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Conserved domains on  [gi|158636004|ref|NP_073192|]
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flotillin-1 [Rattus norvegicus]

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 6.51e-92

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


:

Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 284.46  E-value: 6.51e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   1 MFFTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVK-SEKVYTRHGVPISVTGIAQVKIQGqNKE 79
Cdd:COG2268   27 FYRKVPPNEALVITGRGGGYKV-VTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNS-DPE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  80 MLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQD 159
Cdd:COG2268  105 DIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENN 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 160 YLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIE-----MAKAQRDYELKKATYDIEVNTRRAQA 234
Cdd:COG2268  185 YLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEA 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 235 DLAYQLQVAKTKQQIEeqrVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRlerlAEAEkaqlimqAEAEAE 314
Cdd:COG2268  265 EAAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA----AEAE-------AEAEAE 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 315 SVRmrgeaeafavgARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVt 394
Cdd:COG2268  331 AIR-----------AKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA- 398

                        410       420
                 ....*....|....*....|....
gi 158636004 395 geVLDILSRLPESVERLTGVSISQ 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 6.51e-92

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 284.46  E-value: 6.51e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   1 MFFTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVK-SEKVYTRHGVPISVTGIAQVKIQGqNKE 79
Cdd:COG2268   27 FYRKVPPNEALVITGRGGGYKV-VTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNS-DPE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  80 MLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQD 159
Cdd:COG2268  105 DIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENN 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 160 YLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIE-----MAKAQRDYELKKATYDIEVNTRRAQA 234
Cdd:COG2268  185 YLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEA 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 235 DLAYQLQVAKTKQQIEeqrVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRlerlAEAEkaqlimqAEAEAE 314
Cdd:COG2268  265 EAAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA----AEAE-------AEAEAE 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 315 SVRmrgeaeafavgARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVt 394
Cdd:COG2268  331 AIR-----------AKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA- 398

                        410       420
                 ....*....|....*....|....
gi 158636004 395 geVLDILSRLPESVERLTGVSISQ 418
Cdd:COG2268  399 --VAEALAPLLESLLEETGLDLPG 420
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 30-175 1.20e-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: 1.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  30 FVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQR 109
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKV-GSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158636004 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 6.27e-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: 6.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004    3 FTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLA 82
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRV-LEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   83 AACqmflgKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLH 162
Cdd:pfam01145  80 QNV-----FGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154

                         170       180
                  ....*....|....*....|...
gi 158636004  163 SLGKARTAQVQKDARIGEAEAKR 185
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 84-266 1.35e-17

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 79.63  E-value: 1.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004    84 ACQMFLGKTEAEIAHIALETLEghqRAIMAHMTVEEIYKDRQKfseqVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHS 163
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   164 LGKARTAQVQKDARIGEAEAKRDAGIREAKAKqekvsaqclseIEMAKAQRDYELKKATYDIEVNTRRAQAdLAYQLQVA 243
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK-----------RTLDELLTDQREKISENIREELNEAAEA-WGIKVEDV 141

                          170       180
                   ....*....|....*....|...
gi 158636004   244 KTKQqieeQRVQVQVVERAQQVA 266
Cdd:smart00244 142 EIKD----IRLPEEIKEAMEAQQ 160
PRK12704 PRK12704
phosphodiesterase; Provisional
 176-348 6.95e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 51.32  E-value: 6.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 176 ARIGEAEAKRDAGIREAKAKQEKVSAQCLSEiemakAQRDYELKKATYDIEVNTRRaqADLAYQLQVAKTKQQIEEQRVQ 255
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLE-----AKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEENLDRKLE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 256 vQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYRLERLA-----EAeKAQLI--MQAEAEAESVRMRGEAEaf 325
Cdd:PRK12704 104 -LLEKREEELEKKEKELEQKQQELEKKeeeLEELIEEQLQELERISgltaeEA-KEILLekVEEEARHEAAVLIKEIE-- 179

                        170       180
                 ....*....|....*....|....*
gi 158636004 326 avgARARAEAEQMAKK--AEAFQMY 348
Cdd:PRK12704 180 ---EEAKEEADKKAKEilAQAIQRC 201
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 167-352 3.53e-05

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.61  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  167 ARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATydievntRRAQADLAYQLQVAKTK 246
Cdd:TIGR02794  53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE-------QAAKQAEEKQKQAEEAK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  247 QQIEEQRVQVQVVERAQQVAvqeqEIARREKELEARVRKPAEAERYRLERLAEAEKAQlimQAEAEAESVRMRGEAEAFA 326
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAK----EEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA---KAKAEAEAKAKAEEAKAKA 198

                         170       180
                  ....*....|....*....|....*.
gi 158636004  327 VGARARAEAEQmAKKAEAFQMYQEAA 352
Cdd:TIGR02794 199 EAAKAKAAAEA-AAKAEAEAAAAAAA 223
growth_prot_Scy NF041483
polarized growth protein Scy;
166-353 2.25e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 43.66  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  166 KARTAQVQKDARI--GEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKAtydievntrRAQADlayqlqVA 243
Cdd:NF041483  432 RAKTVELQEEARRlrGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKA---------KADAD------EL 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  244 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKelearvrkpAEAERYRLERLAEAEKaqliMQAEAEAESVRMRGEAE 323
Cdd:NF041483  497 RSTATAESERVRTEAIERATTLRRQAEETLERTR---------AEAERLRAEAEEQAEE----VRAAAERAARELREETE 563

