|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1-418 |
3.64e-92 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 284.84 E-value: 3.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 1 MFFTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVK-SEKVYTRHGVPISVTGIAQVKIQGqNKE 79
Cdd:COG2268 27 FYRKVPPNEALVITGRGGGYKV-VTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYVKVNS-DPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 80 MLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQD 159
Cdd:COG2268 105 DIANAAERFLGRDPEEIEELAEEKLEGALRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 160 YLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIE-----MAKAQRDYELKKATYDIEVNTRRAQA 234
Cdd:COG2268 185 YLDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 235 DLAYQLQVAKTKQQIEeqrVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRlerlaeaekaqlimqAEAEAe 314
Cdd:COG2268 265 EAAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA---------------AEAEA- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 315 svrmrgEAEAFAIGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVt 394
Cdd:COG2268 326 ------EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA- 398
|
410 420
....*....|....*....|....
gi 6679809 395 geVLDILSRLPESVERLTGVSISQ 418
Cdd:COG2268 399 --VAEALAPLLESLLEETGLDLPG 420
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
30-175 |
1.32e-64 |
|
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: 203.89 E-value: 1.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 30 FVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQR 109
Cdd:cd03399 1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQVKV-GSDPEEIAAAAERFLGKSTEEIRELVKETLEGHLR 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6679809 110 AIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKD 175
Cdd:cd03399 80 AIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
3-185 |
6.33e-21 |
|
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: 89.30 E-value: 6.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 3 FTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLA 82
Cdd:pfam01145 1 IIVPPGEVGVVTRFGKLSRV-LEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVNPDDPPKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 83 AACqmflgKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLH 162
Cdd:pfam01145 80 QNV-----FGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAE 154
|
170 180
....*....|....*....|...
gi 6679809 163 SLGKARTAQVQKDARIGEAEAKR 185
Cdd:pfam01145 155 AIEAKQTAEQEAEAEIARAEAEA 177
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
84-266 |
1.56e-17 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 79.24 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 84 ACQMFLGKTEAEIAHIALETLEghqRAIMAHMTVEEIYKDRQKfseqVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHS 163
Cdd:smart00244 1 AAIKVVGEGERGVVERLGRVLR---VLGPGLHFLIPFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 164 LGKARTAQVQKDARIGEAEAKRDAGIREAKAKqekvsaqclseIEMAKAQRDYELKKATYDIEVNTRRAQAdLAYQLQVA 243
Cdd:smart00244 74 LDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK-----------RTLDELLTDQREKISENIREELNEAAEA-WGIKVEDV 141
|
170 180
....*....|....*....|...
gi 6679809 244 KTKQqieeQRVQVQVVERAQQVA 266
Cdd:smart00244 142 EIKD----IRLPEEIKEAMEAQQ 160
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
27-234 |
1.70e-13 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 70.25 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKemlaaacqmFLGKTEAEIAHIAlETLEG 106
Cdd:COG0330 45 GLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQYRITDPAK---------FLYNVENAEEALR-QLAES 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 107 HQRAIMAHMTVEEIYK-DRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKR 185
Cdd:COG0330 115 ALREVIGKMTLDEVLStGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYR 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6679809 186 DAGIREAKAKQEKVsaqclseIEMAKAQRDYELKKATYDIEVNTRRAQA 234
Cdd:COG0330 195 EAAIIRAEGEAQRA-------IIEAEAYREAQILRAEGEAEAFRIVAEA 236
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
1-154 |
2.88e-11 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 61.52 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 1 MFFTCGPNEAMVVSGFCRSPPVMVAGGrVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQnkem 80
Cdd:smart00244 2 AIKVVGEGERGVVERLGRVLRVLGPGL-HFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDP---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679809 81 LAAACQMfLGKTEAEIAHIALETLeghqRAIMAHMTVEEIYKD-RQKFSEQVFKVASSDLVNMGISVVSYTLKDI 154
Cdd:smart00244 77 LRAVYRV-LDADYAVIEQLAQTTL----RSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDI 146
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
227-388 |
6.32e-10 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 59.85 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 227 VNTRRAQ--ADLAYQLQVAKTKQQIEEQRVQVQVVERAQQV--AVQEQEIARREKElearvrkpaeaeryRLERLAEAEK 302
Cdd:COG0330 129 LSTGRDEinAEIREELQEALDPYGIEVVDVEIKDIDPPEEVqdAMEDRMKAERERE--------------AAILEAEGYR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 303 AQLIMQAEAEAESVRMRGEAEAFAIGARARAEAEQMAKKAEAFQMYQEAAQLdMLLEKLPQVAEeisgpltSANKITLVS 382
Cdd:COG0330 195 EAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFY-RSLEALEEVLS-------PNSKVIVLP 266
|
....*.
