|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
5-435 |
1.98e-84 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 265.20 E-value: 1.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 5 HTTGPNEALIVSGGccgSTKKRTIVGGWAWAWWLVTDVQRLSLNVMTLN-PMCENVETSQGVPLTVTGVAQCKIMKMmnv 83
Cdd:COG2268 29 RKVPPNEALVITGR---GGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEvERTEGLITKDGIRVDVDAVFYVKVNSD--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 84 yyfhhqaDELLGTASEQFLGKSVKEIKQTILQTLEGHLRAILGTLTVEEVYKDRDQFAALVREVAAPDVGRMGIEILSFT 163
Cdd:COG2268 103 -------PEDIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 164 IKDVYDDVQYLASLGKAQTAVVKRDADAGVAEANRDAGIREAECEKSAMDVKYSTDTKIEDNT-----RMYKLQKANFDQ 238
Cdd:COG2268 176 ITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARiaeaeAELAKKKAEERR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 239 EINTAKAESQLAYELQAAKIRQRIrneEIQIEVVERRKQIEIESQEVQRKDRELTGTVKLPAEAEAFRlqtlaqakqcqt 318
Cdd:COG2268 256 EAETARAEAEAAYEIAEANAEREV---QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA------------ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 319 iegARAEAErirkigsAEAHAIELVGKAEAERMRMKAHVYKQYGDAAIMNIVLESLPKIAAEVAAPLAKTDEIVLI---G 395
Cdd:COG2268 321 ---AEAEAE-------AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIdggN 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 442616358 396 GNDNITNDVTRLVAQLPPSINALTGVDLSKVLSKIPGAKA 435
Cdd:COG2268 391 GGNGAGSAVAEALAPLLESLLEETGLDLPGLLKGLTGAGA 430
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
34-188 |
1.26e-62 |
|
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: 198.88 E-value: 1.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 34 WAWWLVTDVQRLSLNVMTLNPMCENVETSQGVPLTVTGVAQCKIMKmmnvyyfhhqADELLGTASEQFLGKSVKEIKQTI 113
Cdd:cd03399 1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGS----------DPEEIAAAAERFLGKSTEEIRELV 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442616358 114 LQTLEGHLRAILGTLTVEEVYKDRDQFAALVREVAAPDVGRMGIEILSFTIKDVYDDVQYLASLGKAQTAVVKRD 188
Cdd:cd03399 71 KETLEGHLRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
6-196 |
1.46e-17 |
|
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: 80.06 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 6 TTGPNEALIVSGGccgSTKKRTIVGGWAWAWWLVTDVQRLSLNVMTLNPMCENVETSQGVPLTVTGVAQCKIMKmmnvyy 85
Cdd:pfam01145 2 IVPPGEVGVVTRF---GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 86 fhHQADELLGTASEQflgksvKEIKQTILQTLEGHLRAILGTLTVEEVYKDRDQFAALVREVAAPDVGRMGIEILSFTIK 165
Cdd:pfam01145 73 --DDPPKLVQNVFGS------DDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQIT 144
|
170 180 190
....*....|....*....|....*....|.
gi 442616358 166 DVYDDVQYLASLGKAQTAVVKRDADAGVAEA 196
Cdd:pfam01145 145 DIDPPPEIAEAIEAKQTAEQEAEAEIARAEA 175
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
97-268 |
1.02e-12 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 65.76 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 97 ASEQFLGKSVKEIKQTILQTLEghlRAILGTLTVEEVYKDRDQfaalVREVAAPDVGRMGIEILSFTIKDVYDDVQYLAS 176
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 177 LGKAQTAVVKRDADAGVAEANRDAGIREAECeksamdvKYSTDTKIEDNtrmyKLQKANFDQEINTAKAESqLAYELQAA 256
Cdd:smart00244 74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIG-------KRTLDELLTDQ----REKISENIREELNEAAEA-WGIKVEDV 141
|
170
....*....|..
gi 442616358 257 KIRQRIRNEEIQ 268
Cdd:smart00244 142 EIKDIRLPEEIK 153
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
186-365 |
4.19e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 186 KRDADAGVAEANRDA-GIREAECEKSAMDV-------KYSTDTKIEDNTRMYKLQKANFDQEINTAKAESQLAYELQAAK 257
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAeEVRKAEELRKAEDArkaeaarKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 258 IRQRIRNEEIQIEVVERRKQIEIESQEvQRKDRELTgtvklPAEaEAFRLQTLAQAKQCQTIEGARAEAERIRKIGSAEA 337
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELK-----KAE-EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
|
170 180 190
....*....|....*....|....*....|...