                         170       180       190
                  ....*....|....*....|....*....|
gi 158636004  324 AFAVGARARAEAEQMAKKAEAFQMYQEAAQ 353
Cdd:NF041483  564 RAIAARQAEAAEELTRLHTEAEERLTAAEE 593
growth_prot_Scy NF041483
polarized growth protein Scy;
170-373 5.68e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.04  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  170 AQVQKDARIGEAEAKRDAG-IR-EAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKTKQ 247
Cdd:NF041483  887 ASAEQDAARTRADAREDANrIRsDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEA 966

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  248 QIEEQRVQVqvvERAQQVAVQEQEIARREKELEaRVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAV 327
Cdd:NF041483  967 TGEAERLRA---EAAETVGSAQQHAERIRTEAE-RVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADTL 1042

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158636004  328 GARARAEAEQMAKKA--EAFQMYQEA-AQLDMLLEKLPQVAEEISGPLT 373
Cdd:NF041483 1043 ITEAAAEADQLTAKAqeEALRTTTEAeAQADTMVGAARKEAERIVAEAT 1091
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1-418 6.51e-92

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 284.46  E-value: 6.51e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   1 MFFTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVK-SEKVYTRHGVPISVTGIAQVKIQGqNKE 79
Cdd:COG2268   27 FYRKVPPNEALVITGRGGGYKV-VTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNS-DPE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  80 MLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQD 159
Cdd:COG2268  105 DIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENN 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 160 YLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIE-----MAKAQRDYELKKATYDIEVNTRRAQA 234
Cdd:COG2268  185 YLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEA 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 235 DLAYQLQVAKTKQQIEeqrVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRlerlAEAEkaqlimqAEAEAE 314
Cdd:COG2268  265 EAAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA----AEAE-------AEAEAE 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 315 SVRmrgeaeafavgARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVt 394
Cdd:COG2268  331 AIR-----------AKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA- 398

                        410       420
                 ....*....|....*....|....
gi 158636004 395 geVLDILSRLPESVERLTGVSISQ 418
Cdd:COG2268  399 --VAEALAPLLESLLEETGLDLPG 420
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 30-175 1.20e-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: 1.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  30 FVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQR 109
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKV-GSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158636004 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 6.27e-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: 6.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004    3 FTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLA 82
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRV-LEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   83 AACqmflgKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLH 162
Cdd:pfam01145  80 QNV-----FGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154

                         170       180
                  ....*....|....*....|...
gi 158636004  163 SLGKARTAQVQKDARIGEAEAKR 185
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 84-266 1.35e-17

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 79.63  E-value: 1.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004    84 ACQMFLGKTEAEIAHIALETLEghqRAIMAHMTVEEIYKDRQKfseqVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHS 163
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   164 LGKARTAQVQKDARIGEAEAKRDAGIREAKAKqekvsaqclseIEMAKAQRDYELKKATYDIEVNTRRAQAdLAYQLQVA 243
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK-----------RTLDELLTDQREKISENIREELNEAAEA-WGIKVEDV 141

                          170       180
                   ....*....|....*....|...
gi 158636004   244 KTKQqieeQRVQVQVVERAQQVA 266
Cdd:smart00244 142 EIKD----IRLPEEIKEAMEAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 27-234 1.67e-13

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 70.25  E-value: 1.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKemlaaacqmFLGKTEAEIAHIAlETLEG 106
Cdd:COG0330   45 GLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAK---------FLYNVENAEEALR-QLAES 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 107 HQRAIMAHMTVEEIYK-DRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKR 185
Cdd:COG0330  115 ALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYR 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 158636004 186 DAGIREAKAKQEKVsaqclseIEMAKAQRDYELKKATYDIEVNTRRAQA 234
Cdd:COG0330  195 EAAIIRAEGEAQRA-------IIEAEAYREAQILRAEGEAEAFRIVAEA 236
PHB smart00244
prohibitin homologues; prohibitin homologues
 1-154 2.72e-11

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 61.52  E-value: 2.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004     1 MFFTCGPNEAMVVSGFCRSPPVMVAGGrVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQnkem 80
Cdd:smart00244   2 AIKVVGEGERGVVERLGRVLRVLGPGL-HFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDP---- 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158636004    81 LAAACQMfLGKTEAEIAHIALETLeghqRAIMAHMTVEEIYKD-RQKFSEQVFKVASSDLVNMGISVVSYTLKDI 154
Cdd:smart00244  77 LRAVYRV-LDADYAVIEQLAQTTL----RSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDI 146
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 227-388 3.92e-10

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 60.24  E-value: 3.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 227 VNTRRAQ--ADLAYQLQVAKTKQQIEEQRVQVQVVERAQQV--AVQEQEIARREKElearvrkpaeaeryRLERLAEAEK 302
Cdd:COG0330  129 LSTGRDEinAEIREELQEALDPYGIEVVDVEIKDIDPPEEVqdAMEDRMKAERERE--------------AAILEAEGYR 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 303 AQLIMQAEAEAESVRMRGEAEAFAVGARARAEAEQMAKKAEAFQMYQEAAQLdMLLEKLPQVAEeisgpltSANKITLVS 382
Cdd:COG0330  195 EAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFY-RSLEALEEVLS-------PNSKVIVLP 266


