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Conserved domains on  [gi|528509224|ref|XP_005159498|]
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flotillin-1a isoform X1 [Danio rerio]

Protein Classification

flotillin family protein( domain architecture ID 11455184)

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
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1-418 7.64e-93

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


:

Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 286.77  E-value: 7.64e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224   1 MFYTCGPNEAMVVSGFCRSPPVmISGGRVFVFPCVQQIQRISLNTLTLNVK-SDKVYTRHGVPISVTGIAQMKIQGQNKQ 79
Cdd:COG2268   27 FYRKVPPNEALVITGRGGGYKV-VTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNSDPED 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  80 MLAAAcQMFLGKSDSEIAHIALETLEGHQRAIIAHLTVEEIYKDRKKFSEQVFKVASSDLVNMGISVVSYTLKDVHDDQD 159
Cdd:COG2268  106 IANAA-ERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENN 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 160 YLHSLGKARTAQVQKDARIGEAKNKRDAVIREAHAMQEKVSAQYMNEIE-----MAKAQRDYELKKAIYDIEVFTKKAES 234
Cdd:COG2268  185 YLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEA 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 235 EMAYQLQVAKTKQRIEeekMQVLVVERSQQITLQEQEISRKEKELEAKVKKPAEAERYRLEKlaeaerlqlimEAEAEAE 314
Cdd:COG2268  265 EAAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEA-----------EAEAEAE 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 315 SIRvrgeaeayaveAKGRAEAEQMAKKAEAFQHYKEGAMVDMLLEKLPMMADEISKPLSATNKVTMVSSGGSEIGAAKLt 394
Cdd:COG2268  331 AIR-----------AKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA- 398

                        410       420
                 ....*....|....*....|....
gi 528509224 395 geVLDIMTKLPETIEKLTGVNISQ 418
Cdd:COG2268  399 --VAEALAPLLESLLEETGLDLPG 420
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1-418 7.64e-93

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 286.77  E-value: 7.64e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224   1 MFYTCGPNEAMVVSGFCRSPPVmISGGRVFVFPCVQQIQRISLNTLTLNVK-SDKVYTRHGVPISVTGIAQMKIQGQNKQ 79
Cdd:COG2268   27 FYRKVPPNEALVITGRGGGYKV-VTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNSDPED 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  80 MLAAAcQMFLGKSDSEIAHIALETLEGHQRAIIAHLTVEEIYKDRKKFSEQVFKVASSDLVNMGISVVSYTLKDVHDDQD 159
Cdd:COG2268  106 IANAA-ERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENN 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 160 YLHSLGKARTAQVQKDARIGEAKNKRDAVIREAHAMQEKVSAQYMNEIE-----MAKAQRDYELKKAIYDIEVFTKKAES 234
Cdd:COG2268  185 YLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEA 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 235 EMAYQLQVAKTKQRIEeekMQVLVVERSQQITLQEQEISRKEKELEAKVKKPAEAERYRLEKlaeaerlqlimEAEAEAE 314
Cdd:COG2268  265 EAAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEA-----------EAEAEAE 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 315 SIRvrgeaeayaveAKGRAEAEQMAKKAEAFQHYKEGAMVDMLLEKLPMMADEISKPLSATNKVTMVSSGGSEIGAAKLt 394
Cdd:COG2268  331 AIR-----------AKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA- 398

                        410       420
                 ....*....|....*....|....
gi 528509224 395 geVLDIMTKLPETIEKLTGVNISQ 418
Cdd:COG2268  399 --VAEALAPLLESLLEETGLDLPG 420
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 30-175 2.76e-62

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: 197.73  E-value: 2.76e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  30 FVFPCVQQIQRISLNTLTLNVKSDKVYTRHGVPISVTGIAQMKIqGQNKQMLAAACQMFLGKSDSEIAHIALETLEGHQR 109
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKV-GSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528509224 110 AIIAHLTVEEIYKDRKKFSEQVFKVASSDLVNMGISVVSYTLKDVHDDQDYLHSLGKARTAQVQKD 175
Cdd:cd03399   80 AIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 3-185 4.75e-21

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: 89.69  E-value: 4.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224    3 YTCGPNEAMVVSGFCRSPPVmISGGRVFVFPCVQQIQRISLNTLTLNVKSDKVYTRHGVPISVTGIAQMKIQGQNKQMLA 82
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRV-LEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224   83 AACqmflgKSDSEIAHIALETLEGHQRAIIAHLTVEEIYKDRKKFSEQVFKVASSDLVNMGISVVSYTLKDVHDDQDYLH 162
Cdd:pfam01145  80 QNV-----FGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154

                         170       180
                  ....*....|....*....|...
gi 528509224  163 SLGKARTAQVQKDARIGEAKNKR 185
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 84-255 1.73e-14

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 70.77  E-value: 1.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224    84 ACQMFLGKSDSEIAHIALETLEghqRAIIAHLTVEEIYKDRKKfseqVFKVASSDLVNMGISVVSYTLKDVHDDQDYLHS 163
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224   164 LGKARTAQVQKDARIGEAKNKRDAVIREAHAmqekvsaqymnEIEMAKAQRDYELKKAIYDIEVFTKKAESeMAYQLQVA 243
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIG-----------KRTLDELLTDQREKISENIREELNEAAEA-WGIKVEDV 141

