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Conserved domains on  [gi|544497955|ref|XP_005583328|]
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flotillin-2 isoform X1 [Macaca fascicularis]

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 544497955   5 HTVGPNEALVVSGGccGSDYKQYVFGGwAWAWWCISDTQRISLEIMTLQ-PRCEDVETAEGVALTVTGVAQVKIMTEKEL 83
Cdd:COG2268   29 RKVPPNEALVITGR--GGGYKVVTGGG-AFVLPVLHRAERMSLSTMTIEvERTEGLITKDGIRVDVDAVFYVKVNSDPED 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  84 LAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDY 163
Cdd:COG2268  106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 164 LSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADT-----KIADSKRAFELQKSAFSEEVNIKTAEAQ 238
Cdd:COG2268  186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 239 LAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAegekvkqvllaqaeaek 318
Cdd:COG2268  266 AAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA----------------- 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 319 irkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSK--VTSEVN 396
Cdd:COG2268  326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVA 400

                        410       420
                 ....*....|....*....|.
gi 544497955 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 544497955   5 HTVGPNEALVVSGGccGSDYKQYVFGGwAWAWWCISDTQRISLEIMTLQ-PRCEDVETAEGVALTVTGVAQVKIMTEKEL 83
Cdd:COG2268   29 RKVPPNEALVITGR--GGGYKVVTGGG-AFVLPVLHRAERMSLSTMTIEvERTEGLITKDGIRVDVDAVFYVKVNSDPED 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  84 LAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDY 163
Cdd:COG2268  106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 164 LSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADT-----KIADSKRAFELQKSAFSEEVNIKTAEAQ 238
Cdd:COG2268  186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 239 LAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAegekvkqvllaqaeaek 318
Cdd:COG2268  266 AAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA----------------- 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 319 irkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSK--VTSEVN 396
Cdd:COG2268  326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVA 400

                        410       420
                 ....*....|....*....|.
gi 544497955 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 544497955  34 WAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRS 113
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544497955 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 544497955    6 TVGPNEALVVSGGccgSDYKQYVFGGWAWAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLA 85
Cdd:pfam01145   2 IVPPGEVGVVTRF---GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955   86 VAceQFLGKNvqDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLS 165
Cdd:pfam01145  79 VQ--NVFGSD--DLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154

                         170       180
                  ....*....|....*....|...
gi 544497955  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 544497955    87 ACEQFLGKNVQDIKNVVLQTLEghlRSILGTLTVEQIYQDRdqfaKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSS 166
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDV----KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955   167 LGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVkfmadtkiadskraFELQKSAFSEEVN--IKTAEAQLAYELQ 244
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDEL--------------LTDQREKISENIReeLNEAAEAWGIKVE 139

                          170       180
                   ....*....|....*....|....*
gi 544497955   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 544497955  185 EAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAfSEEVNIKTAEAQLAYELQGAR---------EQQKIRQE 255
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARieevmklyeEEKKMKAE 1610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  256 EIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEaavieamgK 335
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK--------K 1682

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544497955  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 544497955  207 MADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATV 286
Cdd:TIGR02794  59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  287 RRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEA-AVIEAMGKAEAERMKLKAEAYQKYGDA---AKMALVLE 362
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAkAKAEAEAKAKAEEAKAKAEAAKAKAAAeaaAKAEAEAA 218

                         170       180
                  ....*....|....*....|....*...
gi 544497955  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 544497955   5 HTVGPNEALVVSGGccGSDYKQYVFGGwAWAWWCISDTQRISLEIMTLQ-PRCEDVETAEGVALTVTGVAQVKIMTEKEL 83
Cdd:COG2268   29 RKVPPNEALVITGR--GGGYKVVTGGG-AFVLPVLHRAERMSLSTMTIEvERTEGLITKDGIRVDVDAVFYVKVNSDPED 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  84 LAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDY 163
Cdd:COG2268  106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 164 LSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADT-----KIADSKRAFELQKSAFSEEVNIKTAEAQ 238
Cdd:COG2268  186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 239 LAYELQGAREQQKIRQeeiEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAegekvkqvllaqaeaek 318
Cdd:COG2268  266 AAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA----------------- 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 319 irkigEAEAAVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLTKVDEIVVLSGDNSK--VTSEVN 396
Cdd:COG2268  326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVA 400

