|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
89-399 |
1.27e-112 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 336.89 E-value: 1.27e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 89 QEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQK-HSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGL 167
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 168 EETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKKVHEEEIAELQAQIQYAQISVEM 247
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 248 DVT-KPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMN 326
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990539 327 EALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETR 399
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-400 |
2.95e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 106 ERVHELEQQNKVLEAELLVLRqkhsepsrfralyeqeIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSR 185
Cdd:COG1196 213 ERYRELKEELKELEAELLLLK----------------LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 186 EDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKKVHEE---EIAELQAQIQYAQISVEmdvtkpDLSAALKDIR 262
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEleeELAELEEELEELEEELE------ELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 263 AQYEKLAAKNMQNAEEwfksRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEAcrgmnEALEKQLQELEDKQNA 342
Cdd:COG1196 351 EELEEAEAELAEAEEA----LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-----EEAEEALLERLERLEE 421
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 105990539 343 DISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRL 400
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-400 |
1.39e-10 |
|
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: 64.31 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 106 ERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSR 185
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 186 EDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKKVHEEEIAELQA-QIQYAQISVEMDVTKPDLSAALKDIRAQ 264
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 265 YEKLaaKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDK---QN 341
Cdd:TIGR02168 844 EEQI--EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREleeLR 921
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 105990539 342 ADISAMQDTINKLENELRTTKSEMArylKEYQDLLNVKMALDIEIAAYRKLLEGEETRL 400
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
75-289 |
2.97e-10 |
|
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: 63.15 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 75 QVAAISNDLKSIRTQ---EKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAE 151
Cdd:TIGR02168 790 QIEQLKEELKALREAldeLRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 152 DATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSL-MDEISFLKKVHEEE 230
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLeVRIDNLQERLSEEY 949
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990539 231 IAELQAQIQYAQiSVEMDVTKpdLSAALKDIRAQYEKLAAKNMqNAEEWF---KSRFTVLTE 289
Cdd:TIGR02168 950 SLTLEEAEALEN-KIEDDEEE--ARRRLKRLENKIKELGPVNL-AAIEEYeelKERYDFLTA 1007
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
92-397 |
3.76e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 92 AQLQDLNDRFASFIERVHELEQQNKVLEAELlvlrqkhsepsrfrALYEQEIRDLRLAAEDATNEKQALQGEREGLEETL 171
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAEL--------------AELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 172 RNLQARYEEEVLSREDAEGRLmearkgaDEAALARAELEKRIDSLmdeisflkkvhEEEIAELQAQIQYAQISVEmdvtk 251
Cdd:COG1196 298 ARLEQDIARLEERRRELEERL-------EELEEELAELEEELEEL-----------EEELEELEEELEEAEEELE----- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 252 pDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEacRGMNEALEK 331
Cdd:COG1196 355 -EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE--LEELEEALA 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 105990539 332 QLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEE 397
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-381 |
1.47e-09 |
|
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: 60.84 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 88 TQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEpsrfralyeqeirdLRLAAEDATNEKQALQGEREGL 167
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE--------------LEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 168 EETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKKVHEEEIAELQAQiqyAQISVEM 247
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL---ESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 248 DVTKPDLSAALKDIRAQYEKLAAK---NMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRG 324
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 105990539 325 MNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMA 381
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
70-340 |
2.71e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 70 NLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLA 149
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 150 AEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLkkvhEE 229
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA----LR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 230 EIAELQAQIQYAQISVEmdvtkpDLSAALKDIRAQYEKLAAKNMQNAEEwfksrftvLTESAAKNTDAVRAAKDEVSESR 309
Cdd:COG1196 394 AAAELAAQLEELEEAEE------ALLERLERLEEELEELEEALAELEEE--------EEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270
....*....|....*....|....*....|.
