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Conserved domains on  [gi|94538362|ref|NP_004466|]
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flotillin-2 isoform 1 [Homo sapiens]

Protein Classification

flotillin family protein( domain architecture ID 11455184)

flotillin family protein may act as a scaffolding protein within caveolar membranes, functionally participating in the formation of caveolae or caveolae-like vesicles

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
5-417 1.55e-83

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


:

Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 262.89  E-value: 1.55e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   5 HTVGPNEALVVSGGccGSDYKQYVFGGwAWAWWCISDTQRISLEIMTLQ-PRCEDVETAEGVALTVTGVAQVKIMTEKEL 83
Cdd:COG2268  29 RKVPPNEALVITGR--GGGYKVVTGGG-AFVLPVLHRAERMSLSTMTIEvERTEGLITKDGIRVDVDAVFYVKVNSDPED 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  84 LAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDY 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 164 LSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADT-----KIADSKRAFELQKSAFSEEVNIKTAEAQ 238
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAE 265
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 239 LAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAegekvkqvllaqaeaek 318
Cdd:COG2268 266 AAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA----------------- 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 319 irkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSK--VTSEVN 396
Cdd:COG2268 326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVA 400
                       410       420
                ....*....|....*....|.
gi 94538362 397 RLLAELPASVHALTGVDLSKI 417
Cdd:COG2268 401 EALAPLLESLLEETGLDLPGL 421
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
5-417 1.55e-83

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 262.89  E-value: 1.55e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   5 HTVGPNEALVVSGGccGSDYKQYVFGGwAWAWWCISDTQRISLEIMTLQ-PRCEDVETAEGVALTVTGVAQVKIMTEKEL 83
Cdd:COG2268  29 RKVPPNEALVITGR--GGGYKVVTGGG-AFVLPVLHRAERMSLSTMTIEvERTEGLITKDGIRVDVDAVFYVKVNSDPED 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  84 LAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDY 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 164 LSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADT-----KIADSKRAFELQKSAFSEEVNIKTAEAQ 238
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAE 265
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 239 LAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAegekvkqvllaqaeaek 318
Cdd:COG2268 266 AAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA----------------- 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 319 irkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSK--VTSEVN 396
Cdd:COG2268 326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVA 400
                       410       420
                ....*....|....*....|.
gi 94538362 397 RLLAELPASVHALTGVDLSKI 417
Cdd:COG2268 401 EALAPLLESLLEETGLDLPGL 421
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
34-178 2.68e-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: 205.43  E-value: 2.68e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  34 WAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRS 113
Cdd:cd03399   1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRA 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94538362 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 2.80e-20

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 87.76  E-value: 2.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362     6 TVGPNEALVVSGGccgSDYKQYVFGGWAWAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLA 85
Cdd:pfam01145   2 IVPPGEVGVVTRF---GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362    86 VAceQFLGKNvqDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLS 165
Cdd:pfam01145  79 VQ--NVFGSD--DLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154
                         170       180
                  ....*....|....*....|...
gi 94538362   166 SLGKTQTAVVQRDADIGVAEAER 188
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
87-269 4.60e-13

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 66.53  E-value: 4.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362     87 ACEQFLGKNVQDIKNVVLQTLEghlRSILGTLTVEQIYQDRdqfaKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSS 166
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDV----KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362    167 LGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVkfmadtkiadskraFELQKSAFSEEVN--IKTAEAQLAYELQ 244
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDEL--------------LTDQREKISENIReeLNEAAEAWGIKVE 139
                          170       180
                   ....*....|....*....|....*
gi 94538362    245 GAReqqkIRQEEIEIEVVQRKKQIA 269
Cdd:smart00244 140 DVE----IKDIRLPEEIKEAMEAQQ 160
PTZ00121 PTZ00121
MAEBL; Provisional
185-401 2.04e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   185 EAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAfSEEVNIKTAEAQLAYELQGAR---------EQQKIRQE 255
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARieevmklyeEEKKMKAE 1610
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   256 EIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEaavieamgK 335
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK--------K 1682
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94538362   336 AEAERMKlKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSKVTSEVNRLLAE 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 6.20e-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: 47.92  E-value: 6.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   207 MADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATV 286
Cdd:TIGR02794  59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   287 RRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEA-AVIEAMGKAEAERMKLKAEAYQKYGDA---AKMALVLE 362
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAkAKAEAEAKAKAEEAKAKAEAAKAKAAAeaaAKAEAEAA 218
                         170       180
                  ....*....|....*....|....*...
gi 94538362   363 ALPQIAAKIAAPLTKVDEIVVLSGDNSK 390
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLASGSNA 246
 
