|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1-370 |
7.18e-72 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 230.92 E-value: 7.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 1 MFFTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVK-SEKVYTRHGVPISVTGIAQ--------- 70
Cdd:COG2268 27 FYRKVPPNEALVITGRGGGYKV-VTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYvkvnsdped 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 71 --------------------------------------EIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDY 112
Cdd:COG2268 106 ianaaerflgrdpeeieelaeeklegalravaaqmtveELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 113 LHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIE-----MAKAQRDYELKKAAYDIEVNTRRAQAD 187
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEAE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 188 LAYQLQVAKTKQQIEeqrVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKlerlaeaeksqlimqAEAEAas 267
Cdd:COG2268 266 AAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA---------------AEAEA-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 268 vrmrgEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVtg 347
Cdd:COG2268 326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA-- 398
|
410 420
....*....|....*....|...
gi 974141105 348 eVLDILTRLPESVERLTGVSISQ 370
Cdd:COG2268 399 -VAEALAPLLESLLEETGLDLPG 420
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
30-127 |
1.85e-32 |
|
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: 118.76 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 30 FVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQ--------------------------------------- 70
Cdd:cd03399 1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQvkvgsdpeeiaaaaerflgksteeirelvketleghlra 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974141105 71 --------EIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKD 127
Cdd:cd03399 81 ivgtmtveEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
71-218 |
5.74e-12 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 63.45 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 71 EIYKDRQKfseqVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKqek 150
Cdd:smart00244 33 PFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK--- 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974141105 151 vsaqylseIEMAKAQRDYELKKAAYDIEVNTRRAQAdLAYQLQVAKTKQqieeQRVQVQVVERAQQVA 218
Cdd:smart00244 106 --------RTLDELLTDQREKISENIREELNEAAEA-WGIKVEDVEIKD----IRLPEEIKEAMEAQQ 160
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
3-137 |
8.85e-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: 60.41 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 3 FTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQ------------ 70
Cdd:pfam01145 1 IIVPPGEVGVVTRFGKLSRV-LEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIyrvnpddppklv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 71 -------------------------------EIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKA 119
Cdd:pfam01145 80 qnvfgsddlqellrrvlesalreiiarytleELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159
|
170
....*....|....*...
gi 974141105 120 RTAQVQKDARIGEAEAKR 137
Cdd:pfam01145 160 QTAEQEAEAEIARAEAEA 177
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
128-300 |
2.54e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 128 ARIGEAEAKRDAGIREAKAKqekvsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRaqADLAYQLQVAKTKQQIEEQRVQ 207
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-----AEAIKKEALLEAKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 208 vQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYKLERLA-----EAeKSQLIMQAEAEA---ASVRMRgeaea 276
Cdd:PRK12704 104 -LLEKREEELEKKEKELEQKQQELEKKeeeLEELIEEQLQELERISgltaeEA-KEILLEKVEEEArheAAVLIK----- 176
|
170 180
....*....|....*....|....*.
gi 974141105 277 fAIGARARAEAEQMAKK--AEAFQLY 300
Cdd:PRK12704 177 -EIEEEAKEEADKKAKEilAQAIQRC 201
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
118-305 |
6.63e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.20 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 118 KARTAQVQKDARI--GEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAaydievntrRAQADlayqlqVA 195
Cdd:NF041483 432 RAKTVELQEEARRlrGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKA---------KADAD------EL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 196 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAE---------AERYKLERLAEAEKSQLIMQAEAEAA 266
Cdd:NF041483 497 RSTATAESERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEeqaeevraaAERAARELREETERAIAARQAEAAEE 576
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 974141105 267 SVRMRGEAEAFAIGAR-----ARAEAEQMAKKA--EAFQLYQEAAQ 305
Cdd:NF041483 577 LTRLHTEAEERLTAAEealadARAEAERIRREAaeETERLRTEAAE 622
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-331 |
1.65e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 117 GKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVsAQYLSEIEMAKAQRDyELKKAAYDIevntRRAQADLAYQLQVAK 196
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKAL-AELRKELEELEEELE-QLRKELEEL----SRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 197 TKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRkpAEAERYKLERLAEAEKSQLiMQAEAEAASVRMR-GEAE 275
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEEL-KALREALDELRAElTLLN 816
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 974141105 276 AFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKIT 331
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
118-305 |
2.01e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.66 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 118 KARTAQvQKDARIGEAEAKRDAGIREAKAKQEKVSAQ----YLSEIEMAKAQRDYELKKAAYDIE--VNTRRAQA----D 187
Cdd:NF041483 158 RARTES-QARRLLDESRAEAEQALAAARAEAERLAEEarqrLGSEAESARAEAEAILRRARKDAErlLNAASTQAqeatD 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 188 LAYQLQVAkTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEA-RVRKPAEAERYKLERLAEAEKSQLIMQAEAEAA 266
Cdd:NF041483 237 HAEQLRSS-TAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAeKVVAEAKEAAAKQLASAESANEQRTRTAKEEIA 315
|
170 180 190
....*....|....*....|....*....|....*....
