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Conserved domains on  [gi|5031699|ref|NP_005794|]
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flotillin-1 isoform 1 [Homo sapiens]

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 7.47e-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: 7.47e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    1 MFFTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVK-SEKVYTRHGVPISVTGIAQVKIQGQNKE 79
Cdd:COG2268  27 FYRKVPPNEALVITGRGGGYKV-VTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNSDPED 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   80 MLAAAcQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQD 159
Cdd:COG2268 106 IANAA-ERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENN 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  160 YLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIE-----MAKAQRDYELKKAAYDIEVNTRRAQA 234
Cdd:COG2268 185 YLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEA 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  235 DLAYQLQVAKTKQQIEeqrVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKlerlaeaeksqlimqAEAEAa 314
Cdd:COG2268 265 EAAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA---------------AEAEA- 325

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  315 svrmrgEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVt 394
Cdd:COG2268 326 ------EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA- 398

                       410       420
                ....*....|....*....|....
gi 5031699  395 geVLDILTRLPESVERLTGVSISQ 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 7.47e-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: 7.47e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    1 MFFTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVK-SEKVYTRHGVPISVTGIAQVKIQGQNKE 79
Cdd:COG2268  27 FYRKVPPNEALVITGRGGGYKV-VTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNSDPED 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   80 MLAAAcQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQD 159
Cdd:COG2268 106 IANAA-ERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENN 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  160 YLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIE-----MAKAQRDYELKKAAYDIEVNTRRAQA 234
Cdd:COG2268 185 YLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEA 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  235 DLAYQLQVAKTKQQIEeqrVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKlerlaeaeksqlimqAEAEAa 314
Cdd:COG2268 265 EAAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA---------------AEAEA- 325

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  315 svrmrgEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVt 394
Cdd:COG2268 326 ------EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA- 398

                       410       420
                ....*....|....*....|....
gi 5031699  395 geVLDILTRLPESVERLTGVSISQ 418
Cdd:COG2268 399 --VAEALAPLLESLLEETGLDLPG 420
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 30-175 1.17e-64

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: 203.89  E-value: 1.17e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   30 FVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQR 109
Cdd:cd03399   1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKV-GSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLR 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031699  110 AIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKD 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 7.59e-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: 89.30  E-value: 7.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699      3 FTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLA 82
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRV-LEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699     83 AACqmflgKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLH 162
Cdd:pfam01145  80 QNV-----FGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154

                         170       180
                  ....*....|....*....|...
gi 5031699    163 SLGKARTAQVQKDARIGEAEAKR 185
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 84-266 9.23e-18

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 80.01  E-value: 9.23e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699      84 ACQMFLGKTEAEIAHIALETLEghqRAIMAHMTVEEIYKDRQKfseqVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHS 163
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699     164 LGKARTAQVQKDARIGEAEAKRDAGIREAKAKqekvsaqylseIEMAKAQRDYELKKAAYDIEVNTRRAQAdLAYQLQVA 243
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK-----------RTLDELLTDQREKISENIREELNEAAEA-WGIKVEDV 141

                          170       180
                   ....*....|....*....|...
gi 5031699     244 KTKQqieeQRVQVQVVERAQQVA 266
Cdd:smart00244 142 EIKD----IRLPEEIKEAMEAQQ 160
PRK12704 PRK12704
phosphodiesterase; Provisional
 176-348 4.43e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.62  E-value: 4.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   176 ARIGEAEAKRDAGIREAKAKqekvsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRaqADLAYQLQVAKTKQQIEEQRVQ 255
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKKE-----AEAIKKEALLEAKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEENLDRKLE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   256 vQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYKLERLA-----EAeKSQLIMQAEAEA---ASVRMRgeaea 324
Cdd:PRK12704 104 -LLEKREEELEKKEKELEQKQQELEKKeeeLEELIEEQLQELERISgltaeEA-KEILLEKVEEEArheAAVLIK----- 176

                        170       180
                 ....*....|....*....|....*.
gi 5031699   325 fAIGARARAEAEQMAKK--AEAFQLY 348
Cdd:PRK12704 177 -EIEEEAKEEADKKAKEilAQAIQRC 201
growth_prot_Scy NF041483
polarized growth protein Scy;
166-353 7.06e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 45.20  E-value: 7.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    166 KARTAQVQKDARI--GEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAaydievntrRAQADlayqlqVA 243
Cdd:NF041483  432 RAKTVELQEEARRlrGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKA---------KADAD------EL 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    244 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAE---------AERYKLERLAEAEKSQLIMQAEAEAA 314
Cdd:NF041483  497 RSTATAESERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEeqaeevraaAERAARELREETERAIAARQAEAAEE 576

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 5031699    315 SVRMRGEAEAFAIGAR-----ARAEAEQMAKKA--EAFQLYQEAAQ 353
Cdd:NF041483  577 LTRLHTEAEERLTAAEealadARAEAERIRREAaeETERLRTEAAE 622
growth_prot_Scy NF041483
polarized growth protein Scy;
166-353 2.06e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 43.66  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    166 KARTAQvQKDARIGEAEAKRDAGIREAKAKQEKVSAQ----YLSEIEMAKAQRDYELKKAAYDIE--VNTRRAQA----D 235
Cdd:NF041483  158 RARTES-QARRLLDESRAEAEQALAAARAEAERLAEEarqrLGSEAESARAEAEAILRRARKDAErlLNAASTQAqeatD 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    236 LAYQLQVAkTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEA-RVRKPAEAERYKLERLAEAEKSQLIMQAEAEAA 314
Cdd:NF041483  237 HAEQLRSS-TAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAeKVVAEAKEAAAKQLASAESANEQRTRTAKEEIA 315