gi 442616358 338 HAIELVGKAE-----AERMRMKAHVYKQYGDAA 365
Cdd:PTZ00121 1323 KAEEAKKKADaakkkAEEAKKAAEAAKAEAEAA 1355
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
188-355 |
9.66e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 38.65 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 188 DADAGVAEANRDAGIREAECEKSAMDVKystdtkiEDNTRMYKLQKANFDQEINT--AKAESQLAYELQAAKiRQRIRNE 265
Cdd:NF041483 532 EAERLRAEAEEQAEEVRAAAERAARELR-------EETERAIAARQAEAAEELTRlhTEAEERLTAAEEALA-DARAEAE 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 266 EIQIEVVERRKQIEIESQEVQRkdreltgTVKLPAEAEAFRLQTLAQAKQCQtiegARAEAE----RIRKIGSAEAHAIE 341
Cdd:NF041483 604 RIRREAAEETERLRTEAAERIR-------TLQAQAEQEAERLRTEAAADASA----ARAEGEnvavRLRSEAAAEAERLK 672
|
170
....*....|....
gi 442616358 342 LVGKAEAERMRMKA 355
Cdd:NF041483 673 SEAQESADRVRAEA 686
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
5-435 |
1.98e-84 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 265.20 E-value: 1.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 5 HTTGPNEALIVSGGccgSTKKRTIVGGWAWAWWLVTDVQRLSLNVMTLN-PMCENVETSQGVPLTVTGVAQCKIMKMmnv 83
Cdd:COG2268 29 RKVPPNEALVITGR---GGGYKVVTGGGAFVLPVLHRAERMSLSTMTIEvERTEGLITKDGIRVDVDAVFYVKVNSD--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 84 yyfhhqaDELLGTASEQFLGKSVKEIKQTILQTLEGHLRAILGTLTVEEVYKDRDQFAALVREVAAPDVGRMGIEILSFT 163
Cdd:COG2268 103 -------PEDIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 164 IKDVYDDVQYLASLGKAQTAVVKRDADAGVAEANRDAGIREAECEKSAMDVKYSTDTKIEDNT-----RMYKLQKANFDQ 238
Cdd:COG2268 176 ITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARiaeaeAELAKKKAEERR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 239 EINTAKAESQLAYELQAAKIRQRIrneEIQIEVVERRKQIEIESQEVQRKDRELTGTVKLPAEAEAFRlqtlaqakqcqt 318
Cdd:COG2268 256 EAETARAEAEAAYEIAEANAEREV---QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA------------ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 319 iegARAEAErirkigsAEAHAIELVGKAEAERMRMKAHVYKQYGDAAIMNIVLESLPKIAAEVAAPLAKTDEIVLI---G 395
Cdd:COG2268 321 ---AEAEAE-------AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIdggN 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 442616358 396 GNDNITNDVTRLVAQLPPSINALTGVDLSKVLSKIPGAKA 435
Cdd:COG2268 391 GGNGAGSAVAEALAPLLESLLEETGLDLPGLLKGLTGAGA 430
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
34-188 |
1.26e-62 |
|
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: 198.88 E-value: 1.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 34 WAWWLVTDVQRLSLNVMTLNPMCENVETSQGVPLTVTGVAQCKIMKmmnvyyfhhqADELLGTASEQFLGKSVKEIKQTI 113
Cdd:cd03399 1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGS----------DPEEIAAAAERFLGKSTEEIRELV 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442616358 114 LQTLEGHLRAILGTLTVEEVYKDRDQFAALVREVAAPDVGRMGIEILSFTIKDVYDDVQYLASLGKAQTAVVKRD 188
Cdd:cd03399 71 KETLEGHLRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
6-196 |
1.46e-17 |
|
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: 80.06 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 6 TTGPNEALIVSGGccgSTKKRTIVGGWAWAWWLVTDVQRLSLNVMTLNPMCENVETSQGVPLTVTGVAQCKIMKmmnvyy 85
Cdd:pfam01145 2 IVPPGEVGVVTRF---GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 86 fhHQADELLGTASEQflgksvKEIKQTILQTLEGHLRAILGTLTVEEVYKDRDQFAALVREVAAPDVGRMGIEILSFTIK 165
Cdd:pfam01145 73 --DDPPKLVQNVFGS------DDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQIT 144
|
170 180 190
....*....|....*....|....*....|.
