|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
5-417 |
8.16e-87 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 271.36 E-value: 8.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 5 HTVGPNEALVVSGGCCGSDVkqyVYGGWAWAWWCITDTQRLSLEVMTI-LCRCENIETSEGVPLYVTGVAQVKIMTEKEL 83
Cdd:COG2268 29 RKVPPNEALVITGRGGGYKV---VTGGGAFVLPVLHRAERMSLSTMTIeVERTEGLITKDGIRVDVDAVFYVKVNSDPED 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 84 LAVACEQFLGKNVQDVKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDY 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 164 LSSLGKTQTAAVRRDADIGVAEAERDAGIREAECKKEMLDVKFMADT-----KIADSRRAFELQKAAFTEEVNIKTAEAQ 238
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 239 LAYELQSAREQQKIRQeeiEIEVVQRKKQIDVEEKEIIRKEKELIATVKRPAEAEAYRIQQIAegekvrrvllaqaeaek 318
Cdd:COG2268 266 AAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA----------------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 319 irkigEAEAFVIEAIGMAEAERMKLKAEALQSYGEAAQLALVLDALPEIAAKVAAPLSRVDEIVVLSGESGN--VTSEVN 396
Cdd:COG2268 326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVA 400
|
410 420
....*....|....*....|.
gi 2123788168 397 RLLAEIPASVRAITGVDLTKI 417
Cdd:COG2268 401 EALAPLLESLLEETGLDLPGL 421
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
34-178 |
9.35e-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: 204.28 E-value: 9.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 34 WAWWCITDTQRLSLEVMTILCRCENIETSEGVPLYVTGVAQVKIMTEKELLAVACEQFLGKNVQDVKNVVLQTLEGHLRS 113
Cdd:cd03399 1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123788168 114 ILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAAVRRD 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 |
1.25e-19 |
|
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: 85.84 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 6 TVGPNEALVVSGGccgSDVKQYVYGGWAWAWWCITDTQRLSLEVMTILCRCENIETSEGVPLYVTGVAQVKIMTEKELLA 85
Cdd:pfam01145 2 IVPPGEVGVVTRF---GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 86 VAceQFLGKNvqDVKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLS 165
Cdd:pfam01145 79 VQ--NVFGSD--DLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154
|
170 180
....*....|....*....|...
gi 2123788168 166 SLGKTQTAAVRRDADIGVAEAER 188
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
87-265 |
5.22e-13 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 66.53 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 87 ACEQFLGKNVQDVKNVVLQTLEghlRSILGTLTVEQIYQDRdqfaKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSS 166
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDV----KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 167 LGKTQTAAVRRDADIGVAEAERDAGIREAECKKEMLDVkfmadtkIADSRrafeLQKAAFTEEVNIKTAEAqLAYELQSA 246
Cdd:smart00244 74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDEL-------LTDQR----EKISENIREELNEAAEA-WGIKVEDV 141
|
170
....*....|....*....