                 ....*.
gi 158636004 383 SGSGTM 388
Cdd:COG0330  267 PDGNGF 272
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 47-158 2.03e-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: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  47 TLNVKSEKVYTRHGVPISVTGIAQVKIQgqnKEMLAAACQMFLGKTEAEiAHIaLETLEGHQRAIMAHMTVEEIYKDRQK 126
Cdd:cd02106    4 FDDVRVEPVGTADGVPVAVDLVVQFRIT---DYNALPAFYLVDFVKDIK-ADI-RRKIADVLRAAIGRMTLDQIISGRDE 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 158636004 127 FSEQVFKVASSDLVNMGISVVSYTLKDIHDDQ 158
Cdd:cd02106   79 IAKAVKEDLEEDLENFGVVISDVDITSIEPPD 110
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 14-206 1.56e-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: 51.62  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  14 SGFCRSPpvmvagGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqgqnKEMLAAACQMFLGKTE 93
Cdd:cd13435    1 SGGARGP------GVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRI----SDPLNAVIQVANYSHS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  94 AEIahIALETLeghqRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIhddqDYLHSLGKARTAqvq 173
Cdd:cd13435   71 TRL--LAATTL----RNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDV----SLPDSLQRAMAA--- 137

                        170       180       190
                 ....*....|....*....|....*....|...
gi 158636004 174 kdarigEAEAKRDAGIREAKAKQEKVSAQCLSE 206
Cdd:cd13435  138 ------EAEAAREARAKVIAAEGEMKSSRALKE 164
PRK12704 PRK12704
phosphodiesterase; Provisional
 176-348 6.95e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 51.32  E-value: 6.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 176 ARIGEAEAKRDAGIREAKAKQEKVSAQCLSEiemakAQRDYELKKATYDIEVNTRRaqADLAYQLQVAKTKQQIEEQRVQ 255
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLE-----AKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEENLDRKLE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 256 vQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYRLERLA-----EAeKAQLI--MQAEAEAESVRMRGEAEaf 325
Cdd:PRK12704 104 -LLEKREEELEKKEKELEQKQQELEKKeeeLEELIEEQLQELERISgltaeEA-KEILLekVEEEARHEAAVLIKEIE-- 179

                        170       180
                 ....*....|....*....|....*
gi 158636004 326 avgARARAEAEQMAKK--AEAFQMY 348
Cdd:PRK12704 180 ---EEAKEEADKKAKEilAQAIQRC 201
Flot pfam15975
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ...
 310-395 1.54e-06

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: 46.93  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  310 EAEAESVRMRGEAEafAVGARARAEAEQMAKKAEAFQMY---QEAAQLDM-LLEKLPQVAEEISGPLTSANKITLVSSGS 385
Cdd:pfam15975   1 EAEAEADAIKLRAE--AKRKKALAEAEGIRALNEAENALsdeQIALQVKLaLLEALPEIIAESVKPLEKIDGIKILQVDG 78

                          90
                  ....*....|
gi 158636004  386 GTMGAAKVTG 395
Cdd:pfam15975  79 LGGGAAGGGG 88
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 166-369 1.75e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 166 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQcLSEIEMAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKT 245
Cdd:COG1196  257 ELEAELAELEAELEELRLELEELELELEEAQAEEYEL-LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 246 KQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRL-ERLAEAEKAQLIMQAEAEAESVRMRGEAEA 324
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELaEELLEALRAAAELAAQLEELEEAEEALLER 415

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 158636004 325 FAVGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEEIS 369
Cdd:COG1196  416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 154-367 3.36e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 154 IHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAgiREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVNTRRAQ 233
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAELAE--LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 234 ADLAyQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRLERLAEAEKAQLIMQAEAEA 313
Cdd:COG1196  309 ERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 158636004 314 ESVRMRGEAEAFAVGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEE 367
Cdd:COG1196  388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 158-363 3.76e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 158 QDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDyelkkatydiEVNTRRAQADLA 237
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE----------AEAELAEAEEEL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 238 YQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRLE-RLAEAEKAQLIMQAEAEAESV 316
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEeEEALEEAAEEEAELEEEEEAL 461

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 158636004 317 RMRGEAEAFAVGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQ 363
Cdd:COG1196  462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
PTZ00121 PTZ00121
MAEBL; Provisional
 166-367 7.16e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 7.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  166 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAqclseiEMAKAqrdyELKKATYDIEVNTRRAQADlayQLQVAKT 245
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA------EAAKA----EAEAAADEAEAAEEKAEAA---EKKKEEA 1376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  246 KQQIEEQRVQVQVVERAQQVAVQEQEIARREKELE--ARVRKPAEAERYRLERLAEAEKAQliMQAEAEAESVRMRGEAE 323
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAK--KKAEEAKKADEAKKKAE 1454

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 158636004  324 AFAVGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKlpqvAEE 367
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK----AEE 1494
PTZ00121 PTZ00121
MAEBL; Provisional
 166-357 1.32e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  166 KARTAQVQKDARIGEAEAKRDagirEAKAKQEKVSAQCLSEIEmAKAQRDYELKKA--TYDIEVNTRRAQADLAYQLQVA 243
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAAD----EAEAAEEKAEAAEKKKEE-AKKKADAAKKKAeeKKKADEAKKKAEEDKKKADELK 1411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  244 KT---KQQIEEQRVQVQVVERAQQVAVQEQEiARREKELearvRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRG 320
Cdd:PTZ00121 1412 KAaaaKKKADEAKKKAEEKKKADEAKKKAEE-AKKADEA----KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 158636004  321 EAEAFAVGARARAE----AEQMAKKAEAFQMYQEAAQLDML 357
Cdd:PTZ00121 1487 EAKKKAEEAKKKADeakkAAEAKKKADEAKKAEEAKKADEA 1527
PTZ00121 PTZ00121
MAEBL; Provisional
 168-368 1.37e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  168 RTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDyELKKATydiEVNTRRAQADLAYQLQVAKTKQ 247
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAE---EEKKKVEQLKKKEAEEKKKAEE 1651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  248 -QIEEQRVQVqvveRAQQVAVQEQEIARREKEL---EARVRKPAEAERYRLErlaEAEKAQLIMQAEAE----AESVRmR 319
Cdd:PTZ00121 1652 lKKAEEENKI----KAAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKKEAE---EAKKAEELKKKEAEekkkAEELK-K 1723

