|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
99-410 |
2.37e-128 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 386.97 E-value: 2.37e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 99 NEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQ-ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHL 177
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 178 EEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRRNHEEEVADLLAQIQASHITVER 257
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 258 KDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTK 337
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297529 338 ESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 410
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-366 |
5.76e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 5.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 103 QLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIH 182
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 183 RLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRRNHEEEVADLLAQIQAshitVERKDYLK 262
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 263 TDISTALKEIRSQLEcHSDQNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLER 342
Cdd:COG1196 389 LEALRAAAELAAQLE-ELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260
....*....|....*....|....
gi 297529 343 QLSDIEERHNHDLSSYQDTIQQLE 366
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELA 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
127-410 |
9.80e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 9.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 127 EIEAEIQALRqKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSdhLEEDIHRLKERFEEEARLRDDTEAAIRALR 206
Cdd:COG1196 197 ELERQLEPLE-RQAEKAERYRELKEELKELEAELLLLKLRELEAELEE--LEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 207 KDIEEssmvkveLDKKVQSLQDEvaflRRNHEEEVADLLAQIQASHitvERKDYLKTDISTALKEIRSQLEchsDQNMHQ 286
Cdd:COG1196 274 LELEE-------LELELEEAQAE----EYELLAELARLEQDIARLE---ERRRELEERLEELEEELAELEE---ELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 287 AEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERhnhdLSSYQDTIQQLE 366
Cdd:COG1196 337 EEL------EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA----AAELAAQLEELE 406
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 297529 367 NELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 410
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-352 |
1.26e-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: 65.46 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 102 EQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQAL-RQKQashaqlgdAYDQEIRELRATLEMVNHEKAQVQLDSDHLEED 180
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQ--------ILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 181 IHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRRN---HEEEVADLLAQIQAShitVER 257
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiasLNNEIERLEARLERL---EDR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 258 KDYLKTDISTALKEIRSQ--LECHSDQNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRG 335
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAelKELQAELEELEEEL------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
250
....*....|....*..
gi 297529 336 TKESLERQLSDIEERHN 352
Cdd:TIGR02168 490 RLDSLERLQENLEGFSE 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-418 |
4.21e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 122 EQQNKEIEAEIQALRQKQASHAQLGDAYDQ---EIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDT 198
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEEleaELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 199 EAAIRALRKDIEESSMVKVELDKKVQSLQDEVAflrrNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLEc 278
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 279 hsdqnmHQAEEWFKCRYAKLTEAAEQnkEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSY 358
Cdd:COG1196 376 ------EAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297529 359 QDTIQQLENELRGTKWEMARHLRE---YQDLLNVKMALDIEIAAYRKLLEGEETRFSTFSGSI 418
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEaalLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-405 |
2.81e-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: 61.23 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 148 AYDQEIRELRATLEMvnhekaqvqldsdhLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQ 227
Cdd:TIGR02168 674 ERRREIEELEEKIEE--------------LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 228 DEVaflrRNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLEchsdqnmhQAEEwfkcRYAKLTEAAEQNKE 307
Cdd:TIGR02168 740 AEV----EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE--------ELEA----QIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 308 AIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERhnhdLSSYQDTIQQLENELRGTKWEMARHLREYQDLL 387
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALL 879
|
250
....*....|....*...