gi 105990539 310 RLLKAKTLEIEACRGMNEALEKQLQELEDKQ 340
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
149-422 |
3.27e-09 |
|
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: 59.01 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 149 AAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKKVHE 228
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 229 EEIAELQAQIQYAQISVEMDVTKPDLSAAlkdiraqyeklAAKNMQNAEEWFKSrftvLTESAAKNTDAVRAAKDEVSES 308
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPE-----------DFLDAVRRLQYLKY----LAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 309 RRLLKAKTLEIEACRGMNEALEKQLQELEDKQnadisamQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAA 388
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAER-------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 105990539 389 YRKLLEGEET-----RLSFTSVGSITSGYSQSSQVFGRS 422
Cdd:COG4942 239 AAERTPAAGFaalkgKLPWPVSGRVVRRFGERDGGGGRN 277
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-401 |
3.39e-09 |
|
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: 59.69 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 139 YEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMD 218
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 219 EISFLKKVHEEEIAEL-QAQIQYAQISVEMDVTKPDLSAALKDIRAQYEKLAAKNMQNAEEwfKSRFTVLTESAAKNTDA 297
Cdd:TIGR02168 755 ELTELEAEIEELEERLeEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL--NEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 298 VRAAKDEVSESRRLLKAKTLEIEAcrgMNEALEkQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLN 377
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIES---LAAEIE-ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260
....*....|....*....|....
gi 105990539 378 VKMALDIEIAAYRKLLEGEETRLS 401
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-371 |
5.98e-09 |
|
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: 58.91 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 74 SQVAAISNDLKSIRTQE---KAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAA 150
Cdd:TIGR02168 691 EKIAELEKALAELRKELeelEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 151 EDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLkkvhEEE 230
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL----EEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 231 IAELQAQIQYAQISVE-MDVTKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRftvltesaakntDAVRAAKDEVSESR 309
Cdd:TIGR02168 847 IEELSEDIESLAAEIEeLEELIEELESELEALLNERASLEEALALLRSELEELS------------EELRELESKRSELR 914
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990539 310 RLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKE 371
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
73-342 |
3.83e-08 |
|
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: 56.22 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 73 LSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAED 152
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 153 ATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLkkvhEEEIA 232
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 233 ELQAQIQYAQISVEMdvTKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRA---AKDEVSESR 309
Cdd:TIGR02168 397 SLNNEIERLEARLER--LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAleeLREELEEAE 474
|
250 260 270
....*....|....*....|....*....|...
gi 105990539 310 RLLKAKTLEIEACRGMNEALEKQLQELEDKQNA 342
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
68-265 |
2.97e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 68 LENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLR 147
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 148 LAAEDATNEKQALQGEREGLEETLRNL---QARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLK 224
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALlerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 105990539 225 KVHEEEIAELQAQIQYAQISVEMDVTKPDLSAALKDIRAQY 265
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
9-88 |
3.74e-07 |
|
Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.
Pssm-ID: 461414 [Multi-domain] Cd Length: 83 Bit Score: 47.77 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 9 YYSTSYKRRYVE--TPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPS-LENLDLSQVAAISNDLKS 85
Cdd:pfam04732 1 YSSSSYRRMFGDssSSRPSYSSSSGSRSVSSRSYSRSSSSSPSSSSRRSSRSSSRSSYPSLaADSLDFSLADALNQEFKA 80
|
...
gi 105990539 86 IRT 88
Cdd:pfam04732 81 TRT 83
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
83-383 |
1.55e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 83 LKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAEL-----LVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEK 157
Cdd:pfam15921 215 FRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESqnkieLLLQQHQDRIEQLISEHEVEITGLTEKASSARSQA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 158 QALQGEREGLEETLRNLQARYEEEVlsredaegrlmearkgadeaalarAELEKRIDSLMDEISFLKKVHEEEIAELQAQ 237
Cdd:pfam15921 295 NSIQSQLEIIQEQARNQNSMYMRQL------------------------SDLESTVSQLRSELREAKRMYEDKIEELEKQ 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 238 IQYA------------QISVEMDVTKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTesaakntdavraakdeV 305
Cdd:pfam15921 351 LVLAnseltearterdQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSIT----------------I 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 306 SESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINK---LENELRTTKsEMARylKEYQDLLNVKMAL 382
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTK-EMLR--KVVEELTAKKMTL 491
|
.