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 5031699    315 svRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQ 353
Cdd:NF041483  316 --RLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAE 352
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 189-344 1.96e-03

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: 40.21  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    189 IREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQ 268
Cdd:TIGR02794  55 IQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKA 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031699    269 EQEiARREKELEARVRKPAEAERyKLERLAEAEKSQLIMQAEAEAASvRMRGEAEAFAIGARARAEAEQMAKKAEA 344
Cdd:TIGR02794 135 KAE-AEAERKAKEEAAKQAEEEA-KAKAAAEAKKKAEEAKKKAEAEA-KAKAEAEAKAKAEEAKAKAEAAKAKAAA 207
growth_prot_Scy NF041483
polarized growth protein Scy;
170-343 5.81e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.04  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    170 AQVQKDARIGEAEAKRDAG-IREAKAKQekvsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQ 248
Cdd:NF041483  887 ASAEQDAARTRADAREDANrIRSDAAAQ----ADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQL 962

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    249 IEEQRVQVQVV--ERAQQVAVQEQEIARREKELEaRVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFA 326
Cdd:NF041483  963 IAEATGEAERLraEAAETVGSAQQHAERIRTEAE-RVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADT 1041

                         170
                  ....*....|....*..
gi 5031699    327 IGARARAEAEQMAKKAE 343
Cdd:NF041483 1042 LITEAAAEADQLTAKAQ 1058
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1-418 7.47e-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: 7.47e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    1 MFFTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVK-SEKVYTRHGVPISVTGIAQVKIQGQNKE 79
Cdd:COG2268  27 FYRKVPPNEALVITGRGGGYKV-VTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNSDPED 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   80 MLAAAcQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQD 159
Cdd:COG2268 106 IANAA-ERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENN 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  160 YLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIE-----MAKAQRDYELKKAAYDIEVNTRRAQA 234
Cdd:COG2268 185 YLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEA 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  235 DLAYQLQVAKTKQQIEeqrVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKlerlaeaeksqlimqAEAEAa 314
Cdd:COG2268 265 EAAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA---------------AEAEA- 325

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  315 svrmrgEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVt 394
Cdd:COG2268 326 ------EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA- 398

                       410       420
                ....*....|....*....|....
gi 5031699  395 geVLDILTRLPESVERLTGVSISQ 418
Cdd:COG2268 399 --VAEALAPLLESLLEETGLDLPG 420
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 30-175 1.17e-64

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: 203.89  E-value: 1.17e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   30 FVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQR 109
Cdd:cd03399   1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKV-GSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLR 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031699  110 AIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKD 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 7.59e-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: 89.30  E-value: 7.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699      3 FTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLA 82
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRV-LEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699     83 AACqmflgKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLH 162
Cdd:pfam01145  80 QNV-----FGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154

                         170       180
                  ....*....|....*....|...
gi 5031699    163 SLGKARTAQVQKDARIGEAEAKR 185
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 84-266 9.23e-18

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 80.01  E-value: 9.23e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699      84 ACQMFLGKTEAEIAHIALETLEghqRAIMAHMTVEEIYKDRQKfseqVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHS 163
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699     164 LGKARTAQVQKDARIGEAEAKRDAGIREAKAKqekvsaqylseIEMAKAQRDYELKKAAYDIEVNTRRAQAdLAYQLQVA 243
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK-----------RTLDELLTDQREKISENIREELNEAAEA-WGIKVEDV 141

                          170       180
                   ....*....|....*....|...
gi 5031699     244 KTKQqieeQRVQVQVVERAQQVA 266
Cdd:smart00244 142 EIKD----IRLPEEIKEAMEAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 27-234 3.89e-13

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 69.48  E-value: 3.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKemlaaacqmFLGKTEAEIAHIAlETLEG 106
Cdd:COG0330  45 GLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAK---------FLYNVENAEEALR-QLAES 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  107 HQRAIMAHMTVEEIY-KDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKR 185
Cdd:COG0330 115 ALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYR 194

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5031699  186 DAGIREAKAKQEKVsaqylseIEMAKAQRDYELKKAAYDIEVNTRRAQA 234
Cdd:COG0330 195 EAAIIRAEGEAQRA-------IIEAEAYREAQILRAEGEAEAFRIVAEA 236
PHB smart00244
prohibitin homologues; prohibitin homologues
 1-154 3.10e-11

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 61.52  E-value: 3.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699       1 MFFTCGPNEAMVVSGFCRSPPVMVAGGrVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQnkem 80
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVLRVLGPGL-HFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDP---- 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031699      81 LAAACQMfLGKTEAEIAHIALETLeghqRAIMAHMTVEEIYKD-RQKFSEQVFKVASSDLVNMGISVVSYTLKDI 154
Cdd:smart00244  77 LRAVYRV-LDADYAVIEQLAQTTL----RSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDI 146
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 47-158 2.19e-09