gi 442616358 166 DVYDDVQYLASLGKAQTAVVKRDADAGVAEA 196
Cdd:pfam01145 145 DIDPPPEIAEAIEAKQTAEQEAEAEIARAEA 175
|
|
| SPFH_like |
cd02106 |
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
48-170 |
1.73e-16 |
|
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: 75.09 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 48 NVMTLNPMCENVETSQGVPLTVTGVAQCKIMKMMNVYYFhhqadellgtaseqFLGKSVKEIKQTILQTLEGHLRAILGT 127
Cdd:cd02106 1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAF--------------YLVDFVKDIKADIRRKIADVLRAAIGR 66
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 442616358 128 LTVEEVYKDRDQFAALVREVAAPDVGRMGIEILSFTIKDVYDD 170
Cdd:cd02106 67 MTLDQIISGRDEIAKAVKEDLEEDLENFGVVISDVDITSIEPP 109
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
97-268 |
1.02e-12 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 65.76 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 97 ASEQFLGKSVKEIKQTILQTLEghlRAILGTLTVEEVYKDRDQfaalVREVAAPDVGRMGIEILSFTIKDVYDDVQYLAS 176
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 177 LGKAQTAVVKRDADAGVAEANRDAGIREAECeksamdvKYSTDTKIEDNtrmyKLQKANFDQEINTAKAESqLAYELQAA 256
Cdd:smart00244 74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIG-------KRTLDELLTDQ----REKISENIREELNEAAEA-WGIKVEDV 141
|
170
....*....|..
gi 442616358 257 KIRQRIRNEEIQ 268
Cdd:smart00244 142 EIKDIRLPEEIK 153
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
25-279 |
1.92e-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: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 25 KRTIVGGWAWAWWLVTDVQRLSLNVMTLNPMCENVETSQGVPLTVTGVAQCKIMKMMNVYYfhhqadellgtaseqflgk 104
Cdd:COG0330 39 VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAKFLY------------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 105 SVKEIKQTILQTLEGHLRAILGTLTVEEVY-KDRDQFAALVREVAAPDVGRMGIEILSFTIKDVYDDVQYLASLGKAQTA 183
Cdd:COG0330 100 NVENAEEALRQLAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 184 VVKRDADAGVAEANRDAGIREAECEKSAmdvkystdtKIEdntrmykLQKANFDQEINTAKAESQlayelqaakiRQRIR 263
Cdd:COG0330 180 EREREAAILEAEGYREAAIIRAEGEAQR---------AII-------EAEAYREAQILRAEGEAE----------AFRIV 233
|
250
....*....|....*..
gi 442616358 264 NEEIQ-IEVVERRKQIE 279
Cdd:COG0330 234 AEAYSaAPFVLFYRSLE 250
|
|
| Flot |
pfam15975 |
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ... |
322-397 |
1.02e-06 |
|
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, archaea and eukaryotes. The family is found in association with pfam01145, another integral membrane-associated domain. Flotillins in vertebrates are associated with sphingolipids and cholesterol-enriched membrane microdomains known as lipid-rafts. These rafts along with other membrane components are important in cell-signalling. Flotillins in other organizms have roles in viral pathogenesis, endocytosis, and membrane shaping.
Pssm-ID: 435047 [Multi-domain] Cd Length: 121 Bit Score: 47.32 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 322 ARAEAERIRkigsAEAHAIELVGKAEAERMRMKAHVYKQYGDAAI-MNI---VLESLPKIAAEVAAPLAKTDEIVLIGGN 397
Cdd:pfam15975 2 AEAEADAIK----LRAEAKRKKALAEAEGIRALNEAENALSDEQIaLQVklaLLEALPEIIAESVKPLEKIDGIKILQVD 77
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
194-360 |
8.50e-06 |
|
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: 48.20 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 194 AEANRDAGIReAECEKSAMDVKYSTD-TKIEDNTR-MYKLQKANFDQEINTAKAESQLAYElqaakiRQRiRNEEIQIEV 271
Cdd:pfam17380 327 AEMDRQAAIY-AEQERMAMERERELErIRQEERKReLERIRQEEIAMEISRMRELERLQME------RQQ-KNERVRQEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 272 VERRKQiEIESQEVQRKDRELTgtvklpAEAEAFRL-QTLAQAKQCQTIEGARA-EAERIRKIGSAEAHAIELVGKAEAE 349
Cdd:pfam17380 399 EAARKV-KILEEERQRKIQQQK------VEMEQIRAeQEEARQREVRRLEEERArEMERVRLEEQERQQQVERLRQQEEE 471
|
170
....*....|.