Name Accession Description Interval E-value
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
5-417 1.55e-83

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 262.89  E-value: 1.55e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   5 HTVGPNEALVVSGGccGSDYKQYVFGGwAWAWWCISDTQRISLEIMTLQ-PRCEDVETAEGVALTVTGVAQVKIMTEKEL 83
Cdd:COG2268  29 RKVPPNEALVITGR--GGGYKVVTGGG-AFVLPVLHRAERMSLSTMTIEvERTEGLITKDGIRVDVDAVFYVKVNSDPED 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  84 LAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDY 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 164 LSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADT-----KIADSKRAFELQKSAFSEEVNIKTAEAQ 238
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAE 265
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 239 LAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAegekvkqvllaqaeaek 318
Cdd:COG2268 266 AAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA----------------- 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 319 irkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSK--VTSEVN 396
Cdd:COG2268 326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVA 400
                       410       420
                ....*....|....*....|.
gi 94538362 397 RLLAELPASVHALTGVDLSKI 417
Cdd:COG2268 401 EALAPLLESLLEETGLDLPGL 421
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
34-178 2.68e-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: 205.43  E-value: 2.68e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  34 WAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRS 113
Cdd:cd03399   1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRA 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94538362 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 2.28e-22

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: 91.27  E-value: 2.28e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  48 EIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVAceqfLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDR 127
Cdd:cd02106   1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFY----LVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGR 76
                        90       100       110
                ....*....|....*....|....*....|...
gi 94538362 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 2.80e-20

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


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 87.76  E-value: 2.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362     6 TVGPNEALVVSGGccgSDYKQYVFGGWAWAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLA 85
Cdd:pfam01145   2 IVPPGEVGVVTRF---GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362    86 VAceQFLGKNvqDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLS 165
Cdd:pfam01145  79 VQ--NVFGSD--DLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154
                         170       180
                  ....*....|....*....|...
gi 94538362   166 SLGKTQTAVVQRDADIGVAEAER 188
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
PHB smart00244
prohibitin homologues; prohibitin homologues
87-269 4.60e-13

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 66.53  E-value: 4.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362     87 ACEQFLGKNVQDIKNVVLQTLEghlRSILGTLTVEQIYQDRdqfaKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSS 166
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDV----KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362    167 LGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVkfmadtkiadskraFELQKSAFSEEVN--IKTAEAQLAYELQ 244
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDEL--------------LTDQREKISENIReeLNEAAEAWGIKVE 139
                          170       180
                   ....*....|....*....|....*
gi 94538362    245 GAReqqkIRQEEIEIEVVQRKKQIA 269
Cdd:smart00244 140 DVE----IKDIRLPEEIKEAMEAQQ 160
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
31-360 1.56e-11