gi 974141105 267 svRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQ 305
Cdd:NF041483 316 --RLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAE 352
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
122-295 |
5.88e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 39.04 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 122 AQVQKDARIGEAEAKRDAG-IREAKAKQekvsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQ 200
Cdd:NF041483 887 ASAEQDAARTRADAREDANrIRSDAAAQ----ADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQL 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 201 IEEQRVQVQVV--ERAQQVAVQEQEIARREKELEaRVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFA 278
Cdd:NF041483 963 IAEATGEAERLraEAAETVGSAQQHAERIRTEAE-RVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADT 1041
|
170
....*....|....*..
gi 974141105 279 IGARARAEAEQMAKKAE 295
Cdd:NF041483 1042 LITEAAAEADQLTAKAQ 1058
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1-370 |
7.18e-72 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 230.92 E-value: 7.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 1 MFFTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVK-SEKVYTRHGVPISVTGIAQ--------- 70
Cdd:COG2268 27 FYRKVPPNEALVITGRGGGYKV-VTGGGAFVLPVLHRAERMSLSTMTIEVErTEGLITKDGIRVDVDAVFYvkvnsdped 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 71 --------------------------------------EIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDY 112
Cdd:COG2268 106 ianaaerflgrdpeeieelaeeklegalravaaqmtveELNEDREKFAEKVQEVAGTDLAKNGLELESVAITDLEDENNY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 113 LHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIE-----MAKAQRDYELKKAAYDIEVNTRRAQAD 187
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREietarIAEAEAELAKKKAEERREAETARAEAE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 188 LAYQLQVAKTKQQIEeqrVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKlerlaeaeksqlimqAEAEAas 267
Cdd:COG2268 266 AAYEIAEANAEREVQ---RQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQA---------------AEAEA-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 268 vrmrgEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSGSGTMGAAKVtg 347
Cdd:COG2268 326 -----EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKITIIDGGNGGNGAGSA-- 398
|
410 420
....*....|....*....|...
gi 974141105 348 eVLDILTRLPESVERLTGVSISQ 370
Cdd:COG2268 399 -VAEALAPLLESLLEETGLDLPG 420
|
|
| SPFH_flotillin |
cd03399 |
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ... |
30-127 |
1.85e-32 |
|
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: 118.76 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 30 FVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQ--------------------------------------- 70
Cdd:cd03399 1 FVIPFLQRVQRLSLETMTIDVKVEEVLTKDGIPVDVTAVAQvkvgsdpeeiaaaaerflgksteeirelvketleghlra 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974141105 71 --------EIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKD 127
Cdd:cd03399 81 ivgtmtveEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAEVKKD 145
|
|
| PHB |
smart00244 |
prohibitin homologues; prohibitin homologues |
71-218 |
5.74e-12 |
|
prohibitin homologues; prohibitin homologues
Pssm-ID: 214581 [Multi-domain] Cd Length: 160 Bit Score: 63.45 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 71 EIYKDRQKfseqVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKqek 150
Cdd:smart00244 33 PFIDDVKK----VDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRAVYRVLDADYAVIEQLAQTTLRSVIGK--- 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974141105 151 vsaqylseIEMAKAQRDYELKKAAYDIEVNTRRAQAdLAYQLQVAKTKQqieeQRVQVQVVERAQQVA 218
Cdd:smart00244 106 --------RTLDELLTDQREKISENIREELNEAAEA-WGIKVEDVEIKD----IRLPEEIKEAMEAQQ 160
|
|
| Band_7 |
pfam01145 |
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ... |
3-137 |
8.85e-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: 60.41 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 3 FTCGPNEAMVVSGFCRSPPVmVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQ------------ 70
Cdd:pfam01145 1 IIVPPGEVGVVTRFGKLSRV-LEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIyrvnpddppklv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 71 -------------------------------EIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKA 119
Cdd:pfam01145 80 qnvfgsddlqellrrvlesalreiiarytleELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159
|
170
....*....|....*...
