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Conserved domains on  [gi|17137546|ref|NP_477358|]
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flotillin 1, isoform A [Drosophila melanogaster]

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];
5-420 3.79e-97

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


:

Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 297.94  E-value: 3.79e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   5 FVTCGPNEALVVSGCcYMKPLLVPGGRAFVWPVGQQVQRISLNTMTLQVE-SPCVYTSQGVPISVTGIAQVKVQGqNEDM 83
Cdd:COG2268  28 YRKVPPNEALVITGR-GGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNS-DPED 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  84 LLTACEQFLGKSEAEINHIALVTLEGHQRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGY 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 164 LRSLGMARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTD-----IAKAQRDFELKKAAYDVEVQTKKAEAE 238
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEAE 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 239 MAYELQAAKTKQRIkeeQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKFRMEKLAEANKQRVVMEAEAEAES 318
Cdd:COG2268 266 AAYEIAEANAEREV---QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEG 342

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 319 IRirgeaeafaiaakakaeaeqmaMKAEAYREYREAAMVEMLLDTLPKVAAEVAAPLSQAKKITMVSSGTGDIGAAKLtg 398
Cdd:COG2268 343 KR----------------------ALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA-- 398

                       410       420
                ....*....|....*....|..
gi 17137546 399 eVLSIVNKVPELVKNITGVDIA 420
Cdd:COG2268 399 -VAEALAPLLESLLEETGLDLP 419
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
5-420 3.79e-97

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 297.94  E-value: 3.79e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   5 FVTCGPNEALVVSGCcYMKPLLVPGGRAFVWPVGQQVQRISLNTMTLQVE-SPCVYTSQGVPISVTGIAQVKVQGqNEDM 83
Cdd:COG2268  28 YRKVPPNEALVITGR-GGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNS-DPED 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  84 LLTACEQFLGKSEAEINHIALVTLEGHQRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGY 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 164 LRSLGMARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTD-----IAKAQRDFELKKAAYDVEVQTKKAEAE 238
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEAE 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 239 MAYELQAAKTKQRIkeeQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKFRMEKLAEANKQRVVMEAEAEAES 318
Cdd:COG2268 266 AAYEIAEANAEREV---QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEG 342

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 319 IRirgeaeafaiaakakaeaeqmaMKAEAYREYREAAMVEMLLDTLPKVAAEVAAPLSQAKKITMVSSGTGDIGAAKLtg 398
Cdd:COG2268 343 KR----------------------ALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA-- 398

                       410       420
                ....*....|....*....|..
gi 17137546 399 eVLSIVNKVPELVKNITGVDIA 420
Cdd:COG2268 399 -VAEALAPLLESLLEETGLDLP 419
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 33-178 1.06e-68

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: 214.29  E-value: 1.06e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  33 FVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVQGQNEdMLLTACEQFLGKSEAEINHIALVTLEGHQR 112
Cdd:cd03399   1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPE-EIAAAAERFLGKSTEEIRELVKETLEGHLR 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17137546 113 AIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGYLRSLGMARTAEVKRD 178
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 ...
 6-190 2.99e-20

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: 87.38  E-value: 2.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546     6 VTCGPNEALVVSGCCYMKPLLVPGGRaFVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVQGQNEDMLL 85
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLH-FIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546    86 TACeqflgKSEAEINHIALVTLEGHQRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGYLR 165
Cdd:pfam01145  80 QNV-----FGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154

                         170       180
                  ....*....|....*....|....*
gi 17137546   166 SLGMARTAEVKRDARIgeAEARAEA 190
Cdd:pfam01145 155 AIEAKQTAEQEAEAEI--ARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 87-269 1.17e-18

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 82.71  E-value: 1.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546     87 ACEQFLGKSEAEINHIALVTLEghqRAIMGSMTVEEIYKDRKKfskqVFEVASSDLANMGITVVSYTIKDLRDEEGYLRS 166
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546    167 LGMARTAEVKRDARIGEAEARAEAHIKEAIAEeqrmaarflndTDIAKAQRDFELKKAAYDVEVQTKKAEAeMAYELQAA 246
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK-----------RTLDELLTDQREKISENIREELNEAAEA-WGIKVEDV 141