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


Pssm-ID: 259797 [Multi-domain]  Cd Length: 110  Bit Score: 54.68  E-value: 2.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   47 TLNVKSEKVYTRHGVPISVTGIAQVKIQgqnKEMLAAACQMFLGKTEAEiAHIaLETLEGHQRAIMAHMTVEEIYKDRQK 126
Cdd:cd02106   4 FDDVRVEPVGTADGVPVAVDLVVQFRIT---DYNALPAFYLVDFVKDIK-ADI-RRKIADVLRAAIGRMTLDQIISGRDE 78

                        90       100       110
                ....*....|....*....|....*....|..
gi 5031699  127 FSEQVFKVASSDLVNMGISVVSYTLKDIHDDQ 158
Cdd:cd02106  79 IAKAVKEDLEEDLENFGVVISDVDITSIEPPD 110
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 227-388 2.33e-08

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 54.85  E-value: 2.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  227 VNTRRAQ--ADLAYQLQVAKTKQQIEEQRVQVQVVERAQQV--AVQEQEIARREKElearvrkpaeaeryKLERLAEAEK 302
Cdd:COG0330 129 LSTGRDEinAEIREELQEALDPYGIEVVDVEIKDIDPPEEVqdAMEDRMKAERERE--------------AAILEAEGYR 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  303 SQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLdMLLEKLPQVAEeisgpltSANKITLVS 382
Cdd:COG0330 195 EAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFY-RSLEALEEVLS-------PNSKVIVLP 266


                ....*.
gi 5031699  383 SGSGTM 388
Cdd:COG0330 267 PDGNGF 272
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 14-206 2.62e-07

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: 50.85  E-value: 2.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   14 SGFCRSPpvmvagGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqgqnKEMLAAACQMFLGKTE 93
Cdd:cd13435   1 SGGARGP------GVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRI----SDPLNAVIQVANYSHS 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   94 AEIahIALETLeghqRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIhddqDYLHSLGKARTAqvq 173
Cdd:cd13435  71 TRL--LAATTL----RNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDV----SLPDSLQRAMAA--- 137

                       170       180       190
                ....*....|....*....|....*....|...
gi 5031699  174 kdarigEAEAKRDAGIREAKAKQEKVSAQYLSE 206
Cdd:cd13435 138 ------EAEAAREARAKVIAAEGEMKSSRALKE 164
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-368 7.21e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 7.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  160 YLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLS----EIEMAKAQRDYELKKAAYDIEVNTRRAQAD 235
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEleelELELEEAQAEEYELLAELARLEQDIARLEE 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  236 LAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEArvrkpAEAERYKLERLAEAEKSQLIMQAEAEAAS 315
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-----AEAELAEAEEALLEAEAELAEAEEELEEL 384

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 5031699  316 VRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEI 368
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-369 7.40e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 7.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  166 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKT 245
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEE-YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  246 KQQIEEQRVQVQVVE-RAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEA 324
Cdd:COG1196 336 EEELEELEEELEEAEeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031699  325 FAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEIS 369
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 162-363 1.16e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  162 HSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQ 241
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  242 VAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLE-RLAEAEKSQLIMQAEAEAASVRMRG 320
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEeEEALEEAAEEEAELEEEEEALLELL 465

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 5031699  321 EAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQ 363
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
PRK12704 PRK12704
phosphodiesterase; Provisional
 176-348 4.43e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.62  E-value: 4.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   176 ARIGEAEAKRDAGIREAKAKqekvsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRaqADLAYQLQVAKTKQQIEEQRVQ 255
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKKE-----AEAIKKEALLEAKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEENLDRKLE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   256 vQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYKLERLA-----EAeKSQLIMQAEAEA---ASVRMRgeaea 324
Cdd:PRK12704 104 -LLEKREEELEKKEKELEQKQQELEKKeeeLEELIEEQLQELERISgltaeEA-KEILLEKVEEEArheAAVLIK----- 176

                        170       180
                 ....*....|....*....|....*.
gi 5031699   325 fAIGARARAEAEQMAKK--AEAFQLY 348
Cdd:PRK12704 177 -EIEEEAKEEADKKAKEilAQAIQRC 201
PTZ00121 PTZ00121
MAEBL; Provisional
 166-367 5.14e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    166 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAqylseiEMAKAqrdyELKKAAYDIEVNTRRAQADlayQLQVAKT 245
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA------EAAKA----EAEAAADEAEAAEEKAEAA---EKKKEEA 1376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    246 KQQIEEQRVQVQVVERAQQVAVQEQEIARREKELE--ARVRKPAEAERYKLERLAEAEksQLIMQAEAEAASVRMRGEAE 323
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKAD--EAKKKAEEAKKADEAKKKAE 1454

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 5031699    324 AFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKlpqvAEE 367
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK----AEE 1494
PTZ00121 PTZ00121
MAEBL; Provisional
 156-368 1.21e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    156 DDQDYLHSLGKARTAQVQKDARIGEA-----EAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTR 230
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    231 RAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKElEAR----VRKPAEAERYKLERLAEAEKSQLI 306
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-EAKkaeeLKKKEAEEKKKAEELKKAEEENKI 1730

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5031699    307 MQAEAEAASVRMRGEAEafaigaRARAEAEQmAKKAEAFQLYQEAAQLDMLLEKLPQVAEEI 368
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAE------EAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
Flot pfam15975
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ...
 310-395 1.28e-05

