQRQ 299
Cdd:smart00244 154 ---EAMEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
138-311 2.27e-29

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: 112.03  E-value: 2.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506  138 KVVQEYERVIIFRLGhlLPGRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRM--ENASLL 215
Cdd:pfam01145   1 IIVPPGEVGVVTRFG--KLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506  216 LSSLAHVSKAIQFL---VQTTMKRLLAHRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLAV 292
Cdd:pfam01145  79 VQNVFGSDDLQELLrrvLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEA 158
                         170
                  ....*....|....*....
gi 224908506  293 EAEAQRQAKVRVIAAEGEK 311
Cdd:pfam01145 159 KQTAEQEAEAEIARAEAEA 177
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
175-284 1.06e-23

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: 94.46  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 175 YKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENASLLLSSLAHVSKAIQFLVQTTMKRLLAHRSLTEILLERKSIA 254
Cdd:cd08829    2 YKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEIN 81
                         90       100       110
                 ....*....|....*....|....*....|
gi 224908506 255 QDVKVALDAVTCIWGIKVERTEIKDVRLPA 284
Cdd:cd08829   82 AKLLEALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
157-282 2.89e-23

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: 94.00  E-value: 2.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 157 GRA---KGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENASLLLSSLAHVSKAIQFLVQTT 233
Cdd:cd13436    1 GRLqkpRGPGIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 224908506 234 MKRLLAHRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRL 282
Cdd:cd13436   81 LTNSLSKKTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSDVKV 129
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
140-355 3.41e-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: 96.45  E-value: 3.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 140 VQEYERVIIFRLGHLlpGRAKGPGLFFF--LPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENASLLLS 217
Cdd:cd13438    1 VPPGERGLLYRDGKL--VRTLEPGRYAFwkFGRKVQVELVDLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 218 SLAHVSKAIQFLVQTTMKRLLAHRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLAVEAEAQ 297
Cdd:cd13438   79 TVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAE 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 224908506 298 RQAKVRVIAAEGEKAASESLRMAAEILSGTPAAVQLRYLHTLqslstEKPATVVLPLP 355
Cdd:cd13438  159 KRAQANLIRAREETAATRSLLNAAKLMEENPALLRLRELEAL-----EKIAEKVGHIS 211
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
136-325 1.44e-18

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: 84.46  E-value: 1.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 136 CIKVVQEYERVIIFRLGHLLpGRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENASLL 215
Cdd:cd03405    1 SVFIVDETEQAVVLQFGKPV-RVITEPGLHFKLPFIQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 216 LSSLAHVSKAIQFL---VQTTMKRLLAHRSLTEIL-LERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHSLA 291
Cdd:cd03405   80 YQSVGGEEGAESRLddiVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESVY 159
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 224908506 292 VEAEAQRQAKVRVIAAEGEKAA----SESLRMAAEILS 325
Cdd:cd03405  160 ERMRAERERIAAEYRAEGEEEAekirAEADRERTVILA 197
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
137-313 9.23e-18

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: 80.64  E-value: 9.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 137 IKVVQEYERVIIFRLGHLLPGRAKGPGLFFFLPCLDTYYKVDLRLQTLEIPFhEVVTKDMFIMEIDAVCYYRM--ENASL 214
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITL-TVLSKDGQTVNIDLSVLYRPdpEKLPE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 215 LLSSL--AHVSKAIQFLVQTTMKRLLAHRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHslAV 292
Cdd:cd03401   80 LYQNLgpDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEK--AI 157
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 224908506 293 EA------EAQR----------QAKVRVIAAEGEKAA 313
Cdd:cd03401  158 EAkqvaeqEAERakfelekaeqEAERKVIEAEGEAEA 194
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
115-315 7.23e-13