gi 974141105 120 RTAQVQKDARIGEAEAKR 137
Cdd:pfam01145 160 QTAEQEAEAEIARAEAEA 177
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
179-340 |
2.81e-08 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 54.46 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 179 VNTRRAQ--ADLAYQLQVAKTKQQIEEQRVQVQVVERAQQV--AVQEQEIARREKElearvrkpaeaeryKLERLAEAEK 254
Cdd:COG0330 129 LSTGRDEinAEIREELQEALDPYGIEVVDVEIKDIDPPEEVqdAMEDRMKAERERE--------------AAILEAEGYR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 255 SQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLdMLLEKLPQVAEeisgpltSANKITLVS 334
Cdd:COG0330 195 EAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEAYSAAPFVLFY-RSLEALEEVLS-------PNSKVIVLP 266
|
....*.
gi 974141105 335 SGSGTM 340
Cdd:COG0330 267 PDGNGF 272
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
27-186 |
2.56e-07 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 51.38 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 27 GRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQ------------------------------------ 70
Cdd:COG0330 45 GLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNIVDVDAVVQyritdpakflynvenaeealrqlaesalrevigkmt 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 71 --EIY-KDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAK 147
Cdd:COG0330 125 ldEVLsTGRDEINAEIREELQEALDPYGIEVVDVEIKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGE 204
|
170 180 190
....*....|....*....|....*....|....*....
gi 974141105 148 QEKVsaqylseIEMAKAQRDYELKKAAYDIEVNTRRAQA 186
Cdd:COG0330 205 AQRA-------IIEAEAYREAQILRAEGEAEAFRIVAEA 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
112-320 |
5.81e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 112 YLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLS----EIEMAKAQRDYELKKAAYDIEVNTRRAQAD 187
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEleelELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 188 LAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEArvrkpAEAERYKLERLAEAEKSQLIMQAEAEAAS 267
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-----AEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 974141105 268 VRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEI 320
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
118-321 |
6.07e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 118 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKT 197
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEE-YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 198 KQQIEEQRVQVQVVE-RAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEA 276
Cdd:COG1196 336 EEELEELEEELEEAEeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 974141105 277 FAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEIS 321
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
114-315 |
9.74e-07 |
|
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: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 114 HSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQ 193
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 194 VAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLE-RLAEAEKSQLIMQAEAEAASVRMRG 272
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEeEEALEEAAEEEAELEEEEEALLELL 465
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 974141105 273 EAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQ 315
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
128-300 |
2.54e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 128 ARIGEAEAKRDAGIREAKAKqekvsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRaqADLAYQLQVAKTKQQIEEQRVQ 207
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-----AEAIKKEALLEAKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 208 vQVVERAQQVAVQEQEIARREKELEAR---VRKPAEAERYKLERLA-----EAeKSQLIMQAEAEA---ASVRMRgeaea 276
Cdd:PRK12704 104 -LLEKREEELEKKEKELEQKQQELEKKeeeLEELIEEQLQELERISgltaeEA-KEILLEKVEEEArheAAVLIK----- 176
|
170 180
....*....|....*....|....*.
gi 974141105 277 fAIGARARAEAEQMAKK--AEAFQLY 300
Cdd:PRK12704 177 -EIEEEAKEEADKKAKEilAQAIQRC 201
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-319 |
5.99e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 118 KARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAqylseiEMAKAqrdyELKKAAYDIEVNTRRAQADlayQLQVAKT 197
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA------EAAKA----EAEAAADEAEAAEEKAEAA---EKKKEEA 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 198 KQQIEEQRVQVQVVERAQQVAVQEQEIARREKELE--ARVRKPAEAERYKLERLAEAEksQLIMQAEAEAASVRMRGEAE 275
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKAD--EAKKKAEEAKKADEAKKKAE 1454
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 974141105 276 AFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKlpqvAEE 319
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK----AEE 1494
|
|
| Flot |
pfam15975 |
Flotillin; Flotillin is a family of lipid-membrane-associated proteins found in bacteria, ... |
262-347 |