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 158636004  320 GEAEAFAVGARARAEAEQMAKKAEAFQMYQ-EAAQLDMLLEKLPQVAEEI 368
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEEAKKDEeEKKKIAHLKKEEEKKAEEI 1773
PTZ00121 PTZ00121
MAEBL; Provisional
 164-367 1.69e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  164 LGKARTAQVQKDARigEAEAKRDAgiREAKAKQEKVSAQCLSEIEMAKAQ---RDYELKKATYDIEVNTRRAQADLAYQL 240
Cdd:PTZ00121 1527 AKKAEEAKKADEAK--KAEEKKKA--DELKKAEELKKAEEKKKAEEAKKAeedKNMALRKAEEAKKAEEARIEEVMKLYE 1602

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  241 QVAKTK----QQIEEQRVQVQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYRLERLAEAEKAQLIMQAEAEA 313
Cdd:PTZ00121 1603 EEKKMKaeeaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 158636004  314 ESVRMRGEAEAFAVGARARAEAEQMAKKAE-----AFQMYQEAAQLDMLLEKLPQVAEE 367
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAeekkkAEELKKAEEENKIKAEEAKKEAEE 1741
PTZ00121 PTZ00121
MAEBL; Provisional
 166-353 1.74e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  166 KARTAQVQKDARIGEaEAKRDAGIR---EAKAKQEKVSAQCLSEIEMAK----AQRDYELKKATydievNTRRAQADLAY 238
Cdd:PTZ00121 1135 KAEDARKAEEARKAE-DAKRVEIARkaeDARKAEEARKAEDAKKAEAARkaeeVRKAEELRKAE-----DARKAEAARKA 1208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  239 Q-LQVAKTKQQIEEQRvQVQVVERAQQVAVQEQEIARREKE-LEARVRKPAEAERYRLERLA------EAEKAQLIMQAE 310
Cdd:PTZ00121 1209 EeERKAEEARKAEDAK-KAEAVKKAEEAKKDAEEAKKAEEErNNEEIRKFEEARMAHFARRQaaikaeEARKADELKKAE 1287

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 158636004  311 A--------EAESVRMRGEAEAFAVGAR----ARAEAEQMAKKAEAFQMYQEAAQ 353
Cdd:PTZ00121 1288 EkkkadeakKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKKKADAAKKKAEEAK 1342
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 167-352 3.53e-05

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.61  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  167 ARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATydievntRRAQADLAYQLQVAKTK 246
Cdd:TIGR02794  53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE-------QAAKQAEEKQKQAEEAK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  247 QQIEEQRVQVQVVERAQQVAvqeqEIARREKELEARVRKPAEAERYRLERLAEAEKAQlimQAEAEAESVRMRGEAEAFA 326
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAK----EEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA---KAKAEAEAKAKAEEAKAKA 198

                         170       180
                  ....*....|....*....|....*.
gi 158636004  327 VGARARAEAEQmAKKAEAFQMYQEAA 352
Cdd:TIGR02794 199 EAAKAKAAAEA-AAKAEAEAAAAAAA 223
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 27-206 4.95e-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: 44.08  E-value: 4.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqgQNKEMLAAACQMFLGKTEAeiahIALETLeg 106
Cdd:cd03403    8 GLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRV--QNATIAVTNVENADRSTRL----LAQTTL-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 107 hqRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHddqdylhslgkaRTAQVQKdARIGEAEAKRD 186
Cdd:cd03403   80 --RNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVR------------LPVQLQR-AMAAEAEAARE 144

                        170       180
                 ....*....|....*....|
gi 158636004 187 AGIREAKAKQEKVSAQCLSE 206
Cdd:cd03403  145 ARAKVIAAEGEQNASRALKE 164
PTZ00121 PTZ00121
MAEBL; Provisional
 166-351 5.71e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 5.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  166 KARTAQVQKDARIGEAEAKRDAGirEAKAKQEKVSAQCLSEIEmAKAQRDyELKKATYDIEVNTRRAQADLAYQLQVAKT 245
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAA--EAAKAEAEAAADEAEAAE-EKAEAA-EKKKEEAKKKADAAKKKAEEKKKADEAKK 1398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  246 KQqiEEQRVQVQVVERAQQVAVQEQEIARR--EKELEARVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAE 323
Cdd:PTZ00121 1399 KA--EEDKKKADELKKAAAAKKKADEAKKKaeEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476

                         170       180       190
                  ....*....|....*....|....*....|..
gi 158636004  324 AFAVGAR----ARAEAEQMAKKAEAFQMYQEA 351
Cdd:PTZ00121 1477 KKAEEAKkadeAKKKAEEAKKKADEAKKAAEA 1508
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 2-187 6.64e-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: 43.66  E-value: 6.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   2 FFTCGPNEAMVVSGFCRSPPVMVAG-GRVFVLPCIQQIQRISLNTLTLNVKSEkVYTRHGVPISVTGIAQVKIqgqNKEM 80
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGVKDEVLGeGLHFKIPWIQVVIIYDVRTQPREITLT-VLSKDGQTVNIDLSVLYRP---DPEK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  81 LAaacQMF--LGKTEAE--IAHIALETLeghqRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHD 156
Cdd:cd03401   77 LP---ELYqnLGPDYEErvLPPIVREVL----KAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDF 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 158636004 157 DQDYLHS----------LGKAR----TAQVQKDARIGEAEAKRDA 187
Cdd:cd03401  150 PDEYEKAieakqvaeqeAERAKfeleKAEQEAERKVIEAEGEAEA 194
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 33-194 7.42e-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: 7.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  33 PCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFlgkteaEIAHIALETLeghqRAIM 112
Cdd:cd08826    1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRY------ATSQLAQTTL----RSVV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 113 AHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREA 192
Cdd:cd08826   71 GQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLA 150