                          170       180
                   ....*....|....*....|...
gi 17137546    247 KTKQRikeeQMQVKVIERTQEIA 269
Cdd:smart00244 142 EIKDI----RLPEEIKEAMEAQQ 160
PTZ00121 PTZ00121
MAEBL; Provisional
 169-358 2.38e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   169 MARTAEVKRDARigEAEARAEAHIK----EAIAEEQRMAARFLNDTDIAKAQRDfELKKA--AYDVEVQTKKAEAEMAYE 242
Cdd:PTZ00121 1462 AKKKAEEAKKAD--EAKKKAEEAKKadeaKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAeeAKKADEAKKAEEAKKADE 1538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   243 LQAAKTKQRiKEEQMQVKVIERTQEIAVQEQEimRRERELEATIRRPAE----AEKFRMEKLAEANKQRVVMEAE----A 314
Cdd:PTZ00121 1539 AKKAEEKKK-ADELKKAEELKKAEEKKKAEEA--KKAEEDKNMALRKAEeakkAEEARIEEVMKLYEEEKKMKAEeakkA 1615

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 17137546   315 EAESIR---IRGEAEAFAIAAKAKAEAEQMAMKAEAYREYREAAMVE 358
Cdd:PTZ00121 1616 EEAKIKaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
5-420 3.79e-97

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 297.94  E-value: 3.79e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   5 FVTCGPNEALVVSGCcYMKPLLVPGGRAFVWPVGQQVQRISLNTMTLQVE-SPCVYTSQGVPISVTGIAQVKVQGqNEDM 83
Cdd:COG2268  28 YRKVPPNEALVITGR-GGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNS-DPED 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  84 LLTACEQFLGKSEAEINHIALVTLEGHQRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGY 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 164 LRSLGMARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTD-----IAKAQRDFELKKAAYDVEVQTKKAEAE 238
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEAE 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 239 MAYELQAAKTKQRIkeeQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKFRMEKLAEANKQRVVMEAEAEAES 318
Cdd:COG2268 266 AAYEIAEANAEREV---QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEG 342

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 319 IRirgeaeafaiaakakaeaeqmaMKAEAYREYREAAMVEMLLDTLPKVAAEVAAPLSQAKKITMVSSGTGDIGAAKLtg 398
Cdd:COG2268 343 KR----------------------ALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA-- 398

                       410       420
                ....*....|....*....|..
gi 17137546 399 eVLSIVNKVPELVKNITGVDIA 420
Cdd:COG2268 399 -VAEALAPLLESLLEETGLDLP 419
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 33-178 1.06e-68

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: 214.29  E-value: 1.06e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  33 FVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVQGQNEdMLLTACEQFLGKSEAEINHIALVTLEGHQR 112
Cdd:cd03399   1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPE-EIAAAAERFLGKSTEEIRELVKETLEGHLR 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17137546 113 AIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGYLRSLGMARTAEVKRD 178
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 ...
 6-190 2.99e-20

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: 87.38  E-value: 2.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546     6 VTCGPNEALVVSGCCYMKPLLVPGGRaFVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVQGQNEDMLL 85
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLH-FIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546    86 TACeqflgKSEAEINHIALVTLEGHQRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGYLR 165
Cdd:pfam01145  80 QNV-----FGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154

                         170       180
                  ....*....|....*....|....*
gi 17137546   166 SLGMARTAEVKRDARIgeAEARAEA 190
Cdd:pfam01145 155 AIEAKQTAEQEAEAEI--ARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 87-269 1.17e-18

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 82.71  E-value: 1.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546     87 ACEQFLGKSEAEINHIALVTLEghqRAIMGSMTVEEIYKDRKKfskqVFEVASSDLANMGITVVSYTIKDLRDEEGYLRS 166
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546    167 LGMARTAEVKRDARIGEAEARAEAHIKEAIAEeqrmaarflndTDIAKAQRDFELKKAAYDVEVQTKKAEAeMAYELQAA 246
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK-----------RTLDELLTDQREKISENIREELNEAAEA-WGIKVEDV 141