gi 105990539 383 D 383
Cdd:pfam15921 492 E 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-394 |
2.11e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 152 DATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARK--GADEAALARAELEKRIDSLMDEISFLKKVHeE 229
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDASS-D 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 230 EIAELQAQIQYAQisvemdvtkpdlsAALKDIRAQYEKLAAKNMQNAEEWfksrfTVLTESAAKNTDAVRAAKDEVSESR 309
Cdd:COG4913 686 DLAALEEQLEELE-------------AELEELEEELDELKGEIGRLEKEL-----EQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 310 RLLKAKTLEieacrgmNEALEKQLQELEDKQNADISAMQDTINKLENELRTTkseMARYLKEYQDLLNvkmALDIEIAA- 388
Cdd:COG4913 748 RALLEERFA-------AALGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETA---DLDADLESl 814
|
....*...
gi 105990539 389 --YRKLLE 394
Cdd:COG4913 815 peYLALLD 822
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
89-270 |
2.66e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 89 QEKAQLQDLNDRFASFIERVHELEQQNKVLEAellvLRQKHSEpsRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLE 168
Cdd:COG4913 249 EQIELLEPIRELAERYAAARERLAELEYLRAA----LRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 169 ETLRNLQARYEEEVLSR-EDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFlkkvHEEEIAELQAQIQ-----YAQ 242
Cdd:COG4913 323 EELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPA----SAEEFAALRAEAAalleaLEE 398
|
170 180
....*....|....*....|....*...
gi 105990539 243 ISVEMDVTKPDLSAALKDIRAQYEKLAA 270
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
99-398 |
6.46e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 99 DRFASFIERVHELEQQNKVLEAELL-----------VLRQKHSEPSRFRALYEqEIRDLRLAAEDATNEKQALQGEREGL 167
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEevlreineissELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 168 EETLRNLQARYEE---EVLSREDAEGRLMEARKGADEAALARAELEKRIDSLmDEISFLKKVHEEEIAELQAQIQYAQis 244
Cdd:PRK03918 258 EEKIRELEERIEElkkEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEINGIEERIKELE-- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 245 vEMDVTKPDLSAALKDIRAQYEKLA--------AKNMQNAEEWFKSRFTVLT-ESAAKNTDAVRAAKDEVSESRRLLKAK 315
Cdd:PRK03918 335 -EKEERLEELKKKLKELEKRLEELEerhelyeeAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 316 TLEIEacrGMNEALEKQLQELED--------KQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIA 387
Cdd:PRK03918 414 IGELK---KEIKELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330
....*....|.
gi 105990539 388 AYRKLLEGEET 398
Cdd:PRK03918 491 KESELIKLKEL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-290 |
1.22e-05 |
|
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: 48.13 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 72 DLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEpsrfralYEQEIRDLRLAAE 151
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-------LEEQLETLRSKVA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 152 DATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALA--RAELEKRIDSLMDEISFLKKVhEE 229
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEelEEELEELQEELERLEEALEEL-RE 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990539 230 EIAELQAQIQYAQISVEmdvTKPDLSAALKDIRAQYEKL--AAKNMQNAEEWFKSRFTVLTES 290
Cdd:TIGR02168 469 ELEEAEQALDAAERELA---QLQARLDSLERLQENLEGFseGVKALLKNQSGLSGILGVLSEL 528
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
92-276 |
2.84e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 92 AQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREgleetL 171
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE-----Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 172 RNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKKVHEEEIAELQAQIqyAQISVEMDVTK 251
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL--EELEAEREELA 169
|
170 180
....*....|....*....|....*
gi 105990539 252 PDLSAalkDIRAQYEKLAAKNMQNA 276
Cdd:COG1579 170 AKIPP---ELLALYERIRKRKNGLA 191
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
73-239 |
3.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 73 LSQVAAISNDLKSIRtQEKAQLQDLNDRFASFI--ERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLA- 149
Cdd:COG4913 254 LEPIRELAERYAAAR-ERLAELEYLRAALRLWFaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQi 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 150 AEDATNEKQALQGEREGLEETLRNLQ---ARYEEEV----LSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISF 222
Cdd:COG4913 333 RGNGGDRLEQLEREIERLERELEERErrrARLEALLaalgLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
170
....*....|....*..