gi 297529 388 NVKMALDIEIAAYRKLLE 405
Cdd:TIGR02168 880 NERASLEEALALLRSELE 897
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
100-378 |
7.57e-09 |
|
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: 59.70 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 100 EKEQLQGLNDRFAGYIEKVHY-LEQQNKEIEAEIQALRQkqaSHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLE 178
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEeISELEKRLEEIEQLLEE---LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 179 EDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRRNHEEEVADLLAQIQASHITVERK 258
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 259 DYLKTDISTALKEIRSQLEchsdqnmhqaeewfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKE 338
Cdd:TIGR02169 395 EKLKREINELKRELDRLQE----------------ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 297529 339 SLERQLSDIEERHNHDlssyQDTIQQLENELRGTKWEMAR 378
Cdd:TIGR02169 459 QLAADLSKYEQELYDL----KEEYDRVEKELSKLQRELAE 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
100-346 |
1.47e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 100 EKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEE 179
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 180 DIHRLKERFEEEARLRDDTEAAIRALRKDIEEssmvkveldkkvqsLQDEVAFLRRNHEEEVADLLAQIQASHITVERKD 259
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEE--------------LAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 260 YLKTDISTALKEIRSQLECHSDQNMHQAEEwfKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKES 339
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEA--AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
....*..
gi 297529 340 LERQLSD 346
Cdd:COG1196 496 LLEAEAD 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
121-344 |
3.04e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 121 LEQQNKEIEAEIQALRQKQASHAQLgDAYDQEIRELRATLEMVNHEKAQVQLDS-----DHLEEDIHRLKERFEEEARLR 195
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELleaelEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 196 DDTEAAIRALRKDIEESSMVKVE-LDKKVQSLQDEVAfLRRNHEEEVADLLAQIQASHITVERkdylktdistALKEIRS 274
Cdd:COG4913 319 DALREELDELEAQIRGNGGDRLEqLEREIERLERELE-ERERRRARLEALLAALGLPLPASAE----------EFAALRA 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 275 QLECHSDQnmhqaeewfkcryakLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQL 344
Cdd:COG4913 388 EAAALLEA---------------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-370 |
3.09e-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: 57.76 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 97 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 176
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 177 LEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRRN---HEEEVADLLAQIQASHI 253
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAlalLRSELEELSEELRELES 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 254 TVERKDYLKTDISTALKEIRSQLECHSDQNMHQAEEwFKCRYAKLTEAAEQNKEAI----RSAKEEIAEYRRQLQS---- 325
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQER-LSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKElgpv 987
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 297529 326 --KSI-ELESVRGTKESLERQLSDIEERhnhdLSSYQDTIQQLENELR 370
Cdd:TIGR02168 988 nlAAIeEYEELKERYDFLTAQKEDLTEA----KETLEEAIEEIDREAR 1031
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
140-422 |
2.97e-07 |
|
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: 53.61 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 140 ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEssmvkveL 219
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 220 DKKVQSLQDEVAFLRrnheEEVADLLAQIQAShitvERKDYLKTDISTalkeirsqlechsdQNMHQAEEWFKcRYAKLT 299
Cdd:COG4942 89 EKEIAELRAELEAQK----EELAELLRALYRL----GRQPPLALLLSP--------------EDFLDAVRRLQ-YLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 300 EAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHnhdlssyQDTIQQLENELRGTKWEMARH 379
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER-------QKLLARLEKELAELAAELAEL 218
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 297529 380 LREYQDLLNVKMALDIEIAAYRKLLEGeeTRFSTFSGSITGPL 422
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERTPA--AGFAALKGKLPWPV 259
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
97-387 |
5.33e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 97 RSNEKEQLQGLNDRFAGYIEK-----VHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVnhekaqvq 171
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL-------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 172 ldsDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEessmvkvELDKKVQSLQDEVAfLRRNHEEEVADLLAQIQAS 251
Cdd:PRK02224 254 ---ETLEAEIEDLRETIAETEREREELAEEVRDLRERLE-------ELEEERDDLLAEAG-LDDADAEAVEARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 252 HITVERK-DYLKTDISTALKEIRSQLEchsdqNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 330