                          170       180
                   ....*....|....*....|...
gi 17137546    247 KTKQRikeeQMQVKVIERTQEIA 269
Cdd:smart00244 142 EIKDI----RLPEEIKEAMEAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 30-237 6.12e-13

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 68.71  E-value: 6.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  30 GRAFVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVqgqnedmllTACEQFLGKSEAEINHIALVTlEG 109
Cdd:COG0330  45 GLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRI---------TDPAKFLYNVENAEEALRQLA-ES 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 110 HQRAIMGSMTVEEIY-KDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGYLRSLGMARTAEVKRDARIGEAEARA 188
Cdd:COG0330 115 ALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYR 194

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 17137546 189 EAHIKEAIAEEQRMAARflndtdiAKAQRDFELKKAAYDVEVQTKKAEA 237
Cdd:COG0330 195 EAAIIRAEGEAQRAIIE-------AEAYREAQILRAEGEAEAFRIVAEA 236
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 49-159 6.48e-10

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: 56.22  E-value: 6.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  49 MTLQVESPCVYTSQGVPISVTGIAQVKVQGQNedmLLTACEQFLGKSEAEiNHIaLVTLEGHQRAIMGSMTVEEIYKDRK 128
Cdd:cd02106   3 QFDDVRVEPVGTADGVPVAVDLVVQFRITDYN---ALPAFYLVDFVKDIK-ADI-RRKIADVLRAAIGRMTLDQIISGRD 77

                        90       100       110
                ....*....|....*....|....*....|.
gi 17137546 129 KFSKQVFEVASSDLANMGITVVSYTIKDLRD 159
Cdd:cd02106  78 EIAKAVKEDLEEDLENFGVVISDVDITSIEP 108
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 36-213 7.53e-07

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: 49.05  E-value: 7.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  36 PVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVQGQNEDMLltACEQFlgksEAEINHIALVTLeghqRAIM 115
Cdd:cd08826   1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVL--AVEDY----RYATSQLAQTTL----RSVV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 116 GSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGYLRSlgMARTAEVKRD--ARIGEAEARAEAhik 193
Cdd:cd08826  71 GQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRA--MARQAEAERErrAKIIKAEGELQA--- 145

                       170       180
                ....*....|....*....|
gi 17137546 194 eaiAEEQRMAARFLNDTDIA 213
Cdd:cd08826 146 ---AEKLAEAAEILAKSPGA 162
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 170-317 5.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 5.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 170 ARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDFELKKAAYDVEVQTKKAEAEMAYELQAAKTK 249
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17137546 250 QRIKEEQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKFRMEKLAEANKQRVVMEAEAEAE 317
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 170-355 6.32e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 6.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 170 ARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDtDIAKAQRDFELKKAAYDVEVQTKKAEAEMAYELQAAKTK 249
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 250 QRIKEEQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKFRMEKLAEANKQRVVMEAEAEAESIRIRGEAEAFA 329
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400

                       170       180
                ....*....|....*....|....*.
gi 17137546 330 IAAKAKAEAEQMAMKAEAYREYREAA 355
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEEL 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 154-373 6.66e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 6.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 154 IKDLRDEEGYLRSLGMARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDFELKKAAYDVEVQTK 233
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 234 KAEAEMAYE---LQAAKTKQRIKEEQMQVKVIERTQEIAVQEQEIMRRERELEATIRRPAEAEKfrmEKLAEANKQRVVM 310
Cdd:COG1196 374 LAEAEEELEelaEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE---EEEEEALEEAAEE 450

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17137546 311 EAEAEAESIRIRGEAEAFAIAAKAKAEAEQMAMKAEAYREYREAAMVEMLLDTLPKVAAEVAA 373
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 276-323 1.03e-04

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: 43.63  E-value: 1.03e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17137546 276 MRRERELEATIRRpAEAEKFRMEKLAEANKQRVVMEAEAEAESIRIRG 323
Cdd:cd03405 162 MRAERERIAAEYR-AEGEEEAEKIRAEADRERTVILAEAYREAEEIRG 208
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 27-208 1.20e-04

