|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
89-400 |
1.30e-114 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 342.29 E-value: 1.30e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 89 QEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQK-HSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGL 167
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 168 EETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEM 247
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 248 DVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMN 327
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13929098 328 EALEKQLQELEDKQNADISAMQDTINKLENELRSTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETR 400
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-401 |
5.12e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 106 ERVHELEQQNKVLEAELLVLRqkhsepsrfralyeqeIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSR 185
Cdd:COG1196 213 ERYRELKEELKELEAELLLLK----------------LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 186 EDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLkkvhEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQ 265
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 266 YEKLAAKNMQNAEEwfksRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEAcrgmnEALEKQLQELEDKQNADI 345
Cdd:COG1196 353 LEEAEAELAEAEEA----LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-----EEAEEALLERLERLEEEL 423
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 13929098 346 SAMQDTINKLENELRSTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRL 401
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-401 |
2.27e-11 |
|
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: 66.62 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 106 ERVHELEQQNKVLEAELLVLRQKHSEpsrfralYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSR 185
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 186 EDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLK---KVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDI 262
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 263 RAQYEKLA--AKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDK 340
Cdd:TIGR02168 837 ERRLEDLEeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13929098 341 ---QNADISAMQDTINKLENELRSTKSEMArylKEYQDLLNVKMALDIEIAAYRKLLEGEETRL 401
Cdd:TIGR02168 917 leeLREKLAQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
75-290 |
3.86e-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: 62.77 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 75 QVAAISNDLKSIRTQ---EKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAE 151
Cdd:TIGR02168 790 QIEQLKEELKALREAldeLRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 152 DATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSL-MDEIAFLKKVHEEE 230
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLeVRIDNLQERLSEEY 949
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13929098 231 IAELQAQIQyaqiSVEMDVSSKPDLSAALKDIRAQYEKLAAKNMqNAEEWF---KSRFTVLTE 290
Cdd:TIGR02168 950 SLTLEEAEA----LENKIEDDEEEARRRLKRLENKIKELGPVNL-AAIEEYeelKERYDFLTA 1007
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-388 |
9.70e-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: 61.61 E-value: 9.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 139 YEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMD 218
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 219 EIAFL-----------------KKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKD--IRAQYEKLAAKNMQNAEE 279
Cdd:TIGR02168 755 ELTELeaeieeleerleeaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlnEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 280 WFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEAcrgmNEALEKQLQELEDKQNADISAMQDTINKLENEL 359
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA----LLNERASLEEALALLRSELEELSEELRELESKR 910
|
250 260
....*....|....*....|....*....
gi 13929098 360 RstksEMARYLKEYQDLLNvKMALDIEIA 388
Cdd:TIGR02168 911 S----ELRRELEELREKLA-QLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
92-395 |
1.17e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 92 AQLQDLNDRFASFIERVHELEQQNKVLEAELlvlrqkhsepsrfrALYEQEIRDLRLAAEDATNEKQALQGEREGLEETL 171
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAEL--------------AELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 172 RNLQARYEEEVLSREDAEGRLmearkgaDEAALARAELEKRIDSLmdeiaflkkvhEEEIAELQAQIQYAQISVEmdvss 251
Cdd:COG1196 298 ARLEQDIARLEERRRELEERL-------EELEEELAELEEELEEL-----------EEELEELEEELEEAEEELE----- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 252 kpDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEacRGMNEALE 331
Cdd:COG1196 355 --EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE--LEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13929098 332 KQLQELEDKQNADISAMQDTINKLENELRSTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLE 395
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
88-382 |
1.52e-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: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 88 TQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEpsrfralyeqeirdLRLAAEDATNEKQALQGEREGL 167
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE--------------LEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 168 EETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQ-YAQISVE 246
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 247 MDvsskpDLSAALKDIRAQYEKLAAK---NMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEAC 323
Cdd:TIGR02168 381 LE-----TLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 13929098 324 RGMNEALEKQLQELEDKQNADISAMQDTINKLENELRSTKSEMARYLKEYQDLLNVKMA 382
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
70-341 |
3.49e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 70 NLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLA 149
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 150 AEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLkkvhEE 229
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA----LR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 230 EIAELQAQIQYAQISVEmdvsskpDLSAALKDIRAQYEKLAAKNMQNAEEwfksrftvLTESAAKNTDAVRAAKDEVSES 309
Cdd:COG1196 394 AAAELAAQLEELEEAEE-------ALLERLERLEEELEELEEALAELEEE--------EEEEEEALEEAAEEEAELEEEE 458
|
250 260 270
....*....|....*....|....*....|..