                          170
                   ....*....|..
gi 528509224   244 KTKQRIEEEKMQ 255
Cdd:smart00244 142 EIKDIRLPEEIK 153
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 168-358 1.87e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 49.80  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 168 RTAQVQKDARIGEAKNKRDAVIREAHAMQEK-VSAQYMNEIEMAKAQRDYELKKAI---YDIEVFTKKAESEMAYQLQVA 243
Cdd:PRK09510  66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQaAEQERLKQLEKERLAAQEQKKQAEeaaKQAALKQKQAEEAAAKAAAAA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 244 KTKQRIEEEKMQVLVVERSQQITLQEQEISRKEKELEAKVKKPAEAERY---RLEKLAEAE---RLQLIMEAEAEAESir 317
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKaaaEAKKKAEAEakkKAAAEAKKKAAAEA-- 223

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528509224 318 vRGEAEAYAVEAKGRAEAEQMAKKAEAFQHYKEGAMVDMLL 358
Cdd:PRK09510 224 -KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 166-357 4.51e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.22  E-value: 4.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  166 KARTAQVQKDARIGEAKNKRDAVIREAHAMQEKVSAQYMNEIEMAKAQRDYELKKAIYDIEvftKKAESEMAYQLQVAKT 245
Cdd:TIGR02794  48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE---QAAKQAEEKQKQAEEA 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  246 KQRIEEEKMQVLVVERSQQitlqEQEISRKEKELEAKVKKPAEAERYRLEKLAEAERLQlimEAEAEAESIRVRGEAEAY 325
Cdd:TIGR02794 125 KAKQAAEAKAKAEAEAERK----AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA---KAKAEAEAKAKAEEAKAK 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 528509224  326 A--------VEAKGRAEAEQ-MAKKAEAFQHYKEGAMVDML 357
Cdd:TIGR02794 198 AeaakakaaAEAAAKAEAEAaAAAAAEAERKADEAELGDIF 238
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1-418 7.64e-93

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 286.77  E-value: 7.64e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224   1 MFYTCGPNEAMVVSGFCRSPPVmISGGRVFVFPCVQQIQRISLNTLTLNVK-SDKVYTRHGVPISVTGIAQMKIQGQNKQ 79
Cdd:COG2268   27 FYRKVPPNEALVITGRGGGYKV-VTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNSDPED 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  80 MLAAAcQMFLGKSDSEIAHIALETLEGHQRAIIAHLTVEEIYKDRKKFSEQVFKVASSDLVNMGISVVSYTLKDVHDDQD 159
Cdd:COG2268  106 IANAA-ERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENN 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 160 YLHSLGKARTAQVQKDARIGEAKNKRDAVIREAHAMQEKVSAQYMNEIE-----MAKAQRDYELKKAIYDIEVFTKKAES 234
Cdd:COG2268  185 YLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEA 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 235 EMAYQLQVAKTKQRIEeekMQVLVVERSQQITLQEQEISRKEKELEAKVKKPAEAERYRLEKlaeaerlqlimEAEAEAE 314
Cdd:COG2268  265 EAAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEA-----------EAEAEAE 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 315 SIRvrgeaeayaveAKGRAEAEQMAKKAEAFQHYKEGAMVDMLLEKLPMMADEISKPLSATNKVTMVSSGGSEIGAAKLt 394
Cdd:COG2268  331 AIR-----------AKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA- 398

                        410       420
                 ....*....|....*....|....
gi 528509224 395 geVLDIMTKLPETIEKLTGVNISQ 418
Cdd:COG2268  399 --VAEALAPLLESLLEETGLDLPG 420
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 30-175 2.76e-62

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: 197.73  E-value: 2.76e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  30 FVFPCVQQIQRISLNTLTLNVKSDKVYTRHGVPISVTGIAQMKIqGQNKQMLAAACQMFLGKSDSEIAHIALETLEGHQR 109
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKV-GSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528509224 110 AIIAHLTVEEIYKDRKKFSEQVFKVASSDLVNMGISVVSYTLKDVHDDQDYLHSLGKARTAQVQKD 175
Cdd:cd03399   80 AIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 3-185 4.75e-21

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: 89.69  E-value: 4.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224    3 YTCGPNEAMVVSGFCRSPPVmISGGRVFVFPCVQQIQRISLNTLTLNVKSDKVYTRHGVPISVTGIAQMKIQGQNKQMLA 82
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRV-LEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224   83 AACqmflgKSDSEIAHIALETLEGHQRAIIAHLTVEEIYKDRKKFSEQVFKVASSDLVNMGISVVSYTLKDVHDDQDYLH 162
Cdd:pfam01145  80 QNV-----FGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154

                         170       180
                  ....*....|....*....|...
gi 528509224  163 SLGKARTAQVQKDARIGEAKNKR 185
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 84-255 1.73e-14

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 70.77  E-value: 1.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224    84 ACQMFLGKSDSEIAHIALETLEghqRAIIAHLTVEEIYKDRKKfseqVFKVASSDLVNMGISVVSYTLKDVHDDQDYLHS 163
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224   164 LGKARTAQVQKDARIGEAKNKRDAVIREAHAmqekvsaqymnEIEMAKAQRDYELKKAIYDIEVFTKKAESeMAYQLQVA 243
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIG-----------KRTLDELLTDQREKISENIREELNEAAEA-WGIKVEDV 141