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: 44.24  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    310 EAEAASVRMRGEAEAfaIGARARAEAEQMAKKAEAFQLY---QEAAQLDM-LLEKLPQVAEEISGPLTSANKITLVSSGS 385
Cdd:pfam15975   1 EAEAEADAIKLRAEA--KRKKALAEAEGIRALNEAENALsdeQIALQVKLaLLEALPEIIAESVKPLEKIDGIKILQVDG 78

                          90
                  ....*....|
gi 5031699    386 GTMGAAKVTG 395
Cdd:pfam15975  79 LGGGAAGGGG 88
PTZ00121 PTZ00121
MAEBL; Provisional
 166-357 4.10e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    166 KARTAQVQKDARIGEAEAKRDagirEAKAKQEKVSAQYLSEIEmAKAQRDyELKKAAYDI---EVNTRRAQADLAYQLQV 242
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAAD----EAEAAEEKAEAAEKKKEE-AKKKAD-AAKKKAEEKkkaDEAKKKAEEDKKKADEL 1410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    243 AKT---KQQIEEQRVQVQVVERAQQVAVQEQEiARREKELearvRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMR 319
Cdd:PTZ00121 1411 KKAaaaKKKADEAKKKAEEKKKADEAKKKAEE-AKKADEA----KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 5031699    320 GEAEAFAIGARARAE----AEQMAKKAEAFQLYQEAAQLDML 357
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADeakkAAEAKKKADEAKKAEEAKKADEA 1527
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 168-358 4.35e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.57  E-value: 4.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   168 RTAQVQKDARIGEAEAKRDAGIREAKAKQEK-VSAQYLSEIEMAKAQRDYELKKA---AYDIEVNTRRAQADLAYQLQVA 243
Cdd:PRK09510  66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQaAEQERLKQLEKERLAAQEQKKQAeeaAKQAALKQKQAEEAAAKAAAAA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   244 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERY---KLERLAEAEKSQLIMQAEAEAASVRMRG 320
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKaaaEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 5031699   321 EAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLL 358
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
PTZ00121 PTZ00121
MAEBL; Provisional
 151-377 6.93e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    151 LKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIR--EAKAKQEKVSAQYLSEIEMAKAQRDyelkkaAYDIEVN 228
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKaeDARKAEEARKAEDARKAEEARKAED------AKRVEIA 1157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    229 TRRAQADLAYQLQVAKTKQQIEEQRVQVQVvERAQQVAVQEQ----EIARREKElearVRKPAEAERYKLERLAEAEKSQ 304
Cdd:PTZ00121 1158 RKAEDARKAEEARKAEDAKKAEAARKAEEV-RKAEELRKAEDarkaEAARKAEE----ERKAEEARKAEDAKKAEAVKKA 1232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    305 LIMQAEAEAA----SVRMRGEAEAF-------------AIGARARAEAEQMAK-----KAEAFQLYQEAAQLDMLLEK-- 360
Cdd:PTZ00121 1233 EEAKKDAEEAkkaeEERNNEEIRKFeearmahfarrqaAIKAEEARKADELKKaeekkKADEAKKAEEKKKADEAKKKae 1312

                         250       260
                  ....*....|....*....|....
gi 5031699    361 -------LPQVAEEISGPLTSANK 377
Cdd:PTZ00121 1313 eakkadeAKKKAEEAKKKADAAKK 1336
growth_prot_Scy NF041483
polarized growth protein Scy;
166-353 7.06e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 45.20  E-value: 7.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    166 KARTAQVQKDARI--GEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAaydievntrRAQADlayqlqVA 243
Cdd:NF041483  432 RAKTVELQEEARRlrGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKA---------KADAD------EL 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    244 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAE---------AERYKLERLAEAEKSQLIMQAEAEAA 314
Cdd:NF041483  497 RSTATAESERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEeqaeevraaAERAARELREETERAIAARQAEAAEE 576

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 5031699    315 SVRMRGEAEAFAIGAR-----ARAEAEQMAKKA--EAFQLYQEAAQ 353
Cdd:NF041483  577 LTRLHTEAEERLTAAEealadARAEAERIRREAaeETERLRTEAAE 622
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 27-206 7.28e-05

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: 43.69  E-value: 7.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqgQNKEMLAAACQMFLGKTEAeiahIALETLeg 106
Cdd:cd03403   8 GLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRV--QNATIAVTNVENADRSTRL----LAQTTL-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  107 hqRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHddqdylhslgkaRTAQVQKdARIGEAEAKRD 186
Cdd:cd03403  80 --RNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVR------------LPVQLQR-AMAAEAEAARE 144

                       170       180
                ....*....|....*....|
gi 5031699  187 AGIREAKAKQEKVSAQYLSE 206
Cdd:cd03403 145 ARAKVIAAEGEQNASRALKE 164
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 33-194 7.33e-05

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: 43.27  E-value: 7.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   33 PCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFlgkteaEIAHIALETLeghqRAIM 112
Cdd:cd08826   1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRY------ATSQLAQTTL----RSVV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  113 AHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREA 192
Cdd:cd08826  71 GQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLA 150


                ..
gi 5031699  193 KA 194
Cdd:cd08826 151 EA 152
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 27-204 7.69e-05

