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Conserved domains on  [gi|13929186|ref|NP_114018|]
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flotillin-2 isoform 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];
5-427 2.65e-85

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


:

Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 267.51  E-value: 2.65e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   5 HTVGPNEALVVSGGccGSDYKQYVFGGwAWAWWCISDTQRLSLEVMTI-LCRCENIETSEGVPLFVTGVAQVKIMTEKEL 83
Cdd:COG2268  29 RKVPPNEALVITGR--GGGYKVVTGGG-AFVLPVLHRAERMSLSTMTIeVERTEGLITKDGIRVDVDAVFYVKVNSDPED 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  84 LAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDY 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 164 LSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADT-----KIADSKRAFELQKSAFSEEVNIKTAEAQ 238
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAE 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 239 LAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAegekvkqvllaqaeaek 318
Cdd:COG2268 266 AAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA----------------- 325

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 319 irkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEIVVLSGDNSK--VTSEVN 396
Cdd:COG2268 326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVA 400

                       410       420       430
                ....*....|....*....|....*....|.
gi 13929186 397 RLLAELPASVHALTGVDLSKipLIKNATGAQ 427
Cdd:COG2268 401 EALAPLLESLLEETGLDLPG--LLKGLTGAG 429
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
5-427 2.65e-85

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 267.51  E-value: 2.65e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   5 HTVGPNEALVVSGGccGSDYKQYVFGGwAWAWWCISDTQRLSLEVMTI-LCRCENIETSEGVPLFVTGVAQVKIMTEKEL 83
Cdd:COG2268  29 RKVPPNEALVITGR--GGGYKVVTGGG-AFVLPVLHRAERMSLSTMTIeVERTEGLITKDGIRVDVDAVFYVKVNSDPED 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  84 LAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDY 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 164 LSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADT-----KIADSKRAFELQKSAFSEEVNIKTAEAQ 238
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAE 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 239 LAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAegekvkqvllaqaeaek 318
Cdd:COG2268 266 AAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA----------------- 325

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 319 irkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEIVVLSGDNSK--VTSEVN 396
Cdd:COG2268 326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVA 400

                       410       420       430
                ....*....|....*....|....*....|.
gi 13929186 397 RLLAELPASVHALTGVDLSKipLIKNATGAQ 427
Cdd:COG2268 401 EALAPLLESLLEETGLDLPG--LLKGLTGAG 429
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 34-178 2.07e-65

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: 205.82  E-value: 2.07e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  34 WAWWCISDTQRLSLEVMTILCRCENIETSEGVPLFVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRS 113
Cdd:cd03399   1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRA 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13929186 114 ILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRD 178
Cdd:cd03399  81 IVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 6-188 5.94e-20

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 86.61  E-value: 5.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186     6 TVGPNEALVVSGGccgSDYKQYVFGGWAWAWWCISDTQRLSLEVMTILCRCENIETSEGVPLFVTGVAQVKIMTEKELLA 85
Cdd:pfam01145   2 IVPPGEVGVVTRF---GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186    86 VAceQFLGKNvqDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLS 165
Cdd:pfam01145  79 VQ--NVFGSD--DLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154

                         170       180
                  ....*....|....*....|...
gi 13929186   166 SLGKTQTAVVQRDADIGVAEAER 188
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 87-269 2.08e-13

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 67.69  E-value: 2.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186     87 ACEQFLGKNVQDIKNVVLQTLEghlRSILGTLTVEQIYQDRdqfaKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSS 166
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDV----KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186    167 LGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVkfmadtkiadskraFELQKSAFSEEVN--IKTAEAQLAYELQ 244
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDEL--------------LTDQREKISENIReeLNEAAEAWGIKVE 139

                          170       180
                   ....*....|....*....|....*
gi 13929186    245 GAReqqkIRQEEIEIEVVQRKKQIA 269
Cdd:smart00244 140 DVE----IKDIRLPEEIKEAMEAQQ 160
PTZ00121 PTZ00121
MAEBL; Provisional
 185-401 4.33e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   185 EAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAfSEEVNIKTAEAQLAYELQGAR---------EQQKIRQE 255
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARieevmklyeEEKKMKAE 1610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   256 EIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEaavieamgK 335
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK--------K 1682