gi 105990539 223 LKKVHEEEIAELQAQIQ 239
Cdd:COG4913 413 ALRDLRRELRELEAEIA 429
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-289 |
3.64e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 72 DLSQVAAISNDLKSIRTQEKAQLQDLNDRFASF--IERVHELEQQNKVLEAELLVLRQKHSE----PSRFRALYEQ---- 141
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAELERldasSDDLAALEEQleel 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 142 --EIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEE-----EVLSREDAEGRLMEARKGADEAALaRAELEKRID 214
Cdd:COG4913 698 eaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlaRLELRALLEERFAAALGDAVEREL-RENLEERID 776
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990539 215 SLMDEISflkkVHEEEIAELQAQI--QYAQISVEMDVTkpdlSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTE 289
Cdd:COG4913 777 ALRARLN----RAEEELERAMRAFnrEWPAETADLDAD----LESLPEYLALLDRLEEDGLPEYEERFKELLNENSI 845
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
91-225 |
5.54e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 91 KAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSE-PSRFRALYEQEIRDLRLAAEDATNEKQALQ-------- 161
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEallaalgl 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 105990539 162 ---GEREGLEETLRNLQARyeeevlsREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKK 225
Cdd:COG4913 374 plpASAEEFAALRAEAAAL-------LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
75-381 |
6.36e-05 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 75 QVAAISNDLKSI---RTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLvlrqkHSEPSRFRALY---EQEIRDLRL 148
Cdd:TIGR02169 738 RLEELEEDLSSLeqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS-----HSRIPEIQAELsklEEEVSRIEA 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 149 AAEDATNEKQALQGEREGLEETLRNLQARyeeevlsredaegrlmearkgadeaalaRAELEKRIDSLMDEISFLKKvhe 228
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQ----------------------------RIDLKEQIKSIEKEIENLNG--- 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 229 eEIAELQAQIQYAQISVEmdvtkpDLSAALKDIRAQYEKLAAK--NMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVS 306
Cdd:TIGR02169 862 -KKEELEEELEELEAALR------DLESRLGDLKKERDELEAQlrELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990539 307 ESRRLLKAkTLEIEACRGMNEALEKQLQELEdkqnADISAMQDTINKLENELrttkSEMARYLKEYQDLLNVKMA 381
Cdd:TIGR02169 935 EIEDPKGE-DEEIPEEELSLEDVQAELQRVE----EEIRALEPVNMLAIQEY----EEVLKRLDELKEKRAKLEE 1000
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
91-271 |
8.87e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 91 KAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIrDLRLAAEdatnEKQALQGEREGLEET 170
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVASAER----EIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 171 ---LRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEI-SFLKKVHEEEIAELQAQIQYAQISVE 246
Cdd:COG4913 684 sddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeAAEDLARLELRALLEERFAAALGDAV 763
|
170 180
....*....|....*....|....*
gi 105990539 247 MDVTKPDLSAALKDIRAQYEKLAAK 271
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEE 788
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
87-270 |
1.19e-04 |
|
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: 44.37 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 87 RTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREG 166
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 167 LEETL--------RNLQARYEEEVLSREDAE---------GRLMEARKG-ADEAALARAELEKRIDSL---MDEISFLKK 225
Cdd:COG4942 102 QKEELaellralyRLGRQPPLALLLSPEDFLdavrrlqylKYLAPARREqAEELRADLAELAALRAELeaeRAELEALLA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 105990539 226 VHEEEIAELQAQI-QYAQISVEMDVTKPDLSAALKDIRAQYEKLAA 270
Cdd:COG4942 182 ELEEERAALEALKaERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
132-271 |
1.21e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 132 PSRFRALYE-----QEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRL--MEARKGADEAAL 204
Cdd:COG1579 3 PEDLRALLDlqeldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeeVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 205 ARAELEKRIDSLMDEISFLKK---VHEEEIAELQAQI------------QYAQISVEMDVTKPDLSAALKDIRAQYEKLA 269
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRrisDLEDEILELMERIeeleeelaeleaELAELEAELEEKKAELDEELAELEAELEELE 162
|
..