                 ..
gi 158636004 193 KA 194
Cdd:cd08826  151 EA 152
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 166-340 7.99e-05

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 44.94  E-value: 7.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 166 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAqclseiEMAKAQRDYELKKATydIEVNTRRAQAdlayqlqvAKT 245
Cdd:PRK05035 531 RARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQA------ANAEAEEEVDPKKAA--VAAAIARAKA--------KKA 594

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 246 KQQIEEQRVQVQVVERAQQVAVQEQEIARRE--KELEARVRKPAEAERYRLERL------AEAEKAQLIMQAEAEAESVR 317
Cdd:PRK05035 595 AQQAASAEPEEQVAEVDPKKAAVAAAIARAKakKAEQQANAEPEEPVDPRKAAVaaaiarAKARKAAQQQANAEPEEAED 674

                        170       180
                 ....*....|....*....|...
gi 158636004 318 MRGEAEAFAVgarARAEAEQMAK 340
Cdd:PRK05035 675 PKKAAVAAAI---ARAKAKKAAQ 694
mukB PRK04863
chromosome partition protein MukB;
191-299 8.54e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.95  E-value: 8.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  191 EAKAKQEKVSAQCLSEIEMAKAQRDyELKKATYDIEVNTRRAQADLAYQLQVAK----------TKQQIEEQRVQVQVVE 260
Cdd:PRK04863  562 ELEARLESLSESVSEARERRMALRQ-QLEQLQARIQRLAARAPAWLAAQDALARlreqsgeefeDSQDVTEYMQQLLERE 640

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 158636004  261 RAQQvaVQEQEIARREKELEARVRK---PAEAERYRLERLAE 299
Cdd:PRK04863  641 RELT--VERDELAARKQALDEEIERlsqPGGSEDPRLNALAE 680
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 241-344 9.46e-05

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


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 43.82  E-value: 9.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 241 QVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEArvRKPAEaeryrlerLAEAEKAQLIMqaEAEAESVRMRG 320
Cdd:cd03406  163 AIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEA--EKDAE--------VAKIQMQQKIM--EKEAEKKISEI 230

                         90       100
                 ....*....|....*....|....*.
gi 158636004 321 EAEAFAVGARARAEAE--QMAKKAEA 344
Cdd:cd03406  231 EDEMHLAREKARADAEyyRALREAEA 256
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 243-353 1.19e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.03  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 243 AKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRleRLAEAEKAQLIMQAEAEAESVRMRGEA 322
Cdd:PRK09510  74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAA--KQAALKQKQAEEAAAKAAAAAKAKAEA 151

                         90       100       110
                 ....*....|....*....|....*....|.
gi 158636004 323 EAFAVGARARAEAEQMAKKAEAFQMYQEAAQ 353
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 244-305 1.62e-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: 43.44  E-value: 1.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158636004 244 KTKQQIEEQRV-QVQVVERAQQVAvqEQEIARREKELE-----ARVRKPAEAERYRLERLAEAEKAQL 305
Cdd:cd03406  196 RKRAVIEAEKDaEVAKIQMQQKIM--EKEAEKKISEIEdemhlAREKARADAEYYRALREAEANKLKL 261
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 173-378 2.06e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  173 QKDARI-GEAEAKRDAGIREaKAKQEKVSAQCLSEIEMAKAQ---RDYELKKATYDIEVNTRRA-QADLAYQLQVAKTKQ 247
Cdd:pfam17380 389 QKNERVrQELEAARKVKILE-EERQRKIQQQKVEMEQIRAEQeeaRQREVRRLEEERAREMERVrLEEQERQQQVERLRQ 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  248 QIEEQRVQVQVVERAQQVAVQEQEIARR--EKELEARVRKPAEAERYR--LER-LAEAEKAQLIMQAEAEAESVRmRGEA 322
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRklLEKeMEERQKAIYEEERRREAEEER-RKQQ 546

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158636004  323 EafaVGARARAEaEQMAKKAEAFQ----MYQEAAQLDMLLEKLPQVAE-EISGPLTSANKI 378
Cdd:pfam17380 547 E---MEERRRIQ-EQMRKATEERSrleaMEREREMMRQIVESEKARAEyEATTPITTIKPI 603
growth_prot_Scy NF041483
polarized growth protein Scy;
166-353 2.25e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 43.66  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  166 KARTAQVQKDARI--GEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKAtydievntrRAQADlayqlqVA 243
Cdd:NF041483  432 RAKTVELQEEARRlrGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKA---------KADAD------EL 496

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  244 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKelearvrkpAEAERYRLERLAEAEKaqliMQAEAEAESVRMRGEAE 323
Cdd:NF041483  497 RSTATAESERVRTEAIERATTLRRQAEETLERTR---------AEAERLRAEAEEQAEE----VRAAAERAARELREETE 563

                         170       180       190
                  ....*....|....*....|....*....|
gi 158636004  324 AFAVGARARAEAEQMAKKAEAFQMYQEAAQ 353
Cdd:NF041483  564 RAIAARQAEAAEELTRLHTEAEERLTAAEE 593
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 27-200 3.02e-04