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 64.48  E-value: 1.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  31 GWAWAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLavaceqflgKNVQDIKNVVLQTLEGH 110
Cdd:COG0330  45 GLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFL---------YNVENAEEALRQLAESA 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 111 LRSILGTLTVEQIY-QDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVydkvdYLSSlgKTQTAVVQRdadigvAEAERD 189
Cdd:COG0330 116 LREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDI-----DPPE--EVQDAMEDR------MKAERE 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 190 agireaeckkemldvkfmadtkiadsKRAFElqksafseevniktaeaqlaYELQGAREQQKIRqeeieievvqrkkqia 269
Cdd:COG0330 183 --------------------------REAAI--------------------LEAEGYREAAIIR---------------- 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 270 veaqeilrtdkeliatvrrpAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAeaavIEAMGKAEAERMklkAEAYQ 349
Cdd:COG0330 201 --------------------AEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEA----YSAAPFVLFYRS---LEALE 253
                       330
                ....*....|..
gi 94538362 350 K-YGDAAKMALV 360
Cdd:COG0330 254 EvLSPNSKVIVL 265
Flot pfam15975
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ...
313-387 1.81e-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: 52.32  E-value: 1.81e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94538362   313 QAEAEKIRKIGEAEAavIEAMGKAEAERMKLKAEAYQKYGD---AAKMAL-VLEALPQIAAKIAAPLTKVDEIVVLSGD 387
Cdd:pfam15975   1 EAEAEADAIKLRAEA--KRKKALAEAEGIRALNEAENALSDeqiALQVKLaLLEALPEIIAESVKPLEKIDGIKILQVD 77
PTZ00121 PTZ00121
MAEBL; Provisional
185-401 2.04e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   185 EAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAfSEEVNIKTAEAQLAYELQGAR---------EQQKIRQE 255
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARieevmklyeEEKKMKAE 1610
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   256 EIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEaavieamgK 335
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK--------K 1682
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94538362   336 AEAERMKlKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSKVTSEVNRLLAE 401
Cdd:PTZ00121 1683 AEEDEKK-AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
PTZ00121 PTZ00121
MAEBL; Provisional
184-397 5.24e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 5.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   184 AEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEE------- 256
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkkaee 1651
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   257 ---IEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAE----AEKIRKIGEAEAAV 329
Cdd:PTZ00121 1652 lkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEekkkAEELKKAEEENKIK 1731
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 94538362   330 IEAMGKAEAERMKLKAEAYQKYGDAAKMAlvleALPQIAAKIAAPLTKVDEIVVLSG---DNSKVTSEVNR 397
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIA----HLKKEEEKKAEEIRKEKEAVIEEEldeEDEKRRMEVDK 1798
PTZ00121 PTZ00121
MAEBL; Provisional
186-358 6.50e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 6.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   186 AERDAGIReAECKKEMLDVKFMADTKIADSKRAFELQKSAfsEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRK 265
Cdd:PTZ00121 1266 ARRQAAIK-AEEARKADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   266 KQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAER----- 340
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKkkade 1422
                         170
                  ....*....|....*...
gi 94538362   341 MKLKAEAYQKYGDAAKMA 358
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKA 1440
PTZ00121 PTZ00121
MAEBL; Provisional
176-358 1.26e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   176 QRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIAD--------SKRAFELQKSA-----FSEEVNIKTAEAQLAYE 242
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeakkkaeeAKKADEAKKKAeeakkKADAAKKKAEEAKKAAE 1346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   243 LQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKI 322
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 94538362   323 GEAEAAVIEAMGKAE----AERMKLKAEAYQKYGDAAKMA 358
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEeakkADEAKKKAEEAKKAEEAKKKA 1466
PTZ00121 PTZ00121
MAEBL; Provisional
185-356 1.50e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   185 EAERDAGIREAECKKEMLDVKFMADTK-IADSKRAFELQKSafsEEV----NIKTAEAQLAYELQGAREQQKIRQEEIEI 259
Cdd:PTZ00121 1150 DAKRVEIARKAEDARKAEEARKAEDAKkAEAARKAEEVRKA---EELrkaeDARKAEAARKAEEERKAEEARKAEDAKKA 1226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   260 EVVQRKKQIAVEAQEILRTDKELIATVRRPAEAE-----AHRIQQIAEGEKVKQVLLAQAE----AEKIRKiGEAEAAVI 330
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEArmahfARRQAAIKAEEARKADELKKAEekkkADEAKK-AEEKKKAD 1305
                         170       180       190
                  ....*....|....*....|....*....|
gi 94538362   331 EAMGKAE----AERMKLKAEAYQKYGDAAK 356
Cdd:PTZ00121 1306 EAKKKAEeakkADEAKKKAEEAKKKADAAK 1335
PTZ00121 PTZ00121
MAEBL; Provisional
184-381 2.33e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   184 AEAERD-AGIREAECKKEMLDVKFMADTKIADSKRAFELQKSafsEEVNiKTAEAQLAYELQGAREQQKIRQEEIEIEVV 262
Cdd:PTZ00121 1245 AEEERNnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA---EEKK-KADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   263 QRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKqvllaqAEAEKIRKIGE---AEAAVIEAMGKAEAE 339
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK------AEAAEKKKEEAkkkADAAKKKAEEKKKAD 1394
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 94538362   340 RMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEI 381
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
PTZ00121 PTZ00121
MAEBL; Provisional
185-381 2.41e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   185 EAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAfsEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQR 264
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA--DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   265 KKqiaveAQEILRTDKEliatVRRPAEAEAhriqqiaEGEKVKQVLLAQAEAEKIRKigeAEAAVIEAMGKAEAERMKLK 344
Cdd:PTZ00121 1418 KK-----ADEAKKKAEE----KKKADEAKK-------KAEEAKKADEAKKKAEEAKK---AEEAKKKAEEAKKADEAKKK 1478
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 94538362   345 AEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEI 381
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
207-390 6.20e-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: 47.92  E-value: 6.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   207 MADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATV 286
Cdd:TIGR02794  59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   287 RRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEA-AVIEAMGKAEAERMKLKAEAYQKYGDA---AKMALVLE 362
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAkAKAEAEAKAKAEEAKAKAEAAKAKAAAeaaAKAEAEAA 218
                         170       180
                  ....*....|....*....|....*...
gi 94538362   363 ALPQIAAKIAAPLTKVDEIVVLSGDNSK 390
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLASGSNA 246
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
38-190 7.80e-06

