|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
18-365 |
1.35e-68 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 222.06 E-value: 1.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 18 VKIQGqNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYT 97
Cdd:COG2268 97 VKVNS-DPEDIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 98 LKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIE-----MAKAQRDYELKKAAYDI 172
Cdd:COG2268 176 ITDLEDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 173 EVNTRRAQADLAYQLQVAKTKQQIEeqrVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKlerlaeaeksql 252
Cdd:COG2268 256 EAETARAEAEAAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA------------ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 253 imqAEAEAasvrmrgEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGS 332
Cdd:COG2268 321 ---AEAEA-------EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGN 390
|
330 340 350
....*....|....*....|....*....|...
gi 2462495374 333 GTMGAAKVtgeVLDILTRLPESVERLTGVSISQ 365
Cdd:COG2268 391 GGNGAGSA---VAEALAPLLESLLEETGLDLPG 420
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
18-122 |
5.37e-43 |
|
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: 146.50 E-value: 5.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 18 VKIqGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYT 97
Cdd:cd03399 42 VKV-GSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLRAIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFN 120
|
90 100
....*....|....*....|....*
gi 2462495374 98 LKDIHDDQDYLHSLGKARTAQVQKD 122
Cdd:cd03399 121 IKDISDDNGYLESLGRKQAAEVKKD 145
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
31-213 |
1.45e-17 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 78.86 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 31 ACQMFLGKTEAEIAHIALETLEghqRAIMAHMTVEEIYKDRQKfseqVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHS 110
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 111 LGKARTAQVQKDARIGEAEAKRDAGIREAKAKqekvsaqylseIEMAKAQRDYELKKAAYDIEVNTRRAQAdLAYQLQVA 190
Cdd:smart00244 74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK-----------RTLDELLTDQREKISENIREELNEAAEA-WGIKVEDV 141
|
170 180
....*....|....*....|...
gi 2462495374 191 KTKQqieeQRVQVQVVERAQQVA 213
Cdd:smart00244 142 EIKD----IRLPEEIKEAMEAQQ 160
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
49-132 |
5.57e-11 |
|
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: 60.80 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 49 ETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEA 128
Cdd:pfam01145 94 RVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAKQTAEQEAEAEIARA 173
|
....
gi 2462495374 129 EAKR 132
Cdd:pfam01145 174 EAEA 177
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
56-181 |
4.46e-08 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 53.69 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 56 RAIMAHMTVEEIYK-DRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDA 134
Cdd:COG0330 117 REVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREA 196
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462495374 135 GIREAKAKQEKVsaqylseIEMAKAQRDYELKKAAYDIEVNTRRAQA 181
Cdd:COG0330 197 AIIRAEGEAQRA-------IIEAEAYREAQILRAEGEAEAFRIVAEA 236
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
174-335 |
6.49e-08 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 53.30 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 174 VNTRRAQ--ADLAYQLQVAKTKQQIEEQRVQVQVVERAQQV--AVQEQEIARREKElearvrkpaeaeryKLERLAEAEK 249
Cdd:COG0330 129 LSTGRDEinAEIREELQEALDPYGIEVVDVEIKDIDPPEEVqdAMEDRMKAERERE--------------AAILEAEGYR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 250 SQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLdMLLEKLPQVAEeisgpltSANKITLVS 329
Cdd:COG0330 195 EAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFY-RSLEALEEVLS-------PNSKVIVLP 266
|
....*.