gi 105990539 270 AK 271
Cdd:COG1579 163 AE 164
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
112-398 |
1.36e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 112 EQQNKVLeaeLLVLRQKhSEPSrFRALYEQ---EIRDLRlaAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREda 188
Cdd:PRK05771 4 VRMKKVL---IVTLKSY-KDEV-LEALHELgvvHIEDLK--EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLRE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 189 egRLMEARKGADEAALARAE-----LEKRIDSLMDEISFLkkvhEEEIAELQAQIQYAQI--SVEMDvtkPDLSAALKDI 261
Cdd:PRK05771 75 --EKKKVSVKSLEELIKDVEeelekIEKEIKELEEEISEL----ENEIKELEQEIERLEPwgNFDLD---LSLLLGFKYV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 262 RAQYEKLAAKNMQNAEEWFKSRFtVLTESAAKNTD--AVRAAKDEVSESRRLLKAktleieacrgmNEALEKQLQELEDK 339
Cdd:PRK05771 146 SVFVGTVPEDKLEELKLESDVEN-VEYISTDKGYVyvVVVVLKELSDEVEEELKK-----------LGFERLELEEEGTP 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 105990539 340 QNAdISAMQDTINKLENELRTTKSEMARYLKEYQDL-LNVKMALDIEIA---AYRKLLEGEET 398
Cdd:PRK05771 214 SEL-IREIKEELEEIEKERESLLEELKELAKKYLEElLALYEYLEIELEraeALSKFLKTDKT 275
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
127-233 |
1.09e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 127 QKHSEPSRFRALyEQEIRDLRLAAEDATNEK--------QALQGEREGLEETLRNLQARYEEEvlsrEDAEGRLMEARKG 198
Cdd:COG0542 405 EIDSKPEELDEL-ERRLEQLEIEKEALKKEQdeasferlAELRDELAELEEELEALKARWEAE----KELIEEIQELKEE 479
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 105990539 199 ADEAALARAELEKRIDSLMDEISFLKK-----VHEEEIAE 233
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPllreeVTEEDIAE 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
89-244 |
1.15e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 89 QEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQA--------- 159
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLeeleerlee 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 160 ---LQGEREGLEETLRNLQAR-YEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKKVHEEEIAELQ 235
Cdd:COG4717 158 lreLEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
....*....
gi 105990539 236 AQIQYAQIS 244
Cdd:COG4717 238 AAALEERLK 246
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
75-446 |
2.12e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 75 QVAAISNDLKSIR--TQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAED 152
Cdd:pfam15921 449 QMAAIQGKNESLEkvSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 153 ATNEKQALQGEreglEETLRNLQARYEE------------EVLSREDAEGRLMEARKGADEAAL--ARAELEKRIDSL-- 216
Cdd:pfam15921 529 KLQELQHLKNE----GDHLRNVQTECEAlklqmaekdkviEILRQQIENMTQLVGQHGRTAGAMqvEKAQLEKEINDRrl 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 217 -MDEISFLKKVHEEEIAELQAQIQYAQIS-VEMDVTKPDLSAALKDIRAQYEKLAAK---------NMQNAEEWFKSRFT 285
Cdd:pfam15921 605 eLQEFKILKDKKDAKIRELEARVSDLELEkVKLVNAGSERLRAVKDIKQERDQLLNEvktsrnelnSLSEDYEVLKRNFR 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 286 VLTESAAKNTDAVR----AAKDEVSESRRLLKAK--------------TLEIEACRGMNEALEKQLQELED--------- 338
Cdd:pfam15921 685 NKSEEMETTTNKLKmqlkSAQSELEQTRNTLKSMegsdghamkvamgmQKQITAKRGQIDALQSKIQFLEEamtnankek 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 339 --------KQNADISAMQDTINKLENELRTTKSEmARYLKEyqDLLNVKMALD---IEIAAYRKLL---EGEETRLSFTS 404
Cdd:pfam15921 765 hflkeeknKLSQELSTVATEKNKMAGELEVLRSQ-ERRLKE--KVANMEVALDkasLQFAECQDIIqrqEQESVRLKLQH 841
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 105990539 405 VGSITS----GYSQSSQVFGR--SAYGGLQTSSYLMSTRSFPSYYTSH 446
Cdd:pfam15921 842 TLDVKElqgpGYTSNSSMKPRllQPASFTRTHSNVPSSQSTASFLSHH 889
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
185-401 |
2.22e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 185 REDAEGRLMEARKGADEAALARAELEKRIDSLmdeisflkkvheeeiaELQAQI--QYAQisvemdvtkpdLSAALKDIR 262