gi 13929098 310 RRLLKAKTLEIEACRGMNEALEKQLQELEDKQ 341
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
149-423 |
4.82e-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: 58.24 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 149 AAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHE 228
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 229 EEIAELQAQIQYAQISvemdvSSKPDLSAALkdiRAQYEKLAAKNMQnaeewfksRFTVLTESAAKNTDAVRAAKDEVSE 308
Cdd:COG4942 101 AQKEELAELLRALYRL-----GRQPPLALLL---SPEDFLDAVRRLQ--------YLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 309 SRRLLKAKTLEIEACRGMNEALEKQLQELEDKQnadisamQDTINKLENELRSTKSEMARYLKEYQDLLNVKMALDIEIA 388
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAER-------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 13929098 389 AYRKLLEGEET-----RLSFTSVGSITSGYSQSSQVFGRS 423
Cdd:COG4942 238 AAAERTPAAGFaalkgKLPWPVSGRVVRRFGERDGGGGRN 277
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-372 |
4.97e-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: 59.30 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 74 SQVAAISNDLKSIRTQE---KAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAA 150
Cdd:TIGR02168 691 EKIAELEKALAELRKELeelEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 151 EDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLkkvhEEE 230
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL----EEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 231 IAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRftvltesaakntDAVRAAKDEVSESR 310
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS------------EELRELESKRSELR 914
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13929098 311 RLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRSTKSEMARYLKE 372
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
73-343 |
5.91e-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: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 73 LSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAED 152
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 153 ATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLkkvhEEEIA 232
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 233 ELQAQIQYAQISVEMDVSSKPDLSAalkDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRA---AKDEVSES 309
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQ---EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAleeLREELEEA 473
|
250 260 270
....*....|....*....|....*....|....
gi 13929098 310 RRLLKAKTLEIEACRGMNEALEKQLQELEDKQNA 343
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
72-315 |
2.20e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 72 DLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAE 151
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 152 DATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLkkvhEEEI 231
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL----LERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 232 AELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEwfKSRFTVLTESAAKNTDAVRAAKDEVSESRR 311
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL--LAELLEEAALLEAALAELLEELAEAAARLL 494
|
....
gi 13929098 312 LLKA 315
Cdd:COG1196 495 LLLE 498
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
9-88 |
7.78e-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: 47.00 E-value: 7.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 9 YFSTSYKRRYVE--TPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPS-LENLDLSQVAAISNDLKS 85
Cdd:pfam04732 1 YSSSSYRRMFGDssSSRPSYSSSSGSRSVSSRSYSRSSSSSPSSSSRRSSRSSSRSSYPSLaADSLDFSLADALNQEFKA 80
|
...
gi 13929098 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. ... |
83-384 |
1.36e-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: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 83 LKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAEL-----LVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEK 157
Cdd:pfam15921 215 FRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESqnkieLLLQQHQDRIEQLISEHEVEITGLTEKASSARSQA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 158 QALQGEREGLEETLRNLQARYEEEVlsredaegrlmearkgadeaalarAELEKRIDSLMDEIAFLKKVHEEEIAELQAQ 237
Cdd:pfam15921 295 NSIQSQLEIIQEQARNQNSMYMRQL------------------------SDLESTVSQLRSELREAKRMYEDKIEELEKQ 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 238 IQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEwfksrFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKT 317
Cdd:pfam15921 351 LVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKE-----LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRN 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 318 LEIEACRGMNEALEKQLQELEDKQNADISAMQDTINK---LENELRSTKsEMARylKEYQDLLNVKMALD 384
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTK-EMLR--KVVEELTAKKMTLE 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-395 |
2.18e-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: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 152 DATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARK--GADEAALARAELEKRIDSLMDEIAFLKKVHeE 229
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDASS-D 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 230 EIAELQAQIQYAQisvemdvsskpdlsAALKDIRAQYEKLAAKNMQNAEEWfksrfTVLTESAAKNTDAVRAAKDEVSES 309
Cdd:COG4913 686 DLAALEEQLEELE--------------AELEELEEELDELKGEIGRLEKEL-----EQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 310 RRLLKAKTLEieacrgmNEALEKQLQELEDKQNADISAMQDTINKLENELRSTkseMARYLKEYQDLLNvkmALDIEIAA 389
Cdd:COG4913 747 LRALLEERFA-------AALGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETA---DLDADLES 813
|
....*....