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: 41.80  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGqnkemlaaACQMFlgKTEAEIAHIALETLEG 106
Cdd:cd08827   30 GLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIEN--------ASVCL--SSFASISDAMQALVQT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 107 HQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRD 186
Cdd:cd08827  100 TVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAEAQRQAKVKVIAAEGEKA 179

                        170
                 ....*....|....
gi 158636004 187 AGiREAKAKQEKVS 200
Cdd:cd08827  180 AS-EALKAAAESLS 192
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 27-197 3.47e-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: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQgqnkemlAAACQMflgkTEAEIAHIALETL-E 105
Cdd:cd08828    4 GLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQ-------SAVKAV----ANVNNVHIATFLLaQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 106 GHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIhddqdylhslgkaRTAQVQKDARIGEAEAKR 185
Cdd:cd08828   73 TTLRNVLGTQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDV-------------RIPVQMQRAMAAEAEATR 139

                        170
                 ....*....|..
gi 158636004 186 DAGIREAKAKQE 197
Cdd:cd08828  140 EARAKVVAAEGE 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 209-359 4.37e-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: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 209 MAKAQRDYELKKATYDIEVNTRRAQADLAyQLQVAKTKQQIEEQRVQVQVVE-RAQQVAVQEQEIARREKELEARVRKPA 287
Cdd:COG1196  230 LLLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELElELEEAQAEEYELLAELARLEQDIARLE 308

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158636004 288 EAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAVGARARAEAEQMAKKAEAFQMYQEAAQLDMLLE 359
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 166-341 4.46e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.42  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  166 KARTAQVQKDARIgEAEAKRDAGIR----------EAKAKQEKVSAQCLSeIEMAKAQrdyELKKATYDIEVNTRRAQAD 235
Cdd:pfam17380 323 KARQAEMDRQAAI-YAEQERMAMERerelerirqeERKRELERIRQEEIA-MEISRMR---ELERLQMERQQKNERVRQE 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  236 L----AYQLQVAKTKQQIEEQRVQVQVVeRAQQVAVQEQEIARREKEleaRVRkpaEAERYRLERLAEAEKAQLIMQAEA 311
Cdd:pfam17380 398 LeaarKVKILEEERQRKIQQQKVEMEQI-RAEQEEARQREVRRLEEE---RAR---EMERVRLEEQERQQQVERLRQQEE 470

                         170       180       190
                  ....*....|....*....|....*....|
gi 158636004  312 EAESVRMRGEAEafavgARARAEAEQMAKK 341
Cdd:pfam17380 471 ERKRKKLELEKE-----KRDRKRAEEQRRK 495
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 69-310 5.59e-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: 42.52  E-value: 5.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004    69 AQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVS 148
Cdd:pfam12128  616 AREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD 695

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   149 YTLKDIHDDQDylhslGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVN 228
Cdd:pfam12128  696 KKHQAWLEEQK-----EQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVI 770

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   229 TRRAQ--ADLAYQL-QVAKTKQQIEEQRV--QVQVVERAQQVAVQEQEIARREKELEARV-RKPAEAERYR--LERLAEA 300
Cdd:pfam12128  771 AKLKReiRTLERKIeRIAVRRQEVLRYFDwyQETWLQRRPRLATQLSNIERAISELQQQLaRLIADTKLRRakLEMERKA 850

                          250
                   ....*....|
gi 158636004   301 EKAQLIMQAE 310
Cdd:pfam12128  851 SEKQQVRLSE 860
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 168-352 6.00e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 6.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 168 RTAQVQKDARIGEAEAKRDAGIREAKAKQEK-VSAQCLSEIEMAKAQRDYELKKA---TYDIEVNTRRAQADLAYQLQVA 243
Cdd:PRK09510  66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQaAEQERLKQLEKERLAAQEQKKQAeeaAKQAALKQKQAEEAAAKAAAAA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 244 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERyrlERLAEAEKaqlimQAEAEAES-----VRM 318
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAA---KAAAEAKK-----KAEAEAKKkaaaeAKK 217

                        170       180       190
                 ....*....|....*....|....*....|....
gi 158636004 319 RGEAEAFAVGARARAEAEQMAKKAEAFQMYQEAA 352
Cdd:PRK09510 218 KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAA 251
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
180-368 8.33e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  180 EAEAKRDA--GIREAKAKQEKVSAQ------CLSEIEMAKAQRDYELKKATYDievNTRRAQADLayQLQVAKTKQQIEE 251
Cdd:COG4913   246 DAREQIELlePIRELAERYAAARERlaeleyLRAALRLWFAQRRLELLEAELE---ELRAELARL--EAELERLEARLDA 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  252 QRVQVQVVERA------QQVAVQEQEIARREKELEARVRKpaeaeRYRLERLAeaekAQLIMQAEAEAESVrmrgeAEAF 325
Cdd:COG4913   321 LREELDELEAQirgnggDRLEQLEREIERLERELEERERR-----RARLEALL----AALGLPLPASAEEF-----AALR 386

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 158636004  326 AVGARARAEAEQMAKKAEAfQMYQEAAQLDMLLEKLPQVAEEI 368
Cdd:COG4913   387 AEAAALLEALEEELEALEE-ALAEAEAALRDLRRELRELEAEI 428
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 197-356 8.38e-04