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13929186   336 AEAERMKlKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEIVVLSGDNSKVTSEVNRLLAE 401
Cdd:PTZ00121 1683 AEEDEKK-AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 207-390 4.05e-06

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: 48.69  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   207 MADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATV 286
Cdd:TIGR02794  59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   287 RRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEA-AVIEAMGKAEAERMKLKAEAYQKYGDA---AKMALVLE 362
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAkAKAEAEAKAKAEEAKAKAEAAKAKAAAeaaAKAEAEAA 218

                         170       180
                  ....*....|....*....|....*...
gi 13929186   363 ALPQIAAKISAPLTKVDEIVVLSGDNSK 390
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLASGSNA 246
growth_prot_Scy NF041483
polarized growth protein Scy;
229-358 9.93e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 38.27  E-value: 9.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   229 EVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIaveaqeilrtDKELiatVRRPAEAEAHRIQQIAEGEKvkq 308
Cdd:NF041483   93 ERELRDARAQTQRILQEHAEHQARLQAELHTEAVQRRQQL----------DQEL---AERRQTVESHVNENVAWAEQ--- 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 13929186   309 vLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMA 358
Cdd:NF041483  157 -LRARTESQARRLLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESA 205
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
5-427 2.65e-85

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 267.51  E-value: 2.65e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   5 HTVGPNEALVVSGGccGSDYKQYVFGGwAWAWWCISDTQRLSLEVMTI-LCRCENIETSEGVPLFVTGVAQVKIMTEKEL 83
Cdd:COG2268  29 RKVPPNEALVITGR--GGGYKVVTGGG-AFVLPVLHRAERMSLSTMTIeVERTEGLITKDGIRVDVDAVFYVKVNSDPED 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  84 LAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDY 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 164 LSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADT-----KIADSKRAFELQKSAFSEEVNIKTAEAQ 238
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAE 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 239 LAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAegekvkqvllaqaeaek 318
Cdd:COG2268 266 AAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA----------------- 325

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 319 irkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEIVVLSGDNSK--VTSEVN 396
Cdd:COG2268 326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVA 400

                       410       420       430
                ....*....|....*....|....*....|.
gi 13929186 397 RLLAELPASVHALTGVDLSKipLIKNATGAQ 427
Cdd:COG2268 401 EALAPLLESLLEETGLDLPG--LLKGLTGAG 429
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 34-178 2.07e-65

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: 205.82  E-value: 2.07e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  34 WAWWCISDTQRLSLEVMTILCRCENIETSEGVPLFVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRS 113
Cdd:cd03399   1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRA 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13929186 114 ILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRD 178
Cdd:cd03399  81 IVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 48-160 1.70e-20

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: 86.26  E-value: 1.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  48 EVMTILCRCENIETSEGVPLFVTGVAQVKIMTEKELLAVAceqfLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDR 127
Cdd:cd02106   1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFY----LVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGR 76

                        90       100       110
                ....*....|....*....|....*....|...
gi 13929186 128 DQFAKLVREVAAPDVGRMGIEILSFTIKDVYDK 160
Cdd:cd02106  77 DEIAKAVKEDLEEDLENFGVVISDVDITSIEPP 109
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 6-188 5.94e-20

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 86.61  E-value: 5.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186     6 TVGPNEALVVSGGccgSDYKQYVFGGWAWAWWCISDTQRLSLEVMTILCRCENIETSEGVPLFVTGVAQVKIMTEKELLA 85
Cdd:pfam01145   2 IVPPGEVGVVTRF---GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186    86 VAceQFLGKNvqDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLS 165
Cdd:pfam01145  79 VQ--NVFGSD--DLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154

                         170       180
                  ....*....|....*....|...
gi 13929186   166 SLGKTQTAVVQRDADIGVAEAER 188
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 87-269 2.08e-13