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: 45.79  E-value: 7.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  38 CISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEkeLLAVAceqflgkNVQDIKNVVLQTLEGHLRSILGT 117
Cdd:cd08828  11 CTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSA--VKAVA-------NVNNVHIATFLLAQTTLRNVLGT 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94538362 118 LTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDA 190
Cdd:cd08828  82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
41-157 1.23e-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: 44.11  E-value: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  41 DTQRISLEImtlqPRCEdVETAEGVALTVTGVAQVKImtEKELLAVAceqflgkNVQDIKNVVLQTLEGHLRSILGTLTV 120
Cdd:cd13434   2 DLRTQSVDV----PPQE-ILTKDNVTVSVDAVVYYRV--VDPLKAVL-------NVEDYKKATELLAQTTLRNVLGTRTL 67
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 94538362 121 EQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDV 157
Cdd:cd13434  68 DELLSEREEISQQLQEILDEATDPWGIKVERVEIKDI 104
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
61-157 2.39e-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. 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: 45.22  E-value: 2.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  61 TAEGVALTVTGVAQVKImtekellaVACEQFLgKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAP 140
Cdd:cd13438  54 TADKVALRVNLVATYRV--------VDPVKAV-ETVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKE 124
                        90
                ....*....|....*..
gi 94538362 141 DVGRMGIEILSFTIKDV 157
Cdd:cd13438 125 AAAELGVEVLSVGVKDI 141
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
208-373 4.49e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.57  E-value: 4.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  208 ADTKIADSKRAFELQKSAfsEEVNIKTAEAQlayELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVR 287
Cdd:PRK09510  72 KSAKRAEEQRKKKEQQQA--EELQQKQAAEQ---ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  288 RPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAE-RMKLKAEAYQKYGDAAKMALVLEAlPQ 366
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEaKKKAEAEAKKKAAAEAKKKAAAEA-KA 225