gi 6679809 383 SGSGTM 388
Cdd:COG0330 267 PDGNGF 272
|
|
| SPFH_like |
cd02106 |
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
47-158 |
1.99e-09 |
|
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: 54.68 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 47 TLNVKSEKVYTRHGVPISVTGIAQVKIQgqnKEMLAAACQMFLGKTEAEiAHIaLETLEGHQRAIMAHMTVEEIYKDRQK 126
Cdd:cd02106 4 FDDVRVEPVGTADGVPVAVDLVVQFRIT---DYNALPAFYLVDFVKDIK-ADI-RRKIADVLRAAIGRMTLDQIISGRDE 78
|
90 100 110
....*....|....*....|....*....|..
gi 6679809 127 FSEQVFKVASSDLVNMGISVVSYTLKDIHDDQ 158
Cdd:cd02106 79 IAKAVKEDLEEDLENFGVVISDVDITSIEPPD 110
|
|
| SPFH_SLP-4 |
cd13435 |
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ... |
14-206 |
1.39e-07 |
|
Slipin-4 (SLP-4), 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 arthropods. 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 divergent slipin subgroup remain largely uncharacterized. It contains Drosophila Mec2, the gene for which was identified in a screen for genes required for nephrocyte function; it may function together with Sns in maintaining nephrocyte diaphragm.
Pssm-ID: 259813 [Multi-domain] Cd Length: 208 Bit Score: 51.62 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 14 SGFCRSPpvmvagGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqgqnKEMLAAACQMFLGKTE 93
Cdd:cd13435 1 SGGARGP------GVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRI----SDPLNAVIQVANYSHS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 94 AEIahIALETLeghqRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIhddqDYLHSLGKARTAqvq 173
Cdd:cd13435 71 TRL--LAATTL----RNVLGTRNLSELLTERETISHSMQVTLDEATDPWGVQVERVEIKDV----SLPDSLQRAMAA--- 137
|
170 180 190
....*....|....*....|....*....|...
gi 6679809 174 kdarigEAEAKRDAGIREAKAKQEKVSAQCLSE 206
Cdd:cd13435 138 ------EAEAAREARAKVIAAEGEMKSSRALKE 164
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
176-348 |
7.59e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 176 ARIGEAEAKRDAGIREAKAKQEKVSAQCLSEiemakAQRDYELKKATYDIEVNTRRaqADLAYQLQVAKTKQQIEEQRVQ 255
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLE-----AKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 256 vQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYRLERLA-----EAeKAQLI--MQAEAEAESVRMRGEAEaf 325
Cdd:PRK12704 104 -LLEKREEELEKKEKELEQKQQELEKKeeeLEELIEEQLQELERISgltaeEA-KEILLekVEEEARHEAAVLIKEIE-- 179
|
170 180
....*....|....*....|....*
gi 6679809 326 aigARARAEAEQMAKK--AEAFQMY 348
Cdd:PRK12704 180 ---EEAKEEADKKAKEilAQAIQRC 201
|
|
| Flot |
pfam15975 |
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ... |
310-395 |
1.05e-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: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 310 EAEAESVRMRGEAEafAIGARARAEAEQMAKKAEAFQMY---QEAAQLDM-LLEKLPQVAEEISGPLTSANKITLVSSGS 385
Cdd:pfam15975 1 EAEAEADAIKLRAE--AKRKKALAEAEGIRALNEAENALsdeQIALQVKLaLLEALPEIIAESVKPLEKIDGIKILQVDG 78
|
90
....*....|
gi 6679809 386 GTMGAAKVTG 395
Cdd:pfam15975 79 LGGGAAGGGG 88
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-369 |
1.23e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 166 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQcLSEIEMAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKT 245
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYEL-LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 246 KQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRL-ERLAEAEKAQLIMQAEAEAESVRMRGEAEA 324
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELaEELLEALRAAAELAAQLEELEEAEEALLER 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6679809 325 FAIGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEEIS 369
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
158-363 |
2.05e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 158 QDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDyelkkatydiEVNTRRAQADLA 237
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE----------AEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 238 YQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRLE-RLAEAEKAQLIMQAEAEAESV 316
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEeEEALEEAAEEEAELEEEEEAL 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6679809 317 RMRGEAEAFAIGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQ 363
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
154-367 |
4.17e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 154 IHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAgiREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVNTRRAQ 233
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAE--LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 234 ADLAyQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRLERLAEAEKAQLIMQAEAEA 313
Cdd:COG1196 309 ERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6679809 314 ESVRMRGEAEAFAIGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEE 367
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
166-367 |
8.01e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 166 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAqclseiEMAKAqrdyELKKATYDIEVNTRRAQADlayQLQVAKT 245
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA------EAAKA----EAEAAADEAEAAEEKAEAA---EKKKEEA 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 246 KQQIEEQRVQVQVVERAQQVAVQEQEIARREKELE--ARVRKPAEAERYRLERLAEAEKAQliMQAEAEAESVRMRGEAE 323
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAK--KKAEEAKKADEAKKKAE 1454