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: 42.99  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  27 VPGGRAFVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGI----------AQVKVQgqNEDMLLTaceqflgkse 96
Cdd:cd13437  27 VDPGLHKVNPCTEKIIQVDMKTQVIDLPRQSVMTKDNVSVTIDSVvyyriidpykAIYRID--NVKQALI---------- 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  97 aeinHIALVTLeghqRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGYLRSLGMARTAEvk 176
Cdd:cd13437  95 ----ERTQTTL----RSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSAAKAK-- 164

                       170       180       190
                ....*....|....*....|....*....|....*
gi 17137546 177 rdaRIGEAE---ARAEAhikEAiAEEQRMAARFLN 208
Cdd:cd13437 165 ---RIGESKiisAKADV---ES-AKLMREAADILD 192
PTZ00121 PTZ00121
MAEBL; Provisional
 169-358 2.38e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   169 MARTAEVKRDARigEAEARAEAHIK----EAIAEEQRMAARFLNDTDIAKAQRDfELKKA--AYDVEVQTKKAEAEMAYE 242
Cdd:PTZ00121 1462 AKKKAEEAKKAD--EAKKKAEEAKKadeaKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAeeAKKADEAKKAEEAKKADE 1538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   243 LQAAKTKQRiKEEQMQVKVIERTQEIAVQEQEimRRERELEATIRRPAE----AEKFRMEKLAEANKQRVVMEAE----A 314
Cdd:PTZ00121 1539 AKKAEEKKK-ADELKKAEELKKAEEKKKAEEA--KKAEEDKNMALRKAEeakkAEEARIEEVMKLYEEEKKMKAEeakkA 1615

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 17137546   315 EAESIR---IRGEAEAFAIAAKAKAEAEQMAMKAEAYREYREAAMVE 358
Cdd:PTZ00121 1616 EEAKIKaeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 30-209 4.93e-04

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: 41.00  E-value: 4.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  30 GRAFVWPVGQQVQRISLNTMTLQVESPCVYTSQGVPISVTGIAQVKVQgqNEDMLLTACEQFlgksEAEINHIALVTLeg 109
Cdd:cd03403   8 GLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQ--NATIAVTNVENA----DRSTRLLAQTTL-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 110 hqRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRdeegylrslgmaRTAEVKRdARIGEAEARAE 189
Cdd:cd03403  80 --RNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVR------------LPVQLQR-AMAAEAEAARE 144

                       170       180
                ....*....|....*....|
gi 17137546 190 AHIKEAIAEEQRMAARFLND 209
Cdd:cd03403 145 ARAKVIAAEGEQNASRALKE 164
PTZ00121 PTZ00121
MAEBL; Provisional
 156-380 7.73e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 7.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   156 DLRDEEGYLRSLGMARTAEVKRDARigEAEARAEAHIKEA-----IAEEQRMAArflndtDIAKAqrdfELKKAAYDVEV 230
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKAD--EAKKKAEEAKKKAdaakkKAEEAKKAA------EAAKA----EAEAAADEAEA 1361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   231 QTKKAEAEmayELQAAKTKQRIKEEQMQVKVIERTQEIAVQEQEIMRRERELeatirRPAEAEKFRMEKL-AEANKQRVV 309
Cdd:PTZ00121 1362 AEEKAEAA---EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL-----KKAAAAKKKADEAkKKAEEKKKA 1433

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137546   310 MEAEAEAESIRIRGEAEAFAIAAKAKAEAEQMAMKAEAYREYREAAMVEMLLDTLPKVAAEVAAPLSQAKK 380
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 230-307 9.57e-04

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: 40.74  E-value: 9.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 230 VQTKKAEAEMAYELQAAktkqrikEEQMQVKVIERTQEIAVQEQEIMRRERELEATIRRP---AEAEKFRMEKLAEANKQ 306
Cdd:cd03406 187 VVEKEAETERKRAVIEA-------EKDAEVAKIQMQQKIMEKEAEKKISEIEDEMHLAREkarADAEYYRALREAEANKL 259