6.72e-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: 45.01 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 262 EAEAASVRMRGEAEAfaIGARARAEAEQMAKKAEAFQLY---QEAAQLDM-LLEKLPQVAEEISGPLTSANKITLVSSGS 337
Cdd:pfam15975 1 EAEAEADAIKLRAEA--KRKKALAEAEGIRALNEAENALsdeQIALQVKLaLLEALPEIIAESVKPLEKIDGIKILQVDG 78
|
90
....*....|
gi 974141105 338 GTMGAAKVTG 347
Cdd:pfam15975 79 LGGGAAGGGG 88
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
108-320 |
1.35e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 108 DDQDYLHSLGKARTAQVQKDARIGEA-----EAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTR 182
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 183 RAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKElEAR----VRKPAEAERYKLERLAEAEKSQLI 258
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-EAKkaeeLKKKEAEEKKKAEELKKAEEENKI 1730
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 974141105 259 MQAEAEAASVRMRGEAEafaigaRARAEAEQmAKKAEAFQLYQEAAQLDMLLEKLPQVAEEI 320
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAE------EAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| SPFH_SLP-4 |
cd13435 |
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ... |
14-158 |
2.01e-05 |
|
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: 45.07 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 14 SGFCRSPpvmvagGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQEIYKDRQKFSEQVFK-------V 86
Cdd:cd13435 1 SGGARGP------GVFFVLPCIDNYCKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANyshstrlL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 87 ASSDLVN-MGISVVSYTLKD----IHDDQDYLHSLGKARTAQVQ----KD---------ARIGEAEAKRDAGIREAKAKQ 148
Cdd:cd13435 75 AATTLRNvLGTRNLSELLTEretiSHSMQVTLDEATDPWGVQVErveiKDvslpdslqrAMAAEAEAAREARAKVIAAEG 154
|
170
....*....|
gi 974141105 149 EKVSAQYLSE 158
Cdd:cd13435 155 EMKSSRALKE 164
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
120-310 |
3.36e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.57 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 120 RTAQVQKDARIGEAEAKRDAGIREAKAKQEK-VSAQYLSEIEMAKAQRDYELKKA---AYDIEVNTRRAQADLAYQLQVA 195
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQaAEQERLKQLEKERLAAQEQKKQAeeaAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 196 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERY---KLERLAEAEKSQLIMQAEAEAASVRMRG 272
Cdd:PRK09510 146 KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKaaaEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225
|
170 180 190
....*....|....*....|....*....|....*...
gi 974141105 273 EAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLL 310
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-309 |
5.37e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 118 KARTAQVQKDARIGEAEAKRDagirEAKAKQEKVSAQYLSEIEmAKAQRDyELKKAAYDI---EVNTRRAQADLAYQLQV 194
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAAD----EAEAAEEKAEAAEKKKEE-AKKKAD-AAKKKAEEKkkaDEAKKKAEEDKKKADEL 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 195 AKT---KQQIEEQRVQVQVVERAQQVAVQEQEiARREKELearvRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMR 271
Cdd:PTZ00121 1411 KKAaaaKKKADEAKKKAEEKKKADEAKKKAEE-AKKADEA----KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA 1485
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 974141105 272 GEAEAFAIGARARAE----AEQMAKKAEAFQLYQEAAQLDML 309
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADeakkAAEAKKKADEAKKAEEAKKADEA 1527
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
118-305 |
6.63e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.20 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 118 KARTAQVQKDARI--GEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAaydievntrRAQADlayqlqVA 195
Cdd:NF041483 432 RAKTVELQEEARRlrGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKA---------KADAD------EL 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 196 KTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAE---------AERYKLERLAEAEKSQLIMQAEAEAA 266
Cdd:NF041483 497 RSTATAESERVRTEAIERATTLRRQAEETLERTRAEAERLRAEAEeqaeevraaAERAARELREETERAIAARQAEAAEE 576
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 974141105 267 SVRMRGEAEAFAIGAR-----ARAEAEQMAKKA--EAFQLYQEAAQ 305
Cdd:NF041483 577 LTRLHTEAEERLTAAEealadARAEAERIRREAaeETERLRTEAAE 622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
103-329 |
9.77e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 103 LKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIR--EAKAKQEKVSAQYLSEIEMAKAQRDyelkkaAYDIEVN 180
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKaeDARKAEEARKAEDARKAEEARKAED------AKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 181 TRRAQADLAYQLQVAKTKQQIEEQRVQVQVvERAQQVAVQEQ----EIARREKElearVRKPAEAERYKLERLAEAEKSQ 256
Cdd:PTZ00121 1158 RKAEDARKAEEARKAEDAKKAEAARKAEEV-RKAEELRKAEDarkaEAARKAEE----ERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 257 LIMQAEAEAA----SVRMRGEAEAF-------------AIGARARAEAEQMAK-----KAEAFQLYQEAAQLDMLLEK-- 312
Cdd:PTZ00121 1233 EEAKKDAEEAkkaeEERNNEEIRKFeearmahfarrqaAIKAEEARKADELKKaeekkKADEAKKAEEKKKADEAKKKae 1312
|
250 260
....*....|....*....|....