gi 13929098 390 ---YRKLLE 395
Cdd:COG4913 814 lpeYLALLD 822
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
112-399 |
4.23e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.54 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 112 EQQNKVLeaeLLVLRQKhSEPSrFRALYEQ---EIRDLRlaAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREda 188
Cdd:PRK05771 4 VRMKKVL---IVTLKSY-KDEV-LEALHELgvvHIEDLK--EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLRE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 189 egRLMEARKGADEAALARAE-----LEKRIDSLMDEIAFLkkvhEEEIAELQAQIQyaQISVEMDVSSKPDLSAALKDIR 263
Cdd:PRK05771 75 --EKKKVSVKSLEELIKDVEeelekIEKEIKELEEEISEL----ENEIKELEQEIE--RLEPWGNFDLDLSLLLGFKYVS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 264 AQYEKLAAKNMQNAEEWFKSRFtVLTESAAKNTD--AVRAAKDEVSESRRLLKAktleieacrgmNEALEKQLQELEDKQ 341
Cdd:PRK05771 147 VFVGTVPEDKLEELKLESDVEN-VEYISTDKGYVyvVVVVLKELSDEVEEELKK-----------LGFERLELEEEGTPS 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13929098 342 NAdISAMQDTINKLENELRSTKSEMARYLKEYQDL-LNVKMALDIEIA---AYRKLLEGEET 399
Cdd:PRK05771 215 EL-IREIKEELEEIEKERESLLEELKELAKKYLEElLALYEYLEIELEraeALSKFLKTDKT 275
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
99-399 |
4.41e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 99 DRFASFIERVHELEQQNKVLEAELL-----------VLRQKHSEPSRFRALYEqEIRDLRLAAEDATNEKQALQGEREGL 167
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEevlreineissELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 168 EETLRNLQARYEE---EVLSREDAEGRLMEARKGADEAALARAELEKRIDSLmDEIAFLKKVHEEEIAELQAQIQYAqis 244
Cdd:PRK03918 258 EEKIRELEERIEElkkEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEINGIEERIKEL--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 245 vEMDVSSKPDLSAALKDIRAQYEKLA--------AKNMQNAEEWFKSRFTVLT-ESAAKNTDAVRAAKDEVSESRRLLKA 315
Cdd:PRK03918 334 -EEKEERLEELKKKLKELEKRLEELEerhelyeeAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 316 KTLEIEACRGmneALEKQLQELED--------KQNADISAMQDTINKLENELRSTKSEMARYLKEYQDLLNVKMALDIEI 387
Cdd:PRK03918 413 RIGELKKEIK---ELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
|
330
....*....|..