                          170
                   ....*....|..
gi 528509224   244 KTKQRIEEEKMQ 255
Cdd:smart00244 142 EIKDIRLPEEIK 153
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 2-234 1.84e-11

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 64.48  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224   2 FYTCGPNEAMVVSGFCRspPVMISG-GRVFVFPCVQQIQRISLNTLTLNVKSDKVYTRHGVPISVTGIAQMKIQGQNKqm 80
Cdd:COG0330   21 VYIVPQGERGVVLRFGK--YVRTLEpGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAK-- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  81 laaacqmFLGKSDSEIAHIAlETLEGHQRAIIAHLTVEEIY-KDRKKFSEQVFKVASSDLVNMGISVVSYTLKDVHDDQD 159
Cdd:COG0330   97 -------FLYNVENAEEALR-QLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEE 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528509224 160 YLHSLGKARTAQVQKDARIGEAKNKRDAVIREAHAMQEKVsaqymneIEMAKAQRDYELKKAIYDIEVFTKKAES 234
Cdd:COG0330  169 VQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRA-------IIEAEAYREAQILRAEGEAEAFRIVAEA 236
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 47-158 1.15e-08

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: 52.75  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  47 TLNVKSDKVYTRHGVPISVTGIAQMKIQGQNkqmLAAACQMFLGKSDSEiAHIaLETLEGHQRAIIAHLTVEEIYKDRKK 126
Cdd:cd02106    4 FDDVRVEPVGTADGVPVAVDLVVQFRITDYN---ALPAFYLVDFVKDIK-ADI-RRKIADVLRAAIGRMTLDQIISGRDE 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 528509224 127 FSEQVFKVASSDLVNMGISVVSYTLKDVHDDQ 158
Cdd:cd02106   79 IAKAVKEDLEEDLENFGVVISDVDITSIEPPD 110
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 287-387 2.45e-07

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 51.76  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 287 AEAERYRLEKLAEAERLQLIMEAEAEAESIRVRGEAEAYAVEAKGRAEAEQMAKKAEAFQhykegAMVDMLLEKlpmMAD 366
Cdd:COG0330  179 AEREREAAILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYS-----AAPFVLFYR---SLE 250

                         90       100
                 ....*....|....*....|.
gi 528509224 367 EISKPLSATNKVTMVSSGGSE 387
Cdd:COG0330  251 ALEEVLSPNSKVIVLPPDGNG 271
Flot pfam15975
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ...
 308-385 9.55e-07

Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, archaea and eukaryotes. The family is found in association with pfam01145, another integral membrane-associated domain. Flotillins in vertebrates are associated with sphingolipids and cholesterol-enriched membrane microdomains known as lipid-rafts. These rafts along with other membrane components are important in cell-signalling. Flotillins in other organizms have roles in viral pathogenesis, endocytosis, and membrane shaping.


Pssm-ID: 435047 [Multi-domain]  Cd Length: 121  Bit Score: 47.32  E-value: 9.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  308 EAEAEAESIRVRGEaeayAVEAKGRAEAEQMAKKAEAFQHYKEGAMVDM----LLEKLPMMADEISKPLSATNKVTMVSS 383
Cdd:pfam15975   1 EAEAEADAIKLRAE----AKRKKALAEAEGIRALNEAENALSDEQIALQvklaLLEALPEIIAESVKPLEKIDGIKILQV 76


                  ..
gi 528509224  384 GG 385
Cdd:pfam15975  77 DG 78
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 168-358 1.87e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 49.80  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 168 RTAQVQKDARIGEAKNKRDAVIREAHAMQEK-VSAQYMNEIEMAKAQRDYELKKAI---YDIEVFTKKAESEMAYQLQVA 243
Cdd:PRK09510  66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQaAEQERLKQLEKERLAAQEQKKQAEeaaKQAALKQKQAEEAAAKAAAAA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 244 KTKQRIEEEKMQVLVVERSQQITLQEQEISRKEKELEAKVKKPAEAERY---RLEKLAEAE---RLQLIMEAEAEAESir 317
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKaaaEAKKKAEAEakkKAAAEAKKKAAAEA-- 223

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528509224 318 vRGEAEAYAVEAKGRAEAEQMAKKAEAFQHYKEGAMVDMLL 358
Cdd:PRK09510 224 -KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
PTZ00121 PTZ00121
MAEBL; Provisional
 180-370 1.03e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  180 EAKNKRDAVIREAHAMQEKvSAQYMNEIEMAKAqrdyELKKAIYDIEVFTKKAEsemAYQLQVAKTKQRIEEEKMQVLVV 259
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKK-AEEAKKAAEAAKA----EAEAAADEAEAAEEKAE---AAEKKKEEAKKKADAAKKKAEEK 1390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  260 ERSQQITLQEQEISRKEKEleakVKKPAEAERYRLEKLAEAERLQLIMEAEAEAESIRVRGEAEAYAVEAKGRAEAEQMA 339
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADE----LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466