                .
gi 17137546 307 R 307
Cdd:cd03406 260 K 260
PRK12704 PRK12704
phosphodiesterase; Provisional
 170-321 1.24e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  170 ARTAEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDFELKKaaydVEVQTKKAEAEMAYELQAAKTK 249
Cdd:PRK12704  33 IKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQK----LEKRLLQKEENLDRKLELLEKR 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17137546  250 QRikeeqmqvKVIERTQEIAVQEQEIMRRERELEATIrrpAEAEKfRMEKLA-----EAnKQRVV--MEAEAEAESIRI 321
Cdd:PRK12704 109 EE--------ELEKKEKELEQKQQELEKKEEELEELI---EEQLQ-ELERISgltaeEA-KEILLekVEEEARHEAAVL 174
PTZ00121 PTZ00121
MAEBL; Provisional
 174-320 1.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   174 EVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDFELKKAaYDVEVQTKKAEAEMAYElQAAKTKQRIK 253
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL-YEEEKKMKAEEAKKAEE-AKIKAEELKK 1627

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17137546   254 EEQMQVKV--IERTQEIAVQEQEIMRRERELE----ATIRRPAEAEKFRMEKL--AEANKQRVVMEAEAEAESIR 320
Cdd:PTZ00121 1628 AEEEKKKVeqLKKKEAEEKKKAEELKKAEEENkikaAEEAKKAEEDKKKAEEAkkAEEDEKKAAEALKKEAEEAK 1702
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 33-204 2.83e-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: 2.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  33 FVWPVGQQVQRISLNTMTLQVESPcVYTSQGVPISVTGIAQVKVqgqNEDMLLTAcEQFLGKSEAEInhiaLVTLEGHQ- 111
Cdd:cd03401  30 FKIPWIQVVIIYDVRTQPREITLT-VLSKDGQTVNIDLSVLYRP---DPEKLPEL-YQNLGPDYEER----VLPPIVREv 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546 112 -RAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGYLRSLGMARTAEVKRDARIGEAE-ARAE 189
Cdd:cd03401 101 lKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEAKQVAEQEAERAKFELEkAEQE 180

                       170
                ....*....|....*
gi 17137546 190 AHIKEAIAEEQRMAA 204
Cdd:cd03401 181 AERKVIEAEGEAEAQ 195
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 96-213 2.89e-03

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: 38.38  E-value: 2.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546  96 EAEINHIALVTLeghqRAIMGSMTVEEIYKDRKKFSKQVFEVASSDLANMGITVVSYTIKDLRDEEGYLRSLGMARTAEV 175
Cdd:cd13775  47 RAAVSLAAQTAL----RDAIGRSELAELLSRREQIDEELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAER 122

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17137546 176 KRDARIGEAEARAEahikeaIAEEQRMAARFLNDTDIA 213
Cdd:cd13775 123 EKNARVILAEAEKE------IAEMFVEAAEVYENNPIA 154
PTZ00121 PTZ00121
MAEBL; Provisional
 155-380 4.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   155 KDLRDEEGYLRSLGMARTAEVKRDARIGEAEARAEAHIKeaiAEEQRMAARFLNDTDIAKAQrdfELKKAAYD--VEVQT 232
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKK---AEDARKAEEARKAEDARKAE---EARKAEDAkrVEIAR 1158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   233 KKAEAEMAYELQAAKTKQRIKEEQMQVKViERTQEIAVQE-----------------QEIMRRERELEATIRRPAEAEKF 295
Cdd:PTZ00121 1159 KAEDARKAEEARKAEDAKKAEAARKAEEV-RKAEELRKAEdarkaeaarkaeeerkaEEARKAEDAKKAEAVKKAEEAKK 1237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   296 RMEKLAEANKQRVVMEAEAEAESIRIRGEAEAFAIAAKAKAEAEQMAmKAEAYREYREAAMVEML--LDTLPKVAAEvAA 373
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK-KAEEKKKADEAKKAEEKkkADEAKKKAEE-AK 1315