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: 43.72  E-value: 7.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGqnkemlaaACQMFlgKTEAEIAHIALETLEG 106
Cdd:cd08827  30 GLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIEN--------ASVCL--SSFASISDAMQALVQT 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  107 HQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKartaqvqkdarigEAEAKRD 186
Cdd:cd08827 100 TVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAV-------------EAEAQRQ 166

                       170
                ....*....|....*...
gi 5031699  187 AGIREAKAKQEKVSAQYL 204
Cdd:cd08827 167 AKVKVIAAEGEKAASEAL 184
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 2-187 8.36e-05

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: 43.27  E-value: 8.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    2 FFTCGPNEAMVVSGFCRSPPVMVAG-GRVFVLPCIQQIQRISLNTLTLNVKSEkVYTRHGVPISVTGIAQVKIqgqNKEM 80
Cdd:cd03401   1 FYTVDAGEVGVVFRRGKGVKDEVLGeGLHFKIPWIQVVIIYDVRTQPREITLT-VLSKDGQTVNIDLSVLYRP---DPEK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   81 LAaacQMF--LGKTEAE--IAHIALETLeghqRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHD 156
Cdd:cd03401  77 LP---ELYqnLGPDYEErvLPPIVREVL----KAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDF 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5031699  157 DQDYLHS----------LGKAR----TAQVQKDARIGEAEAKRDA 187
Cdd:cd03401 150 PDEYEKAieakqvaeqeAERAKfeleKAEQEAERKVIEAEGEAEA 194
PTZ00121 PTZ00121
MAEBL; Provisional
 166-368 1.69e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    166 KARTAQVQKDARiGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDyELKKAAydievntrraQADLAYQLQVAKT 245
Cdd:PTZ00121 1465 KAEEAKKADEAK-KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAE----------EAKKADEAKKAEE 1532

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    246 KQQIEEQRvQVQVVERAQQVAVQEqEIARREKelearVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAF 325
Cdd:PTZ00121 1533 AKKADEAK-KAEEKKKADELKKAE-ELKKAEE-----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 5031699    326 AIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKlpQVAEEI 368
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK--KEAEEK 1646
PTZ00121 PTZ00121
MAEBL; Provisional
 164-367 1.69e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    164 LGKARTAQVQKDARigEAEAKRDAgiREAKAKQEKVSAQylseiEMAKAQrdyELKKAAYDIEV-NTRRAQADLAYQLQV 242
Cdd:PTZ00121 1515 AKKAEEAKKADEAK--KAEEAKKA--DEAKKAEEKKKAD-----ELKKAE---ELKKAEEKKKAeEAKKAEEDKNMALRK 1582

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    243 AKTKQQIEEQRVQV-------QVVERAQQVAVQEQEIARRE---KELEAR-----VRKPAEAERYKLERLAEAE------ 301
Cdd:PTZ00121 1583 AEEAKKAEEARIEEvmklyeeEKKMKAEEAKKAEEAKIKAEelkKAEEEKkkveqLKKKEAEEKKKAEELKKAEeenkik 1662

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031699    302 KSQLIMQAEAEAASVR-MRGEAEAFAIGARARAEAEQMAKKAEafQLYQEAAQLDMLLEKLPQVAEE 367
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEeAKKAEEDEKKAAEALKKEAEEAKKAE--ELKKKEAEEKKKAEELKKAEEE 1727
growth_prot_Scy NF041483
polarized growth protein Scy;
166-353 2.06e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 43.66  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    166 KARTAQvQKDARIGEAEAKRDAGIREAKAKQEKVSAQ----YLSEIEMAKAQRDYELKKAAYDIE--VNTRRAQA----D 235
Cdd:NF041483  158 RARTES-QARRLLDESRAEAEQALAAARAEAERLAEEarqrLGSEAESARAEAEAILRRARKDAErlLNAASTQAqeatD 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    236 LAYQLQVAkTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEA-RVRKPAEAERYKLERLAEAEKSQLIMQAEAEAA 314
Cdd:NF041483  237 HAEQLRSS-TAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAeKVVAEAKEAAAKQLASAESANEQRTRTAKEEIA 315

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 5031699    315 svRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQ 353
Cdd:NF041483  316 --RLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAE 352
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 241-347 2.41e-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: 42.67  E-value: 2.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  241 QVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEArvRKPAEaeryklerLAEAEKSQLIMQAEAEAASVRMrg 320
Cdd:cd03406 163 AIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEA--EKDAE--------VAKIQMQQKIMEKEAEKKISEI-- 230

                        90       100
                ....*....|....*....|....*....
gi 5031699  321 EAEAFAIGARARAEAE--QMAKKAEAFQL 347
Cdd:cd03406 231 EDEMHLAREKARADAEyyRALREAEANKL 259
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 244-305 3.07e-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: 42.28  E-value: 3.07e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031699  244 KTKQQIEEQRV-QVQVVERAQQVAvqEQEIARREKELE-----ARVRKPAEAERYKLERLAEAEKSQL 305
Cdd:cd03406 196 RKRAVIEAEKDaEVAKIQMQQKIM--EKEAEKKISEIEdemhlAREKARADAEYYRALREAEANKLKL 261
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 69-310 3.10e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.29  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699      69 AQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVS 148
Cdd:pfam12128  616 AREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD 695

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699     149 YTLKDIHDDQDylhslGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVN 228
Cdd:pfam12128  696 KKHQAWLEEQK-----EQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVI 770