                         170       180       190
                  ....*....|....*....|....*....|.
gi 528509224  340 KKAEAFQHYKEGAMVDMLLEKLPMMADEISK 370
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKK 1497
PRK12704 PRK12704
phosphodiesterase; Provisional
 176-348 1.27e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.47  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 176 ARIGEAKNKRDAVIREAhamqeKVSAQYMNEIEMAKAQRDYELKKAIYDIEVftKKAESEMAYQLQVAKTKQRIEEEKMQ 255
Cdd:PRK12704  31 AKIKEAEEEAKRILEEA-----KKEAEAIKKEALLEAKEEIHKLRNEFEKEL--RERRNELQKLEKRLLQKEENLDRKLE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 256 vLVVERSQQITLQEQEISRKEKELEAKVKKPAEAERYRLEKL-------AEAERLQLI--MEAEAEAESIRVRGEAEAya 326
Cdd:PRK12704 104 -LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisgltAEEAKEILLekVEEEARHEAAVLIKEIEE-- 180

                        170       180
                 ....*....|....*....|....
gi 528509224 327 vEAKgrAEAEQMAKK--AEAFQHY 348
Cdd:PRK12704 181 -EAK--EEADKKAKEilAQAIQRC 201
PTZ00121 PTZ00121
MAEBL; Provisional
 164-350 1.31e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  164 LGKARTAQVQKDARIGEAKNKRDAV-----IREAHAMQEKVSAQYMNEIEMAKAQRDYELKKA-------IYDIEVFTKK 231
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELkkaeeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeearieeVMKLYEEEKK 1606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  232 AESEMAYQLQVAKTK----QRIEEEKMQVLVVERSQQITLQEQEISRKEKElEAKVKKPAEAERYRLEKlAEAERLQLIM 307
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKaeelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-ENKIKAAEEAKKAEEDK-KKAEEAKKAE 1684

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 528509224  308 EAEAEAESIRVRGEAEAYAVEAKGRAEAEQMaKKAEAFQHYKE 350
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEK-KKAEELKKAEE 1726
PTZ00121 PTZ00121
MAEBL; Provisional
 166-343 1.33e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  166 KARTAQVQKDARIGEAKNKRDAV-----IREAHAMQEKvsAQYMNEIEMAKAQRDYELKKAiydiEVFTKKAEsEMAYQL 240
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEAkkaeeKKKADEAKKK--AEEAKKADEAKKKAEEAKKKA----DAAKKKAE-EAKKAA 1345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  241 QVAKTKQRIEEEKMQVlVVERSQQITLQEQEISRKEKELEAK---VKKPAEAERYRLEKLAEAERLQLIMEAEAEAESIR 317
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEA-AEEKAEAAEKKKEEAKKKADAAKKKaeeKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424

                         170       180       190
                  ....*....|....*....|....*....|
gi 528509224  318 VRGEAEAYAVEAKGRAE----AEQMAKKAE 343
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEeakkADEAKKKAE 1454
PTZ00121 PTZ00121
MAEBL; Provisional
 166-357 1.60e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  166 KARTAQVQKDARIGEAKNKRDavirEAHAMQEKVSAQYMNEIEmAKAQRDYELKKA--IYDIEVFTKKAESEMAYQLQVA 243
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAAD----EAEAAEEKAEAAEKKKEE-AKKKADAAKKKAeeKKKADEAKKKAEEDKKKADELK 1411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  244 KT---KQRIEEEKMQVLVVERSQQITLQEQEiSRKEKELeakvKKPAEAERYRLEKLAEAERLQLIMEAEAEAESIRVRG 320
Cdd:PTZ00121 1412 KAaaaKKKADEAKKKAEEKKKADEAKKKAEE-AKKADEA----KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 528509224  321 EAEAYAVEAKGRAE----AEQMAKKAEAFQHYKEGAMVDML 357
Cdd:PTZ00121 1487 EAKKKAEEAKKKADeakkAAEAKKKADEAKKAEEAKKADEA 1527
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 166-357 4.51e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.22  E-value: 4.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  166 KARTAQVQKDARIGEAKNKRDAVIREAHAMQEKVSAQYMNEIEMAKAQRDYELKKAIYDIEvftKKAESEMAYQLQVAKT 245
Cdd:TIGR02794  48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE---QAAKQAEEKQKQAEEA 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  246 KQRIEEEKMQVLVVERSQQitlqEQEISRKEKELEAKVKKPAEAERYRLEKLAEAERLQlimEAEAEAESIRVRGEAEAY 325
Cdd:TIGR02794 125 KAKQAAEAKAKAEAEAERK----AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA---KAKAEAEAKAKAEEAKAK 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 528509224  326 A--------VEAKGRAEAEQ-MAKKAEAFQHYKEGAMVDML 357
Cdd:TIGR02794 198 AeaakakaaAEAAAKAEAEAaAAAAAEAERKADEAELGDIF 238
PTZ00121 PTZ00121
MAEBL; Provisional
 166-343 5.50e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  166 KARTAQVQKDARigEAKNKRDAVIREAHAMQEKVSAQYMNEIEMAKAQRDYELKKAIYDIEVFTKKAESEMAYQlqVAKT 245
Cdd:PTZ00121 1314 AKKADEAKKKAE--EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK--KAEE 1389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  246 KQRIEEEKMQVLVVERSQQITLQEQEISRKEKELEAKV--KKPAEAERYRLEKLAEAERLQLIMEAEAEAESIRVRGEAE 323
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469