Cdd:PRK02224 323 DEELRDRlEECRVAAQAHNEEAESLRE-----DADDLEE----RAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 297529 331 ESVRGTKESLERQLSDIEERHNhDLSSYQDTIQQLENELRGTKWEMARHLREYQDLL 387
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEALL 449
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
115-368 |
5.81e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 115 IEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMvnhekAQVQLDSDHLEEDIHRLKERFEeeaRL 194
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY-----SWDEIDVASAEREIAELEAELE---RL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 195 RDDTeAAIRALRKDIEESSMVKVELDKKVQSLQDEvaflRRNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRS 274
Cdd:COG4913 681 DASS-DDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 275 QLEChSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEE-IAEYRRQLQSKSIELESVrgtkESLERQLSDIEerhNH 353
Cdd:COG4913 756 AAAL-GDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESL----PEYLALLDRLE---ED 827
|
250
....*....|....*
gi 297529 354 DLSSYQDTIQQLENE 368
Cdd:COG4913 828 GLPEYEERFKELLNE 842
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-392 |
7.73e-07 |
|
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: 53.14 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 121 LEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRatLEMVNHEKAQVQLDS---------DHLEEDIHRLKERFEEE 191
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEIEELQKelyalaneiSRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 192 ARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRRNHEEEVADLLAQIQASHITVERKDYLKTDISTALKE 271
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 272 ---IRSQLECHSDQnMHQAEEwfkcRYAKLTEAAEQNKEAIRSAkeEIAEYRRQLQSKSIELESVRGTKESLERQLSDIE 348
Cdd:TIGR02168 395 iasLNNEIERLEAR-LERLED----RRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 297529 349 ER---HNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMA 392
Cdd:TIGR02168 468 EEleeAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
95-407 |
1.56e-06 |
|
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: 51.98 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 95 LSRSNEKEQLQGlndRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS 174
Cdd:TIGR02168 673 LERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 175 DHLEEDIHRL------------------KERFEEEARLRDDTEAAIRALRKDIEESSmvkvELDKKVQSLQDEVAFLRRN 236
Cdd:TIGR02168 750 AQLSKELTELeaeieeleerleeaeeelAEAEAEIEELEAQIEQLKEELKALREALD----ELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 237 HEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLEchsdqnmhqaeewfkcRYAKLTEAAEQNKEAIRSAKEEI 316
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE----------------LIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 317 AEYRRQLQSKSIELESVRGTKESLERQLsdieERHNHDLSSYQDTIQQLENELRGTKwemARHLREYQDLLNVKMALDIE 396
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRREL----EELREKLAQLELRLEGLEVRIDNLQ---ERLSEEYSLTLEEAEALENK 962
|
330
....*....|.
gi 297529 397 IAAYRKLLEGE 407
Cdd:TIGR02168 963 IEDDEEEARRR 973
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
122-302 |
1.65e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 122 EQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS-DHLEEDIHRLKERFEEEARLRDDTEA 200
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 201 AIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRRNHEEEVADLLAQIQAshitverkdyLKTDISTALKEIRSQLECHS 280
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD----------LRRELRELEAEIASLERRKS 436
|
170 180
....*....|....*....|....
gi 297529 281 --DQNMHQAEEWFkCRYAKLTEAA 302
Cdd:COG4913 437 niPARLLALRDAL-AEALGLDEAE 459
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-404 |
3.29e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 101 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEI--RELRATLEMVNHEKAQVQLDSDHLE 178
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 179 EdihrLKERFEEEARLRDDTEAAIRALRKDIEessmvkvELDKKVQSLQDEVAFLRRNHeEEVADLLAQIQASHITverK 258
Cdd:COG4913 689 A----LEEQLEELEAELEELEEELDELKGEIG-------RLEKELEQAEEELDELQDRL-EAAEDLARLELRALLE---E 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 259 DYLKTDISTALKEIRSQLEchsDQNMHQAEEWFKCRyAKLTEAAEQNKEAIRSAK-------EEIAEYRRQLQS-KSIEL 330
Cdd:COG4913 754 RFAAALGDAVERELRENLE---ERIDALRARLNRAE-EELERAMRAFNREWPAETadldadlESLPEYLALLDRlEEDGL 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 331 ----------------ESVRGTKESLERQLSDIEERhnhdlssyqdtIQQLENELRGTKWEMARHLReyqdlLNVKMALD 394
Cdd:COG4913 830 peyeerfkellnensiEFVADLLSKLRRAIREIKER-----------IDPLNDSLKRIPFGPGRYLR-----LEARPRPD 893
|
330
....*....|
gi 297529 395 IEIAAYRKLL 404
Cdd:COG4913 894 PEVREFRQEL 903
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
10-98 |
3.45e-06 |
|
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: 45.85 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 10 NPSAYRRvpTETRSSFSRVSGSPSSGFR---SQSWSRGSPSTVSSSYTRS-AVAPRLAYSSAMLSSAESSldfsQSSSLL 85
Cdd:pfam04732 2 SSSSYRR--MFGDSSSSRPSYSSSSGSRsvsSRSYSRSSSSSPSSSSRRSsRSSSRSSYPSLAADSLDFS----LADALN 75
|
90
....*....|...