gi 2462495374 330 SGSGTM 335
Cdd:COG0330 267 PDGNGF 272
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
113-316 |
4.64e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 113 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKT 192
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEE-YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 193 KQQIEEQRVQVQVVE-RAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEA 271
Cdd:COG1196 336 EEELEELEEELEEAEeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462495374 272 FAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEIS 316
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-315 |
5.07e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 107 YLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLS----EIEMAKAQRDYELKKAAYDIEVNTRRAQAD 182
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEleelELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 183 LAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEArvrkpAEAERYKLERLAEAEKSQLIMQAEAEAAS 262
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-----AEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462495374 263 VRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEI 315
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
109-310 |
6.19e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 109 HSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQ 188
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 189 VAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLE-RLAEAEKSQLIMQAEAEAASVRMRG 267
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEeEEALEEAAEEEAELEEEEEALLELL 465
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462495374 268 EAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQ 310
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
123-295 |
2.03e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 123 ARIGEAEAKRDAGIREAKAKqekvsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRaqADLAYQLQVAKTKQQIEEQRVQ 202
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-----AEAIKKEALLEAKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 203 vQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYKLERLA-----EAeKSQLIMQAEAEA---ASVRMRgeaea 271
Cdd:PRK12704 104 -LLEKREEELEKKEKELEQKQQELEKKeeeLEELIEEQLQELERISgltaeEA-KEILLEKVEEEArheAAVLIK----- 176
|
170 180
....*....|....*....|....*.
gi 2462495374 272 fAIGARARAEAEQMAKK--AEAFQLY 295
Cdd:PRK12704 177 -EIEEEAKEEADKKAKEilAQAIQRC 201
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
113-307 |
6.34e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 113 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAqylseiEMAKAqrdyELKKAAYDIEVNTRRAQADlayQLQVAKT 192
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA------EAAKA----EAEAAADEAEAAEEKAEAA---EKKKEEA 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 193 KQQIEEQRVQVQVVERAQQVAVQEQEIARREKELE--ARVRKPAEAERYKLERLAEAEksQLIMQAEAEAASVRMRGEAE 270
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKAD--EAKKKAEEAKKADEAKKKAE 1454
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462495374 271 AFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEK 307
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
|
| Flot |
pfam15975 |
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ... |
257-342 |
8.01e-05 |
|
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: 41.92 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 257 EAEAASVRMRGEAEAfaIGARARAEAEQMAKKAEAFQLY---QEAAQLDM-LLEKLPQVAEEISGPLTSANKITLVSSGS 332
Cdd:pfam15975 1 EAEAEADAIKLRAEA--KRKKALAEAEGIRALNEAENALsdeQIALQVKLaLLEALPEIIAESVKPLEKIDGIKILQVDG 78
|
90
....*....|
gi 2462495374 333 GTMGAAKVTG 342
Cdd:pfam15975 79 LGGGAAGGGG 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-315 |
1.10e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 103 DDQDYLHSLGKARTAQVQKDARIGEA-----EAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTR 177
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 178 RAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKElEAR----VRKPAEAERYKLERLAEAEKSQLI 253
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-EAKkaeeLKKKEAEEKKKAEELKKAEEENKI 1730
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462495374 254 MQAEAEAASVRMRGEAEafaigaRARAEAEQmAKKAEAFQLYQEAAQLDMLLEKLPQVAEEI 315
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAE------EAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
188-294 |
3.89e-04 |
|
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: 41.90 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 188 QVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEArvRKPAEaeryklerLAEAEKSQLIMQAEAEAASVRMrg 267
Cdd:cd03406 163 AIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEA--EKDAE--------VAKIQMQQKIMEKEAEKKISEI-- 230
|
90 100
....*....|....*....|....*....