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 67.69  E-value: 2.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186     87 ACEQFLGKNVQDIKNVVLQTLEghlRSILGTLTVEQIYQDRdqfaKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSS 166
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDV----KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186    167 LGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVkfmadtkiadskraFELQKSAFSEEVN--IKTAEAQLAYELQ 244
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDEL--------------LTDQREKISENIReeLNEAAEAWGIKVE 139

                          170       180
                   ....*....|....*....|....*
gi 13929186    245 GAReqqkIRQEEIEIEVVQRKKQIA 269
Cdd:smart00244 140 DVE----IKDIRLPEEIKEAMEAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 42-360 7.46e-11

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 62.55  E-value: 7.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  42 TQRLSLEVMTILcrcenieTSEGVPLFVTGVAQVKIMTEKELLavaceqflgKNVQDIKNVVLQTLEGHLRSILGTLTVE 121
Cdd:COG0330  63 EQVLDVPPQEVL-------TKDNNIVDVDAVVQYRITDPAKFL---------YNVENAEEALRQLAESALREVIGKMTLD 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 122 QIY-QDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVydkvdYLSSlgKTQTAVVQRdadigvAEAERDagireaeckke 200
Cdd:COG0330 127 EVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDI-----DPPE--EVQDAMEDR------MKAERE----------- 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 201 mldvkfmadtkiadsKRAFElqksafseevniktaeaqlaYELQGAREQQKIRqeeieievvqrkkqiaveaqeilrtdk 280
Cdd:COG0330 183 ---------------REAAI--------------------LEAEGYREAAIIR--------------------------- 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 281 eliatvrrpAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAeaavIEAMGKAEAERMklkAEAYQK-YGDAAKMAL 359
Cdd:COG0330 201 ---------AEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEA----YSAAPFVLFYRS---LEALEEvLSPNSKVIV 264


                .
gi 13929186 360 V 360
Cdd:COG0330 265 L 265
Flot pfam15975
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ...
 313-387 1.19e-08

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: 53.10  E-value: 1.19e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13929186   313 QAEAEKIRKIGEAEAavIEAMGKAEAERMKLKAEAYQKYGD---AAKMAL-VLEALPQIAAKISAPLTKVDEIVVLSGD 387
Cdd:pfam15975   1 EAEAEADAIKLRAEA--KRKKALAEAEGIRALNEAENALSDeqiALQVKLaLLEALPEIIAESVKPLEKIDGIKILQVD 77
PTZ00121 PTZ00121
MAEBL; Provisional
 185-401 4.33e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   185 EAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAfSEEVNIKTAEAQLAYELQGAR---------EQQKIRQE 255
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARieevmklyeEEKKMKAE 1610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   256 EIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEaavieamgK 335
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK--------K 1682

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13929186   336 AEAERMKlKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEIVVLSGDNSKVTSEVNRLLAE 401
Cdd:PTZ00121 1683 AEEDEKK-AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
PTZ00121 PTZ00121
MAEBL; Provisional
 186-358 4.84e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   186 AERDAGIReAECKKEMLDVKFMADTKIADSKRAFELQKSAfsEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRK 265
Cdd:PTZ00121 1266 ARRQAAIK-AEEARKADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   266 KQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAER----- 340
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKkkade 1422

                         170
                  ....*....|....*...
gi 13929186   341 MKLKAEAYQKYGDAAKMA 358
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKA 1440
PTZ00121 PTZ00121
MAEBL; Provisional
 184-380 5.47e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 5.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   184 AEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEE------- 256
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkkaee 1651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   257 ---IEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAE----AEKIRKIGEAEAAV 329
Cdd:PTZ00121 1652 lkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEekkkAEELKKAEEENKIK 1731