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699     229 TRRAQ--ADLAYQL-QVAKTKQQIEEQRV--QVQVVERAQQVAVQEQEIARREKELE---ARVRKPAEAERYKLERLAEA 300
Cdd:pfam12128  771 AKLKReiRTLERKIeRIAVRRQEVLRYFDwyQETWLQRRPRLATQLSNIERAISELQqqlARLIADTKLRRAKLEMERKA 850

                          250
                   ....*....|
gi 5031699     301 EKSQLIMQAE 310
Cdd:pfam12128  851 SEKQQVRLSE 860
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 27-197 3.46e-04

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: 40.79  E-value: 3.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQgqnkemlAAACQMflgkTEAEIAHIALETL-E 105
Cdd:cd08828   4 GLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQ-------SAVKAV----ANVNNVHIATFLLaQ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  106 GHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIhddqdylhslgkaRTAQVQKDARIGEAEAKR 185
Cdd:cd08828  73 TTLRNVLGTQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDV-------------RIPVQMQRAMAAEAEATR 139

                       170
                ....*....|..
gi 5031699  186 DAGIREAKAKQE 197
Cdd:cd08828 140 EARAKVVAAEGE 151
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
180-368 3.69e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   180 EAEAKRDA--GIRE-----AKAKQEKVSAQYL-SEIEMAKAQRDYELKKAAYDievNTRRAQADLayQLQVAKTKQQIEE 251
Cdd:COG4913  246 DAREQIELlePIRElaeryAAARERLAELEYLrAALRLWFAQRRLELLEAELE---ELRAELARL--EAELERLEARLDA 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   252 QRVQVQVVERA------QQVAVQEQEIARREKELEARVRKpaeAERYKlERLAEAEksqliMQAEAEAAS-VRMRGEAEA 324
Cdd:COG4913  321 LREELDELEAQirgnggDRLEQLEREIERLERELEERERR---RARLE-ALLAALG-----LPLPASAEEfAALRAEAAA 391

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 5031699   325 FAigarARAEAEQMAKKAEAFQLYQEAAQLDmllEKLPQVAEEI 368
Cdd:COG4913  392 LL----EALEEELEALEEALAEAEAALRDLR---RELRELEAEI 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 194-369 4.17e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 4.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  194 AKQEKVSAQYLsEIEMAKAQRDYELKKAAYDiEVNTRRAQADLAYQLQVAKTKQQIEEQR-VQVQVVERAQQVAVQEQEI 272
Cdd:COG1196 206 ERQAEKAERYR-ELKEELKELEAELLLLKLR-ELEAELEELEAELEELEAELEELEAELAeLEAELEELRLELEELELEL 283

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  273 AR---REKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAfQLYQ 349
Cdd:COG1196 284 EEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA-ELAE 362

                       170       180
                ....*....|....*....|
gi 5031699  350 EAAQLDMLLEKLPQVAEEIS 369
Cdd:COG1196 363 AEEALLEAEAELAEAEEELE 382
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 190-359 4.51e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 4.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  190 REAKAKQEKVSAQYLseiemAKAQRDYELKKAAYDIEVNTRRAQADLAyQLQVAKTKQQIEEQRVQVQVVE-RAQQVAVQ 268
Cdd:COG1196 216 RELKEELKELEAELL-----LLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELElELEEAQAE 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  269 EQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLY 348
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                       170
                ....*....|.
gi 5031699  349 QEAAQLDMLLE 359
Cdd:COG1196 370 AEAELAEAEEE 380
PTZ00121 PTZ00121
MAEBL; Provisional
 166-343 7.90e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 7.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    166 KARTAQVQKDARIGEAEAKR------DAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAydievNTRRAQadlayQ 239
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKaeeernNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE-----EKKKAD-----E 1294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    240 LQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARV---RKPAEAERYKLERLA-EAEKSQLIMQAeAEAAS 315
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAeeaKKAAEAAKAEAEAAAdEAEAAEEKAEA-AEKKK 1373

                         170       180
                  ....*....|....*....|....*...
gi 5031699    316 VRMRGEAEAFAIGARARAEAEQMAKKAE 343
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAE 1401
mukB PRK04863
chromosome partition protein MukB;
191-299 8.12e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 8.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    191 EAKAKQEKVSAQYLSEIEMAKAQRDyELKKAAYDIEVNTRRAQADLAYQLQVAK----------TKQQIEEQRVQVQVVE 260
Cdd:PRK04863  562 ELEARLESLSESVSEARERRMALRQ-QLEQLQARIQRLAARAPAWLAAQDALARlreqsgeefeDSQDVTEYMQQLLERE 640

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 5031699    261 RAQQvaVQEQEIARREKELEARVRK---PAEAERYKLERLAE 299
Cdd:PRK04863  641 RELT--VERDELAARKQALDEEIERlsqPGGSEDPRLNALAE 680
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 164-326 9.65e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 9.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  164 LGKARTAQVQKDARIGEAEAKRDAgIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRR---------AQA 234
Cdd:COG4942  71 IRALEQELAALEAELAELEKEIAE-LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRlqylkylapARR 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  235 DLAYQLQ-----VAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKE-LEARVRKPAEAERYKLERLAEAEKS--QLI 306
Cdd:COG4942 150 EQAEELRadlaeLAALRAELEAERAELEALLAELEEERAALEALKAERQkLLARLEKELAELAAELAELQQEAEEleALI 229