gi 2462495374 268 EAEAFAIGARARAEAE--QMAKKAEAFQL 294
Cdd:cd03406 231 EDEMHLAREKARADAEyyRALREAEANKL 259
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
191-252 |
4.73e-04 |
|
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: 41.51 E-value: 4.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462495374 191 KTKQQIEEQRV-QVQVVERAQQVAvqEQEIARREKELE-----ARVRKPAEAERYKLERLAEAEKSQL 252
Cdd:cd03406 196 RKRAVIEAEKDaEVAKIQMQQKIM--EKEAEKKISEIEdemhlAREKARADAEYYRALREAEANKLKL 261
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
113-304 |
5.57e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 113 KARTAQVQKDARIGEAEAKRDagirEAKAKQEKVSAQYLSEIEMAK----AQRDYELKKAAYDIEVNTRRAQADLAYQLQ 188
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAAD----EAEAAEEKAEAAEKKKEEAKKkadaAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 189 VAKTKQQIEEQRVQVQVVERAQQVAVQEQEiARREKELearvRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGE 268
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEE-AKKADEA----KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462495374 269 AEAFAIGARARAE----AEQMAKKAEAFQLYQEAAQLDML 304
Cdd:PTZ00121 1488 AKKKAEEAKKKADeakkAAEAKKKADEAKKAEEAKKADEA 1527
|
|
| SPFH_like |
cd02106 |
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
49-105 |
7.82e-04 |
|
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: 38.88 E-value: 7.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495374 49 ETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQ 105
Cdd:cd02106 54 RKIADVLRAAIGRMTLDQIISGRDEIAKAVKEDLEEDLENFGVVISDVDITSIEPPD 110
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
115-305 |
8.77e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 115 RTAQVQKDARIGEAEAKRDAGIREAKAKQEK-VSAQYLSEIEMAKAQRDYELKKA---AYDIEVNTRRAQADLAYQLQVA 190
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQaAEQERLKQLEKERLAAQEQKKQAeeaAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 191 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERY---KLERLAEAEKSQLIMQAEAEAASVRMRG 267
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKaaaEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462495374 268 EAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLL 305
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| SPFH_prohibitin |
cd03401 |
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
56-134 |
9.68e-04 |
|
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.
Pssm-ID: 259799 [Multi-domain] Cd Length: 195 Bit Score: 39.80 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 56 RAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHS----------LGKAR----TAQVQK 121
Cdd:cd03401 102 KAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAieakqvaeqeAERAKfeleKAEQEA 181
|
90
....*....|...
gi 2462495374 122 DARIGEAEAKRDA 134
Cdd:cd03401 182 ERKVIEAEGEAEA 194
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
98-324 |
1.80e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 98 LKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIR--EAKAKQEKVSAQYLSEIEMAKAQRDyelkkaAYDIEVN 175
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKaeDARKAEEARKAEDARKAEEARKAED------AKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 176 TRRAQADLAYQLQVAKTKQQIEEQRVQVQVvERAQQVAVQEQ----EIARREKElearVRKPAEAERYKLERLAEAEKSQ 251
Cdd:PTZ00121 1158 RKAEDARKAEEARKAEDAKKAEAARKAEEV-RKAEELRKAEDarkaEAARKAEE----ERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 252 LIMQAEAEAA----SVRMRGEAEAF-------------AIGARARAEAEQMAK-----KAEAFQLYQEAAQLDMLLEK-- 307
Cdd:PTZ00121 1233 EEAKKDAEEAkkaeEERNNEEIRKFeearmahfarrqaAIKAEEARKADELKKaeekkKADEAKKAEEKKKADEAKKKae 1312
|
250 260
....*....|....*....|....
gi 2462495374 308 -------LPQVAEEISGPLTSANK 324
Cdd:PTZ00121 1313 eakkadeAKKKAEEAKKKADAAKK 1336
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
127-315 |
1.88e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 127 EAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDyELKKAAydievntrraQADLAYQLQVAKTKQQIEEQRvQVQVV 206
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAE----------EAKKADEAKKAEEAKKADEAK-KAEEK 1545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 207 ERAQQVavQEQEIARREKElearVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMA 286
Cdd:PTZ00121 1546 KKADEL--KKAEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
170 180
....*....|....*....|....*....
gi 2462495374 287 KKAEAFQLYQEAAQLDMLLEKlpQVAEEI 315
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKK--KEAEEK 1646
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
137-306 |
2.35e-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: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 137 REAKAKQEKVSAQYLseiemAKAQRDYELKKAAYDIEVNTRRAQADLAyQLQVAKTKQQIEEQRVQVQVVE-RAQQVAVQ 215
Cdd:COG1196 216 RELKEELKELEAELL-----LLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELElELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 216 EQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLY 295
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170
....*....|.