gi 2123788168 247 REQQKIRQEEIeIEVVQRK 265
Cdd:smart00244 142 EIKDIRLPEEI-KEAMEAQ 159
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
184-401 |
1.21e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 184 AEAERDAG-IREAECKKEMLDVKFMADTKIADSRRAFELQKAafteEVNIKTAEAQLAYELQSAREQQKIRQEEIEIEVV 262
Cdd:PTZ00121 1542 AEEKKKADeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA----EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 263 QRKKQIDVEEKEIIRKEKELIATVKRPAEAEAYRIQQIAEGEKVRRVLLAQAEAEKIRKIGEAEafvieaigmAEAERMK 342
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK---------KAEEDEK 1688
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2123788168 343 LKAEALQSYGEAAQLALVLDALPEIAAKVAAPLSRVDEIVVLSGESGNVTSEVNRLLAE 401
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
207-407 |
1.03e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 207 MADTKIADSRRAFELQKAAFTEEVNIKTAEAQLAYELQSAREQQKIRQEEIEIEVVQRKKQIDVEEKEIIRKEKELIATV 286
Cdd:TIGR02794 59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 287 KRPAEAEAYRIQQIAEGEKVRRVLLAQAEAEKIRKIGEAEAFVI-EAIGMAEAERMKLKAEALQSYGEA---AQLALVLD 362
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKaEAEAKAKAEEAKAKAEAAKAKAAAeaaAKAEAEAA 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2123788168 363 ALPEIAAKVAAPLSRVDEIVVLSGES----------GNVTSEVNRLLAEIPASVR 407
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLASGSnaekqggargAAAGSEVDKYAAIIQQAIQ 273
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
5-417 |
8.16e-87 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 271.36 E-value: 8.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 5 HTVGPNEALVVSGGCCGSDVkqyVYGGWAWAWWCITDTQRLSLEVMTI-LCRCENIETSEGVPLYVTGVAQVKIMTEKEL 83
Cdd:COG2268 29 RKVPPNEALVITGRGGGYKV---VTGGGAFVLPVLHRAERMSLSTMTIeVERTEGLITKDGIRVDVDAVFYVKVNSDPED 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 84 LAVACEQFLGKNVQDVKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDY 163
Cdd:COG2268 106 IANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 164 LSSLGKTQTAAVRRDADIGVAEAERDAGIREAECKKEMLDVKFMADT-----KIADSRRAFELQKAAFTEEVNIKTAEAQ 238
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEReietaRIAEAEAELAKKKAEERREAETARAEAE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 239 LAYELQSAREQQKIRQeeiEIEVVQRKKQIDVEEKEIIRKEKELIATVKRPAEAEAYRIQQIAegekvrrvllaqaeaek 318
Cdd:COG2268 266 AAYEIAEANAEREVQR---QLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA----------------- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 319 irkigEAEAFVIEAIGMAEAERMKLKAEALQSYGEAAQLALVLDALPEIAAKVAAPLSRVDEIVVLSGESGN--VTSEVN 396
Cdd:COG2268 326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGngAGSAVA 400
|
410 420
....*....|....*....|.
gi 2123788168 397 RLLAEIPASVRAITGVDLTKI 417
Cdd:COG2268 401 EALAPLLESLLEETGLDLPGL 421
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
34-178 |
9.35e-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: 204.28 E-value: 9.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 34 WAWWCITDTQRLSLEVMTILCRCENIETSEGVPLYVTGVAQVKIMTEKELLAVACEQFLGKNVQDVKNVVLQTLEGHLRS 113
Cdd:cd03399 1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKVGSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2123788168 114 ILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAAVRRD 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 |
5.52e-20 |
|
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons, and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259797 [Multi-domain] Cd Length: 110 Bit Score: 84.72 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 48 EVMTILCRCENIETSEGVPLYVTGVAQVKIMTEKELLAVAceqfLGKNVQDVKNVVLQTLEGHLRSILGTLTVEQIYQDR 127
Cdd:cd02106 1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFY----LVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGR 76
|
90 100 110
....*....|....*....|....*....|...
gi 2123788168 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 |
1.25e-19 |
|
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: 85.84 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 6 TVGPNEALVVSGGccgSDVKQYVYGGWAWAWWCITDTQRLSLEVMTILCRCENIETSEGVPLYVTGVAQVKIMTEKELLA 85
Cdd:pfam01145 2 IVPPGEVGVVTRF---GKLSRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 86 VAceQFLGKNvqDVKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLS 165
Cdd:pfam01145 79 VQ--NVFGSD--DLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154
|
170 180
....*....|....*....|...
gi 2123788168 166 SLGKTQTAAVRRDADIGVAEAER 188
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
87-265 |
5.22e-13 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 66.53 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 87 ACEQFLGKNVQDVKNVVLQTLEghlRSILGTLTVEQIYQDRdqfaKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSS 166
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDV----KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 167 LGKTQTAAVRRDADIGVAEAERDAGIREAECKKEMLDVkfmadtkIADSRrafeLQKAAFTEEVNIKTAEAqLAYELQSA 246
Cdd:smart00244 74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGKRTLDEL-------LTDQR----EKISENIREELNEAAEA-WGIKVEDV 141
|
170
....*....|....*....