gi 297529 86 NggsggDYKLSRS 98
Cdd:pfam04732 76 Q-----EFKATRT 83
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
123-378 |
3.60e-06 |
|
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: 50.15 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 123 QQNKEIEAEIQALRqkqashaqlgdaydQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAI 202
Cdd:COG4942 20 DAAAEAEAELEQLQ--------------QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 203 RALRKDIEEssmVKVELDKKVQSLQDEVAFLRRNHEEEVADLLAQIQASHITVERKDYLKtDISTALKEIRSQLEchsdq 282
Cdd:COG4942 86 AELEKEIAE---LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELR----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 283 nmhqaeewfkcryaKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTI 362
Cdd:COG4942 157 --------------ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
250
....*....|....*.
gi 297529 363 QQLENELRGTKWEMAR 378
Cdd:COG4942 223 EELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
100-247 |
3.83e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 100 EKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYD--QEIRELRATLEMVN----------HEK 167
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPerleeleerlEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 168 AQVQLDSDHLEEDIHRLKERFEEEARLRD-DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRRNHEEEVADLLA 246
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
.
gi 297529 247 Q 247
Cdd:COG4717 239 A 239
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
97-387 |
2.14e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 97 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 176
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 177 LEEDIHRL-KERFEEEARLRD------DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLR------RNHEEEVAD 243
Cdd:pfam07888 155 MKERAKKAgAQRKEEEAERKQlqaklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttaHRKEAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 244 LLAQIQAS----HITVERKDYLKTDI-STALKEIRSQLECH-------------SDQNMHQAEEwfKCRYAKLTEAAEQN 305
Cdd:pfam07888 235 LLEELRSLqerlNASERKVEGLGEELsSMAAQRDRTQAELHqarlqaaqltlqlADASLALREG--RARWAQERETLQQS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 306 KEAirsAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQD 385
Cdd:pfam07888 313 AEA---DKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQE 389
|
..