gi 974141105 313 -------LPQVAEEISGPLTSANK 329
Cdd:PTZ00121 1313 eakkadeAKKKAEEAKKKADAAKK 1336
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-331 |
1.65e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 117 GKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVsAQYLSEIEMAKAQRDyELKKAAYDIevntRRAQADLAYQLQVAK 196
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKAL-AELRKELEELEEELE-QLRKELEEL----SRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 197 TKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRkpAEAERYKLERLAEAEKSQLiMQAEAEAASVRMR-GEAE 275
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEEL-KALREALDELRAElTLLN 816
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 974141105 276 AFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKIT 331
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
193-299 |
1.73e-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: 43.05 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 193 QVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEArvRKPAEaeryklerLAEAEKSQLIMQAEAEAASVRMrg 272
Cdd:cd03406 163 AIRRNYEAMEAEKTKLLIAEQHQKVVEKEAETERKRAVIEA--EKDAE--------VAKIQMQQKIMEKEAEKKISEI-- 230
|
90 100
....*....|....*....|....*....
gi 974141105 273 EAEAFAIGARARAEAE--QMAKKAEAFQL 299
Cdd:cd03406 231 EDEMHLAREKARADAEyyRALREAEANKL 259
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
118-305 |
2.01e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.66 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 118 KARTAQvQKDARIGEAEAKRDAGIREAKAKQEKVSAQ----YLSEIEMAKAQRDYELKKAAYDIE--VNTRRAQA----D 187
Cdd:NF041483 158 RARTES-QARRLLDESRAEAEQALAAARAEAERLAEEarqrLGSEAESARAEAEAILRRARKDAErlLNAASTQAqeatD 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 188 LAYQLQVAkTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEA-RVRKPAEAERYKLERLAEAEKSQLIMQAEAEAA 266
Cdd:NF041483 237 HAEQLRSS-TAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAeKVVAEAKEAAAKQLASAESANEQRTRTAKEEIA 315
|
170 180 190
....*....|....*....|....*....|....*....
gi 974141105 267 svRMRGEAEAFAIGARARAEAEQMAKKAEAFQLYQEAAQ 305
Cdd:NF041483 316 --RLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAE 352
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-320 |
2.06e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 118 KARTAQVQKDARiGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDyELKKAAydievntrraQADLAYQLQVAKT 197
Cdd:PTZ00121 1465 KAEEAKKADEAK-KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD-EAKKAE----------EAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 198 KQQIEEQRvQVQVVERAQQVAVQEqEIARREKelearVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAF 277
Cdd:PTZ00121 1533 AKKADEAK-KAEEKKKADELKKAE-ELKKAEE-----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 974141105 278 AIGARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKlpQVAEEI 320
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK--KEAEEK 1646
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
116-319 |
2.09e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 116 LGKARTAQVQKDARigEAEAKRDAgiREAKAKQEKVSAQylseiEMAKAQrdyELKKAAYDIEV-NTRRAQADLAYQLQV 194
Cdd:PTZ00121 1515 AKKAEEAKKADEAK--KAEEAKKA--DEAKKAEEKKKAD-----ELKKAE---ELKKAEEKKKAeEAKKAEEDKNMALRK 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 195 AKTKQQIEEQRVQV-------QVVERAQQVAVQEQEIARRE---KELEAR-----VRKPAEAERYKLERLAEAE------ 253
Cdd:PTZ00121 1583 AEEAKKAEEARIEEvmklyeeEKKMKAEEAKKAEEAKIKAEelkKAEEEKkkveqLKKKEAEEKKKAEELKKAEeenkik 1662
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 974141105 254 KSQLIMQAEAEAASVR-MRGEAEAFAIGARARAEAEQMAKKAEafQLYQEAAQLDMLLEKLPQVAEE 319
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEeAKKAEEDEKKAAEALKKEAEEAKKAE--ELKKKEAEEKKKAEELKKAEEE 1727
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
196-257 |
2.24e-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: 42.67 E-value: 2.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974141105 196 KTKQQIEEQRV-QVQVVERAQQVAvqEQEIARREKELE-----ARVRKPAEAERYKLERLAEAEKSQL 257
Cdd:cd03406 196 RKRAVIEAEKDaEVAKIQMQQKIM--EKEAEKKISEIEdemhlAREKARADAEYYRALREAEANKLKL 261
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-321 |
3.48e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 146 AKQEKVSAQYLsEIEMAKAQRDYELKKAAYDiEVNTRRAQADLAYQLQVAKTKQQIEEQR-VQVQVVERAQQVAVQEQEI 224
Cdd:COG1196 206 ERQAEKAERYR-ELKEELKELEAELLLLKLR-ELEAELEELEAELEELEAELEELEAELAeLEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 225 AR---REKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAfQLYQ 301
Cdd:COG1196 284 EEaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA-ELAE 362
|
170 180
....*....|....*....|
gi 974141105 302 EAAQLDMLLEKLPQVAEEIS 321
Cdd:COG1196 363 AEEALLEAEAELAEAEEELE 382
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
142-311 |
3.79e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 142 REAKAKQEKVSAQYLseiemAKAQRDYELKKAAYDIEVNTRRAQADLAyQLQVAKTKQQIEEQRVQVQVVE-RAQQVAVQ 220
Cdd:COG1196 216 RELKEELKELEAELL-----LLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELElELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 221 EQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEAFQLY 300
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170
....*....|.