gi 13929098 388 AAYRKLLEGEET 399
Cdd:PRK03918 490 KKESELIKLKEL 501
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
89-272 |
1.74e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 89 QEKAQLQDLNDRFASFIERVHELEQQNKVLEAellvLRQKHSEpsRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLE 168
Cdd:COG4913 249 EQIELLEPIRELAERYAAARERLAELEYLRAA----LRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 169 ETLRNLQARYEEEVLSR-EDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFlkkvHEEEIAELQAQIQYAqisvem 247
Cdd:COG4913 323 EELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPA----SAEEFAALRAEAAAL------ 392
|
170 180
....*....|....*....|....*
gi 13929098 248 dvssKPDLSAALKDIRAQYEKLAAK 272
Cdd:COG4913 393 ----LEALEEELEALEEALAEAEAA 413
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
87-279 |
1.91e-05 |
|
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: 47.07 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 87 RTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREG 166
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 167 LEETL--------RNLQARYEEEVLSREDAEGRLMEARKgADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQ--- 235
Cdd:COG4942 102 QKEELaellralyRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEall 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13929098 236 AQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEE 279
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
91-225 |
3.33e-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: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 91 KAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSE-PSRFRALYEQEIRDLRLAAEDATNEKQALQ-------- 161
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEallaalgl 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13929098 162 ---GEREGLEETLRNLQARyeeevlsREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKK 225
Cdd:COG4913 374 plpASAEEFAALRAEAAAL-------LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-290 |
3.33e-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: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 72 DLSQVAAISNDLKSIRTQEKAQLQDLNDRFASF--IERVHELEQQNKVLEAELLVLRQKHSE----PSRFRALYEQ---- 141
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAELERldasSDDLAALEEQleel 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 142 --EIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEE-----EVLSREDAEGRLMEARKGADEAALaRAELEKRID 214
Cdd:COG4913 698 eaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlaRLELRALLEERFAAALGDAVEREL-RENLEERID 776
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13929098 215 SLMDEIAflkkVHEEEIAELQAQI--QYAQISVEMDVSskpdlSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTE 290
Cdd:COG4913 777 ALRARLN----RAEEELERAMRAFnrEWPAETADLDAD-----LESLPEYLALLDRLEEDGLPEYEERFKELLNENSI 845
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
73-239 |
3.48e-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: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 73 LSQVAAISNDLKSIRtQEKAQLQDLNDRFASFI--ERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLA- 149
Cdd:COG4913 254 LEPIRELAERYAAAR-ERLAELEYLRAALRLWFaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQi 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 150 AEDATNEKQALQGEREGLEETLRNLQ---ARYEEEV----LSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAF 222
Cdd:COG4913 333 RGNGGDRLEQLEREIERLERELEERErrrARLEALLaalgLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
170
....*....|....*..
gi 13929098 223 LKKVHEEEIAELQAQIQ 239
Cdd:COG4913 413 ALRDLRRELRELEAEIA 429
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
95-360 |
4.97e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 95 QDLNDrfASFIERVHELEQQNKVLEAELLVLRQKHSEPS----RFRALYEQEIRDLRLAaEDATNEKQALQGEREGLEE- 169
Cdd:PRK02224 459 QPVEG--SPHVETIEEDRERVEELEAELEDLEEEVEEVEerleRAEDLVEAEDRIERLE-ERREDLEELIAERRETIEEk 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 170 --TLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHE--EEIAELQAQIQ-----Y 240
Cdd:PRK02224 536 reRAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTllAAIADAEDEIErlrekR 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 241 AQISvEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEwFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEI 320
Cdd:PRK02224 616 EALA-ELNDERRERLAEKRERKRELEAEFDEARIEEARE-DKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL 693
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 13929098 321 EACRGMNEALEKQLQELEDKQNaDISAMQDTINKLENELR 360
Cdd:PRK02224 694 EELRERREALENRVEALEALYD-EAEELESMYGDLRAELR 732
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
92-277 |
7.12e-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: 44.53 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 92 AQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREgleetL 171
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE-----Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 172 RNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSS 251
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
170 180
....*....|....*....|....*.