gi 2123788168 247 REQQKIRQEEIeIEVVQRK 265
Cdd:smart00244 142 EIKDIRLPEEI-KEAMEAQ 159
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
40-200 |
2.55e-09 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 57.93 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 40 TDTQRLSLEVMTILcrcenieTSEGVPLYVTGVAQVKIMTEKELLavaceqflgKNVQDVKNVVLQTLEGHLRSILGTLT 119
Cdd:COG0330 61 VREQVLDVPPQEVL-------TKDNNIVDVDAVVQYRITDPAKFL---------YNVENAEEALRQLAESALREVIGKMT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 120 VEQIY-QDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAAVRRDADIGVAEAERDAGIREAECK 198
Cdd:COG0330 125 LDEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGE 204
|
..
gi 2123788168 199 KE 200
Cdd:COG0330 205 AQ 206
|
|
| Flot |
pfam15975 |
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ... |
313-396 |
5.93e-09 |
|
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, archaea and eukaryotes. The family is found in association with pfam01145, another integral membrane-associated domain. Flotillins in vertebrates are associated with sphingolipids and cholesterol-enriched membrane microdomains known as lipid-rafts. These rafts along with other membrane components are important in cell-signalling. Flotillins in other organizms have roles in viral pathogenesis, endocytosis, and membrane shaping.
Pssm-ID: 435047 [Multi-domain] Cd Length: 121 Bit Score: 53.87 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 313 QAEAEKIRKIGEAEAfvIEAIGMAEAERMKLKAEALQSYGE---AAQLAL-VLDALPEIAAKVAAPLSRVDEIVVLS--G 386
Cdd:pfam15975 1 EAEAEADAIKLRAEA--KRKKALAEAEGIRALNEAENALSDeqiALQVKLaLLEALPEIIAESVKPLEKIDGIKILQvdG 78
|
90
....*....|
gi 2123788168 387 ESGNVTSEVN 396
Cdd:pfam15975 79 LGGGAAGGGG 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
184-401 |
1.21e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 184 AEAERDAG-IREAECKKEMLDVKFMADTKIADSRRAFELQKAafteEVNIKTAEAQLAYELQSAREQQKIRQEEIEIEVV 262
Cdd:PTZ00121 1542 AEEKKKADeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA----EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 263 QRKKQIDVEEKEIIRKEKELIATVKRPAEAEAYRIQQIAEGEKVRRVLLAQAEAEKIRKIGEAEafvieaigmAEAERMK 342
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK---------KAEEDEK 1688
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2123788168 343 LKAEALQSYGEAAQLALVLDALPEIAAKVAAPLSRVDEIVVLSGESGNVTSEVNRLLAE 401
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
176-358 |
2.38e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 176 RRDADIGVAEAERDAGIREAECKKemldvkfmadtKIADSRRAFELQKAaftEEVNIKTAEAQLAYELQSAREQQKIRQE 255
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKK-----------KADEAKKAEEKKKA---DEAKKKAEEAKKADEAKKKAEEAKKKAD 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 256 EIEIEVVQRKKQIDVEEKEIIRKEKELIATVKRPAEAEAYRIQQIAEGEKVRRVLLAQAEAEKIRKIGEAEAFVIEAIGM 335
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412
|
170 180
....*....|....*....|...