gi 2462495374 296 QEAAQLDMLLE 306
Cdd:COG1196 370 AEAELAEAEEE 380
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
138-246 |
2.84e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 138 EAKAKQEKVSAQYLSEIEMAKAQRDyELKKAAYDIEVNTRRAQADLAYQLQVAK----------TKQQIEEQRVQVQVVE 207
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQ-QLEQLQARIQRLAARAPAWLAAQDALARlreqsgeefeDSQDVTEYMQQLLERE 640
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2462495374 208 RAQQvaVQEQEIARREKELEARVRK---PAEAERYKLERLAE 246
Cdd:PRK04863 641 RELT--VERDELAARKQALDEEIERlsqPGGSEDPRLNALAE 680
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
141-316 |
3.21e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 141 AKQEKVSAQYLsEIEMAKAQRDYELKKAAYDiEVNTRRAQADLAYQLQVAKTKQQIEEQR-VQVQVVERAQQVAVQEQEI 219
Cdd:COG1196 206 ERQAEKAERYR-ELKEELKELEAELLLLKLR-ELEAELEELEAELEELEAELEELEAELAeLEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 220 AR---REKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAfQLYQ 296
Cdd:COG1196 284 EEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA-ELAE 362
|
170 180
....*....|....*....|
gi 2462495374 297 EAAQLDMLLEKLPQVAEEIS 316
Cdd:COG1196 363 AEEALLEAEAELAEAEEELE 382
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
19-257 |
4.10e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.44 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 19 KIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTL 98
Cdd:pfam12128 619 KQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKH 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 99 KDIHDDQDylhslGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRR 178
Cdd:pfam12128 699 QAWLEEQK-----EQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKL 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 179 AQ--ADLAYQL-QVAKTKQQIEEQRV--QVQVVERAQQVAVQEQEIARREKELE---ARVRKPAEAERYKLERLAEAEKS 250
Cdd:pfam12128 774 KReiRTLERKIeRIAVRRQEVLRYFDwyQETWLQRRPRLATQLSNIERAISELQqqlARLIADTKLRRAKLEMERKASEK 853
|
....*..
gi 2462495374 251 QLIMQAE 257
Cdd:pfam12128 854 QQVRLSE 860
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-314 |
4.47e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 111 LGKARTAQVQKDARigEAEAKRDAgiREAKAKQEKVSAQylseiEMAKAQrdyELKKAAYDIEV-NTRRAQADLAYQLQV 189
Cdd:PTZ00121 1515 AKKAEEAKKADEAK--KAEEAKKA--DEAKKAEEKKKAD-----ELKKAE---ELKKAEEKKKAeEAKKAEEDKNMALRK 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 190 AKTKQQIEEQRVQV-------QVVERAQQVAVQEQEIARRE---KELEAR-----VRKPAEAERYKLERLAEAEKSQLIM 254
Cdd:PTZ00121 1583 AEEAKKAEEARIEEvmklyeeEKKMKAEEAKKAEEAKIKAEelkKAEEEKkkveqLKKKEAEEKKKAEELKKAEEENKIK 1662
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462495374 255 QA-------EAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEafQLYQEAAQLDMLLEKLPQVAEE 314
Cdd:PTZ00121 1663 AAeeakkaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE--ELKKKEAEEKKKAEELKKAEEE 1727
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
113-300 |
4.56e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 39.04 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 113 KARTAQVQKDARI--GEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAaydievntrRAQADlayqlqVA 190
Cdd:NF041483 432 RAKTVELQEEARRlrGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKA---------KADAD------EL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 191 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAE---------AERYKLERLAEAEKSQLIMQAEAEAA 261
Cdd:NF041483 497 RSTATAESERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEeqaeevraaAERAARELREETERAIAARQAEAAEE 576
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462495374 262 SVRMRGEAEAFAIGAR-----ARAEAEQMAKKA--EAFQLYQEAAQ 300
Cdd:NF041483 577 LTRLHTEAEERLTAAEealadARAEAERIRREAaeETERLRTEAAE 622
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-315 |
5.92e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 127 EAEAKRDA--GIRE-----AKAKQEKVSAQYL-SEIEMAKAQRDYELKKAAYDievNTRRAQADLayQLQVAKTKQQIEE 198