                       170       180
                ....*....|....*....|
gi 5031699  307 MQAEAEAASVRMRGEAEAFA 326
Cdd:COG4942 230 ARLEAEAAAAAERTPAAGFA 249
PTZ00121 PTZ00121
MAEBL; Provisional
 164-368 1.00e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    164 LGKARTAQVQKDARIGEAEAKrdagIREAKAKQEKVSAQYLSEIEMAKaqRDYELKKAAYDIEVNTRRAQADLAYQLQVA 243
Cdd:PTZ00121 1193 LRKAEDARKAEAARKAEEERK----AEEARKAEDAKKAEAVKKAEEAK--KDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    244 KTKQQIE-EQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEA 322
Cdd:PTZ00121 1267 RRQAAIKaEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 5031699    323 EAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMllEKLPQVAEEI 368
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA--DAAKKKAEEK 1390
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 189-344 1.96e-03

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: 40.21  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    189 IREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQ 268
Cdd:TIGR02794  55 IQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKA 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031699    269 EQEiARREKELEARVRKPAEAERyKLERLAEAEKSQLIMQAEAEAASvRMRGEAEAFAIGARARAEAEQMAKKAEA 344
Cdd:TIGR02794 135 KAE-AEAERKAKEEAAKQAEEEA-KAKAAAEAKKKAEEAKKKAEAEA-KAKAEAEAKAKAEEAKAKAEAAKAKAAA 207
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
173-358 2.30e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 2.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  173 QKDARIGEAEAKRD---AGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLA-YQLQVAKTKQQ 248
Cdd:COG4717  75 ELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAeLPERLEELEER 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  249 IEEQRvqvqvvERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEA--EKSQLIMQAEAEAASVRMRGEaeafa 326
Cdd:COG4717 155 LEELR------ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEleELQQRLAELEEELEEAQEELE----- 223

                       170       180       190
                ....*....|....*....|....*....|..
gi 5031699  327 igaRARAEAEQMAKKAEAFQLYQEAAQLDMLL 358
Cdd:COG4717 224 ---ELEEELEQLENELEAAALEERLKEARLLL 252
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 220-367 2.33e-03

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: 40.32  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    220 KAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARR-------EKELEARVRKPAEAERY 292
Cdd:pfam15709 375 REELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRklqelqrKKQQEEAERAEAEKQRQ 454

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031699    293 K--LERLAEAEKSQLIMQAEAEAASVRMRGEAEafaigARARAEAEQMAKKAEafqlyqEAAQLdmLLEKLPQVAEE 367
Cdd:pfam15709 455 KelEMQLAEEQKRLMEMAEEERLEYQRQKQEAE-----EKARLEAEERRQKEE------EAARL--ALEEAMKQAQE 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 171-384 2.77e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699     171 QVQKDARIGEAEAKRDAgIREAKAKQEKVSAQYLSEIEMAKAqrdyELKKAAYDIEVNTRRAQADlayqlqvaktKQQIE 250
Cdd:TIGR02168  318 LEELEAQLEELESKLDE-LAEELAELEEKLEELKEELESLEA----ELEELEAELEELESRLEEL----------EEQLE 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699     251 EQRVQVqvVERAQQVAVQEQEIARREKELE---ARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAI 327
Cdd:TIGR02168  383 TLRSKV--AQLELQIASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 5031699     328 GARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSG 384
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 197-344 3.06e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 39.60  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    197 EKVSAQYLSEIEmakaqRDYELKKAAYDI-----EVNTRRAQAdLAYQLQVAKtkQQIEEQRVQVQVVERA---QQVAVQ 268
Cdd:pfam05262 180 KKVVEALREDNE-----KGVNFRRDMTDLkeresQEDAKRAQQ-LKEELDKKQ--IDADKAQQKADFAQDNadkQRDEVR 251

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031699    269 EQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAAsvRMRGEAEAFAIGARARAEaEQMAKKAEA 344
Cdd:pfam05262 252 QKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEA--LKAKDHKAFDLKQESKAS-EKEAEDKEL 324
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 27-131 3.17e-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: 37.76  E-value: 3.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqgqnKEMLAAACQMF-LGKTEAEIAHIALETle 105
Cdd:cd13436  10 GIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRI----WDPVLSVMAVQdLNTSTRTTAQTSLTN-- 83

                        90       100
                ....*....|....*....|....*.
gi 5031699  106 ghqraIMAHMTVEEIYKDRQKFSEQV 131
Cdd:cd13436  84 -----SLSKKTVREIQSDRRKINEEL 104
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 287-364 5.50e-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: 38.26  E-value: 5.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  287 AEAERYKLErlAEAEKSQLIMQAEAEAAsvRMRGEAEAFA--IGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQV 364
Cdd:cd03404 184 QDKERLINE--AQAYANEVIPRARGEAA--RIIQEAEAYKaeVVARAEGDAARFLALLAEYRKAPEVTRERLYLETMEEV 259
growth_prot_Scy NF041483
polarized growth protein Scy;
170-343 5.81e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.04  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    170 AQVQKDARIGEAEAKRDAG-IREAKAKQekvsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQ 248
Cdd:NF041483  887 ASAEQDAARTRADAREDANrIRSDAAAQ----ADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQL 962