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13929186   330 IEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDE 380
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
PTZ00121 PTZ00121
MAEBL; Provisional
 176-358 8.72e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 8.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   176 QRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIAD--------SKRAFELQKSA-----FSEEVNIKTAEAQLAYE 242
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeakkkaeeAKKADEAKKKAeeakkKADAAKKKAEEAKKAAE 1346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   243 LQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKI 322
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 13929186   323 GEAEAAVIEAMGKAE----AERMKLKAEAYQKYGDAAKMA 358
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEeakkADEAKKKAEEAKKAEEAKKKA 1466
PTZ00121 PTZ00121
MAEBL; Provisional
 185-356 1.00e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   185 EAERDAGIREAECKKEMLDVKFMADTK-IADSKRAFELQKSafsEEV----NIKTAEAQLAYELQGAREQQKIRQEEIEI 259
Cdd:PTZ00121 1150 DAKRVEIARKAEDARKAEEARKAEDAKkAEAARKAEEVRKA---EELrkaeDARKAEAARKAEEERKAEEARKAEDAKKA 1226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   260 EVVQRKKQIAVEAQEILRTDKELIATVRRPAEAE-----AHRIQQIAEGEKVKQVLLAQAE----AEKIRKiGEAEAAVI 330
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEArmahfARRQAAIKAEEARKADELKKAEekkkADEAKK-AEEKKKAD 1305

                         170       180       190
                  ....*....|....*....|....*....|
gi 13929186   331 EAMGKAE----AERMKLKAEAYQKYGDAAK 356
Cdd:PTZ00121 1306 EAKKKAEeakkADEAKKKAEEAKKKADAAK 1335
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 207-390 4.05e-06

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: 48.69  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   207 MADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATV 286
Cdd:TIGR02794  59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   287 RRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEA-AVIEAMGKAEAERMKLKAEAYQKYGDA---AKMALVLE 362
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAkAKAEAEAKAKAEEAKAKAEAAKAKAAAeaaAKAEAEAA 218

                         170       180
                  ....*....|....*....|....*...
gi 13929186   363 ALPQIAAKISAPLTKVDEIVVLSGDNSK 390
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLASGSNA 246
PTZ00121 PTZ00121
MAEBL; Provisional
 184-381 4.77e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   184 AEAERD-AGIREAECKKEMLDVKFMADTKIADSKRAFELQKSafsEEVNiKTAEAQLAYELQGAREQQKIRQEEIEIEVV 262
Cdd:PTZ00121 1245 AEEERNnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA---EEKK-KADEAKKAEEKKKADEAKKKAEEAKKADEA 1320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   263 QRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKqvllaqAEAEKIRKIGE---AEAAVIEAMGKAEAE 339
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK------AEAAEKKKEEAkkkADAAKKKAEEKKKAD 1394

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 13929186   340 RMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEI 381
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 208-356 2.03e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 46.34  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  208 ADTKIADSKRAFELQKSAfsEEVNIKTAEAQlayELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVR 287
Cdd:PRK09510  72 KSAKRAEEQRKKKEQQQA--EELQQKQAAEQ---ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK 146

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  288 RPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAE-RMKLKAEAYQKYGDAAK 356
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEaKKKAEAEAKKKAAAEAK 216
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 59-157 2.22e-05

Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, podocin, and other members of the stomatin-like protein family (SLPs or slipins). The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome. Bacterial and archaebacterial SLPs and many of the eukaryotic family members remain uncharacterized.


Pssm-ID: 259812 [Multi-domain]  Cd Length: 108  Bit Score: 43.33  E-value: 2.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  59 IETSEGVPLFVTGVAQVKImtEKELLAVAceqflgkNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVA 138
Cdd:cd13434  15 ILTKDNVTVSVDAVVYYRV--VDPLKAVL-------NVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQEIL 85

                        90
                ....*....|....*....
gi 13929186 139 APDVGRMGIEILSFTIKDV 157
Cdd:cd13434  86 DEATDPWGIKVERVEIKDI 104
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 38-190 4.42e-05