                         170       180
                  ....*....|....*....|....
gi 528509224  324 AYAVEAKGRAE----AEQMAKKAE 343
Cdd:PTZ00121 1470 KKADEAKKKAEeakkADEAKKKAE 1493
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 241-337 7.71e-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: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 44.21  E-value: 7.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 241 QVAKTKQRIEEEKMQVLVVERSQQITLQEQEISRKEKELEAKvkKPAEAERYRLE-KLAEAERLQLIMEAEAEAESIRVR 319
Cdd:cd03406  163 AIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEAE--KDAEVAKIQMQqKIMEKEAEKKISEIEDEMHLAREK 240

                         90
                 ....*....|....*...
gi 528509224 320 GEAEAYAVEAKGRAEAEQ 337
Cdd:cd03406  241 ARADAEYYRALREAEANK 258
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 14-192 8.79e-05

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: 43.53  E-value: 8.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  14 SGFCRSPpvmisgGRVFVFPCVQQIQRISLNTLTLNVKSDKVYTRHGVPISVTGIAQMKIqgqnKQMLAAACQMFLGKSD 93
Cdd:cd13435    1 SGGARGP------GVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRI----SDPLNAVIQVANYSHS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  94 SEIahIALETLeghqRAIIAHLTVEEIYKDRKKFSEQVFKVASSDLVNMGISVVSYTLKDVHDDQDYLHSLgkARTAQVQ 173
Cdd:cd13435   71 TRL--LAATTL----RNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDVSLPDSLQRAM--AAEAEAA 142

                        170       180
                 ....*....|....*....|...
gi 528509224 174 KDAR----IGEAKNKRDAVIREA 192
Cdd:cd13435  143 REARakviAAEGEMKSSRALKEA 165
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 214-305 9.30e-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: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 43.82  E-value: 9.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 214 RDYE--------LKKAIYDIEVFTKKAESEmayqlqvaKTKQRIEEEKM-QVLVVERSQQITlqEQEISRKEKELE---- 280
Cdd:cd03406  166 RNYEameaektkLLIAEQHQKVVEKEAETE--------RKRAVIEAEKDaEVAKIQMQQKIM--EKEAEKKISEIEdemh 235

                         90       100
                 ....*....|....*....|....*.
gi 528509224 281 -AKVKKPAEAERYRLEKLAEAERLQL 305
Cdd:cd03406  236 lAREKARADAEYYRALREAEANKLKL 261
PTZ00121 PTZ00121
MAEBL; Provisional
 180-350 1.04e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  180 EAKNKRDavirEAHAMQEKVSAQYMNEIEMAK----AQRDYELKKAiydiEVFTKKAESEMAYQLQVAKTKQRIEEEK-M 254
Cdd:PTZ00121 1507 EAKKKAD----EAKKAEEAKKADEAKKAEEAKkadeAKKAEEKKKA----DELKKAEELKKAEEKKKAEEAKKAEEDKnM 1578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  255 QVLVVERSQQITLQEQEISRKEKELEAKVK----KPAEAERYRLEKL--AEAERLQLIMEAEAEAESIR----VRGEAEA 324
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKkaeeLKKAEEE 1658

                         170       180
                  ....*....|....*....|....*..
gi 528509224  325 YAVEAKGRA-EAEQMAKKAEAFQHYKE 350
Cdd:PTZ00121 1659 NKIKAAEEAkKAEEDKKKAEEAKKAEE 1685
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-344 1.52e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 166 KARTAQVQKDARIGEAKNKRDAVIREAHAMQEKVSAQYMNEIEMAKAQ-RDYELKKAIYDIEVFTKKAESEMAYQLQVAK 244
Cdd:COG1196  214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAElAELEAELEELRLELEELELELEEAQAEEYEL 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 245 TKQRIEEEKMQVLVVERSQQITLQEQEISRKEKELEAKVKKpAEAERYRLEKLAEAERLQLIMEAEAEAESIRVRGEAEA 324
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE-LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180
                 ....*....|....*....|
gi 528509224 325 YAVEAKGRAEAEQMAKKAEA 344
Cdd:COG1196  373 ELAEAEEELEELAEELLEAL 392
PTZ00121 PTZ00121
MAEBL; Provisional
 168-374 1.58e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  168 RTAQVQKDARIGEAKNKRDAVIREAHAMQEKVSAQYMNEIEMAKAQRDyELKKAIydiEVFTKKAESEMAYQLQVAKTKQ 247
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAE---EEKKKVEQLKKKEAEEKKKAEE 1651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  248 -RIEEEKMQVlvveRSQQITLQEQEISRKEKEL---EAKVKKPAEAERYRLEKLAEAERLQLIMEAEA-EAESIRVRGEA 322
Cdd:PTZ00121 1652 lKKAEEENKI----KAAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKkKAEELKKAEEE 1727

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528509224  323 EAYAVEAKGRaEAEQMAKKA-EAFQHYKEGAMVDMLLEKLPMMADEISKPLSA 374
Cdd:PTZ00121 1728 NKIKAEEAKK-EAEEDKKKAeEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-344 1.76e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 166 KARTAQVQKDARIGEAKNKRDAVIREAHAMQEKVsAQYMNEIEMAKAQRDYELKKAIYDievftkkAESEMAYQLQVAKT 245
Cdd:COG1196  257 ELEAELAELEAELEELRLELEELELELEEAQAEE-YELLAELARLEQDIARLEERRREL-------EERLEELEEELAEL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 246 KQRIEEEKMQVLvvERSQQITLQEQEISRKEKELEAKVKKPAEAERYRLEKLAEAER-----LQLIMEAEAEAESIRVRG 320
Cdd:COG1196  329 EEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEElaeelLEALRAAAELAAQLEELE 406