gi 13929098 252 KPdlsaalKDIRAQYEKLAAKNMQNA 277
Cdd:COG1579 172 IP------PELLALYERIRKRKNGLA 191
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
75-382 |
8.06e-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: 45.44 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 75 QVAAISNDLKSI---RTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLvlrqkHSEPSRFRALY---EQEIRDLRL 148
Cdd:TIGR02169 738 RLEELEEDLSSLeqeIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS-----HSRIPEIQAELsklEEEVSRIEA 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 149 AAEDATNEKQALQGEREGLEETLRNLQARyeeevlsREDAEGRlmearkgadeaalaRAELEKRIDSLMDEIAFLkkvhE 228
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQ-------RIDLKEQ--------------IKSIEKEIENLNGKKEEL----E 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 229 EEIAELQAQIQyaqisvemdvsskpDLSAALKDIRAQYEKLAAK--NMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEV 306
Cdd:TIGR02169 868 EELEELEAALR--------------DLESRLGDLKKERDELEAQlrELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13929098 307 SESRRLLKAkTLEIEACRGMNEALEKQLQELEdkqnADISAMQDTINKLENELRSTksemARYLKEYQDLLNVKMA 382
Cdd:TIGR02169 934 SEIEDPKGE-DEEIPEEELSLEDVQAELQRVE----EEIRALEPVNMLAIQEYEEV----LKRLDELKEKRAKLEE 1000
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
83-401 |
1.21e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 83 LKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALyEQEIRDLR-----LAAEDATNEK 157
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK-KEELERLKkrltgLTPEKLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 158 QALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAEL--EKRIDSLMDEIAFLKKVHEE--EIAE 233
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKElkEIEE 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 234 LQAQIQYAQISVEMDVSSKPDLSA---ALKDIRAQYEKLAAKNMQNAEEWFKsRFTVLTESAAKNTDAVRAAKDEVSESR 310
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKlkeLAEQLKELEEKLKKYNLEELEKKAE-EYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 311 RLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLE------NELRSTKSEMARYLKEYQDLLNvkmald 384
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEE------ 626
|
330
....*....|....*..
gi 13929098 385 iEIAAYRKLLEGEETRL 401
Cdd:PRK03918 627 -ELDKAFEELAETEKRL 642
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
87-337 |
1.81e-04 |
|
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: 44.56 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 87 RTQEKAQLQDLNdrFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAeDATNEKQALQGEREG 166
Cdd:COG3096 424 KARALCGLPDLT--PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIA-GEVERSQAWQTAREL 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 167 LEetlrnlQARYEEEVLSREDA-EGRLMEARKGADEAALAR---AELEKRIDSLMDEIAFLkkvhEEEIAELQAQIQYAQ 242
Cdd:COG3096 501 LR------RYRSQQALAQRLQQlRAQLAELEQRLRQQQNAErllEEFCQRIGQQLDAAEEL----EELLAELEAQLEELE 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 243 ISVEMDVSSKPDLSAALKDIRAQYEKLAAKnmqnAEEWFKS-----RFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKT 317
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELAAR----APAWLAAqdaleRLREQSGEALADSQEVTAAMQQLLEREREATVER 646
|
250 260
....*....|....*....|
gi 13929098 318 LEIEACRgmnEALEKQLQEL 337
Cdd:COG3096 647 DELAARK---QALESQIERL 663
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
144-389 |
1.95e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 144 RDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEevlsredaegrlMEARKGADEAALARAELEKRIDSLMDEIAFL 223
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEE------------FRQKNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 224 kkvhEEEIAELQAQIQYAQISVEMDVSSKPDL--SAALKDIRAQYEKLaaknmqnaeewfKSRFTVLTESAAKNTDAVRA 301
Cdd:COG3206 232 ----RAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAEL------------EAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 302 AKDEVSESRRLLKAKTLEI-EACRGMNEALEKQLQELEdKQNADISAMQDTINKLENELRSTKSEMARYLKEYQDLLNVK 380
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQ-AQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
|
....*....
gi 13929098 381 MALDIEIAA 389
Cdd:COG3206 375 EEARLAEAL 383
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
91-243 |
2.52e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 91 KAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIrDLRLAAEdatnEKQALQGEREGLEET 170
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-DVASAER----EIAELEAELERLDAS 683
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13929098 171 ---LRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEI-AFLKKVHEEEIAELQAQIQYAQI 243
Cdd:COG4913 684 sddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeAAEDLARLELRALLEERFAAALG 760
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
127-233 |
9.30e-04 |
|
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: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 127 QKHSEPSRFRALyEQEIRDLRLAAEDATNEK--------QALQGEREGLEETLRNLQARYEEEvlsrEDAEGRLMEARKG 198
Cdd:COG0542 405 EIDSKPEELDEL-ERRLEQLEIEKEALKKEQdeasferlAELRDELAELEEELEALKARWEAE----KELIEEIQELKEE 479
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 13929098 199 ADEAALARAELEKRIDSLMDEIAFLKK-----VHEEEIAE 233
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPllreeVTEEDIAE 519
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-364 |
1.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 141 QEIRDLRLAAEDATNEKQALQGeregleetLRNLQARYEEEVLSREDAEGRLMEARkgADEAALARAELEKRIDSLMDEI 220
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEP--------IRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 221 AFLkkvhEEEIAELQAQIQyaqisvemdvsskpDLSAALKDIRAQYEKLAAKNMQNAE---EWFKSRFTVLTESAAKNTD 297
Cdd:COG4913 305 ARL----EAELERLEARLD--------------ALREELDELEAQIRGNGGDRLEQLEreiERLERELEERERRRARLEA 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13929098 298 AVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRSTKS 364
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
89-244 |
1.52e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 89 QEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQA--------- 159
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLeeleerlee 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 160 ---LQGEREGLEETLRNLQAR-YEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQ 235
Cdd:COG4717 158 lreLEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
....*....