                 ....*..
gi 94538362  367 IAAKIAA 373
Cdd:PRK09510 226 AAAKAAA 232
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
288-350 5.84e-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: 44.40  E-value: 5.84e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94538362 288 RPAEAEAHRiqqiAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQK 350
Cdd:cd03405 166 RERIAAEYR----AEGEEEAEKIRAEADRERTVILAEAYREAEEIRGEGDAEAARIYAEAYGK 224
PTZ00121 PTZ00121
MAEBL; Provisional
171-401 6.38e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   171 QTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSA----FSEEVNIKTAEAQLAYELQGA 246
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAeeakKADEAKKKAEEAKKADEAKKK 1491
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   247 REQQKIRQEEIEIEVVQRKK-QIAVEAQEILRTDKELIATVRRPAEA-----------EAHRIQQIAEGEKVKQVLLAQA 314
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKaDEAKKAEEAKKADEAKKAEEAKKADEakkaeekkkadELKKAEELKKAEEKKKAEEAKK 1571
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   315 E----------AEKIRKIGEAEAAVI------EAMGKAE----AERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAP 374
Cdd:PTZ00121 1572 AeedknmalrkAEEAKKAEEARIEEVmklyeeEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
                         250       260
                  ....*....|....*....|....*..
gi 94538362   375 LTKVDEIVVLSGDNSKVTSEVNRLLAE 401
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAE 1678
PTZ00121 PTZ00121
MAEBL; Provisional
184-397 1.67e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   184 AEAERDAGIREAECKKEMLDVKFMADTKIADS---KRAFELQKSafSEEVNIKTAEaqlayeLQGAREQQKIRQEEIEIE 260
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekKKAEELKKA--EEENKIKAAE------EAKKAEEDKKKAEEAKKA 1683
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   261 VVQRKKqiAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAER 340
Cdd:PTZ00121 1684 EEDEKK--AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 94538362   341 MKLKAEAYQKYGDAAKMALVLEALPQiaaKIAAPLTKVDEIVVLSGDNSKVTSEVNR 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 3.99e-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: 3.99e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94538362  95 NVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDV 157
Cdd:cd08829  45 GVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAKLLEALDEATDPWGVKVTRVEIKDI 107
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
247-342 5.30e-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: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   247 REQQKIRQEEIEIEVVQRKKqiaVEAQEILRTDKEliATVRRpaEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKigEAE 326
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRE---LERLQMERQQKN--ERVRQ--ELEAARKVKILEEERQRKIQQQKVEMEQIRA--EQE 430
                          90
                  ....*....|....*.
gi 94538362   327 AAVIEAMGKAEAERMK 342
Cdd:pfam17380 431 EARQREVRRLEEERAR 446
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
290-367 7.60e-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: 40.96  E-value: 7.60e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 94538362 290 AEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQI 367
Cdd:cd03404 182 ARQDKERLINEAQAYANEVIPRARGEAARIIQEAEAYKAEVVARAEGDAARFLALLAEYRKAPEVTRERLYLETMEEV 259
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
34-231 1.42e-03

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


Pssm-ID: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 40.26  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  34 WAWWCI-SDTQRISLEIMTLQPRCEdVETAEGVALTVTGVAQVKIMTEKELLAvaceqF--LGKNVQDIKNVVLQTLegh 110
Cdd:cd03407  26 FIIPPIeSVAGRVSLRVQQLDVRVE-TKTKDNVFVTLVVSVQYRVVPEKVYDA-----FykLTNPEQQIQSYVFDVV--- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 111 lRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDA 190
Cdd:cd03407  97 -RASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRLREAAEEKAEAEKIL 175
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 94538362 191 GIREAECKKEmldVKFMADTKIADSKRAF--ELQKS--AFSEEVN 231
Cdd:cd03407 176 QVKAAEAEAE---AKRLQGVGIAEQRKAIvdGLRESieDFQEAVP 217
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
237-363 2.30e-03

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.83  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   237 AQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIAtVRRPAEAEAHRiQQIAEGEKVKQVLLAQAEA 316
Cdd:TIGR02794  53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAA-EKAAKQAEQAA-KQAEEKQKQAEEAKAKQAA 130
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 94538362   317 EKIRKiGEAEA---AVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEA 363
Cdd:TIGR02794 131 EAKAK-AEAEAerkAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA 179
PRK11029 PRK11029
protease modulator HflC;
221-350 3.12e-03