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPL----------------ERQAEKaeRYRE-----------LKEELKELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 263 AQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELE---DK 339
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiAR 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990539 340 QNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLS 401
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
72-376 |
2.34e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 72 DLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEqqnkVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAae 151
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIAETEREREELAEEVRDLRER-- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 152 datnekqalqgeREGLEETLRNLQARYEEEVLSREDAEGRlmearkgadeaalaRAELEKRIDSLmdeisflkkvhEEEI 231
Cdd:PRK02224 288 ------------LEELEEERDDLLAEAGLDDADAEAVEAR--------------REELEDRDEEL-----------RDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 232 AELQAQIQyaqisvemdvtkpdlsAALKDIRAQYEKLAAKNMQNAEewfksrftvLTESAAKNTDAVRAAKDEVSESRRL 311
Cdd:PRK02224 331 EECRVAAQ----------------AHNEEAESLREDADDLEERAEE---------LREEAAELESELEEAREAVEDRREE 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990539 312 LKAKTLEIEACRGMNEALEKQLQELEDKqNADISAMQDTINKLENELRTTKSEMARYLKEYQDLL 376
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDF-LEELREERDELREREAELEATLRTARERVEEAEALL 449
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
78-242 |
3.34e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 78 AISNDLKSIRTQEKAQLQdlndrfasfiervHELEQQNKVLEAELLVLRQKHSepSRFRALYEQeIRDLRLAAEDATNEK 157
Cdd:pfam01576 316 AAQQELRSKREQEVTELK-------------KALEEETRSHEAQLQEMRQKHT--QALEELTEQ-LEQAKRNKANLEKAK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 158 QALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKKVHEE-------- 229
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEaegknikl 459
|
170
....*....|....*
gi 105990539 230 --EIAELQAQIQYAQ 242
Cdd:pfam01576 460 skDVSSLESQLQDTQ 474
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
74-358 |
3.54e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 74 SQVAAISNDLKSIRTQ---EKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRAL------------ 138
Cdd:PRK02224 384 EEIEELEEEIEELRERfgdAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpveg 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 139 ---------YEQEIRDLRLAAEDATNEKQALQGEREGLEEtLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAEL 209
Cdd:PRK02224 464 sphvetieeDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 210 EKRIDSLMDEisflKKVHEEEIAELQAQIQYAQISV-EMDVTKPDLSAALKDIRAQYEKLAAknMQNAEEWFKSRFTVLT 288
Cdd:PRK02224 543 RERAAELEAE----AEEKREAAAEAEEEAEEAREEVaELNSKLAELKERIESLERIRTLLAA--IADAEDEIERLREKRE 616
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 105990539 289 ESAAKNtDAVRAAKDEVSESRRLLKAKTLE--IEACRGMNEALEKQLQELEDK---QNADISAMQDTINKLENEL 358
Cdd:PRK02224 617 ALAELN-DERRERLAEKRERKRELEAEFDEarIEEAREDKERAEEYLEQVEEKldeLREERDDLQAEIGAVENEL 690
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
188-445 |
3.57e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 188 AEGRLMEARKGADEAALARAELEKRIDSLMDEISFLkkvhEEEIAELQAQIQYAQisVEMDVTKPDLSAALKDIRAQYEK 267
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEEL----NEEYNELQAELEALQ--AEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 268 LA--AKNMQNAEEWFK------------------SRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNE 327
Cdd:COG3883 88 LGerARALYRSGGSVSyldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 328 ALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEyQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGS 407
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA-AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260 270
....*....|....*....|....*....|....*...