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6679809 324 AFAIGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKlpqvAEE 367
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK----AEE 1494
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
166-353 |
1.11e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.90 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 166 KARTAQVQKDARI--GEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKAtydievntrRAQADlayqlqVA 243
Cdd:NF041483 432 RAKTVELQEEARRlrGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKA---------KADAD------EL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 244 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAE---------AERYRLERLAEAEKAQLIMQAEAEAE 314
Cdd:NF041483 497 RSTATAESERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEeqaeevraaAERAARELREETERAIAARQAEAAEE 576
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6679809 315 SVRMRGEAEAFAIGAR-----ARAEAEQMAKKA--EAFQMYQEAAQ 353
Cdd:NF041483 577 LTRLHTEAEERLTAAEealadARAEAERIRREAaeETERLRTEAAE 622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
168-368 |
1.53e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 168 RTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDyELKKATydiEVNTRRAQADLAYQLQVAKTKQ 247
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAE---EEKKKVEQLKKKEAEEKKKAEE 1651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 248 -QIEEQRVQVqvveRAQQVAVQEQEIARREKEL---EARVRKPAEAERYRLErlaEAEKAQLIMQAEAE----AESVRmR 319
Cdd:PTZ00121 1652 lKKAEEENKI----KAAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKKEAE---EAKKAEELKKKEAEekkkAEELK-K 1723
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6679809 320 GEAEAFAIGARARAEAEQMAKKAEAFQMYQ-EAAQLDMLLEKLPQVAEEI 368
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEEAKKDEeEKKKIAHLKKEEEKKAEEI 1773
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
166-357 |
1.64e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 166 KARTAQVQKDARIGEAEAKRDagirEAKAKQEKVSAQCLSEIEmAKAQRDYELKKA--TYDIEVNTRRAQADLAYQLQVA 243
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAAD----EAEAAEEKAEAAEKKKEE-AKKKADAAKKKAeeKKKADEAKKKAEEDKKKADELK 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 244 KT---KQQIEEQRVQVQVVERAQQVAVQEQEiARREKELearvRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRG 320
Cdd:PTZ00121 1412 KAaaaKKKADEAKKKAEEKKKADEAKKKAEE-AKKADEA----KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6679809 321 EAEAFAIGARARAE----AEQMAKKAEAFQMYQEAAQLDML 357
Cdd:PTZ00121 1487 EAKKKAEEAKKKADeakkAAEAKKKADEAKKAEEAKKADEA 1527
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
164-367 |
1.93e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 164 LGKARTAQVQKDARigEAEAKRDAgiREAKAKQEKVSAQCLSEIEMAKAQ---RDYELKKATYDIEVNTRRAQADLAYQL 240
Cdd:PTZ00121 1527 AKKAEEAKKADEAK--KAEEKKKA--DELKKAEELKKAEEKKKAEEAKKAeedKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 241 QVAKTK----QQIEEQRVQVQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYRLERLAEAEKAQLIMQAEAEA 313
Cdd:PTZ00121 1603 EEKKMKaeeaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6679809 314 ESVRMRGEAEAFAIGARARAEAEQMAKKAE-----AFQMYQEAAQLDMLLEKLPQVAEE 367
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAeekkkAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
166-353 |
2.16e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 166 KARTAQVQKDARIGEaEAKRDAGIR---EAKAKQEKVSAQCLSEIEMAK----AQRDYELKKATydievNTRRAQADLAY 238
Cdd:PTZ00121 1135 KAEDARKAEEARKAE-DAKRVEIARkaeDARKAEEARKAEDAKKAEAARkaeeVRKAEELRKAE-----DARKAEAARKA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 239 Q-LQVAKTKQQIEEQRvQVQVVERAQQVAVQEQEIARREKE-LEARVRKPAEAERYRLERLA------EAEKAQLIMQAE 310
Cdd:PTZ00121 1209 EeERKAEEARKAEDAK-KAEAVKKAEEAKKDAEEAKKAEEErNNEEIRKFEEARMAHFARRQaaikaeEARKADELKKAE 1287
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6679809 311 A--------EAESVRMRGEAEAFAIGAR----ARAEAEQMAKKAEAFQMYQEAAQ 353
Cdd:PTZ00121 1288 EkkkadeakKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKKKADAAKKKAEEAK 1342
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
167-352 |
3.59e-05 |
|
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: 45.61 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 167 ARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATydievntRRAQADLAYQLQVAKTK 246
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE-------QAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 247 QQIEEQRVQVQVVERAQQVAvqeqEIARREKELEARVRKPAEAERYRLERLAEAEKAQlimQAEAEAESVRMRGEAEAFA 326
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAK----EEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEA---KAKAEAEAKAKAEEAKAKA 198
|
170 180
....*....|....*....|....*.
gi 6679809 327 IGARARAEAEQmAKKAEAFQMYQEAA 352
Cdd:TIGR02794 199 EAAKAKAAAEA-AAKAEAEAAAAAAA 223
|
|
| SPFH_stomatin |
cd03403 |
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ... |
27-206 |
4.90e-05 |
|
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; Stomatin (or band 7) is widely expressed and, highly expressed in red blood cells. It localizes predominantly to the plasma membrane and to intracellular vesicles of the endocytic pathway, where it is present in higher order homo-oligomeric complexes (of between 9 and 12 monomers). Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and, is implicated in trafficking of Glut1 glucose transporters. This subgroup found in animals, also contains proteins similar to Caenorhabditis elegans MEC-2. MEC-2 interacts with MEC-4, which is part of the degenerin channel complex required for response to gentle body touch.