gi 13929098 236 AQIQYAQIS 244
Cdd:COG4717 238 AAALEERLK 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
147-402 |
1.57e-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: 41.59 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 147 RLAAEDATNEK-QALQGEREGLEETLrnLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFL-- 223
Cdd:TIGR02169 202 RLRREREKAERyQALLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnk 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 224 --KKVHEEE-------IAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEwfksrftvlTESAAK 294
Cdd:TIGR02169 280 kiKDLGEEEqlrvkekIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---------IEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 295 NTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRSTKSEMARYLKEYQ 374
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430
|
250 260
....*....|....*....|....*...
gi 13929098 375 DLLNVKMALDIEIAAYRKLLEGEETRLS 402
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLE 458
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
188-443 |
2.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 188 AEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLkkvhEEEIAELQAQIQYAQISVEmdvSSKPDLSAALKDIRAQYE 267
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEEL----NEEYNELQAELEALQAEID---KLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 268 KLA--AKNMQNAEEWFkSRFTVLTES-----AAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDK 340
Cdd:COG3883 87 ELGerARALYRSGGSV-SYLDVLLGSesfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 341 QNADISAMQDTINKLENELRSTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSITSGYSQSSQVF 420
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
250 260
....*....|....*....|...
gi 13929098 421 GRSAYSGLQSSSYLMSARAFPAY 443
Cdd:COG3883 246 AAGAGAAGAAGAAAGSAGAAGAA 268
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
78-359 |
2.64e-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: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 78 AISNDLKSIRTQEKAQLQdlndrfasfiervHELEQQNKVLEAELLVLRQKHSepSRFRALYEQeIRDLRLAAEDATNEK 157
Cdd:pfam01576 316 AAQQELRSKREQEVTELK-------------KALEEETRSHEAQLQEMRQKHT--QALEELTEQ-LEQAKRNKANLEKAK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 158 QALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEE-------- 229
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEaegknikl 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 230 --EIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAqyEKLAAKNMQNAEEwfksrftvltESAAKNTDAVRAAKDEVS 307
Cdd:pfam01576 460 skDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLED--ERNSLQEQLEEEE----------EAKRNVERQLSTLQAQLS 527
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 13929098 308 ESRRLLKAKTLEIEAC----RGMNEALEKQLQELEDKQNAdISAMQDTINKLENEL 359
Cdd:pfam01576 528 DMKKKLEEDAGTLEALeegkKRLQRELEALTQQLEEKAAA-YDKLEKTKNRLQQEL 582
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
74-221 |
2.87e-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: 40.13 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 74 SQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYE-------QEIRDL 146
Cdd:COG4942 76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKylaparrEQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 147 RLAAEDATNEKQALQGEREGLEETLRNLQA---RYEEEVLSREDAEGRLmEARKGADEAALA-----RAELEKRIDSLMD 218
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEeraALEALKAERQKLLARL-EKELAELAAELAelqqeAEELEALIARLEA 234
|
...
gi 13929098 219 EIA 221
Cdd:COG4942 235 EAA 237
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
185-402 |
3.64e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 185 REDAEGRLMEARKGADEAALARAELEKRIDSLmdeiaflkkvheeeiaELQAQI--QYAQisvemdvsskpdLSAALKDI 262
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPL----------------ERQAEKaeRYRE------------LKEELKEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 263 RAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELE---D 339
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiA 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13929098 340 KQNADISAMQDTINKLENELRSTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLS 402
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
140-239 |
3.75e-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: 39.48 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 140 EQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVlsredaegRLMEArKGADEAALARAELEKRIDSLMDE 219
Cdd:cd16269 197 EKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHL--------RQLKE-KMEEERENLLKEQERALESKLKE 267
|
90 100
....*....|....*....|.