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: 43.48  E-value: 4.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  38 CISDTQRLSLEVMTILCRCENIETSEGVPLFVTGVAQVKIMTEkeLLAVAceqflgkNVQDIKNVVLQTLEGHLRSILGT 117
Cdd:cd08828  11 CTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSA--VKAVA-------NVNNVHIATFLLAQTTLRNVLGT 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13929186 118 LTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDA 190
Cdd:cd08828  82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 288-350 4.69e-05

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: 44.79  E-value: 4.69e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13929186 288 RPAEAEAHRiqqiAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQK 350
Cdd:cd03405 166 RERIAAEYR----AEGEEEAEKIRAEADRERTVILAEAYREAEEIRGEGDAEAARIYAEAYGK 224
PTZ00121 PTZ00121
MAEBL; Provisional
 171-380 5.19e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   171 QTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSA----FSEEVNIKTAEAQLAYELQGA 246
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAeeakKADEAKKKAEEAKKADEAKKK 1491

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   247 REQQKIRQEEIEIEVVQRKK-QIAVEAQEILRTDKELIATVRRPAEA-----------EAHRIQQIAEGEKVKQVLLAQA 314
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKaDEAKKAEEAKKADEAKKAEEAKKADEakkaeekkkadELKKAEELKKAEEKKKAEEAKK 1571

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13929186   315 EAEK----IRKIGE---AEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDE 380
Cdd:PTZ00121 1572 AEEDknmaLRKAEEakkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
PTZ00121 PTZ00121
MAEBL; Provisional
 176-356 1.08e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   176 QRDADIGVAEAERDAG-IREAECKKEMLDVKFMADTKIADS--------KRAFELQKSAfsEEVNIKTAEAQLAYELQGA 246
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADeAEAAEEKAEAAEKKKEEAKKKADAakkkaeekKKADEAKKKA--EEDKKKADELKKAAAAKKK 1419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   247 REQQKIRQEEI-EIEVVQRKKQIAVEAQEILRTDKEliatvRRPAEAEAHRIQQIAEGEKVKQvllaqaEAEKIRKIGEA 325
Cdd:PTZ00121 1420 ADEAKKKAEEKkKADEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKKKAEEAKKADEAKK------KAEEAKKADEA 1488

                         170       180       190
                  ....*....|....*....|....*....|.
gi 13929186   326 EAAVIEAmgKAEAERMKLKAEAYQKYGDAAK 356
Cdd:PTZ00121 1489 KKKAEEA--KKKADEAKKAAEAKKKADEAKK 1517
PTZ00121 PTZ00121
MAEBL; Provisional
 184-397 1.12e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   184 AEAERDAGIREAECKKEMLDVKFMADTKIADS---KRAFELQKSafSEEVNIKTAEaqlayeLQGAREQQKIRQEEIEIE 260
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekKKAEELKKA--EEENKIKAAE------EAKKAEEDKKKAEEAKKA 1683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   261 VVQRKKqiAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAER 340
Cdd:PTZ00121 1684 EEDEKK--AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 13929186   341 MKLKAEAYQKYGDAAKMALVLEALPQiaaKISAPLTKVDEIVVLSGDNSKVTSEVNR 397
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDE---EDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 95-157 3.59e-04

Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in all three kingdoms of life. The conserved domain common to these families has also been referred to as the Band 7 domain. Individual proteins of the SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This subgroup of the SLPs remains largely uncharacterized. It includes human SLP-2 which is upregulated and involved in the progression and development in several types of cancer, including esophageal squamous cell carcinoma, endometrial adenocarcinoma, breast cancer, and glioma.


Pssm-ID: 259811 [Multi-domain]  Cd Length: 111  Bit Score: 39.76  E-value: 3.59e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13929186  95 NVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDV 157
Cdd:cd08829  45 GVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAKLLEALDEATDPWGVKVTRVEIKDI 107
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 59-157 3.66e-04

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial SLPs remain uncharacterized.