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    249 IEEQRVQVQVV--ERAQQVAVQEQEIARREKELEaRVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFA 326
Cdd:NF041483  963 IAEATGEAERLraEAAETVGSAQQHAERIRTEAE-RVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADT 1041

                         170
                  ....*....|....*..
gi 5031699    327 IGARARAEAEQMAKKAE 343
Cdd:NF041483 1042 LITEAAAEADQLTAKAQ 1058
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-380 6.34e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 6.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699      73 IQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAImahmtvEEIYKDRQKFSEQvfkvASSDLVNMGISVVSYTLK 152
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEEL------EEELEQLRKELEE----LSRQISALRKDLARLEAE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699     153 dIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQylseieMAKAQRDYELKKAAYDIEVNTRRA 232
Cdd:TIGR02168  742 -VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ------IEQLKEELKALREALDELRAELTL 814

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699     233 QADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELearvrkpaEAERYKLERLAEAEKSQLIMQAEAE 312
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI--------EELEELIEELESELEALLNERASLE 886

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5031699     313 AASVRMRGEAEAFAIGARArAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITL 380
Cdd:TIGR02168  887 EALALLRSELEELSEELRE-LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 191-379 6.58e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.17  E-value: 6.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   191 EAKAKQEKVS------AQYLSEIEMAKAQRD--YELKKAAYDiEVNtrRAQADlayqlQVAKtkQQIEEQRVQVQVVERA 262
Cdd:COG3096  445 AFRAKEQQATeevlelEQKLSVADAARRQFEkaYELVCKIAG-EVE--RSQAW-----QTAR--ELLRRYRSQQALAQRL 514

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   263 QQVAVQEQEIARREKELEARVRKPAE-AERYKLERLAEAEKSQLIMQAEAEAASVrmrGEAEAFAIGARARAEAEQMAKK 341
Cdd:COG3096  515 QQLRAQLAELEQRLRQQQNAERLLEEfCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLR 591

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 5031699   342 AEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKIT 379
Cdd:COG3096  592 ARIKELAARAPAWLAAQDALERLREQSGEALADSQEVT 629
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
155-346 6.74e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 6.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   155 HDDQDYLHS---LG-------KARTAQVQK--------DARIGEAEAKRDAgIREAKAKQEKVSAQYLSEIEMAKAQRDY 216
Cdd:COG4913  592 KDDRRRIRSryvLGfdnraklAALEAELAEleeelaeaEERLEALEAELDA-LQERREALQRLAEYSWDEIDVASAEREI 670

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699   217 ELKKAAYDievNTRRAQADL-AYQLQVAKTKQQIEEQRVQVQVVERA-----QQVAVQEQEIARREKELEARVRKPAEAE 290
Cdd:COG4913  671 AELEAELE---RLDASSDDLaALEEQLEELEAELEELEEELDELKGEigrleKELEQAEEELDELQDRLEAAEDLARLEL 747

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 5031699   291 RYKLERLAEAEKSQLIMQAEAEAASVRMRGEAeafaigARARAEAEQMAKKAEAFQ 346
Cdd:COG4913  748 RALLEERFAAALGDAVERELRENLEERIDALR------ARLNRAEEELERAMRAFN 797
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 266-349 7.40e-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: 37.85  E-value: 7.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699  266 AVQEQEIARREKElEARVRkpAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAfaigARARAEAEQMAKKAEAF 345
Cdd:cd03405 157 SVYERMRAERERI-AAEYR--AEGEEEAEKIRAEADRERTVILAEAYREAEEIRGEGDA----EAARIYAEAYGKDPEFY 229


                ....
gi 5031699  346 QLYQ 349
Cdd:cd03405 230 SFYR 233
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 194-406 7.41e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.88  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    194 AKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIE--------VNTRRAQADLAY-QLQVAKTKQQIEEqrvqvqvVERAQQ 264
Cdd:PRK10929  125 AQQEQDRAREISDSLSQLPQQQTEARRQLNEIErrlqtlgtPNTPLAQAQLTAlQAESAALKALVDE-------LELAQL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    265 VAVQEQEIARREKELearvrkpAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEA 344
Cdd:PRK10929  198 SANNRQELARLRSEL-------AKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINREL 270

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031699    345 FQ-LYQEAAQLDMLLEKLPQVAEEIsgpLTSANKITLVSSGSGTMGAAKVTGEVL-DILTRLPE 406
Cdd:PRK10929  271 SQaLNQQAQRMDLIASQQRQAASQT---LQVRQALNTLREQSQWLGVSNALGEALrAQVARLPE 331
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 167-357 8.29e-03

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: 38.29  E-value: 8.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    167 ARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTK 246
Cdd:TIGR02794  53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEA 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031699    247 QQIEEQRVQVQVVERAQQVAVQE-----QEIARREKElEARVRKPAEAeryKLERLAEAEKSQLIMQAEAEAASVRMRGE 321
Cdd:TIGR02794 133 KAKAEAEAERKAKEEAAKQAEEEakakaAAEAKKKAE-EAKKKAEAEA---KAKAEAEAKAKAEEAKAKAEAAKAKAAAE 208

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 5031699    322 AEafaigARARAEAeQMAKKAEAFQLYQEAAQLDML 357
Cdd:TIGR02794 209 AA-----AKAEAEA-AAAAAAEAERKADEAELGDIF 238
 
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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