Cdd:COG4913 246 DAREQIELlePIRElaeryAAARERLAELEYLrAALRLWFAQRRLELLEAELE---ELRAELARL--EAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 199 QRVQVQVVERA------QQVAVQEQEIARREKELEARVRKpaeAERYKlERLAEAEksqliMQAEAEAAS-VRMRGEAEA 271
Cdd:COG4913 321 LREELDELEAQirgnggDRLEQLEREIERLERELEERERR---RARLE-ALLAALG-----LPLPASAEEfAALRAEAAA 391
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462495374 272 FAigarARAEAEQMAKKAEAFQLYQEAAQLDmllEKLPQVAEEI 315
Cdd:COG4913 392 LL----EALEEELEALEEALAEAEAALRDLR---RELRELEAEI 428
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
111-273 |
6.35e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.21 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 111 LGKARTAQVQKDARIGEAEAKRDAgIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRR---------AQA 181
Cdd:COG4942 71 IRALEQELAALEAELAELEKEIAE-LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRlqylkylapARR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 182 DLAYQLQ-----VAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKE-LEARVRKPAEAERYKLERLAEAEKS--QLI 253
Cdd:COG4942 150 EQAEELRadlaeLAALRAELEAERAELEALLAELEEERAALEALKAERQkLLARLEKELAELAAELAELQQEAEEleALI 229
|
170 180
....*....|....*....|
gi 2462495374 254 MQAEAEAASVRMRGEAEAFA 273
Cdd:COG4942 230 ARLEAEAAAAAERTPAAGFA 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
115-315 |
6.42e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 115 RTAQVQKDARIGEAEAKRDA----GIREAKAKQEKVSAQYLSEIEMAKaqRDYELKKAAYDIEVNTRRAQADLAYQLQVA 190
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAeeerKAEEARKAEDAKKAEAVKKAEEAK--KDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 191 KTKQQIE-EQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEA 269
Cdd:PTZ00121 1267 RRQAAIKaEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462495374 270 EAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMllEKLPQVAEEI 315
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA--DAAKKKAEEK 1390
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
113-290 |
7.24e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 113 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAaydiEVNTRRAQADLAYQLQVAKT 192
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA----DELKKAEEKKKADEAKKAEE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 193 KQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARV---RKPAEAERYKLERLA-EAEKSQLIMQAeAEAASVRMRGE 268
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAeeaKKAAEAAKAEAEAAAdEAEAAEEKAEA-AEKKKEEAKKK 1379
|
170 180
....*....|....*....|..
gi 2462495374 269 AEAFAIGARARAEAEQMAKKAE 290
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAE 1401
|
|
| SPFH_HflK |
cd03404 |
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ... |
234-311 |
8.44e-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: 37.49 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 234 AEAERYKLErlAEAEKSQLIMQAEAEAAsvRMRGEAEAFA--IGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQV 311
Cdd:cd03404 184 QDKERLINE--AQAYANEVIPRARGEAA--RIIQEAEAYKaeVVARAEGDAARFLALLAEYRKAPEVTRERLYLETMEEV 259
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
141-353 |
8.53e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 38.11 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 141 AKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIE--------VNTRRAQADLAY-QLQVAKTKQQIEEqrvqvqvVERAQQ 211
Cdd:PRK10929 125 AQQEQDRAREISDSLSQLPQQQTEARRQLNEIErrlqtlgtPNTPLAQAQLTAlQAESAALKALVDE-------LELAQL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462495374 212 VAVQEQEIARREKELearvrkpAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEA 291
Cdd:PRK10929 198 SANNRQELARLRSEL-------AKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINREL 270
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462495374 292 FQ-LYQEAAQLDMLLEKLPQVAEEIsgpLTSANKITLVSSGSGTMGAAKVTGEVL-DILTRLPE 353
Cdd:PRK10929 271 SQaLNQQAQRMDLIASQQRQAASQT---LQVRQALNTLREQSQWLGVSNALGEALrAQVARLPE 331
|
|
| |