Pssm-ID: 259816 [Multi-domain]  Cd Length: 215  Bit Score: 41.75  E-value: 3.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  59 IETSEGVPLFVTGVAQVKImtekellaVACEQFLgKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVA 138
Cdd:cd13438  52 ILTADKVALRVNLVATYRV--------VDPVKAV-ETVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAV 122

                        90
                ....*....|....*....
gi 13929186 139 APDVGRMGIEILSFTIKDV 157
Cdd:cd13438 123 KEAAAELGVEVLSVGVKDI 141
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 247-342 3.88e-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: 42.80  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   247 REQQKIRQEEIEIEVVQRKKqiaVEAQEILRTDKEliATVRRpaEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKigEAE 326
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRE---LERLQMERQQKN--ERVRQ--ELEAARKVKILEEERQRKIQQQKVEMEQIRA--EQE 430

                          90
                  ....*....|....*.
gi 13929186   327 AAVIEAMGKAEAERMK 342
Cdd:pfam17380 431 EARQREVRRLEEERAR 446
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 290-372 6.02e-04

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: 41.34  E-value: 6.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 290 AEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAA 369
Cdd:cd03404 182 ARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGDAARFLALLAEYRKAPEVTRERLYLETMEEVLS 261


                ...
gi 13929186 370 KIS 372
Cdd:cd03404 262 NAS 264
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 228-381 6.50e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 6.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 228 EEVNIKTAEAQLAyELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRpAEAEAHRIQQIAEGEKVK 307
Cdd:COG1196 251 LEAELEELEAELA-ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER-RRELEERLEELEEELAEL 328

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13929186 308 QVLLAQAEAEKIrkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEI 381
Cdd:COG1196 329 EEELEELEEELE----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 237-363 7.31e-04

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: 41.37  E-value: 7.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   237 AQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIAtVRRPAEAEAHRiQQIAEGEKVKQVLLAQAEA 316
Cdd:TIGR02794  53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAA-EKAAKQAEQAA-KQAEEKQKQAEEAKAKQAA 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 13929186   317 EKIRKiGEAEA---AVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEA 363
Cdd:TIGR02794 131 EAKAK-AEAEAerkAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA 179
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 245-363 1.95e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  245 GAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAE-----AHRIQQIAEGEKVKQVLLAQAEAEKI 319
Cdd:PRK09510  73 SAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEeaakqAALKQKQAEEAAAKAAAAAKAKAEAE 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 13929186  320 RKIGEAEAAVIEAMGKAEAE---RMKLKAEAYQKYGDAAKMALVLEA 363
Cdd:PRK09510 153 AKRAAAAAKKAAAEAKKKAEaeaAKKAAAEAKKKAEAEAAAKAAAEA 199
PRK11029 PRK11029
protease modulator HflC;
221-350 2.43e-03

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 39.72  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  221 LQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIE----------IEVVQ-RKKQIAVEAQ------EILRTDKELI 283
Cdd:PRK11029 155 LNSGSAGTEDEVATPAADDAIASAAERVEAETKGKVPVinpnsmaalgIEVVDvRIKQINLPTEvsdaiyNRMRAEREAV 234

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13929186  284 AtvRRpaeaeaHRIQQIAEGEKVKqvllAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQK 350
Cdd:PRK11029 235 A--RR------HRSQGQEEAEKLR----ATADYEVTRTLAEAERQGRIMRGEGDAEAAKLFADAFSQ 289
SPFH_like_u1 cd03408
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 67-157 2.88e-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: 259806  Cd Length: 217  Bit Score: 39.07  E-value: 2.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  67 LFVTGVA-QVKIMTEKELLavacEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEqiyqdrdqFAKLVREVAAPDVGRM 145
Cdd:cd03408 117 LFLTEVVgTQGTFTTDEIE----EQLRSEIVQALKDAIAELSISGLDLALEANLDE--------LSAALKEKLAPEFEKY 184

                        90
                ....*....|..
gi 13929186 146 GIEILSFTIKDV 157
Cdd:cd03408 185 GLELTSFGIESI 196
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 175-402 4.34e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 4.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 175 VQRDADIGVAEAERDAGIREAECKKEMLDVKFmadTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQ 254
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAEL---AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 255 EEIEIEVVQRKKQIAVEAQEI---LRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIE 331
Cdd:COG1196 308 EERRRELEERLEELEEELAELeeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13929186 332 AMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKISAPLTKVDEIVVLSGDNSKVTSEVNRLLAEL 402
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 95-190 4.85e-03

Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of the SPFH family (stomatin, prohibitin, flotillin, and HflK/C); This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized.