Pssm-ID: 259801 [Multi-domain] Cd Length: 202 Bit Score: 44.08 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqgQNKEMLAAACQMFLGKTEAeiahIALETLeg 106
Cdd:cd03403 8 GLFFILPCIDSYRKVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRV--QNATIAVTNVENADRSTRL----LAQTTL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 107 hqRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHddqdylhslgkaRTAQVQKdARIGEAEAKRD 186
Cdd:cd03403 80 --RNVLGTKNLSEILSDRETISHQMQSTLDEATDPWGVKVERVEIKDVR------------LPVQLQR-AMAAEAEAARE 144
|
170 180
....*....|....*....|
gi 6679809 187 AGIREAKAKQEKVSAQCLSE 206
Cdd:cd03403 145 ARAKVIAAEGEQNASRALKE 164
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
166-340 |
5.32e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 166 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAqclseiEMAKAQRDYELKKATydIEVNTRRAQAdlayqlqvAKT 245
Cdd:PRK05035 531 RARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQA------ANAEAEEEVDPKKAA--VAAAIARAKA--------KKA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 246 KQQIEEQRVQVQVVERAQQVAVQEQEIARRE--KELEARVRKPAEAERYRLERL------AEAEKAQLIMQAEAEAESVR 317
Cdd:PRK05035 595 AQQAASAEPEEQVAEVDPKKAAVAAAIARAKakKAEQQANAEPEEPVDPRKAAVaaaiarAKARKAAQQQANAEPEEAED 674
|
170 180
....*....|....*....|...
gi 6679809 318 MRGEAEAFAIgarARAEAEQMAK 340
Cdd:PRK05035 675 PKKAAVAAAI---ARAKAKKAAQ 694
|
|
| SPFH_prohibitin |
cd03401 |
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ... |
2-187 |
6.64e-05 |
|
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: 43.66 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 2 FFTCGPNEAMVVSGFCRSPPVMVAG-GRVFVLPCIQQIQRISLNTLTLNVKSEkVYTRHGVPISVTGIAQVKIqgqNKEM 80
Cdd:cd03401 1 FYTVDAGEVGVVFRRGKGVKDEVLGeGLHFKIPWIQVVIIYDVRTQPREITLT-VLSKDGQTVNIDLSVLYRP---DPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 81 LAaacQMF--LGKTEAE--IAHIALETLeghqRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHD 156
Cdd:cd03401 77 LP---ELYqnLGPDYEErvLPPIVREVL----KAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDF 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6679809 157 DQDYLHS----------LGKAR----TAQVQKDARIGEAEAKRDA 187
Cdd:cd03401 150 PDEYEKAieakqvaeqeAERAKfeleKAEQEAERKVIEAEGEAEA 194
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
166-351 |
7.07e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 166 KARTAQVQKDARIGEAEAKRDAGirEAKAKQEKVSAQCLSEIEmAKAQRDyELKKATYDIEVNTRRAQADLAYQLQVAKT 245
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAA--EAAKAEAEAAADEAEAAE-EKAEAA-EKKKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 246 KQqiEEQRVQVQVVERAQQVAVQEQEIARR--EKELEARVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAE 323
Cdd:PTZ00121 1399 KA--EEDKKKADELKKAAAAKKKADEAKKKaeEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
170 180 190
....*....|....*....|....*....|..
gi 6679809 324 AFAIGAR----ARAEAEQMAKKAEAFQMYQEA 351
Cdd:PTZ00121 1477 KKAEEAKkadeAKKKAEEAKKKADEAKKAAEA 1508
|
|
| SPFH_eoslipins_u1 |
cd08826 |
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ... |
33-194 |
7.29e-05 |
|
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria 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. This subgroup contains PH1511 from the hyperthermophilic archaeon Pyrococcus horikoshi.