                  ....*..
gi 17137546   374 PLSQAKK 380
Cdd:PTZ00121 1316 KADEAKK 1322
PTZ00121 PTZ00121
MAEBL; Provisional
 165-380 5.92e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   165 RSLGMARTAEVKR---DARIGEAEARAEA--HIKEAI--AEEQRMAARFLNDTDIAKAQR----DFELKKAAYDVEVQTK 233
Cdd:PTZ00121 1200 RKAEAARKAEEERkaeEARKAEDAKKAEAvkKAEEAKkdAEEAKKAEEERNNEEIRKFEEarmaHFARRQAAIKAEEARK 1279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   234 KAEAEMAYELQAAKtKQRIKEEQMQVKVIERTQEIAVQEQEIMRREREleatIRRPAEAEKfrmEKLAEANKQRVVMEAE 313
Cdd:PTZ00121 1280 ADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE----AKKKADAAK---KKAEEAKKAAEAAKAE 1351

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17137546   314 AEAESIRIRGEAEAFAIAAKAKAEAEQMAMKAEAYREYREAAmvemllDTLPKVAAEVAAPLSQAKK 380
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA------DEAKKKAEEDKKKADELKK 1412
PTZ00121 PTZ00121
MAEBL; Provisional
 173-358 6.91e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 6.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   173 AEVKRDARIGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDfELKKAAYDV----EVQTKKAEAEMAYELQaAKT 248
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKkkadEAKKKAEEAKKADEAK-KKA 1453

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   249 KQRIKEEQMQVKVIE-RTQEIAVQEQEIMRREREL---------EATIRRPAEAEKFRMEKLAEANKQRVVMEAEAEAES 318
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEaKKADEAKKKAEEAKKADEAkkkaeeakkKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA 1533

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 17137546   319 IRIRGEAEAFAIAAKAKAEAEQMAMKAEAYREYREAAMVE 358
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
PTZ00121 PTZ00121
MAEBL; Provisional
 171-354 6.91e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 6.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   171 RTAEVKRDAR--IGEAEARAEAHIKEAIAEEQRMAARFLNDTDIAKAQRDfELKKAAydvEVQTKKAEAEMAYELQAAKt 248
Cdd:PTZ00121 1451 KKAEEAKKAEeaKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAD-EAKKAA---EAKKKADEAKKAEEAKKAD- 1525

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   249 KQRIKEEQMQVKVIERTQEiaVQEQEIMRRERELeatiRRPAEAEKFRMEKLAEANKQRVVMEAE--AEAESIRIrgeae 326
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEE--KKKADELKKAEEL----KKAEEKKKAEEAKKAEEDKNMALRKAEeaKKAEEARI----- 1594

                         170       180
                  ....*....|....*....|....*...
gi 17137546   327 afaiAAKAKAEAEQMAMKAEAYREYREA 354
Cdd:PTZ00121 1595 ----EEVMKLYEEEKKMKAEEAKKAEEA 1618
PTZ00121 PTZ00121
MAEBL; Provisional
 170-380 8.56e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 8.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   170 ARTAEVKRDA---RIGEAEARAEAHIKEAiaEEQRMAARFLNDTDIAKAQRDfELKKAAYD---VEVQTKKAEAEMAYEL 243
Cdd:PTZ00121 1359 AEAAEEKAEAaekKKEEAKKKADAAKKKA--EEKKKADEAKKKAEEDKKKAD-ELKKAAAAkkkADEAKKKAEEKKKADE 1435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137546   244 QAAKTKQRIKEEQMQVKVIE-RTQEIAVQEQEIMRRERELEATI---RRPAEAEKFRMEKLAEANKQRVVMEAEAEAESI 319
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEaKKAEEAKKKAEEAKKADEAKKKAeeaKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137546   320 RirgeaEAFAIAAKAKAEAEQMAMKAEAYREYREAAMVEMLLDTLPKVAAEVAAPLSQAKK 380
Cdd:PTZ00121 1516 K-----KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK 1571
 
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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