gi 297529 386 LL 387
Cdd:pfam07888 390 LL 391
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
93-352 |
2.64e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 93 YKLSRSNEKEQLQGLNDRFAGYIEKVHYLEqqnkEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQL 172
Cdd:PRK02224 225 YEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 173 DSDHLEEDIHRLKERfeeearlRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLR-RNHE--EEVADLLAQIQ 249
Cdd:PRK02224 301 EAGLDDADAEAVEAR-------REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEeRAEElrEEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 250 ASHITVERKDYLKTDISTALKEIRSQLEcHSDQNMHQAEEWFKCRYAKLTEAAEQNKE---AIRSAKEEIAEYRRQLQS- 325
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFG-DAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAg 452
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 297529 326 ------KSIE-------LESVRGTKESLERQLSDIEERHN 352
Cdd:PRK02224 453 kcpecgQPVEgsphvetIEEDRERVEELEAELEDLEEEVE 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
116-387 |
2.78e-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: 48.14 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 116 EKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEmvnhekaQVQLDSDHLEEDIHRLKERFEEEARLR 195
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG-------EIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 196 DDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFL-RRNHEEEVADLLAQIQASHITVERKDYLKTDISTALKE--I 272
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 273 RSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHN 352
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250 260 270
....*....|....*....|....*....|....*
gi 297529 353 hDLSSYQDTIQQLENELRGTKWEMARHLREYQDLL 387
Cdd:TIGR02169 907 -ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
96-329 |
3.55e-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: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 96 SRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQAS-HAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS 174
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElRAELEAQKEELAELLRALYRLGRQPPLALLLSP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 175 DHLEEDIHRLkERFEEEARLRddtEAAIRALRKDIEESSMVKVELDKKVQSLQDevafLRRNHEEEVADLLAQIQashit 254
Cdd:COG4942 129 EDFLDAVRRL-QYLKYLAPAR---REQAEELRADLAELAALRAELEAERAELEA----LLAELEEERAALEALKA----- 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297529 255 vERKDYLKtDISTALKEIRSQLechsdqnmhqaeewfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIE 329
Cdd:COG4942 196 -ERQKLLA-RLEKELAELAAEL-------------------AELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
126-332 |
6.35e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 126 KEIEAEIQALRQKQASHAQLgdaYDQEIRELRATLEMVNHEKAQVQLdsdhLEEDIHRLKERFEEEARLRDDTEAAIRAL 205
Cdd:COG4717 49 ERLEKEADELFKPQGRKPEL---NLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 206 RKDIEessmvKVELDKKVQSLQDEVAFLrrnhEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLECHSDQNMH 285
Cdd:COG4717 122 EKLLQ-----LLPLYQELEALEAELAEL----PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 297529 286 QAEEWFKcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELES 332
Cdd:COG4717 193 ELQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
97-276 |
2.87e-04 |
|
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: 44.67 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 97 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEI--QALRQKQASHAQLgdayDQEIRELRATLEMVNHEKAQVQLDS 174
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLshSRIPEIQAELSKL----EEEVSRIEARLREIEQKLNRLTLEK 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 175 DHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFL---RRNHEEEVADLLAQIQAS 251
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLkkeRDELEAQLRELERKIEEL 908
|
170 180
....*....|....*....|....*
gi 297529 252 HITVERKDYLKTDISTALKEIRSQL 276
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
133-374 |
3.59e-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: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 133 QALRQKQASHAQLGDAYDQEIRELRATLE---------MVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIR 203
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 204 ALRKDIEESSMVKVEL--DKKVQSLQDEVAFLRRnheeEVADLLAQIQASHITVERkdyLKTDISTALKEIRSQLEchsd 281
Cdd:COG3206 244 ALRAQLGSGPDALPELlqSPVIQQLRAQLAELEA----ELAELSARYTPNHPDVIA---LRAQIAALRAQLQQEAQ---- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 282 qnmhqaeewfkcryaKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDT 361
Cdd:COG3206 313 ---------------RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
250
....*....|...