gi 2123788168 336 AEAErmKLKAEALQSYGEAAQLA 358
Cdd:PTZ00121 1413 AAAA--KKKADEAKKKAEEKKKA 1433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
174-358 |
9.50e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 174 AVRRDADIGVAEAERDAGIREAECKKEMLDVKfmadtKIADSRRAFELQKAaftEEV----NIKTAEAQLAYELQSAREQ 249
Cdd:PTZ00121 1145 ARKAEDAKRVEIARKAEDARKAEEARKAEDAK-----KAEAARKAEEVRKA---EELrkaeDARKAEAARKAEEERKAEE 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 250 QKIRQEEIEIEVVQRKKQIDVEEKEIIRKEKELIATVKRPAEA----------------EAYRIQQIAEGEKVRRVLLAQ 313
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEarmahfarrqaaikaeEARKADELKKAEEKKKADEAK 1296
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2123788168 314 aEAEKIRKIGEAEAFVIEAIGMAE----AERMKLKAEALQSYGEAAQLA 358
Cdd:PTZ00121 1297 -KAEEKKKADEAKKKAEEAKKADEakkkAEEAKKKADAAKKKAEEAKKA 1344
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
171-380 |
2.20e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 171 QTAAVRRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIADSRRAFELQKAA----FTEEVNIKTAEAQLAYELQSA 246
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAeeakKADEAKKKAEEAKKADEAKKK 1491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 247 REQQKIRQEEIEIEVVQRKKQIDVEEKEIIRKEKEL-IATVKRPAEA-----------EAYRIQQIAEGEKVRRVLLAQA 314
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkKAEEAKKADEakkaeekkkadELKKAEELKKAEEKKKAEEAKK 1571
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2123788168 315 E----------AEKIRKIGEAEafvIEAIGMAEAERMKLKAEALQSYGEAAQLALVLDALPEIAAKVAAPLSRVDE 380
Cdd:PTZ00121 1572 AeedknmalrkAEEAKKAEEAR---IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
|
| SPFH_SLPs |
cd13434 |
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ... |
59-157 |
8.48e-06 |
|
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: 44.49 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 59 IETSEGVPLYVTGVAQVKImtEKELLAVAceqflgkNVQDVKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVA 138
Cdd:cd13434 15 ILTKDNVTVSVDAVVYYRV--VDPLKAVL-------NVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQEIL 85
|
90
....*....|....*....
gi 2123788168 139 APDVGRMGIEILSFTIKDV 157
Cdd:cd13434 86 DEATDPWGIKVERVEIKDI 104
|
|
| SPFH_SLP-3 |
cd08828 |
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ... |
38-190 |
2.31e-05 |
|
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this slipin subgroup remain uncharacterized, except for Caenorhabditis elegans UNC-1. Mutations in the unc-1 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.
Pssm-ID: 259810 [Multi-domain] Cd Length: 154 Bit Score: 44.25 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 38 CITDTQRLSLEVMTILCRCENIETSEGVPLYVTGVAQVKIMTEkeLLAVAceqflgkNVQDVKNVVLQTLEGHLRSILGT 117
Cdd:cd08828 11 CTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSA--VKAVA-------NVNNVHIATFLLAQTTLRNVLGT 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2123788168 118 LTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAAVRRDADIGVAEAERDA 190
Cdd:cd08828 82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGEMNA 154
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
169-346 |
4.01e-05 |
|
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: 45.88 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 169 KTQTAAVRRDADIgVAEAERDAGIREAECKKEMLDVKFMADTKIADSRRAFELQKAAFTEEVNIKTAEA--QLAYELQSA 246
Cdd:pfam17380 323 KARQAEMDRQAAI-YAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKneRVRQELEAA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 247 ReQQKIRQEEieievVQRKKQIDVEEKEIIRKEKELIATVK-------RPAEAEAYRIQQIAEGEKVRRvlLAQAEAEKI 319
Cdd:pfam17380 402 R-KVKILEEE-----RQRKIQQQKVEMEQIRAEQEEARQREvrrleeeRAREMERVRLEEQERQQQVER--LRQQEEERK 473
|
170 180
....*....|....*....|....*..
gi 2123788168 320 RKIGEAEAFVIEAIGMAEAERMKLKAE 346
Cdd:pfam17380 474 RKKLELEKEKRDRKRAEEQRRKILEKE 500
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
208-373 |
8.31e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 208 ADTKIADSRRAFELQKAAftEEVNIKTAEAQlayELQSAREQQKIRQEEIEIEVVQRKKQIDVEEKEIIRKEKELIATVK 287
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQA--EELQQKQAAEQ---ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 288 RPAEAEAYRIQQIAEGEKVRRVLLAQAEAEKiRKIGEAEAFVIEAIGMAEAERMKLKAEALQSYGEAAQLALVLDALPEI 367
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKKKAEAEAAK-KAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225
|
....*.