                        410       420
                 ....*....|....*....|.
gi 544497955 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 544497955  34 WAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRS 113
Cdd:cd03399    1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544497955 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 544497955  48 EIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVAceqfLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDR 127
Cdd:cd02106    1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFY----LVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGR 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 544497955 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 544497955    6 TVGPNEALVVSGGccgSDYKQYVFGGWAWAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLA 85
Cdd:pfam01145   2 IVPPGEVGVVTRF---GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955   86 VAceQFLGKNvqDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLS 165
Cdd:pfam01145  79 VQ--NVFGSD--DLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154

                         170       180
                  ....*....|....*....|...
gi 544497955  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 544497955    87 ACEQFLGKNVQDIKNVVLQTLEghlRSILGTLTVEQIYQDRdqfaKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSS 166
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDV----KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955   167 LGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVkfmadtkiadskraFELQKSAFSEEVN--IKTAEAQLAYELQ 244
Cdd:smart00244  74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDEL--------------LTDQREKISENIReeLNEAAEAWGIKVE 139

                          170       180
                   ....*....|....*....|....*
gi 544497955   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 544497955  31 GWAWAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLavaceqflgKNVQDIKNVVLQTLEGH 110
Cdd:COG0330   45 GLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFL---------YNVENAEEALRQLAESA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 111 LRSILGTLTVEQIY-QDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVydkvdYLSSlgKTQTAVVQRdadigvAEAERD 189
Cdd:COG0330  116 LREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDI-----DPPE--EVQDAMEDR------MKAERE 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 190 agireaeckkemldvkfmadtkiadsKRAFElqksafseevniktaeaqlaYELQGAREQQKIRqeeieievvqrkkqia 269
Cdd:COG0330  183 --------------------------REAAI--------------------LEAEGYREAAIIR---------------- 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 270 veaqeilrtdkeliatvrrpAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAeaavIEAMGKAEAERMklkAEAYQ 349
Cdd:COG0330  201 --------------------AEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEA----YSAAPFVLFYRS---LEALE 253

                        330
                 ....*....|..
gi 544497955 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 544497955  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 544497955  185 EAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAfSEEVNIKTAEAQLAYELQGAR---------EQQKIRQE 255
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARieevmklyeEEKKMKAE 1610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  256 EIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEaavieamgK 335
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK--------K 1682

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544497955  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 544497955  184 AEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEE------- 256
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkkaee 1651

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  257 ---IEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAE----AEKIRKIGEAEAAV 329
Cdd:PTZ00121 1652 lkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEekkkAEELKKAEEENKIK 1731

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544497955  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 544497955  186 AERDAGIReAECKKEMLDVKFMADTKIADSKRAFELQKSAfsEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRK 265
Cdd:PTZ00121 1266 ARRQAAIK-AEEARKADELKKAEEKKKADEAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  266 KQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAER----- 340
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKkkade 1422

                         170
                  ....*....|....*...
gi 544497955  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 544497955  176 QRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIAD--------SKRAFELQKSA-----FSEEVNIKTAEAQLAYE 242
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeakkkaeeAKKADEAKKKAeeakkKADAAKKKAEEAKKAAE 1346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  243 LQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKI 322
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 544497955  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 544497955  185 EAERDAGIREAECKKEMLDVKFMADTK-IADSKRAFELQKSafsEEV----NIKTAEAQLAYELQGAREQQKIRQEEIEI 259
Cdd:PTZ00121 1150 DAKRVEIARKAEDARKAEEARKAEDAKkAEAARKAEEVRKA---EELrkaeDARKAEAARKAEEERKAEEARKAEDAKKA 1226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  260 EVVQRKKQIAVEAQEILRTDKELIATVRRPAEAE-----AHRIQQIAEGEKVKQVLLAQAE----AEKIRKiGEAEAAVI 330
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEArmahfARRQAAIKAEEARKADELKKAEekkkADEAKK-AEEKKKAD 1305