                        170       180
                 ....*....|....*....|....
gi 528509224 321 EAEAYAVEAKGRAEAEQMAKKAEA 344
Cdd:COG1196  407 EAEEALLERLERLEEELEELEEAL 430
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-344 1.90e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 160 YLHSLGKARTAQVQKDARIGEAKNKRDAVIREAHAMQEKVS------AQYMNEIEMAKAQRdYELKKAIYDIEVfTKKAE 233
Cdd:COG1196  230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEelrlelEELELELEEAQAEE-YELLAELARLEQ-DIARL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 234 SEMAYQLQVAKTKQRIEEEKMQVLVVERSQQITLQEQEISRKEKELEAKVKKPAEAERYRLEKLAE-AERLQLIMEAEAE 312
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElAEAEEELEELAEE 387

                        170       180       190
                 ....*....|....*....|....*....|..
gi 528509224 313 AESIRVRGEAEAYAVEAKGRAEAEQMAKKAEA 344
Cdd:COG1196  388 LLEALRAAAELAAQLEELEEAEEALLERLERL 419
PRK01558 PRK01558
V-type ATP synthase subunit E; Provisional
 277-344 3.39e-04

V-type ATP synthase subunit E; Provisional


Pssm-ID: 179302  Cd Length: 198  Bit Score: 41.67  E-value: 3.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 277 KELEAKVKKpaeaeryrlEKLAEAERL--QLIMEAEAEAESIRVRGEAEAYAVEAKGRAEAEQMAKKAEA 344
Cdd:PRK01558   6 KDLINKIKK---------DGLEEAERLanEIILEAKEEAEEIIAKAEEEAKELKAKAEKEANDYKRHALE 66
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 246-344 6.23e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.86  E-value: 6.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  246 KQRIEEEKMQVLVVERSQQITL---------QEQEISRKEKELEAKVK----KPAEAERYRL----EKLAEAERLQLIME 308
Cdd:pfam15709 393 KQRLEEERQRQEEEERKQRLQLqaaqerarqQQEEFRRKLQELQRKKQqeeaERAEAEKQRQkeleMQLAEEQKRLMEMA 472

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 528509224  309 AEAEAESIRVRGEAEAyaveaKGRAEAEQMAKKAEA 344
Cdd:pfam15709 473 EEERLEYQRQKQEAEE-----KARLEAEERRQKEEE 503
PTZ00121 PTZ00121
MAEBL; Provisional
 138-350 9.73e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 9.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  138 DLVNMGISVVSYTLKDVHD-DQDYLHSLGKARTAQVQKDARIG------EAKNKRDAVIREAHAmQEKVSAQYMNEIEMA 210
Cdd:PTZ00121 1031 ELTEYGNNDDVLKEKDIIDeDIDGNHEGKAEAKAHVGQDEGLKpsykdfDFDAKEDNRADEATE-EAFGKAEEAKKTETG 1109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  211 KAQRDYELKKAIYDIEVFTKKAESEMAYQLQVAKTKQRIEEEKmQVLVVERSQQItlQEQEISRKEKELEaKVKKPAEAE 290
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAK-RVEIARKAEDA--RKAEEARKAEDAK-KAEAARKAE 1185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528509224  291 RYR----LEKLAEAERLQLIMEAEAEAESIRVRGEAEAYAVEAKGRAEA----EQMAKKAEAFQHYKE 350
Cdd:PTZ00121 1186 EVRkaeeLRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEakkdAEEAKKAEEERNNEE 1253
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
155-346 1.09e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  155 HDDQDYLHS---LG-------KARTAQVQK--------DARIGEAKNKRDAVIREAHAMQeKVSAQYMNEIEMAKAQRDY 216
Cdd:COG4913   592 KDDRRRIRSryvLGfdnraklAALEAELAEleeelaeaEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREI 670

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  217 --------ELKKAIYDIEVFTKKAEsemayQLQVAKTKQRIEEEKMQVLVVERSQQITLQEQEISRKEKELEAKVKKPAE 288
Cdd:COG4913   671 aeleaeleRLDASSDDLAALEEQLE-----ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528509224  289 AERYRLEKlaeaeRLQLIMEAEAEAEsIRVRGEAEAYAVEAKGRAEAEQMAKKAEAFQ 346
Cdd:COG4913   746 ELRALLEE-----RFAAALGDAVERE-LRENLEERIDALRARLNRAEEELERAMRAFN 797
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 27-131 1.10e-03

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: 38.92  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  27 GRVFVFPCVQQIQRISLNTLTLNVKSDKVYTRHGVPISVTGIAQMKIQGQNKQMLAAacqMFLGKSDSEIAHIALETleg 106
Cdd:cd13436   10 GIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAV---QDLNTSTRTTAQTSLTN--- 83

                         90       100
                 ....*....|....*....|....*
gi 528509224 107 hqraIIAHLTVEEIYKDRKKFSEQV 131
Cdd:cd13436   84 ----SLSKKTVREIQSDRRKINEEL 104
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 226-351 1.25e-03