gi 105990539 408 ITSGYSQSSQVFGRSAYGGLQTSSYLMSTRSFPSYYTS 445
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGG 284
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
144-388 |
3.70e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 144 RDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEevlsredaegrlMEARKGADEAALARAELEKRIDSLMDEISFL 223
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEE------------FRQKNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 224 kkvhEEEIAELQAQIQYAQISVEMDV-TKPDL--SAALKDIRAQYEKLaaknmqnaeewfKSRFTVLTESAAKNTDAVRA 300
Cdd:COG3206 232 ----RAELAEAEARLAALRAQLGSGPdALPELlqSPVIQQLRAQLAEL------------EAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 301 AKDEVSESRRLLKAKTLEI-EACRGMNEALEKQLQELEdKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVK 379
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQ-AQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
|
....*....
gi 105990539 380 MALDIEIAA 388
Cdd:COG3206 375 EEARLAEAL 383
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
83-400 |
4.90e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 83 LKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALyEQEIRDLR-----LAAEDATNEK 157
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK-KEELERLKkrltgLTPEKLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 158 QALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAEL--EKRIDSLMDEISFLKKVHEE--EIAE 233
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKElkEIEE 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 234 LQAQIQYAQISVEMDVTKPD----LSAALKDIRAQYEKLAAKNMQNAEEWFKsRFTVLTESAAKNTDAVRAAKDEVSESR 309
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESelikLKELAEQLKELEEKLKKYNLEELEKKAE-EYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 310 RLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLE------NELRTTKSEMARYLKEYQDLLNvkmald 383
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEE------ 626
|
330
....*....|....*..
gi 105990539 384 iEIAAYRKLLEGEETRL 400
Cdd:PRK03918 627 -ELDKAFEELAETEKRL 642
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
74-221 |
5.08e-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: 39.36 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 74 SQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYE-------QEIRDL 146
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKylaparrEQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 147 RLAAEDATNEKQALQGEREGLEETLRNLQA---RYEEEVLSREDAEGRLmEARKGADEAALA-----RAELEKRIDSLMD 218
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEeraALEALKAERQKLLARL-EKELAELAAELAelqqeAEELEALIARLEA 234
|
...
gi 105990539 219 EIS 221
Cdd:COG4942 235 EAA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-359 |
5.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 141 QEIRDLRLAAEDATNEKQALQGeregleetLRNLQARYEEEVLSREDAEGRLMEARkgADEAALARAELEKRIDSLMDEI 220
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP--------IRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 221 SFLkkvhEEEIAELQAQIQyaqisvemdvtkpDLSAALKDIRAQYEKLAAKNMQNAE---EWFKSRFTVLTESAAKNTDA 297
Cdd:COG4913 305 ARL----EAELERLEARLD-------------ALREELDELEAQIRGNGGDRLEQLEreiERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 105990539 298 VRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELR 359
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
140-239 |
5.55e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.10 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 140 EQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVlsredaegRLMEArKGADEAALARAELEKRIDSLMDE 219
Cdd:cd16269 197 EKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHL--------RQLKE-KMEEERENLLKEQERALESKLKE 267
|
90 100
....*....|....*....|.
gi 105990539 220 I-SFLKKVHEEEIAELQAQIQ 239
Cdd:cd16269 268 QeALLEEGFKEQAELLQEEIR 288
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
68-374 |
5.74e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 68 LENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLR 147
Cdd:TIGR04523 297 ISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 148 laaedatNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADeaalaraELEKRIDSLMDEISFLKkvh 227
Cdd:TIGR04523 377 -------KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE-------LLEKEIERLKETIIKNN--- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 228 eEEIAELQAQIQYAQISV-EMDVTKPDLSAALKDIRAQYEKLaAKNMQNAEEWFKSRFTVLTESAAKNTD---AVRAAKD 303
Cdd:TIGR04523 440 -SEIKDLTNQDSVKELIIkNLDNTRESLETQLKVLSRSINKI-KQNLEQKQKELKSKEKELKKLNEEKKEleeKVKDLTK 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 304 EVSESrrLLKAKTLEIEACRgmneaLEKQLQELEDKQNAD------------ISAMQDTINKLENE---LRTTKSEMARY 368
Cdd:TIGR04523 518 KISSL--KEKIEKLESEKKE-----KESKISDLEDELNKDdfelkkenlekeIDEKNKEIEELKQTqksLKKKQEEKQEL 590
|
....*.