                         170       180       190
                  ....*....|....*....|....*....|
gi 544497955  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 544497955  184 AEAERD-AGIREAECKKEMLDVKFMADTKIADSKRAFELQKSafsEEVNiKTAEAQLAYELQGAREQQKIRQEEIEIEVV 262
Cdd:PTZ00121 1245 AEEERNnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA---EEKK-KADEAKKAEEKKKADEAKKKAEEAKKADEA 1320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  263 QRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKqvllaqAEAEKIRKIGE---AEAAVIEAMGKAEAE 339
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK------AEAAEKKKEEAkkkADAAKKKAEEKKKAD 1394

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 544497955  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 544497955  185 EAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAfsEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQR 264
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA--DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  265 KKqiaveAQEILRTDKEliatVRRPAEAEAhriqqiaEGEKVKQVLLAQAEAEKIRKigeAEAAVIEAMGKAEAERMKLK 344
Cdd:PTZ00121 1418 KK-----ADEAKKKAEE----KKKADEAKK-------KAEEAKKADEAKKKAEEAKK---AEEAKKKAEEAKKADEAKKK 1478

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 544497955  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 544497955  207 MADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATV 286
Cdd:TIGR02794  59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  287 RRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEA-AVIEAMGKAEAERMKLKAEAYQKYGDA---AKMALVLE 362
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAkAKAEAEAKAKAEEAKAKAEAAKAKAAAeaaAKAEAEAA 218

                         170       180
                  ....*....|....*....|....*...
gi 544497955  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 544497955  38 CISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEkeLLAVAceqflgkNVQDIKNVVLQTLEGHLRSILGT 117
Cdd:cd08828   11 CTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSA--VKAVA-------NVNNVHIATFLLAQTTLRNVLGT 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544497955 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 544497955  41 DTQRISLEImtlqPRCEdVETAEGVALTVTGVAQVKImtEKELLAVAceqflgkNVQDIKNVVLQTLEGHLRSILGTLTV 120
Cdd:cd13434    2 DLRTQSVDV----PPQE-ILTKDNVTVSVDAVVYYRV--VDPLKAVL-------NVEDYKKATELLAQTTLRNVLGTRTL 67

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 544497955 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 544497955  61 TAEGVALTVTGVAQVKImtekellaVACEQFLgKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAP 140
Cdd:cd13438   54 TADKVALRVNLVATYRV--------VDPVKAV-ETVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKE 124

                         90
                 ....*....|....*..
gi 544497955 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 544497955 208 ADTKIADSKRAFELQKSAfsEEVNIKTAEAQlayELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVR 287
Cdd:PRK09510  72 KSAKRAEEQRKKKEQQQA--EELQQKQAAEQ---ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 288 RPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAE-RMKLKAEAYQKYGDAAKMALVLEAlPQ 366
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEaKKKAEAEAKKKAAAEAKKKAAAEA-KA 225


                 ....*..
gi 544497955 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 544497955 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 544497955  171 QTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSA----FSEEVNIKTAEAQLAYELQGA 246
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAeeakKADEAKKKAEEAKKADEAKKK 1491

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  247 REQQKIRQEEIEIEVVQRKK-QIAVEAQEILRTDKELIATVRRPAEA-----------EAHRIQQIAEGEKVKQVLLAQA 314
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKaDEAKKAEEAKKADEAKKAEEAKKADEakkaeekkkadELKKAEELKKAEEKKKAEEAKK 1571

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  315 E----------AEKIRKIGEAEAAVI------EAMGKAE----AERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAP 374
Cdd:PTZ00121 1572 AeedknmalrkAEEAKKAEEARIEEVmklyeeEKKMKAEeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651