gi 442616358 350 RMRMKAHVYKQ 360
Cdd:pfam17380 472 RKRKKLELEKE 482
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
186-365 |
4.19e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 186 KRDADAGVAEANRDA-GIREAECEKSAMDV-------KYSTDTKIEDNTRMYKLQKANFDQEINTAKAESQLAYELQAAK 257
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAeEVRKAEELRKAEDArkaeaarKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 258 IRQRIRNEEIQIEVVERRKQIEIESQEvQRKDRELTgtvklPAEaEAFRLQTLAQAKQCQTIEGARAEAERIRKIGSAEA 337
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELK-----KAE-EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
|
170 180 190
....*....|....*....|....*....|...
gi 442616358 338 HAIELVGKAE-----AERMRMKAHVYKQYGDAA 365
Cdd:PTZ00121 1323 KAEEAKKKADaakkkAEEAKKAAEAAKAEAEAA 1355
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
169-350 |
1.79e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 169 DDVQYLASLGKAQTavVKRDADAGVAEANRDAGIREAECEKSAMDVKYSTDTKIEDNTRMYKLQKANFDQEiNTAKAESQ 248
Cdd:PTZ00121 1549 DELKKAEELKKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEEL 1625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 249 LAYELQAAKIRQRIRNEEIQIEVVERRKQIE----IESQEVQRKDREltgTVKLPAEAEAFRLQTLAQAKQCQTIEGARA 324
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeenkIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
170 180
....*....|....*....|....*.
gi 442616358 325 EAERIRKIGSAEAHAIELVGKAEAER 350
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEEN 1728
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
179-355 |
4.94e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 179 KAQTAVVKRDAD-AGVAEANRDAG-IREAECEKSAMDVKYSTDTKIEDNTRMYKLQKANFDQEINTAKAESQLAYELQAA 256
Cdd:PTZ00121 1526 EAKKAEEAKKADeAKKAEEKKKADeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 257 KIRQrirnEEIQIEVVERRKQIEIESQEVQRKDREltgTVKLPAEAEAFRLQTLAQAKQCQTI---EGARAEAERIRKig 333
Cdd:PTZ00121 1606 KMKA----EEAKKAEEAKIKAEELKKAEEEKKKVE---QLKKKEAEEKKKAEELKKAEEENKIkaaEEAKKAEEDKKK-- 1676
|
170 180
....*....|....*....|..
gi 442616358 334 SAEAHAIELVGKAEAERMRMKA 355
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEA 1698
|
|
| SPFH_alloslipin |
cd13437 |
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ... |
105-216 |
5.96e-04 |
|
Alloslipin, 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 some eukaryotes and viruses. 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. This diverse subgroup of the SLPs remains largely uncharacterized.
Pssm-ID: 259815 [Multi-domain] Cd Length: 222 Bit Score: 41.06 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 105 SVKEIKQTILQTLEGHLRAILGTLTVEEVYKDRDQFAALVREVAAPDVGRMGIEILSFTIKDVYDDVQYLASLGKAqtAV 184
Cdd:cd13437 85 RIDNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSLSSA--AK 162
|
90 100 110
....*....|....*....|....*....|....*....
gi 442616358 185 VKRDADAGV--AEANRDAG--IREAE---CEKSAMDVKY 216
Cdd:cd13437 163 AKRIGESKIisAKADVESAklMREAAdilDSKAAMQIRY 201
|
|
| SPFH_eoslipins_u2 |
cd13438 |
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ... |
61-167 |
6.09e-04 |
|
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial SLPs remain uncharacterized.
Pssm-ID: 259816 [Multi-domain] Cd Length: 215 Bit Score: 40.98 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 61 TSQGVPLTVTGVAQCKIMkmmNVYYFHHQADELlgtasEQFLgksvkeikQTILQTLeghLRAILGTLTVEEVYKDRDQF 140
Cdd:cd13438 54 TADKVALRVNLVATYRVV---DPVKAVETVDDP-----EEQL--------YLALQLA---LREAVAARTLDELLEDREDL 114
|
90 100
....*....|....*....|....*..