gi 13929098 220 I-AFLKKVHEEEIAELQAQIQ 239
Cdd:cd16269 268 QeALLEEGFKEQAELLQEEIR 288
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
74-364 |
5.01e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 74 SQVAAISNDLKSIRTQ---EKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRAL------------ 138
Cdd:PRK02224 384 EEIEELEEEIEELRERfgdAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpveg 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 139 ---------YEQEIRDLRLAAEDATNEKQALQGEREGLEEtLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAEL 209
Cdd:PRK02224 464 sphvetieeDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 210 EKRIDSLMDEiaflKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAknMQNAEEWFKSRFTVLT 289
Cdd:PRK02224 543 RERAAELEAE----AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA--IADAEDEIERLREKRE 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 290 ESAAKNtDAVRAAKDEVSESRRLLKAKTLE--IEACRGMNEALEKQLQELEDK---QNADISAMQDTINKLENELRSTKS 364
Cdd:PRK02224 617 ALAELN-DERRERLAEKRERKRELEAEFDEarIEEAREDKERAEEYLEQVEEKldeLREERDDLQAEIGAVENELEELEE 695
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
68-375 |
5.08e-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: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 68 LENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLR 147
Cdd:TIGR04523 297 ISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 148 laaedatNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADeaalaraELEKRIDSLMDEIAFLKkvh 227
Cdd:TIGR04523 377 -------KENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE-------LLEKEIERLKETIIKNN--- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 228 eEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLaAKNMQNAEEWFKSRFTVLTESAAKNTD---AVRAAKD 304
Cdd:TIGR04523 440 -SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI-KQNLEQKQKELKSKEKELKKLNEEKKEleeKVKDLTK 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 305 EVSESrrLLKAKTLEIEACRgmneaLEKQLQELEDKQNAD------------ISAMQDTINKLENE---LRSTKSEMARY 369
Cdd:TIGR04523 518 KISSL--KEKIEKLESEKKE-----KESKISDLEDELNKDdfelkkenlekeIDEKNKEIEELKQTqksLKKKQEEKQEL 590
|
....*.
gi 13929098 370 LKEYQD 375
Cdd:TIGR04523 591 IDQKEK 596
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
86-272 |
6.02e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 86 IRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHS--EPSRFRALYEQEIRDLRLAAEDATNEKQALQGE 163
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 164 REGLEETLRNlqaryEEEVLSREDAEGRLMEARKGADEAALARAELEKR-------IDSLMDEIAFLKKVHEEEIAELQA 236
Cdd:COG3206 242 LAALRAQLGS-----GPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190
....*....|....*....|....*....|....*.
gi 13929098 237 QIqyaQISVEMDVSSKPDLSAALKDIRAQYEKLAAK 272
Cdd:COG3206 317 SL---EAELEALQAREASLQAQLAQLEARLAELPEL 349
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
72-377 |
6.16e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 72 DLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEqqnkVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAae 151
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIAETEREREELAEEVRDLRER-- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 152 datnekqalqgeREGLEETLRNLQARYEEEVLSREDAEGRlmearkgadeaalaRAELEKRIDSLMDEIaflkkvheeei 231
Cdd:PRK02224 288 ------------LEELEEERDDLLAEAGLDDADAEAVEAR--------------REELEDRDEELRDRL----------- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13929098 232 aelqaqiqyaqisvemdVSSKPDLSAALKDIRAQYEKLAAKNMQNAEewfksrftvLTESAAKNTDAVRAAKDEVSESRR 311
Cdd:PRK02224 331 -----------------EECRVAAQAHNEEAESLREDADDLEERAEE---------LREEAAELESELEEAREAVEDRRE 384
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13929098 312 LLKAKTLEIEACRGMNEALEKQLQELEDKqNADISAMQDTINKLENELRSTKSEMARYLKEYQDLL 377
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNAEDF-LEELREERDELREREAELEATLRTARERVEEAEALL 449
|
|
| |