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


Pssm-ID: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 40.26  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 226 EVFTKKAESEMAYQLQVAKTKQRIEEEKMQVLVVersqQItlqeqeisrkekELEAKVKKPA----EAERYRL--EKLAE 299
Cdd:cd03407  107 EVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVT----DI------------EPDASVKAAMneinAAQRLREaaEEKAE 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528509224 300 AERLQLIMEAEAEAESIRVRGEAEAyavEAKgRAEAEQMAKKAEAFQHYKEG 351
Cdd:cd03407  171 AEKILQVKAAEAEAEAKRLQGVGIA---EQR-KAIVDGLRESIEDFQEAVPG 218
PTZ00491 PTZ00491
major vault protein; Provisional
 260-370 1.60e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 40.77  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 260 ERSQQITLQEQEiSRKEKELEaKVKKPAEAERYR---LEKLAEAERLQL----IMEAEAEAESIRVRGEAEAYAVEAKGR 332
Cdd:PTZ00491 667 AARHQAELLEQE-ARGRLERQ-KMHDKAKAEEQRtklLELQAESAAVESsgqsRAEALAEAEARLIEAEAEVEQAELRAK 744

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 528509224 333 A-----EAE-QMAKKAEAFQHYKEGAMVDMLLEKLPMMAD-EISK 370
Cdd:PTZ00491 745 AlrieaEAElEKLRKRQELELEYEQAQNELEIAKAKELADiEATK 789
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 287-336 1.60e-03

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: 40.19  E-value: 1.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 528509224 287 AEAERYRLEklAEAERLQLIMEAEAEAEsiRVRGEAEAYAVEAKGRAEAE 336
Cdd:cd03404  184 QDKERLINE--AQAYANEVIPRARGEAA--RIIQEAEAYKAEVVARAEGD 229
PTZ00121 PTZ00121
MAEBL; Provisional
 151-352 2.00e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  151 LKDVHDDQDYLHSLGKARTAQVQKDARIGEAKNKRDAVIR--EAHAMQEKVSAQYMNEIEMAK----------------A 212
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKaeDARKAEEARKAEDARKAEEARkaedakrveiarkaedA 1163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  213 QRDYELKKA--IYDIEVFTKKAESEMAYQLQVAKTKQRIE-----------------EEKMQVLVVERSQQITLQEQEIS 273
Cdd:PTZ00121 1164 RKAEEARKAedAKKAEAARKAEEVRKAEELRKAEDARKAEaarkaeeerkaeearkaEDAKKAEAVKKAEEAKKDAEEAK 1243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  274 RKEKELEAKVKKPAE-------AERYRLEKLAEAERLQLIMEAEA--------EAESIRVRGEAEAYAVEAKGRAE---- 334
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEearmahfARRQAAIKAEEARKADELKKAEEkkkadeakKAEEKKKADEAKKKAEEAKKADEakkk 1323

                         250
                  ....*....|....*...
gi 528509224  335 AEQMAKKAEAFQHYKEGA 352
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEA 1341
PTZ00121 PTZ00121
MAEBL; Provisional
 166-410 2.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  166 KARTAQVQKDARIGEAKNKRDAV-----IREAHAMQEKVSAQYMNEIEMAKAQRDYELKKAIYDI----EVFTKKAESEM 236
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVrkaeeLRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVkkaeEAKKDAEEAKK 1244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  237 AYQLQVAKTKQRIEEEKMQVLVV--------ERSQQITLQEQEISRKEKELEA--KVKKPAEAERYRLEKLAEAERLQLI 306
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARrqaaikaeEARKADELKKAEEKKKADEAKKaeEKKKADEAKKKAEEAKKADEAKKKA 1324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  307 MEAEAEAESIRVRGE-----AEAYAVEAKGRA-EAEQMAKKAEAFQHYKEGAMVDMllEKLPMMADEISKPLSATNKVTM 380
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEeakkaAEAAKAEAEAAAdEAEAAEEKAEAAEKKKEEAKKKA--DAAKKKAEEKKKADEAKKKAEE 1402

                         250       260       270
                  ....*....|....*....|....*....|
gi 528509224  381 VSSGGSEIGAAKLTGEVLDIMTKLPETIEK 410
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
173-354 2.33e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 173 QKDARIGEAKNKRDAVIREAHAMQEKVSAQYMNEIEMAKAQRD---YELKKAIYDIEVFTKKAESEMA-YQLQVAKTKQR 248
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREElekLEKLLQLLPLYQELEALEAELAeLPERLEELEER 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 249 IEEekmqvlVVERSQQITLQEQEISRKEKELEAKVKKPAEAERYRLEKLaeAERLQLIMEAEAEAESIRVRGEAEAYAVE 328
Cdd:COG4717  155 LEE------LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL--AEELEELQQRLAELEEELEEAQEELEELE 226

                        170       180
                 ....*....|....*....|....*.
gi 528509224 329 AKgRAEAEQMAKKAEAFQHYKEGAMV 354
Cdd:COG4717  227 EE-LEQLENELEAAALEERLKEARLL 251
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 189-350 3.29e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  189 IREAHAMQ---EKVSAQYMNEIEMAKAQR----DYELKKAIYDIEVFTKKAESEMAYQLQVaktkQRIEEEKMQVL---- 257
Cdd:pfam17380 377 MRELERLQmerQQKNERVRQELEAARKVKileeERQRKIQQQKVEMEQIRAEQEEARQREV----RRLEEERAREMervr 452