Pssm-ID: 259808 [Multi-domain] Cd Length: 178 Bit Score: 43.27 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 33 PCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFlgkteaEIAHIALETLeghqRAIM 112
Cdd:cd08826 1 PFIDRMVRVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRY------ATSQLAQTTL----RSVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 113 AHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREA 192
Cdd:cd08826 71 GQVELDELLSEREEINKRIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAAEKLA 150
|
..
gi 6679809 193 KA 194
Cdd:cd08826 151 EA 152
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
191-299 |
8.46e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 191 EAKAKQEKVSAQCLSEIEMAKAQRDyELKKATYDIEVNTRRAQADLAYQLQVAK----------TKQQIEEQRVQVQVVE 260
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQ-QLEQLQARIQRLAARAPAWLAAQDALARlreqsgeefeDSQDVTEYMQQLLERE 640
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 6679809 261 RAQQvaVQEQEIARREKELEARVRK---PAEAERYRLERLAE 299
Cdd:PRK04863 641 RELT--VERDELAARKQALDEEIERlsqPGGSEDPRLNALAE 680
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
243-353 |
1.17e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 243 AKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRleRLAEAEKAQLIMQAEAEAESVRMRGEA 322
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAA--KQAALKQKQAEEAAAKAAAAAKAKAEA 151
|
90 100 110
....*....|....*....|....*....|.
gi 6679809 323 EAFAIGARARAEAEQMAKKAEAFQMYQEAAQ 353
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
241-344 |
1.33e-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: 43.44 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 241 QVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEArvRKPAEaeryrlerLAEAEKAQLIMqaEAEAESVRMRG 320
Cdd:cd03406 163 AIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEA--EKDAE--------VAKIQMQQKIM--EKEAEKKISEI 230
|
90 100
....*....|....*....|....*.
gi 6679809 321 EAEAFAIGARARAEAE--QMAKKAEA 344
Cdd:cd03406 231 EDEMHLAREKARADAEyyRALREAEA 256
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
173-378 |
1.34e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 173 QKDARI-GEAEAKRDAGIREaKAKQEKVSAQCLSEIEMAKAQ---RDYELKKATYDIEVNTRRA-QADLAYQLQVAKTKQ 247
Cdd:pfam17380 389 QKNERVrQELEAARKVKILE-EERQRKIQQQKVEMEQIRAEQeeaRQREVRRLEEERAREMERVrLEEQERQQQVERLRQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 248 QIEEQRVQVQVVERAQQVAVQEQEIARR--EKELEARVRKPAEAERYR--LER-LAEAEKAQLIMQAEAEAESVRmRGEA 322
Cdd:pfam17380 468 QEEERKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRklLEKeMEERQKAIYEEERRREAEEER-RKQQ 546
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6679809 323 EafaIGARARAEaEQMAKKAEAFQ----MYQEAAQLDMLLEKLPQVAE-EISGPLTSANKI 378
Cdd:pfam17380 547 E---MEERRRIQ-EQMRKATEERSrleaMEREREMMRQIVESEKARAEyEATTPITTIKPI 603
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
244-305 |
1.62e-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: 43.44 E-value: 1.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6679809 244 KTKQQIEEQRV-QVQVVERAQQVAvqEQEIARREKELE-----ARVRKPAEAERYRLERLAEAEKAQL 305
Cdd:cd03406 196 RKRAVIEAEKDaEVAKIQMQQKIM--EKEAEKKISEIEdemhlAREKARADAEYYRALREAEANKLKL 261
|
|
| SPFH_podocin |
cd08827 |
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ... |
27-200 |
2.97e-04 |
|
Podocin, 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 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. Podocin is expressed in the kidney and mutations in the gene have been linked to familial idiopathic nephrotic syndrome. Podocin interacts with the TRP ion channel TRPV-6 and may function as a scaffolding protein in the organization of lipid-protein domains.
Pssm-ID: 259809 [Multi-domain] Cd Length: 223 Bit Score: 42.18 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGqnkemlaaACQMFlgKTEAEIAHIALETLEG 106
Cdd:cd08827 30 GLFFYLPCLDVCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIEN--------ASVCL--SSFASISDAMQALVQT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 107 HQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRD 186
Cdd:cd08827 100 TVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAEAQRQAKVKVIAAEGEKA 179
|
170
....*....|....
gi 6679809 187 AGiREAKAKQEKVS 200
Cdd:cd08827 180 AS-EALKAAAESLS 192
|
|
| SPFH_SLP-3 |
cd08828 |
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ... |
27-197 |
3.16e-04 |
|
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: 41.17 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQgqnkemlAAACQMflgkTEAEIAHIALETL-E 105
Cdd:cd08828 4 GLILVLPCTDTFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQ-------SAVKAV----ANVNNVHIATFLLaQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 106 GHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIhddqdylhslgkaRTAQVQKDARIGEAEAKR 185
Cdd:cd08828 73 TTLRNVLGTQTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDV-------------RIPVQMQRAMAAEAEATR 139
|
170
....*....|..