gi 105990539 369 LKEYQD 374
Cdd:TIGR04523 591 IDQKEK 596
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
147-401 |
5.92e-03 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 147 RLAAEDATNEK-QALQGEREGLEETLrnLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFL-- 223
Cdd:TIGR02169 202 RLRREREKAERyQALLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnk 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 224 --KKVHEEEIAELQAQIQYAQISVEmdvtkpDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLT-----ESAAKNTD 296
Cdd:TIGR02169 280 kiKDLGEEEQLRVKEKIGELEAEIA------SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElereiEEERKRRD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 297 AVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLL 376
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
250 260
....*....|....*....|....*
gi 105990539 377 NVKMALDIEIAAYRKLLEGEETRLS 401
Cdd:TIGR02169 434 AKINELEEEKEDKALEIKKQEWKLE 458
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
119-373 |
7.00e-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: 39.55 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 119 EAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDAtneKQALQGeregleetLRNLQARYeeEVLSREDAEGRLMEARKG 198
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQL---KEQLQL--------LNKLLPQA--NLLADETLADRLEELREE 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 199 ADEAALARAELE---KRIDSLMDEISFLKKVHEEEiAELQAQIQYAQISVEMDVTKPDlsaALKDIRAQ-----YEKLAA 270
Cdd:COG3096 902 LDAAQEAQAFIQqhgKALAQLEPLVAVLQSDPEQF-EQLQADYLQAKEQQRRLKQQIF---ALSEVVQRrphfsYEDAVG 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 271 KNMQNAE--EWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELE--DKQNADISA 346
Cdd:COG3096 978 LLGENSDlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGvqADAEAEERA 1057
|
250 260
....*....|....*....|....*..
gi 105990539 347 mQDTINKLENELRTTKSEMARYLKEYQ 373
Cdd:COG3096 1058 -RIRRDELHEELSQNRSRRSQLEKQLT 1083
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
86-271 |
8.23e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 86 IRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHS--EPSRFRALYEQEIRDLRLAAEDATNEKQALQGE 163
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 164 REGLEETLRNlqaryEEEVLSREDAEGRLMEARKGADEAALARAELEKR-------IDSLMDEISFLKKVHEEEI----A 232
Cdd:COG3206 242 LAALRAQLGS-----GPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAqrilA 316
|
170 180 190
....*....|....*....|....*....|....*....
gi 105990539 233 ELQAQIQYAQISVEmdvtkpDLSAALKDIRAQYEKLAAK 271
Cdd:COG3206 317 SLEAELEALQAREA------SLQAQLAQLEARLAELPEL 349
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
70-402 |
9.15e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 38.95 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 70 NLDLSQVAAISNDLKS-IRTQEKAQLQDLNDRFASfIERVHELEQQnkvLEAELLVLRQKHSEPSRFRALYEQEIRDLrl 148
Cdd:pfam15921 425 NMEVQRLEALLKAMKSeCQGQMERQMAAIQGKNES-LEKVSSLTAQ---LESTKEMLRKVVEELTAKKMTLESSERTV-- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 149 aaEDATNEKQALQGEREGLEETLRNLQARYE---EEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIsflkk 225
Cdd:pfam15921 499 --SDLTASLQEKERAIEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQI----- 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 226 vheEEIAELQAQiqYAQISVEMDVTKPDLSAALKDIRAQYEKLAA-KNMQNAE-EWFKSRFTVLTESAAKNTDA----VR 299
Cdd:pfam15921 572 ---ENMTQLVGQ--HGRTAGAMQVEKAQLEKEINDRRLELQEFKIlKDKKDAKiRELEARVSDLELEKVKLVNAgserLR 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 105990539 300 AAKDEVSESRRLLKaktlEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDL---- 375
Cdd:pfam15921 647 AVKDIKQERDQLLN----EVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMegsd 722
|
330 340 350
....*....|....*....|....*....|
gi 105990539 376 ---LNVKMALDIEIAAYRKLLEGEETRLSF 402
Cdd:pfam15921 723 ghaMKVAMGMQKQITAKRGQIDALQSKIQF 752
|
|
| |