gi 974141105 301 QEAAQLDMLLE 311
Cdd:COG1196 370 AEAELAEAEEE 380
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
132-320 |
4.35e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 132 EAEAKRDA--GIRE-----AKAKQEKVSAQYL-SEIEMAKAQRDYELKKAAYDievNTRRAQADLayQLQVAKTKQQIEE 203
Cdd:COG4913 246 DAREQIELlePIRElaeryAAARERLAELEYLrAALRLWFAQRRLELLEAELE---ELRAELARL--EAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 204 QRVQVQVVERA------QQVAVQEQEIARREKELEARVRKpaeAERYKlERLAEAEksqliMQAEAEAAS-VRMRGEAEA 276
Cdd:COG4913 321 LREELDELEAQirgnggDRLEQLEREIERLERELEERERR---RARLE-ALLAALG-----LPLPASAEEfAALRAEAAA 391
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 974141105 277 FAigarARAEAEQMAKKAEAFQLYQEAAQLDmllEKLPQVAEEI 320
Cdd:COG4913 392 LL----EALEEELEALEEALAEAEAALRDLR---RELRELEAEI 428
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
143-251 |
7.20e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 143 EAKAKQEKVSAQYLSEIEMAKAQRDyELKKAAYDIEVNTRRAQADLAYQLQVAK----------TKQQIEEQRVQVQVVE 212
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQ-QLEQLQARIQRLAARAPAWLAAQDALARlreqsgeefeDSQDVTEYMQQLLERE 640
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 974141105 213 RAQQvaVQEQEIARREKELEARVRK---PAEAERYKLERLAE 251
Cdd:PRK04863 641 RELT--VERDELAARKQALDEEIERlsqPGGSEDPRLNALAE 680
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-295 |
9.33e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 118 KARTAQVQKDARIGEAEAKR------DAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAydievNTRRAQadlayQ 191
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKaeeernNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE-----EKKKAD-----E 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 192 LQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARV---RKPAEAERYKLERLA-EAEKSQLIMQAeAEAAS 267
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAeeaKKAAEAAKAEAEAAAdEAEAAEEKAEA-AEKKK 1373
|
170 180
....*....|....*....|....*...
gi 974141105 268 VRMRGEAEAFAIGARARAEAEQMAKKAE 295
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
116-278 |
1.06e-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: 40.90 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 116 LGKARTAQVQKDARIGEAEAKRDAgIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRR---------AQA 186
Cdd:COG4942 71 IRALEQELAALEAELAELEKEIAE-LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRlqylkylapARR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 187 DLAYQLQ-----VAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKE-LEARVRKPAEAERYKLERLAEAEKS--QLI 258
Cdd:COG4942 150 EQAEELRadlaeLAALRAELEAERAELEALLAELEEERAALEALKAERQkLLARLEKELAELAAELAELQQEAEEleALI 229
|
170 180
....*....|....*....|
gi 974141105 259 MQAEAEAASVRMRGEAEAFA 278
Cdd:COG4942 230 ARLEAEAAAAAERTPAAGFA 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
120-320 |
1.20e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 120 RTAQVQKDARIGEAEAKRDA----GIREAKAKQEKVSAQYLSEIEMAKaqRDYELKKAAYDIEVNTRRAQADLAYQLQVA 195
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAeeerKAEEARKAEDAKKAEAVKKAEEAK--KDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 196 KTKQQIE-EQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEA 274
Cdd:PTZ00121 1267 RRQAAIKaEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 974141105 275 EAFAIGARARAEAEQMAKKAEAFQLYQEAAQLDMllEKLPQVAEEI 320
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA--DAAKKKAEEK 1390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
125-310 |
1.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 125 QKDARIGEAEAKRD---AGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLA-YQLQVAKTKQQ 200
Cdd:COG4717 75 ELEEELKEAEEKEEeyaELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAeLPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 201 IEEQRvqvqvvERAQQVAVQEQEIARREKELEARVRKPAEAERYKLERLAEA--EKSQLIMQAEAEAASVRMRGEaeafa 278
Cdd:COG4717 155 LEELR------ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEleELQQRLAELEEELEEAQEELE----- 223
|
170 180 190
....*....|....*....|....*....|..