gi 6679809 186 DAGIREAKAKQE 197
Cdd:cd08828 140 EARAKVVAAEGE 151
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
166-341 |
4.46e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 166 KARTAQVQKDARIgEAEAKRDAGIR----------EAKAKQEKVSAQCLSeIEMAKAQrdyELKKATYDIEVNTRRAQAD 235
Cdd:pfam17380 323 KARQAEMDRQAAI-YAEQERMAMERerelerirqeERKRELERIRQEEIA-MEISRMR---ELERLQMERQQKNERVRQE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 236 L----AYQLQVAKTKQQIEEQRVQVQVVeRAQQVAVQEQEIARREKEleaRVRkpaEAERYRLERLAEAEKAQLIMQAEA 311
Cdd:pfam17380 398 LeaarKVKILEEERQRKIQQQKVEMEQI-RAEQEEARQREVRRLEEE---RAR---EMERVRLEEQERQQQVERLRQQEE 470
|
170 180 190
....*....|....*....|....*....|
gi 6679809 312 EAESVRMRGEAEafaigARARAEAEQMAKK 341
Cdd:pfam17380 471 ERKRKKLELEKE-----KRDRKRAEEQRRK 495
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
69-310 |
5.59e-04 |
|
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: 42.52 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 69 AQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVS 148
Cdd:pfam12128 616 AREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 149 YTLKDIHDDQDylhslGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVN 228
Cdd:pfam12128 696 KKHQAWLEEQK-----EQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVI 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 229 TRRAQ--ADLAYQL-QVAKTKQQIEEQRV--QVQVVERAQQVAVQEQEIARREKELEARV-RKPAEAERYR--LERLAEA 300
Cdd:pfam12128 771 AKLKReiRTLERKIeRIAVRRQEVLRYFDwyQETWLQRRPRLATQLSNIERAISELQQQLaRLIADTKLRRakLEMERKA 850
|
250
....*....|
gi 6679809 301 EKAQLIMQAE 310
Cdd:pfam12128 851 SEKQQVRLSE 860
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
209-361 |
5.66e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 209 MAKAQRDYELKKATYDIEVNTRRAQADLAyQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAE 288
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6679809 289 AERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAIGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKL 361
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
197-356 |
7.55e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 41.53 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 197 EKVSAQCLSEIEmakaqRDYELKKATYDI-----EVNTRRAQAdLAYQLQVAKtkQQIEEQRVQVQVVERA---QQVAVQ 268
Cdd:pfam05262 180 KKVVEALREDNE-----KGVNFRRDMTDLkeresQEDAKRAQQ-LKEELDKKQ--IDADKAQQKADFAQDNadkQRDEVR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 269 EQEIARREKELEARVRKPAEAERYRLERLAEAEKAQliMQAEAEAESVRMRGEAEAFAIGARARAEAEQMAKKAEAFQMY 348
Cdd:pfam05262 252 QKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQ--IEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKK 329
|
....*...
gi 6679809 349 QEAAQLDM 356
Cdd:pfam05262 330 REPVAEDL 337
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
168-352 |
7.95e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 168 RTAQVQKDARIGEAEAKRDAGIREAKAKQEK-VSAQCLSEIEMAKAQRDYELKKA---TYDIEVNTRRAQADLAYQLQVA 243
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQaAEQERLKQLEKERLAAQEQKKQAeeaAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 244 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERyrlERLAEAEKaqlimQAEAEAES-----VRM 318
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAA---KAAAEAKK-----KAEAEAKKkaaaeAKK 217
|
170 180 190
....*....|....*....|....*....|....
gi 6679809 319 RGEAEAFAIGARARAEAEQMAKKAEAFQMYQEAA 352
Cdd:PRK09510 218 KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAA 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
180-368 |
9.24e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 180 EAEAKRDA--GIREAKAKQEKVSAQ------CLSEIEMAKAQRDYELKKATYDievNTRRAQADLayQLQVAKTKQQIEE 251
Cdd:COG4913 246 DAREQIELlePIRELAERYAAARERlaeleyLRAALRLWFAQRRLELLEAELE---ELRAELARL--EAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 252 QRVQVQVVERA------QQVAVQEQEIARREKELEARVRKpaeaeRYRLERLAeaekAQLIMQAEAEAES-VRMRGEAEA 324
Cdd:COG4913 321 LREELDELEAQirgnggDRLEQLEREIERLERELEERERR-----RARLEALL----AALGLPLPASAEEfAALRAEAAA 391
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6679809 325 FAigarARAEAEQMAKKAEAFQMYQEAAQLDmllEKLPQVAEEI 368
Cdd:COG4913 392 LL----EALEEELEALEEALAEAEAALRDLR---RELRELEAEI 428
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
166-368 |
1.30e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 166 KARTAQVQKDARIGEAEAKR------DAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATydievNTRRAQadlayQ 239
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKaeeernNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE-----EKKKAD-----E 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 240 LQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARV---RKPAEAERYRLERLAEAEKAQLIMQAEAEAESV 316
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAeeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6679809 317 RMRGEAEAFAIGARARAEAEQMAKKAEAFQMYQE----AAQLDMLLEKLPQVAEEI 368
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADelkkAAAAKKKADEAKKKAEEK 1430
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
194-406 |
1.35e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 194 AKQEKVSAQCLSEIEMAKAQRDYELKKATYDIE--------VNTRRAQADLAY-QLQVAKTKQQIEEqrvqvqvVERAQQ 264
Cdd:PRK10929 125 AQQEQDRAREISDSLSQLPQQQTEARRQLNEIErrlqtlgtPNTPLAQAQLTAlQAESAALKALVDE-------LELAQL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 265 VAVQEQEIARREKELearvrkpAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAIGARARAEAEQMAKKAEA 344
Cdd:PRK10929 198 SANNRQELARLRSEL-------AKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINREL 270
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679809 345 FQMY-QEAAQLDMLLEKLPQVAEEIsgpLTSANKITLVSSGSGTMGAAKVTGEVL-DILSRLPE 406
Cdd:PRK10929 271 SQALnQQAQRMDLIASQQRQAASQT---LQVRQALNTLREQSQWLGVSNALGEALrAQVARLPE 331
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
162-358 |
1.96e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 162 HSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRD-YELKKATYDIEVNTRRAQADLA-YQ 239
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEkLEKLLQLLPLYQELEALEAELAeLP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 240 LQVAKTKQQIEEQRvqvqvvERAQQVAVQEQEIARREKELEARVRKPAEAERYRLERLaeAEKAQLIMQAEAEAESVRMR 319
Cdd:COG4717 146 ERLEELEERLEELR------ELEEELEELEAELAELQEELEELLEQLSLATEEELQDL--AEELEELQQRLAELEEELEE 217
|
170 180 190
....*....|....*....|....*....|....*....