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.53  E-value: 8.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  197 EKVSAQCLSEIEmakaqRDYELKKATYDI-----EVNTRRAQAdLAYQLQVAKtkQQIEEQRVQVQVVERA---QQVAVQ 268
Cdd:pfam05262 180 KKVVEALREDNE-----KGVNFRRDMTDLkeresQEDAKRAQQ-LKEELDKKQ--IDADKAQQKADFAQDNadkQRDEVR 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  269 EQEIARREKELEARVRKPAEAERYRLERLAEAEKAQliMQAEAEAESVRMRGEAEAFAVGARARAEAEQMAKKAEAFQMY 348
Cdd:pfam05262 252 QKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQ--IEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKK 329


                  ....*...
gi 158636004  349 QEAAQLDM 356
Cdd:pfam05262 330 REPVAEDL 337
PTZ00121 PTZ00121
MAEBL; Provisional
 166-368 1.17e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  166 KARTAQVQKDARIGEAEAKR------DAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATydievNTRRAQadlayQ 239
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKaeeernNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE-----EKKKAD-----E 1294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  240 LQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARV---RKPAEAERYRLERLAEAEKAQLIMQAEAEAESV 316
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAeeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 158636004  317 RMRGEAEAFAVGARARAEAEQMAKKAEAFQMYQE----AAQLDMLLEKLPQVAEEI 368
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADelkkAAAAKKKADEAKKKAEEK 1430
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 206-369 1.78e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 206 EIEMAKAQRDYELKKATYDiEVNTRRAQADLAYQLQVAKTKQQIEEQR-VQVQVVERAQQVAVQEQEIAR---REKELEA 281
Cdd:COG1196  217 ELKEELKELEAELLLLKLR-ELEAELEELEAELEELEAELEELEAELAeLEAELEELRLELEELELELEEaqaEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 282 RVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAVGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKL 361
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375


                 ....*...
gi 158636004 362 PQVAEEIS 369
Cdd:COG1196  376 EAEEELEE 383
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 194-406 1.83e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 40.81  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  194 AKQEKVSAQCLSEIEMAKAQRDYELKKATYDIE--------VNTRRAQADLAY-QLQVAKTKQQIEEqrvqvqvVERAQQ 264
Cdd:PRK10929  125 AQQEQDRAREISDSLSQLPQQQTEARRQLNEIErrlqtlgtPNTPLAQAQLTAlQAESAALKALVDE-------LELAQL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  265 VAVQEQEIARREKELearvrkpAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAVGARARAEAEQMAKKAEA 344
Cdd:PRK10929  198 SANNRQELARLRSEL-------AKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINREL 270

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158636004  345 FQMY-QEAAQLDMLLEKLPQVAEEIsgpLTSANKITLVSSGSGTMGAAKVTGEVL-DILSRLPE 406
Cdd:PRK10929  271 SQALnQQAQRMDLIASQQRQAASQT---LQVRQALNTLREQSQWLGVSNALGEALrAQVARLPE 331
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
162-358 1.84e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 162 HSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRD-YELKKATYDIEVNTRRAQADLA-YQ 239
Cdd:COG4717   66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEkLEKLLQLLPLYQELEALEAELAeLP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 240 LQVAKTKQQIEEQRvqvqvvERAQQVAVQEQEIARREKELEARVRKPAEAERYRLERLaeAEKAQLIMQAEAEAESVRMR 319
Cdd:COG4717  146 ERLEELEERLEELR------ELEEELEELEAELAELQEELEELLEQLSLATEEELQDL--AEELEELQQRLAELEEELEE 217

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 158636004 320 GEAEAfavgARARAEAEQMAKKAEAFQMYQEAAQLDMLL 358
Cdd:COG4717  218 AQEEL----EELEEELEQLENELEAAALEERLKEARLLL 252
PTZ00121 PTZ00121
MAEBL; Provisional
 180-322 2.15e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  180 EAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKAtydiEVNTRRAQADLAYQLQVAKTKQQI----EEQRVQ 255
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA----EEDEKKAAEALKKEAEEAKKAEELkkkeAEEKKK 1717

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158636004  256 VQVVERAQQVAVQEQEIARREKELEARvrkpaEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEA 322
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKK-----KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 249-364 2.38e-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: 39.42  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 249 IEEQRVQVQVVERAQQV--AVQEQEIARREKElearvRKPAEAERYRLERLAEA--EKAQLIMQAEAEAESVRmrgeaea 324
Cdd:cd03404  156 IEIVQVQLQDADPPEEVqdAFDDVNAARQDKE-----RLINEAQAYANEVIPRArgEAARIIQEAEAYKAEVV------- 223

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 158636004 325 favgARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQV 364
Cdd:cd03404  224 ----ARAEGDAARFLALLAEYRKAPEVTRERLYLETMEEV 259
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-367 2.86e-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: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004    73 IQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAImahmtvEEIYKDRQKFSEQvfkvASSDLVNMGISVVSYTLK 152
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEEL------EEELEQLRKELEE----LSRQISALRKDLARLEAE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   153 dIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQclseieMAKAQRDYELKKATYDIEVNTRRA 232
Cdd:TIGR02168  742 -VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ------IEQLKEELKALREALDELRAELTL 814

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   233 QADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRLERLAEAEKAQLIMQAEAE 312
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 158636004   313 AESVRMRGEAEAFAVGARARAEAEQMAKKAEAFQMYQEAAQLDmLLEKLPQVAEE 367
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR-IDNLQERLSEE 948
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 27-131 3.53e-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: 37.38  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqgqnKEMLAAACQMF-LGKTEAEIAHIALETle 105
Cdd:cd13436   10 GIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRI----WDPVLSVMAVQdLNTSTRTTAQTSLTN-- 83