gi 2123788168 368 AAKVAA 373
Cdd:PRK09510 226 AAAKAA 231
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
183-346 |
8.48e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 183 VAEAERDAGIREAECKKEMLDvkfmadtkiaDSRRAFELQKaaftEEVNIKTAEAQLAYELQSAREQQKIRQEEIEievv 262
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEE----------DKKKAEEAKK----AEEDEKKAAEALKKEAEEAKKAEELKKKEAE---- 1713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 263 QRKKQIDVEEKEIIRKEKelIATVKRPAEAEAYRIQQ--IAEGEKVRRVLLAQAEAEKIRKIGEAEAFVIEAIGMAEAER 340
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIK--AEEAKKEAEEDKKKAEEakKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
|
....*.
gi 2123788168 341 MKLKAE 346
Cdd:PTZ00121 1792 RRMEVD 1797
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
207-407 |
1.03e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 207 MADTKIADSRRAFELQKAAFTEEVNIKTAEAQLAYELQSAREQQKIRQEEIEIEVVQRKKQIDVEEKEIIRKEKELIATV 286
Cdd:TIGR02794 59 KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 287 KRPAEAEAYRIQQIAEGEKVRRVLLAQAEAEKIRKIGEAEAFVI-EAIGMAEAERMKLKAEALQSYGEA---AQLALVLD 362
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKaEAEAKAKAEEAKAKAEAAKAKAAAeaaAKAEAEAA 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2123788168 363 ALPEIAAKVAAPLSRVDEIVVLSGES----------GNVTSEVNRLLAEIPASVR 407
Cdd:TIGR02794 219 AAAAAEAERKADEAELGDIFGLASGSnaekqggargAAAGSEVDKYAAIIQQAIQ 273
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
209-412 |
3.12e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 209 DTKIADSRRAFELQKAAFTE-EVNIKTAEAQLaYELQSAREQQKIRQEEIEIEVVQRKKQIDVEEKEIIRKEKELIATVK 287
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAElEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 288 RPAEAEAYRIQQIAEGEKvrrvlLAQAEAEKIRKIGEAEAFVIEAIGMAEAERM---KLKAEALQSYGEAAQLALVLDAL 364
Cdd:TIGR02168 755 ELTELEAEIEELEERLEE-----AEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2123788168 365 P-EIAAKVAAPLSRVDEIVVLSGESGNVTSEVNRLLAEIPASVRAITGV 412
Cdd:TIGR02168 830 ErRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
216-402 |
3.12e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 216 RRAFELQKAAFTEEVN-----IKTAEAQLAyELQSAREQQKIRQEEIEIEVVQRKKQIDVEEKEIIRKEKELIATVKRPA 290
Cdd:COG1196 234 LRELEAELEELEAELEeleaeLEELEAELA-ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 291 EAEAyRIQQIAEGEKVRRVLLAQAEAEKIRKIGEAEAFVIEAIGMAEAERMKLKAEALQSYGEAAQLALVLDALPEIAAK 370
Cdd:COG1196 313 ELEE-RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190
....*....|....*....|....*....|..
gi 2123788168 371 VAAPLSRVDEIVVLSGESGNVTSEVNRLLAEI 402
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
|
| SPFH_paraslipin |
cd08829 |
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ... |
95-157 |
3.16e-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: 40.15 E-value: 3.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2123788168 95 NVQDVKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDV 157
Cdd:cd08829 45 GVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEINAKLLEALDEATDPWGVKVTRVEIKDI 107
|
|
| SPFH_eoslipins_u2 |
cd13438 |
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ... |
59-157 |
4.69e-04 |
|
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial SLPs remain uncharacterized.