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 39.34  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  221 LQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIE----------IEVVQ-RKKQIAVEAQ------EILRTDKELI 283
Cdd:PRK11029 155 LNSGSAGTEDEVATPAADDAIASAAERVEAETKGKVPVinpnsmaalgIEVVDvRIKQINLPTEvsdaiyNRMRAEREAV 234
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94538362  284 AtvRRpaeaeaHRIQQIAEGEKVKqvllAQAEAEKIRKIGEAEAAVIEAMGKAEAERMKLKAEAYQK 350
Cdd:PRK11029 235 A--RR------HRSQGQEEAEKLR----ATADYEVTRTLAEAERQGRIMRGEGDAEAAKLFADAFSQ 289
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
175-380 3.56e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 175 VQRDADIGVAEAERDAGIREAECKKEMLDVKFmadTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQ 254
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAEL---AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 255 EEIEIEVVQRKKQIAVEAQEILRTDKELIATVRR------PAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAA 328
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEEleeeleEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 94538362 329 VIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDE 380
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
271-378 6.19e-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: 6.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 271 EAQEILRTdKELIATVRRPA---EAEAHRIQQIAEGEKVKQV-------LLAQAEAEKIRKIGEAEAAVIEAMGKAEAER 340
Cdd:cd03406 169 EAMEAEKT-KLLIAEQHQKVvekEAETERKRAVIEAEKDAEVakiqmqqKIMEKEAEKKISEIEDEMHLAREKARADAEY 247
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 94538362 341 MKLKAEAyqkygDAAKMALVLEALPQIAAKIAAPLTKV 378
Cdd:cd03406 248 YRALREA-----EANKLKLTPEYLELKKYQAIANNTKI 280
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
95-190 6.41e-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: 37.61  E-value: 6.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  95 NVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAV 174
Cdd:cd13775  42 EVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAE 121
                        90
                ....*....|....*.
gi 94538362 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 7.29e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 38.57  E-value: 7.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   169 KTQTAVVQRDADIgVAEAERDAGIREAECKKemldvkfmadTKIADSKRAFELQKSafsEEVNIKTAEAQLAYELQGARE 248
Cdd:pfam17380 323 KARQAEMDRQAAI-YAEQERMAMERERELER----------IRQEERKRELERIRQ---EEIAMEISRMRELERLQMERQ 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362   249 Q--QKIRQEeieIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKqvllaqaEAEKIRKIGEAE 326
Cdd:pfam17380 389 QknERVRQE---LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR-------EMERVRLEEQER 458
                         170       180
                  ....*....|....*....|
gi 94538362   327 AAVIEAMGKAEAERMKLKAE 346
Cdd:pfam17380 459 QQQVERLRQQEEERKRKKLE 478
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
39-332 8.73e-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: 8.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362  39 ISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIM-TEKELLAVaceqflgKNVQDIKNVVLQTLEGHLRSILGT 117
Cdd:cd03405  35 IQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITdPLRFYQSV-------GGEEGAESRLDDIVDSALRNEIGK 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 118 LTVEQ-IYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKdvydKVDYLSSlgkTQTAVVQRdadigvAEAERDagireae 196
Cdd:cd03405 108 RTLAEvVSGGRDELMEEILEQANEEAKEYGIEVVDVRIK----RIDLPEE---VSESVYER------MRAERE------- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538362 197 ckkemldvkfmadtKIADSKRAfelqksafseevniktaeaqlayelQGAREQQKIRqeeieievvqrkkqiaveaqeil 276
Cdd:cd03405 168 --------------RIAAEYRA-------------------------EGEEEAEKIR----------------------- 185
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 94538362 277 rtdkeliatvrrpAEAEAHRIQQIAEgekvkqvllAQAEAEKIRKIGEAEAAVIEA 332
Cdd:cd03405 186 -------------AEADRERTVILAE---------AYREAEEIRGEGDAEAARIYA 219
SPFH_like_u1 cd03408
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
89-157 9.77e-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: 37.15  E-value: 9.77e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 94538362  89 EQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEqiyqdrdqFAKLVREVAAPDVGRMGIEILSFTIKDV 157
Cdd:cd03408 136 EQLRSEIVQALKDAIAELSISGLDLALEANLDE--------LSAALKEKLAPEFEKYGLELTSFGIESI 196
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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