                         90       100
                 ....*....|....*....|....*.
gi 158636004 106 ghqraIMAHMTVEEIYKDRQKFSEQV 131
Cdd:cd13436   84 -----SLSKKTVREIQSDRRKINEEL 104
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 266-349 3.85e-03

High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259803 [Multi-domain]  Cd Length: 249  Bit Score: 38.62  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 266 AVQEQEIARREKELEA-RVRKPAEAERYRlerlAEAEKAQLIMQAEAEAESVRMRGEAEAfavgARARAEAEQMAKKAEA 344
Cdd:cd03405  157 SVYERMRAERERIAAEyRAEGEEEAEKIR----AEADRERTVILAEAYREAEEIRGEGDA----EAARIYAEAYGKDPEF 228


                 ....*
gi 158636004 345 FQMYQ 349
Cdd:cd03405  229 YSFYR 233
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 171-384 5.08e-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: 39.27  E-value: 5.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   171 QVQKDARIGEAEAKRDAgIREAKAKQEKVSAQCLSEIEMAKAqrdyELKKATYDIEVNTRRAQADlayqlqvaktKQQIE 250
Cdd:TIGR02168  318 LEELEAQLEELESKLDE-LAEELAELEEKLEELKEELESLEA----ELEELEAELEELESRLEEL----------EEQLE 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004   251 EQRVQVqvVERAQQVAVQEQEIARREKELE---ARVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAV 327
Cdd:TIGR02168  383 TLRSKV--AQLELQIASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 158636004   328 GARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSG 384
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 164-326 5.23e-03

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: 38.98  E-value: 5.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 164 LGKARTAQVQKDARIGEAEAKRDAgIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVNTRR---------AQA 234
Cdd:COG4942   71 IRALEQELAALEAELAELEKEIAE-LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRlqylkylapARR 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 235 DLAYQLQ-----VAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKE-LEARVRKPAEAERYRLERLAEAEKA--QLI 306
Cdd:COG4942  150 EQAEELRadlaeLAALRAELEAERAELEALLAELEEERAALEALKAERQkLLARLEKELAELAAELAELQQEAEEleALI 229

                        170       180
                 ....*....|....*....|
gi 158636004 307 MQAEAEAESVRMRGEAEAFA 326
Cdd:COG4942  230 ARLEAEAAAAAERTPAAGFA 249
growth_prot_Scy NF041483
polarized growth protein Scy;
170-373 5.68e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.04  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  170 AQVQKDARIGEAEAKRDAG-IR-EAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKTKQ 247
Cdd:NF041483  887 ASAEQDAARTRADAREDANrIRsDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEA 966

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  248 QIEEQRVQVqvvERAQQVAVQEQEIARREKELEaRVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAV 327
Cdd:NF041483  967 TGEAERLRA---EAAETVGSAQQHAERIRTEAE-RVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADTL 1042

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 158636004  328 GARARAEAEQMAKKA--EAFQMYQEA-AQLDMLLEKLPQVAEEISGPLT 373
Cdd:NF041483 1043 ITEAAAEADQLTAKAqeEALRTTTEAeAQADTMVGAARKEAERIVAEAT 1091
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 278-346 6.17e-03

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


Pssm-ID: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 38.33  E-value: 6.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158636004 278 ELEARVRKPA----EAERYRL--ERLAEAEKAQLIMQAEAEAESVRMRGEaeafAVGARARAEAEQMAKKAEAFQ 346
Cdd:cd03407  143 EPDASVKAAMneinAAQRLREaaEEKAEAEKILQVKAAEAEAEAKRLQGV----GIAEQRKAIVDGLRESIEDFQ 213
ASD2 pfam08687
Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which ...
 209-314 7.00e-03

Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure.


Pssm-ID: 462561 [Multi-domain]  Cd Length: 290  Bit Score: 38.01  E-value: 7.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  209 MAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKTKQQ-IEEQRVQVQVVERAQQvAVQE--QEIARREKELEARVR- 284
Cdd:pfam08687  80 APKAELLTKMKDLTTLPSPDQPEEQGEEELDNDLQQKKVElIESLQRKLQVLREEQE-ALQEeiQANAALGAEVEALVQe 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 158636004  285 --KPAEAERYRL----------------ERLAEAEKAQLIMQAEAEAE 314
Cdd:pfam08687 159 vcKPNELEKYRMfigdlekvvslllslsGRLARVENALSSLDSDADAE 206
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 191-300 7.77e-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: 38.78  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004  191 EAKAKQEKVSAQcLSEIEMAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKTKQQIEEQ---RVQV-----QVVERA 262
Cdd:COG3096   561 ELEAQLEELEEQ-AAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEAladSQEVtaamqQLLERE 639

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 158636004  263 QQVAVQEQEIARREKELEARVRK---PAEAERYRLERLAEA 300
Cdd:COG3096   640 REATVERDELAARKQALESQIERlsqPGGAEDPRLLALAER 680
PTZ00491 PTZ00491
major vault protein; Provisional
 262-353 9.47e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 38.46  E-value: 9.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158636004 262 AQQVA-VQEQEiARREKELEaRVRKPAEAERYRLERL-AEAEKAQLIMQ----AEAEAESVRMRGEAEAFAVGARARAEA 335
Cdd:PTZ00491 668 ARHQAeLLEQE-ARGRLERQ-KMHDKAKAEEQRTKLLeLQAESAAVESSgqsrAEALAEAEARLIEAEAEVEQAELRAKA 745

                         90
                 ....*....|....*...
gi 158636004 336 EQMAKKAEAFQMYQEAAQ 353
Cdd:PTZ00491 746 LRIEAEAELEKLRKRQEL 763
 
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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