gi 442616358 141 AALVREVAAPDVGRMGIEILSFTIKDV 167
Cdd:cd13438 115 SEFLLAAVKEAAAELGVEVLSVGVKDI 141
|
|
| SPFH_SLPs |
cd13434 |
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ... |
47-167 |
7.10e-04 |
|
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: 39.10 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 47 LNVMTLNPMCENVETSQGVPLTVTGVAQCKI---MKMMNVYYFHHQADELLGtaseqflgksvkeikQTILqtleghlRA 123
Cdd:cd13434 3 LRTQSVDVPPQEILTKDNVTVSVDAVVYYRVvdpLKAVLNVEDYKKATELLA---------------QTTL-------RN 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 442616358 124 ILGTLTVEEVYKDRDQFAALVREVAAPDVGRMGIEILSFTIKDV 167
Cdd:cd13434 61 VLGTRTLDELLSEREEISQQLQEILDEATDPWGIKVERVEIKDI 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
185-364 |
1.27e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 185 VKRDADAGVAEANRDAGIREAECEKSAMDVKYSTDTKIEDNTRmyKLQKANFDQEINTAKAESQLAYELQAAKIRQRIRN 264
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK--KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 265 EEIQIEVVERRKQIEIESQEVQRKDRELTGTVKlpaEAEAFRLQTLAQAKQCqtiEGARAEAERIRKIGSAEAHAIElvG 344
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE---KAEAAEKKKEEAKKKA---DAAKKKAEEKKKADEAKKKAEE--D 1403
|
170 180
....*....|....*....|
gi 442616358 345 KAEAERMRMKAHVYKQYGDA 364
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEA 1423
|
|
| SPFH_HflK |
cd03404 |
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ... |
300-361 |
1.47e-03 |
|
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.
Pssm-ID: 259802 [Multi-domain] Cd Length: 266 Bit Score: 40.19 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442616358 300 AEAEAFRLQTLAQAKQCQTIEGARAEAERIRKIgsAEAHAIELVGKAEAERMRMKAhVYKQY 361
Cdd:cd03404 182 ARQDKERLINEAQAYANEVIPRARGEAARIIQE--AEAYKAEVVARAEGDAARFLA-LLAEY 240
|
|
| SPFH_paraslipin |
cd08829 |
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ... |
106-167 |
4.33e-03 |
|
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: 36.68 E-value: 4.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442616358 106 VKEIKQTILQTLEGHLRAILGTLTVEEVYKDRDQFAALVREVAAPDVGRMGIEILSFTIKDV 167
Cdd:cd08829 46 VEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAKLLEALDEATDPWGVKVTRVEIKDI 107
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
273-355 |
6.31e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 37.63 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 273 ERRKQIEIESQEVQrkDRELTGTVKLpAEAEafrlQTLAQAKQcqtiegaraEAERIRKIGSAEAHAI--ELVGKAEAER 350
Cdd:PRK07352 50 ERREAILQALKEAE--ERLRQAAQAL-AEAQ----QKLAQAQQ---------EAERIRADAKARAEAIraEIEKQAIEDM 113
|
....*
gi 442616358 351 MRMKA 355
Cdd:PRK07352 114 ARLKQ 118
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
215-355 |
8.37e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 38.62 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 215 KYSTDTKI---EDNTRMY-----KLQKANFDQEINTAKAESQLAYELQAAKIRQRIRN--EEIQIEVVERRKQIEIESQE 284
Cdd:pfam01576 126 KVTTEAKIkklEEDILLLedqnsKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNkhEAMISDLEERLKKEEKGRQE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 285 VQRKDRELTG--------TVKLPAEAEAFRLQTLAQAKQCQTIEgARAEAER------IRKIGSAEAHAIELVGKAEAER 350
Cdd:pfam01576 206 LEKAKRKLEGestdlqeqIAELQAQIAELRAQLAKKEEELQAAL-ARLEEETaqknnaLKKIRELEAQISELQEDLESER 284
|
....*.
gi 442616358 351 -MRMKA 355
Cdd:pfam01576 285 aARNKA 290
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
188-355 |
9.66e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 38.65 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 188 DADAGVAEANRDAGIREAECEKSAMDVKystdtkiEDNTRMYKLQKANFDQEINT--AKAESQLAYELQAAKiRQRIRNE 265
Cdd:NF041483 532 EAERLRAEAEEQAEEVRAAAERAARELR-------EETERAIAARQAEAAEELTRlhTEAEERLTAAEEALA-DARAEAE 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442616358 266 EIQIEVVERRKQIEIESQEVQRkdreltgTVKLPAEAEAFRLQTLAQAKQCQtiegARAEAE----RIRKIGSAEAHAIE 341
Cdd:NF041483 604 RIRREAAEETERLRTEAAERIR-------TLQAQAEQEAERLRTEAAADASA----ARAEGEnvavRLRSEAAAEAERLK 672
|
170
....*....|....
gi 442616358 342 LVGKAEAERMRMKA 355
Cdd:NF041483 673 SEAQESADRVRAEA 686
|
|
| |