                         250       260
                  ....*....|....*....|....*..
gi 544497955  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 544497955  184 AEAERDAGIREAECKKEMLDVKFMADTKIADS---KRAFELQKSafSEEVNIKTAEaqlayeLQGAREQQKIRQEEIEIE 260
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekKKAEELKKA--EEENKIKAAE------EAKKAEEDKKKAEEAKKA 1683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  261 VVQRKKqiAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAAVIEAMGKAEAER 340
Cdd:PTZ00121 1684 EEDEKK--AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 544497955  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 544497955  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 544497955  247 REQQKIRQEEIEIEVVQRKKqiaVEAQEILRTDKEliATVRRpaEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKigEAE 326
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRE---LERLQMERQQKN--ERVRQ--ELEAARKVKILEEERQRKIQQQKVEMEQIRA--EQE 430

                          90
                  ....*....|....*.
gi 544497955  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 544497955 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 544497955  34 WAWWCI-SDTQRISLEIMTLQPRCEdVETAEGVALTVTGVAQVKIMTEKELLAvaceqF--LGKNVQDIKNVVLQTLegh 110
Cdd:cd03407   26 FIIPPIeSVAGRVSLRVQQLDVRVE-TKTKDNVFVTLVVSVQYRVVPEKVYDA-----FykLTNPEQQIQSYVFDVV--- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 111 lRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDA 190
Cdd:cd03407   97 -RASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQRLREAAEEKAEAEKIL 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 544497955 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 544497955  237 AQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIAtVRRPAEAEAHRiQQIAEGEKVKQVLLAQAEA 316
Cdd:TIGR02794  53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAA-EKAAKQAEQAA-KQAEEKQKQAEEAKAKQAA 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 544497955  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 544497955 221 LQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIE----------IEVVQ-RKKQIAVEAQ------EILRTDKELI 283
Cdd:PRK11029 155 LNSGSAGTEDEVATPAADDAIASAAERVEAETKGKVPVinpnsmaalgIEVVDvRIKQINLPTEvsdaiyNRMRAEREAV 234

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544497955 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 544497955 175 VQRDADIGVAEAERDAGIREAECKKEMLDVKFmadTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQ 254
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAEL---AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 255 EEIEIEVVQRKKQIAVEAQEILRTDKELIATVRR------PAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEAA 328
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELEEleeeleEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 544497955 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 544497955 271 EAQEILRTdKELIATVRRPA---EAEAHRIQQIAEGEKVKQV-------LLAQAEAEKIRKIGEAEAAVIEAMGKAEAER 340
Cdd:cd03406  169 EAMEAEKT-KLLIAEQHQKVvekEAETERKRAVIEAEKDAEVakiqmqqKIMEKEAEKKISEIEDEMHLAREKARADAEY 247

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 544497955 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 544497955  95 NVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAV 174
Cdd:cd13775   42 EVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAE 121

                         90
                 ....*....|....*.
gi 544497955 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 544497955  169 KTQTAVVQRDADIgVAEAERDAGIREAECKKemldvkfmadTKIADSKRAFELQKSafsEEVNIKTAEAQLAYELQGARE 248
Cdd:pfam17380 323 KARQAEMDRQAAI-YAEQERMAMERERELER----------IRQEERKRELERIRQ---EEIAMEISRMRELERLQMERQ 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955  249 Q--QKIRQEeieIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKqvllaqaEAEKIRKIGEAE 326
Cdd:pfam17380 389 QknERVRQE---LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR-------EMERVRLEEQER 458

                         170       180
                  ....*....|....*....|
gi 544497955  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 544497955  39 ISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIM-TEKELLAVaceqflgKNVQDIKNVVLQTLEGHLRSILGT 117
Cdd:cd03405   35 IQNVRKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITdPLRFYQSV-------GGEEGAESRLDDIVDSALRNEIGK 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 118 LTVEQ-IYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKdvydKVDYLSSlgkTQTAVVQRdadigvAEAERDagireae 196
Cdd:cd03405  108 RTLAEvVSGGRDELMEEILEQANEEAKEYGIEVVDVRIK----RIDLPEE---VSESVYER------MRAERE------- 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544497955 197 ckkemldvkfmadtKIADSKRAfelqksafseevniktaeaqlayelQGAREQQKIRqeeieievvqrkkqiaveaqeil 276
Cdd:cd03405  168 --------------RIAAEYRA-------------------------EGEEEAEKIR----------------------- 185

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544497955 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 544497955  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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