gi 297529 362 iqQLENELRGTKW 374
Cdd:COG3206 378 --RLAEALTVGNV 388
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
121-263 |
5.69e-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: 42.22 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 121 LEQQNKEIEAEIQALRQKQAshaqlgdAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKER------------- 187
Cdd:COG1579 22 LEHRLKELPAELAELEDELA-------ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeal 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297529 188 ---FEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRRNHEEEVADLLAQIQAshITVERKDYLKT 263
Cdd:COG1579 95 qkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE--LEAEREELAAK 171
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
101-350 |
9.13e-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: 42.44 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 101 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQashaqlgDAYDQEIRELRATLEMVNHEKAQVQLDsdhLEED 180
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-------RALEQELAALEAELAELEKEIAELRAE---LEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 181 IHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRRNHeEEVADLLAQIQAShitverkdy 260
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-AELAALRAELEAE--------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 261 lKTDISTALKEIRSQLechsdqnmhqaeewfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESL 340
Cdd:COG4942 173 -RAELEALLAELEEER-------------------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|
gi 297529 341 ERQLSDIEER 350
Cdd:COG4942 233 EAEAAAAAER 242
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
99-473 |
1.02e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 99 NEKEQLQGLNDRFAGYIEKVhylEQQNKEIEAEiqalrqkQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLE 178
Cdd:PRK01156 353 NQILELEGYEMDYNSYLKSI---ESLKKKIEEY-------SKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 179 EDIHRLKERfeeearlrddteaaIRALRKDIEESSMVKVELDKKVQ------SLQDEVAFLRRNHEEEVADLL------A 246
Cdd:PRK01156 423 SKVSSLNQR--------------IRALRENLDELSRNMEMLNGQSVcpvcgtTLGEEKSNHIINHYNEKKSRLeekireI 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 247 QIQASHITVERKDYLKTDISTALKEIRSQLECHSDQNMHQAE-EWFKCRYAKLTEA---AEQNKEAIRSAKEEIAEYRRQ 322
Cdd:PRK01156 489 EIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADlEDIKIKINELKDKhdkYEEIKNRYKSLKLEDLDSKRT 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 323 ------LQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRgtkwEMARHLREYQDLLNVKMALDIE 396
Cdd:PRK01156 569 swlnalAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIR----EIENEANNLNNKYNEIQENKIL 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 397 IAAYRKLLEGEETRFSTFSG------SITGPLYTHRQPSVTISSKIQKTKVEAPKLKVQHKFVEEIIEEtkVEDEKSEME 470
Cdd:PRK01156 645 IEKLRGKIDNYKKQIAEIDSiipdlkEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE--LSDRINDIN 722
|
...
gi 297529 471 ETL 473
Cdd:PRK01156 723 ETL 725
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
197-405 |
1.54e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 197 DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVaflrrnheeevaDLLAQIQASHITVERKDYLKTDISTALKEIRSQl 276
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAEL------------DALQERREALQRLAEYSWDEIDVASAEREIAEL- 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 277 echsdQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERH----- 351
Cdd:COG4913 674 -----EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelr 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 352 -----------------------NHDLSSYQDTIQQLENELRGTkweMARHLREYQDLLNvkmALDIEIAA---YRKLLE 405
Cdd:COG4913 749 alleerfaaalgdaverelrenlEERIDALRARLNRAEEELERA---MRAFNREWPAETA---DLDADLESlpeYLALLD 822
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
121-248 |
2.63e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 121 LEQQNKEIEAEIQALRQKQAshaqlgDAYDQEIRELRATLEMvnhekaqvqldsdhLEEDIHRLKERFEEEarlrDDTEA 200
Cdd:COG0542 416 LERRLEQLEIEKEALKKEQD------EASFERLAELRDELAE--------------LEEELEALKARWEAE----KELIE 471
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 297529 201 AIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRRNHEEEV-ADLLAQI 248
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVtEEDIAEV 520
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
235-492 |
2.85e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 235 RNHEEEVADLLAQI--QASHITVERKDYLK-TDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRS 311
Cdd:COG1196 185 EENLERLEDILGELerQLEPLERQAEKAERyRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 312 AKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNH---DLSSYQDTIQQLENELRGTKWEMARHLREYQDLLN 388
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 389 VKMALDIEIAAYRKLLEGEETRFSTFSGSItgplythrqpsVTISSKIQKTKVEApkLKVQHKFVEEIIEETKVEDEKSE 468
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAEL-----------AEAEEELEELAEEL--LEALRAAAELAAQLEELEEAEEA 411
|
250 260
....*....|....*....|....