gi 6679809 320 GEAEAfaigARARAEAEQMAKKAEAFQMYQEAAQLDMLL 358
Cdd:COG4717 218 AQEEL----EELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
180-322 |
2.15e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 180 EAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKAtydiEVNTRRAQADLAYQLQVAKTKQQI----EEQRVQ 255
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA----EEDEKKAAEALKKEAEEAKKAEELkkkeAEEKKK 1717
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6679809 256 VQVVERAQQVAVQEQEIARREKELEARvrkpaEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEA 322
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKK-----KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
206-369 |
2.18e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 206 EIEMAKAQRDYELKKATYDiEVNTRRAQADLAYQLQVAKTKQQIEEQR-VQVQVVERAQQVAVQEQEIAR---REKELEA 281
Cdd:COG1196 217 ELKEELKELEAELLLLKLR-ELEAELEELEAELEELEAELEELEAELAeLEAELEELRLELEELELELEEaqaEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 282 RVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAIGARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKL 361
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
....*...
gi 6679809 362 PQVAEEIS 369
Cdd:COG1196 376 EAEEELEE 383
|
|
| SPFH_HflK |
cd03404 |
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ... |
249-364 |
2.36e-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: 39.42 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 249 IEEQRVQVQVVERAQQV--AVQEQEIARREKElearvRKPAEAERYRLERLAEA--EKAQLIMQAEAEAESVRmrgeaea 324
Cdd:cd03404 156 IEIVQVQLQDADPPEEVqdAFDDVNAARQDKE-----RLINEAQAYANEVIPRArgEAARIIQEAEAYKAEVV------- 223
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 6679809 325 faigARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQV 364
Cdd:cd03404 224 ----ARAEGDAARFLALLAEYRKAPEVTRERLYLETMEEV 259
|
|
| SPFH_SLP-1 |
cd13436 |
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ... |
27-131 |
3.53e-03 |
|
Stomatin-like protein 1 (SLP-1), 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 animals. 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. The family contains human SLP-1, which has been found to be expressed in the brain, and Caenorhabditis elegans UNC-24, which is a lipid raft-associated protein required for normal locomotion. It may mediate the correct localization of UNC-1. Mutations in the unc-24 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.
Pssm-ID: 259814 [Multi-domain] Cd Length: 131 Bit Score: 37.38 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIqgqnKEMLAAACQMF-LGKTEAEIAHIALETle 105
Cdd:cd13436 10 GIVLILPCIDNFTRVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRI----WDPVLSVMAVQdLNTSTRTTAQTSLTN-- 83
|
90 100
....*....|....*....|....*.