Pssm-ID: 259816 [Multi-domain] Cd Length: 215 Bit Score: 41.37 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 59 IETSEGVPLYVTGVAQVKImtekellaVACEQFLgKNVQDVKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVA 138
Cdd:cd13438 52 ILTADKVALRVNLVATYRV--------VDPVKAV-ETVDDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAV 122
|
90
....*....|....*....
gi 2123788168 139 APDVGRMGIEILSFTIKDV 157
Cdd:cd13438 123 KEAAAELGVEVLSVGVKDI 141
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
173-364 |
7.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 173 AAVRRDADIGVAEAERDAGIREAECKKEMLDVKFmadTKIADSRRAFELQKAAFTEEVNIKTAEAQLAYELQSAREQQKI 252
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAEL---AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 253 RQEEIEIEVVQRKKQIDVEEKEIIRKEKELIATVKRpAEAEAYRIQQIAEGEKVRRVLLAQAEAEKIRKIGEAEafviEA 332
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEE-LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE----EE 380
|
170 180 190
....*....|....*....|....*....|..
gi 2123788168 333 IGMAEAERMKLKAEALQSYGEAAQLALVLDAL 364
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
184-381 |
9.41e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 184 AEAERDAGIREAECKKEMLDVKFMADTKIADSRRAFELQKAAfteeVNIKTAEAQLAYELQSAREQQKIRQEEIEIEVVQ 263
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA----AEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 264 RKKQID-VEEKEIIRKEKEliaTVKRPAEAEAYRIQQIAEGEKVRRVLLAQAEAEKIRKIGEAEAFVIEAigmAEAERMK 342
Cdd:PTZ00121 1403 DKKKADeLKKAAAAKKKAD---EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA---KKADEAK 1476
|
170 180 190
....*....|....*....|....*....|....*....
gi 2123788168 343 LKAEALQSYGEAAQLALVLDALPEIAAKVAAPLSRVDEI 381
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| SPFH_HflC |
cd03405 |
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ... |
244-358 |
2.37e-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: 39.39 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 244 QSAREQQKIRQEEIEIEVVQ-RKKQID----VEEKEIIRKEKEliatvkRPAEAEAYRiqqiAEGEKVRRVLLAQAEAEK 318
Cdd:cd03405 123 EEILEQANEEAKEYGIEVVDvRIKRIDlpeeVSESVYERMRAE------RERIAAEYR----AEGEEEAEKIRAEADRER 192
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2123788168 319 IRKIGEAEAFVIEAIGMAEAERMKLKAEAlqsYGEAAQLA 358
Cdd:cd03405 193 TVILAEAYREAEEIRGEGDAEAARIYAEA---YGKDPEFY 229
|
|
| SPFH_eoslipins_u3 |
cd13775 |
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ... |
95-190 |
3.50e-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: 38.38 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 95 NVQDVKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAA 174
Cdd:cd13775 42 EVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPWGITVQSVEIRDIIIPKELQDAMSREAQAE 121
|
90
....*....|....*.
gi 2123788168 175 VRRDADIGVAEAERDA 190
Cdd:cd13775 122 REKNARVILAEAEKEI 137
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
211-413 |
6.45e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 211 KIADSRRAFELQKAAFTEEVNIKTAEAQLAYELQSAREQQKIRQEEIEIEVVQRKKQIDVEEKEIIRKEKELIATVKRPA 290
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 291 EAEAYRIQQIAEGEKVRRVLLAQAEAEKIRKIGEAEAfvieaigmaEAERMKLKAEALQsygEAAQLALVLDALPEIAAK 370
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEA---------LEEAAEEEAELEE---EEEALLELLAELLEEAAL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2123788168 371 VAAPLSRVDEIVVLSGESGNVTSEVNRLLAEIPASVRAITGVD 413
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| SPFH_alloslipin |
cd13437 |
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ... |
96-205 |
8.82e-03 |
|
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: 37.59 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2123788168 96 VQDVKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVY---DKVDYLSSLGKTQT 172
Cdd:cd13437 86 IDNVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVlskDLQQSLSSAAKAKR 165
|
90 100 110
....*....|....*....|....*....|....*
gi 2123788168 173 AAvrrDADIGVAEAERDAG--IREAeckKEMLDVK 205
Cdd:cd13437 166 IG---ESKIISAKADVESAklMREA---ADILDSK 194
|
|
| |