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: 67.92  E-value: 7.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 115 WLLVLASLIFIIMTFpfsiwfciKVVQEYERVIIFRLGHLLpgRAKGPGLFFFLPC-LDTYYKVDL-RLQTLEIPFH--- 189
Cdd:cd03404    1 LILLLLLLVWLLSGF--------YTVDPGERGVVLRFGKYV--RTVGPGLHWKLPFpIEVVEKVNVtQVRSVEIGFRvpe 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 190 --EVVTKDMFIMEIDAVCYYRMENASLLLSSLAHVSKAIQFLVQTTMKRLLAHRSLTEILLERKS-IAQDVKVA----LD 262
Cdd:cd03404   71 esLMLTGDENIVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEGRAeIAADVRELlqeiLD 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 224908506 263 AVTCiwGIKVERTEIKDVRLPAGLQHSLAvEAEAQRQAKVRVIaAEGEKAASE 315
Cdd:cd03404  151 RYDL--GIEIVQVQLQDADPPEEVQDAFD-DVNAARQDKERLI-NEAQAYANE 199
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
139-322 3.75e-09

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: 57.21  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 139 VVQEYERVIIFRLGHLLpgRAKGPGLFFFLPCLDTYY-KVDLRLQTLEIPFhEVVTKD-MFIMeIDAVCYYRM--ENASL 214
Cdd:cd03407    1 CVSQSTVAIVERFGKFS--RIAEPGLHFIIPPIESVAgRVSLRVQQLDVRV-ETKTKDnVFVT-LVVSVQYRVvpEKVYD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 215 LLSSLAHVSKAIQFLVQTTMKRLLAHRSLTEILLERKSIAQDVKVALDAVTCIWGIKVERTEIKDVRLPAGLQHS----- 289
Cdd:cd03407   77 AFYKLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAmnein 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 224908506 290 ------LAVE--AEAQRQAKVRviAAEGEKaasESLRMAAE 322
Cdd:cd03407  157 aaqrlrEAAEekAEAEKILQVK--AAEAEA---EAKRLQGV 192
PRK11029 PRK11029
protease modulator HflC;
121-322 1.75e-06

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 49.35  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 121 SLIFIIMTFPFSIWFCIKVVQEYERVIIFRLGHLLPGRAK-----GPGLFFFLPCLDTYYKVDLRLQTLEIPFHEVVTKD 195
Cdd:PRK11029   4 SVIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVLRDDDNkplvyAPGLHFKIPFIETVKMLDARIQTMDNQADRFVTKE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 196 MFIMEIDAVCYYRMENASL--LLSSLAHVSKAiqflvQTTMKRLLAHRSLTEI-LLERKSIAQD--------VKVALDAV 264
Cdd:PRK11029  84 KKDLIVDSYIKWRISDFSRyyLATGGGDISQA-----EVLLKRKFSDRLRSEIgRLDVKDIVTDsrgrltldVRDALNSG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 265 T--------------------------------CI-------WGIKVERTEIKDVRLPAGLQHSLAVEAEAQRQAKVRVI 305
Cdd:PRK11029 159 SagtedevatpaaddaiasaaerveaetkgkvpVInpnsmaaLGIEVVDVRIKQINLPTEVSDAIYNRMRAEREAVARRH 238
                        250
                 ....*....|....*..
gi 224908506 306 AAEGEKAAsESLRMAAE 322
Cdd:PRK11029 239 RSQGQEEA-EKLRATAD 254
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
180-283 6.56e-06

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: 44.66  E-value: 6.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224908506 180 RLQTLEIPFHEVVTKDMFIMEIDAVCYYRMENASLL----LSSLAHVSKA-IQFLVQTTMKRLLAHRSLTEILLERKSIA 254
Cdd:cd02106    1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafyLVDFVKDIKAdIRRKIADVLRAAIGRMTLDQIISGRDEIA 80
                         90       100
                 ....*....|....*....|....*....
gi 224908506 255 QDVKVALDAVTCIWGIKVERTEIKDVRLP 283
Cdd:cd02106   81 KAVKEDLEEDLENFGVVISDVDITSIEPP 109
 
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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