gi 6679809 106 ghqraIMAHMTVEEIYKDRQKFSEQV 131
Cdd:cd13436 84 -----SLSKKTVREIQSDRRKINEEL 104
|
|
| SPFH_like_u4 |
cd03407 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
278-346 |
4.64e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259805 [Multi-domain] Cd Length: 269 Bit Score: 38.72 E-value: 4.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6679809 278 ELEARVRKPA----EAERYRL--ERLAEAEKAQLIMQAEAEAESVRMRGEaeafAIGARARAEAEQMAKKAEAFQ 346
Cdd:cd03407 143 EPDASVKAAMneinAAQRLREaaEEKAEAEKILQVKAAEAEAEAKRLQGV----GIAEQRKAIVDGLRESIEDFQ 213
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
170-373 |
4.95e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 39.42 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 170 AQVQKDARIGEAEAKRDAG-IR-EAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKTKQ 247
Cdd:NF041483 887 ASAEQDAARTRADAREDANrIRsDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEA 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 248 QIEEQRVQVqvvERAQQVAVQEQEIARREKELEaRVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAI 327
Cdd:NF041483 967 TGEAERLRA---EAAETVGSAQQHAERIRTEAE-RVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADTL 1042
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6679809 328 GARARAEAEQMAKKA--EAFQMYQEA-AQLDMLLEKLPQVAEEISGPLT 373
Cdd:NF041483 1043 ITEAAAEADQLTAKAqeEALRTTTEAeAQADTMVGAARKEAERIVAEAT 1091
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
171-384 |
5.13e-03 |
|
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: 39.27 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 171 QVQKDARIGEAEAKRDAgIREAKAKQEKVSAQCLSEIEMAKAqrdyELKKATYDIEVNTRRAQADlayqlqvaktKQQIE 250
Cdd:TIGR02168 318 LEELEAQLEELESKLDE-LAEELAELEEKLEELKEELESLEA----ELEELEAELEELESRLEEL----------EEQLE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 251 EQRVQVqvVERAQQVAVQEQEIARREKELE---ARVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRGEAEAFAI 327
Cdd:TIGR02168 383 TLRSKV--AQLELQIASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6679809 328 GARARAEAEQMAKKAEAFQMYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSG 384
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
164-326 |
5.41e-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: 38.98 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 164 LGKARTAQVQKDARIGEAEAKRDAgIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVNTRR---------AQA 234
Cdd:COG4942 71 IRALEQELAALEAELAELEKEIAE-LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRlqylkylapARR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 235 DLAYQLQ-----VAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKE-LEARVRKPAEAERYRLERLAEAEKA--QLI 306
Cdd:COG4942 150 EQAEELRadlaeLAALRAELEAERAELEALLAELEEERAALEALKAERQkLLARLEKELAELAAELAELQQEAEEleALI 229
|
170 180
....*....|....*....|
gi 6679809 307 MQAEAEAESVRMRGEAEAFA 326
Cdd:COG4942 230 ARLEAEAAAAAERTPAAGFA 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
138-367 |
6.17e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 138 DLVNMGISVVSYTLKDIHD-DQDYLHSLGKARTAQVQKDARIGEAEAKRDAgireaKAKQEKVSAQCLSEiemAKAQRDY 216
Cdd:PTZ00121 1031 ELTEYGNNDDVLKEKDIIDeDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDF-----DAKEDNRADEATEE---AFGKAEE 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 217 ELKKATYDIEVNTRRAQAdlayqlqvaktKQQIEEQRvQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRLER 296
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEA-----------KKKAEDAR-KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEAR 1170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6679809 297 LAE-AEKAQLIMQAEAEAESVRMRGEAEAFAIGARARAEAEqmaKKAEAFQMYQEAAQLDML--LEKLPQVAEE 367
Cdd:PTZ00121 1171 KAEdAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEE---RKAEEARKAEDAKKAEAVkkAEEAKKDAEE 1241
|
|
| ASD2 |
pfam08687 |
Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which ... |
209-314 |
6.81e-03 |
|
Apx/Shroom domain ASD2; This region is found in the actin binding protein Shroom which mediates apical contriction in epithelial cells and is required for neural tube closure.
Pssm-ID: 462561 [Multi-domain] Cd Length: 290 Bit Score: 38.39 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 209 MAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKTKQQ-IEEQRVQVQVVERAQQvAVQE--QEIARREKELEARVR- 284
Cdd:pfam08687 80 APKAELLTKMKDLTTLPSPDQPEEQGEEELDNDLQQKKVElIESLQRKLQVLREEQE-ALQEeiQANAALGAEVEALVQe 158
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 6679809 285 --KPAEAERYRL----------------ERLAEAEKAQLIMQAEAEAE 314
Cdd:pfam08687 159 vcKPNELEKYRMfigdlekvvslllslsGRLARVENALSSLDSDADAE 206
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
73-367 |
7.11e-03 |
|
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: 38.88 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 73 IQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAImahmtvEEIYKDRQKFSEQvfkvASSDLVNMGISVVSYTLK 152
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEEL------EEELEQLRKELEE----LSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 153 dIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQclseieMAKAQRDYELKKATYDIEVNTRRA 232
Cdd:TIGR02168 742 -VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ------IEQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 233 QADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRLERLAEAEKAQLIMQAEAE 312
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6679809 313 AESVRMRGEAEAFAIGARARAEAEQMAKKAEAFQMYQEAAQLDmLLEKLPQVAEE 367
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR-IDNLQERLSEE 948
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
191-300 |
7.57e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 38.78 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6679809 191 EAKAKQEKVSAQcLSEIEMAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKTKQQIEEQ---RVQV-----QVVERA 262
Cdd:COG3096 561 ELEAQLEELEEQ-AAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEAladSQEVtaamqQLLERE 639
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 6679809 263 QQVAVQEQEIARREKELEARVRK---PAEAERYRLERLAEA 300
Cdd:COG3096 640 REATVERDELAARKQALESQIERlsqPGGAEDPRLLALAER 680
|
|
| |