Pssm-ID: 259817 [Multi-domain]  Cd Length: 177  Bit Score: 37.99  E-value: 4.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  95 NVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAV 174
Cdd:cd13775  42 EVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAE 121

                        90
                ....*....|....*.
gi 13929186 175 VQRDADIGVAEAERDA 190
Cdd:cd13775 122 REKNARVILAEAEKEI 137
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 169-346 4.98e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.34  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   169 KTQTAVVQRDADIgVAEAERDAGIREAECKKemldvkfmadTKIADSKRAFELQKSafsEEVNIKTAEAQLAYELQGARE 248
Cdd:pfam17380 323 KARQAEMDRQAAI-YAEQERMAMERERELER----------IRQEERKRELERIRQ---EEIAMEISRMRELERLQMERQ 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   249 Q--QKIRQEeieIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKqvllaqaEAEKIRKIGEAE 326
Cdd:pfam17380 389 QknERVRQE---LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR-------EMERVRLEEQER 458

                         170       180
                  ....*....|....*....|
gi 13929186   327 AAVIEAMGKAEAERMKLKAE 346
Cdd:pfam17380 459 QQQVERLRQQEEERKRKKLE 478
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 271-378 6.41e-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: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 38.43  E-value: 6.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 271 EAQEILRTdKELIATVRRPA---EAEAHRIQQIAEGEKVKQV-------LLAQAEAEKIRKIGEAEAAVIEAMGKAEAER 340
Cdd:cd03406 169 EAMEAEKT-KLLIAEQHQKVvekEAETERKRAVIEAEKDAEVakiqmqqKIMEKEAEKKISEIEDEMHLAREKARADAEY 247

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 13929186 341 MKLKAEAyqkygDAAKMALVLEALPQIAAKISAPLTKV 378
Cdd:cd03406 248 YRALREA-----EANKLKLTPEYLELKKYQAIANNTKI 280
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 94-332 7.91e-03

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


Pssm-ID: 259803 [Multi-domain]  Cd Length: 249  Bit Score: 37.85  E-value: 7.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186  94 KNVQDIKNVVLQTLEGHLRSILGTLTVEQ-IYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKdvydKVDYLSSlgkTQT 172
Cdd:cd03405  84 GGEEGAESRLDDIVDSALRNEIGKRTLAEvVSGGRDELMEEILEQANEEAKEYGIEVVDVRIK----RIDLPEE---VSE 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 173 AVVQRdadigvAEAERDagireaeckkemldvkfmadtKIADSKRAfelqksafseevniktaeaqlayelQGAREQQKI 252
Cdd:cd03405 157 SVYER------MRAERE---------------------RIAAEYRA-------------------------EGEEEAEKI 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186 253 RqeeieievvqrkkqiaveaqeilrtdkeliatvrrpAEAEAHRIQQIAEgekvkqvllAQAEAEKIRKIGEAEAAVIEA 332
Cdd:cd03405 185 R------------------------------------AEADRERTVILAE---------AYREAEEIRGEGDAEAARIYA 219
growth_prot_Scy NF041483
polarized growth protein Scy;
229-358 9.93e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 38.27  E-value: 9.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929186   229 EVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIaveaqeilrtDKELiatVRRPAEAEAHRIQQIAEGEKvkq 308
Cdd:NF041483   93 ERELRDARAQTQRILQEHAEHQARLQAELHTEAVQRRQQL----------DQEL---AERRQTVESHVNENVAWAEQ--- 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 13929186   309 vLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMA 358
Cdd:NF041483  157 -LRARTESQARRLLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESA 205
 
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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