gi 974141105 279 igaRARAEAEQMAKKAEAFQLYQEAAQLDMLL 310
Cdd:COG4717 224 ---ELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
141-296 |
1.87e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 39.83 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 141 IREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQ 220
Cdd:TIGR02794 55 IQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKA 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 974141105 221 EQEiARREKELEARVRKPAEAERyKLERLAEAEKSQLIMQAEAEAASvRMRGEAEAFAIGARARAEAEQMAKKAEA 296
Cdd:TIGR02794 135 KAE-AEAERKAKEEAAKQAEEEA-KAKAAAEAKKKAEEAKKKAEAEA-KAKAEAEAKAKAEEAKAKAEAAKAKAAA 207
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-336 |
2.61e-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: 40.04 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 123 QVQKDARIGEAEAKRDAgIREAKAKQEKVSAQYLSEIEMAKAqrdyELKKAAYDIEVNTRRAQADlayqlqvaktKQQIE 202
Cdd:TIGR02168 318 LEELEAQLEELESKLDE-LAEELAELEEKLEELKEELESLEA----ELEELEAELEELESRLEEL----------EEQLE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 203 EQRVQVqvVERAQQVAVQEQEIARREKELE---ARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAI 279
Cdd:TIGR02168 383 TLRSKV--AQLELQIASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 974141105 280 GARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKITLVSSG 336
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
172-319 |
3.00e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.55 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 172 KAAYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARR-------EKELEARVRKPAEAERY 244
Cdd:pfam15709 375 REELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRklqelqrKKQQEEAERAEAEKQRQ 454
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 974141105 245 K--LERLAEAEKSQLIMQAEAEAASVRMRGEAEafaigARARAEAEQMAKKAEafqlyqEAAQLdmLLEKLPQVAEE 319
Cdd:pfam15709 455 KelEMQLAEEQKRLMEMAEEERLEYQRQKQEAE-----EKARLEAEERRQKEE------EAARL--ALEEAMKQAQE 518
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
149-296 |
4.15e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.22 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 149 EKVSAQYLSEIEmakaqRDYELKKAAYDI-----EVNTRRAQAdLAYQLQVAKtkQQIEEQRVQVQVVERA---QQVAVQ 220
Cdd:pfam05262 180 KKVVEALREDNE-----KGVNFRRDMTDLkeresQEDAKRAQQ-LKEELDKKQ--IDADKAQQKADFAQDNadkQRDEVR 251
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 974141105 221 EQEIARREKELEARVRKPAEAERYKLERLAEAEKSQLIMQAEAEAAsvRMRGEAEAFAIGARARAEaEQMAKKAEA 296
Cdd:pfam05262 252 QKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEA--LKAKDHKAFDLKQESKAS-EKEAEDKEL 324
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
143-331 |
5.85e-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: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 143 EAKAKQEKVS------AQYLSEIEMAKAQRD--YELKKAAYDiEVNtrRAQADlayqlQVAKtkQQIEEQRVQVQVVERA 214
Cdd:COG3096 445 AFRAKEQQATeevlelEQKLSVADAARRQFEkaYELVCKIAG-EVE--RSQAW-----QTAR--ELLRRYRSQQALAQRL 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 215 QQVAVQEQEIARREKELEARVRKPAE-AERYKLERLAEAEKSQLIMQAEAEAASVrmrGEAEAFAIGARARAEAEQMAKK 293
Cdd:COG3096 515 QQLRAQLAELEQRLRQQQNAERLLEEfCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLR 591
|
170 180 190
....*....|....*....|....*....|....*...