gi 297529 469 MEETLTAIAEELAASAKEEKEEAE 492
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEE 435
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
150-370 |
3.52e-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: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 150 DQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEssmVKVELDKKVQSLQDE 229
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---AEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 230 VAFLRRNheEEVADLLAQIQAShitverkdylkTDISTALKEIrSQLECHSDQNMHQAEEwfkcrYAKLTEAAEQNKEAI 309
Cdd:COG3883 92 ARALYRS--GGSVSYLDVLLGS-----------ESFSDFLDRL-SALSKIADADADLLEE-----LKADKAELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297529 310 RSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELR 370
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-480 |
3.89e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 97 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 176
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 177 LEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLR------RNHEEEVADLLAQIQA 250
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLElqiaslNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 251 SH--ITVERKDYLKTDISTALKEIRSQLECHsDQNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSI 328
Cdd:TIGR02168 415 RRerLQQEIEELLKKLEEAELKELQAELEEL-EEELEELQE----ELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 329 ELESVRGTKESLE-------------RQLSDI----------------------EERHNH----DLSSYQDTIQQLE--- 366
Cdd:TIGR02168 490 RLDSLERLQENLEgfsegvkallknqSGLSGIlgvlselisvdegyeaaieaalGGRLQAvvveNLNAAKKAIAFLKqne 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 367 --------------NELRGTKWEMARHLREYQDLL-------------------NVKMALDIEIAAYRKLLEGEETRFST 413
Cdd:TIGR02168 570 lgrvtflpldsikgTEIQGNDREILKNIEGFLGVAkdlvkfdpklrkalsyllgGVLVVDDLDNALELAKKLRPGYRIVT 649
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297529 414 FSGSITGPLYTHRQPSVTISSKIQKTKVEapklkvqhkfveeiIEEtkVEDEKSEMEETLTAIAEEL 480
Cdd:TIGR02168 650 LDGDLVRPGGVITGGSAKTNSSILERRRE--------------IEE--LEEKIEELEEKIAELEKAL 700
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
215-406 |
9.00e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 215 VKVELDK-KVQSLQDEVAFLRRNHEEEVADLLAQIQASHitvERKDYLKTDISTA---LKEIRSQLECHSDQNMHQAEEw 290
Cdd:PRK11281 41 VQAQLDAlNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK---EETEQLKQQLAQApakLRQAQAELEALKDDNDEETRE- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 291 fkcRYAKLTEAAEQNK-----EAIRSAKEEIAEYRRQLQSksielesvrgtkeslerqLSDIEERHNHDLSSYQDTIQQL 365
Cdd:PRK11281 117 ---TLSTLSLRQLESRlaqtlDQLQNAQNDLAEYNSQLVS------------------LQTQPERAQAALYANSQRLQQI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 297529 366 ENELRGTKWEMARHLREYQDLLNVKMA-LDIEIAAYRKLLEG 406
Cdd:PRK11281 176 RNLLKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEG 217
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
99-350 |
9.12e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 39.67 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 99 NEKEQLQGLnDRFAG---YIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELratlemvnhEKAQVQLDSD 175
Cdd:COG0497 139 DPDAQRELL-DAFAGleeLLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL---------EAAALQPGEE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 176 -HLEEDIHRLkERFEEearLRDDTEAAIRALRKDiEESSMVKV-ELDKKVQSLQDevaflrrnHEEEVADLLAQIQASHI 253
Cdd:COG0497 209 eELEEERRRL-SNAEK---LREALQEALEALSGG-EGGALDLLgQALRALERLAE--------YDPSLAELAERLESALI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297529 254 TVErkdylktDISTALKEIRSQLEcHSDQNMHQAEEwfkcRYAklteaaeqnkeAIRSAK-------EEIAEYRRQLQSK 326
Cdd:COG0497 276 ELE-------EAASELRRYLDSLE-FDPERLEEVEE----RLA-----------LLRRLArkygvtvEELLAYAEELRAE 332
|
250 260
....*....|....*....|....
gi 297529 327 SIELESVRGTKESLERQLSDIEER 350
Cdd:COG0497 333 LAELENSDERLEELEAELAEAEAE 356
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