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  258 --VVERSQQITL---QEQEISRKEKELEAKVKKPAEAERYR---LEKLAEaERLQLIMEAEAEAESIRVRGEAEAYAV-E 328
Cdd:pfam17380 453 leEQERQQQVERlrqQEEERKRKKLELEKEKRDRKRAEEQRrkiLEKELE-ERKQAMIEEERKRKLLEKEMEERQKAIyE 531

                         170       180
                  ....*....|....*....|..
gi 528509224  329 AKGRAEAEQMAKKAEAFQHYKE 350
Cdd:pfam17380 532 EERRREAEEERRKQQEMEERRR 553
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 2-187 3.37e-03

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: 38.65  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224   2 FYTCGPNEAMVVsgFCR---SPPVMISGGRVFVFPCVQQIQRISLNTLTLNVKSDkVYTRHGVPISVTGIAQMKIqgqNK 78
Cdd:cd03401    1 FYTVDAGEVGVV--FRRgkgVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLT-VLSKDGQTVNIDLSVLYRP---DP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  79 QMLAaacQMF--LGKSDSE--IAHIALETLeghqRAIIAHLTVEEIYKDRKKFSEQVFKVASSDLVNMGISVVSYTLKDV 154
Cdd:cd03401   75 EKLP---ELYqnLGPDYEErvLPPIVREVL----KAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNI 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528509224 155 HDDQDYLHS----------LGKAR----TAQVQKDARIGEAKNKRDA 187
Cdd:cd03401  148 DFPDEYEKAieakqvaeqeAERAKfeleKAEQEAERKVIEAEGEAEA 194
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 27-200 3.86e-03

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: 38.72  E-value: 3.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  27 GRVFVFPCVQQIQRISLNTLTLNVKSDKVYTRHGVPISVTGIAQMKIQGqnkqmlaaACQMFlgksdSEIAHI--ALETL 104
Cdd:cd08827   30 GLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIEN--------ASVCL-----SSFASIsdAMQAL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 105 -EGHQRAIIAHLTVEEIYKDRKKFSEQVFKVASSDLVNMGISVVSYTLKDVHDDQDYLHSLGKARTAQVQKDARIGEAKN 183
Cdd:cd08827   97 vQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAEAQRQAKVKVIAAEG 176

                        170
                 ....*....|....*..
gi 528509224 184 KRdAVIREAHAMQEKVS 200
Cdd:cd08827  177 EK-AASEALKAAAESLS 192
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 27-154 4.45e-03

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: 37.70  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  27 GRVFVFPCVQQIQRISLNTLTLNVKSDKVYTRHGVPISVTGIAQMKIQgqnkqmlAAACQMflgkSDSEIAHIALETL-E 105
Cdd:cd08828    4 GLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQ-------SAVKAV----ANVNNVHIATFLLaQ 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 528509224 106 GHQRAIIAHLTVEEIYKDRKKFSEQVFKVASSDLVNMGISVVSYTLKDV 154
Cdd:cd08828   73 TTLRNVLGTQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDV 121
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 287-349 4.62e-03

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: 38.62  E-value: 4.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 287 AEAERYR-------LEKLAEAERLQLIMEAEAEAESIRVRGEAEAYAVeakgRAEAEQMAKKAEAFQHYK 349
Cdd:cd03405  168 RIAAEYRaegeeeaEKIRAEADRERTVILAEAYREAEEIRGEGDAEAA----RIYAEAYGKDPEFYSFYR 233
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 166-341 7.29e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 38.57  E-value: 7.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  166 KARTAQVQKDARIgEAKNKRDAVIR--EAHAMQEKVSAQYMNEIEMAKAQRDYELKKAIYDIEVFTKKAESEMAYQLQVA 243
Cdd:pfam17380 323 KARQAEMDRQAAI-YAEQERMAMERerELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAA 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  244 KtKQRIEEEKMQVLVVERSQQITL--QEQEISRKEKELEAKVKKPAEAERYRLEKLAEAERLQLIMEAEAEAESIRVRGE 321
Cdd:pfam17380 402 R-KVKILEEERQRKIQQQKVEMEQirAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE 480

                         170       180
                  ....*....|....*....|
gi 528509224  322 AeayavEAKGRAEAEQMAKK 341
Cdd:pfam17380 481 K-----EKRDRKRAEEQRRK 495
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 27-258 9.20e-03

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: 37.15  E-value: 9.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224  27 GRVFVFPCVQQIQRISLNTLTLNVKSDKVYTRHGVPISVTGIAQMKIqgQNKQMLAAACQmflgKSDSEIAHIALETLeg 106
Cdd:cd03403    8 GLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRV--QNATIAVTNVE----NADRSTRLLAQTTL-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528509224 107 hqRAIIAHLTVEEIYKDRKKFSEQVFKVASSDLVNMGISVVSYTLKDVHddqdylhslgkaRTAQVQKdARIGEAKNKRD 186
Cdd:cd03403   80 --RNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVR------------LPVQLQR-AMAAEAEAARE 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528509224 187 AvireahamQEKVSAQymnEIEMaKAQRdyELKKAIYDIevftkkAESEMAYQLQVAKTKQRIEEEKMQVLV 258
Cdd:cd03403  145 A--------RAKVIAA---EGEQ-NASR--ALKEAADVI------SESPAALQLRYLQTLNTISAEKNSTII 196
 
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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