gi 974141105 294 AEAFQLYQEAAQLDMLLEKLPQVAEEISGPLTSANKIT 331
Cdd:COG3096 592 ARIKELAARAPAWLAAQDALERLREQSGEALADSQEVT 629
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
122-295 |
5.88e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 39.04 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 122 AQVQKDARIGEAEAKRDAG-IREAKAKQekvsAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTKQQ 200
Cdd:NF041483 887 ASAEQDAARTRADAREDANrIRSDAAAQ----ADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQL 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 201 IEEQRVQVQVV--ERAQQVAVQEQEIARREKELEaRVRKPAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFA 278
Cdd:NF041483 963 IAEATGEAERLraEAAETVGSAQQHAERIRTEAE-RVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADT 1041
|
170
....*....|....*..
gi 974141105 279 IGARARAEAEQMAKKAE 295
Cdd:NF041483 1042 LITEAAAEADQLTAKAQ 1058
|
|
| SPFH_HflK |
cd03404 |
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ... |
239-316 |
5.96e-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: 37.88 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 239 AEAERYKLErlAEAEKSQLIMQAEAEAAsvRMRGEAEAFAIG--ARARAEAEQMAKKAEAFQLYQEAAQLDMLLEKLPQV 316
Cdd:cd03404 184 QDKERLINE--AQAYANEVIPRARGEAA--RIIQEAEAYKAEvvARAEGDAARFLALLAEYRKAPEVTRERLYLETMEEV 259
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
146-358 |
6.16e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 38.88 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 146 AKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIE--------VNTRRAQADLAY-QLQVAKTKQQIEEqrvqvqvVERAQQ 216
Cdd:PRK10929 125 AQQEQDRAREISDSLSQLPQQQTEARRQLNEIErrlqtlgtPNTPLAQAQLTAlQAESAALKALVDE-------LELAQL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 217 VAVQEQEIARREKELearvrkpAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAFAIGARARAEAEQMAKKAEA 296
Cdd:PRK10929 198 SANNRQELARLRSEL-------AKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINREL 270
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 974141105 297 FQ-LYQEAAQLDMLLEKLPQVAEEIsgpLTSANKITLVSSGSGTMGAAKVTGEVL-DILTRLPE 358
Cdd:PRK10929 271 SQaLNQQAQRMDLIASQQRQAASQT---LQVRQALNTLREQSQWLGVSNALGEALrAQVARLPE 331
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
107-298 |
7.13e-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: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 107 HDDQDYLHS---LG-------KARTAQVQK--------DARIGEAEAKRDAgIREAKAKQEKVSAQYLSEIEMAKAQRDY 168
Cdd:COG4913 592 KDDRRRIRSryvLGfdnraklAALEAELAEleeelaeaEERLEALEAELDA-LQERREALQRLAEYSWDEIDVASAEREI 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 169 ELKKAAYDievNTRRAQADL-AYQLQVAKTKQQIEEQRVQVQVVERA-----QQVAVQEQEIARREKELEARVRKPAEAE 242
Cdd:COG4913 671 AELEAELE---RLDASSDDLaALEEQLEELEAELEELEEELDELKGEigrleKELEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 974141105 243 RYKLERLAEAEKSQLIMQAEAEAASVRMRGEAeafaigARARAEAEQMAKKAEAFQ 298
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENLEERIDALR------ARLNRAEEELERAMRAFN 797
|
|
| SPFH_HflC |
cd03405 |
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ... |
218-301 |
8.35e-03 |
|
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.
Pssm-ID: 259803 [Multi-domain] Cd Length: 249 Bit Score: 37.47 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 218 AVQEQEIARREKElEARVRkpAEAERYKLERLAEAEKSQLIMQAEAEAASVRMRGEAEAfaigARARAEAEQMAKKAEAF 297
Cdd:cd03405 157 SVYERMRAERERI-AAEYR--AEGEEEAEKIRAEADRERTVILAEAYREAEEIRGEGDA----EAARIYAEAYGKDPEFY 229
|
....
gi 974141105 298 QLYQ 301
Cdd:cd03405 230 SFYR 233
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
119-309 |
8.68e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 37.90 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 119 ARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQYLSEIEMAKAQRDYELKKAAYDIEVNTRRAQADLAYQLQVAKTK 198
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974141105 199 QQIEEQRVQVQVVERAQQVAVQE-----QEIARREKElEARVRKPAEAeryKLERLAEAEKSQLIMQAEAEAASVRMRGE 273
Cdd:TIGR02794 133 KAKAEAEAERKAKEEAAKQAEEEakakaAAEAKKKAE-EAKKKAEAEA---KAKAEAEAKAKAEEAKAKAEAAKAKAAAE 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 974141105 274 AEafaigARARAEAeQMAKKAEAFQLYQEAAQLDML 309
Cdd:TIGR02794 209 AA-----AKAEAEA-AAAAAAEAERKADEAELGDIF 238
|
|
| |
