|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
98-409 |
1.79e-127 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 384.66 E-value: 1.79e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 98 NEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQ-ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHL 176
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 177 EEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVER 256
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 257 KDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTK 336
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112363107 337 ESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 409
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-365 |
1.12e-12 |
|
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: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 102 QLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIH 181
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 182 RLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEvaflRSNHEEEVADLLAQIQASHITVERKDYLK 261
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 262 TDISTALKEIRSQLEcHSDQNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLER 341
Cdd:COG1196 389 LEALRAAAELAAQLE-ELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260
....*....|....*....|....
gi 112363107 342 QLSDIEERHNHDLSSYQDTIQQLE 365
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELA 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-351 |
2.40e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 101 EQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQAL-RQKQashaqlgdAYDQEIRELRATLEMVNHEKAQVQLDSDHLEED 179
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQ--------ILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 180 IHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVE---- 255
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQIASLNNEIERLEARLErled 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 256 RKDYLKTDISTALKEIRSQ--LECHSDQNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVR 333
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAelKELQAELEELEEEL------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
250
....*....|....*...
gi 112363107 334 GTKESLERQLSDIEERHN 351
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSE 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
126-409 |
2.89e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 126 EIEAEIQALRqKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSdhLEEDIHRLKERFEEEARLRDDTEAAIRALR 205
Cdd:COG1196 197 ELERQLEPLE-RQAEKAERYRELKEELKELEAELLLLKLRELEAELEE--LEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 206 KDIEEssmvkveLDKKVQSLQDEVAflrsNHEEEVADLLAQIQAshiTVERKDYLKTDISTALKEIRSQLEchsDQNMHQ 285
Cdd:COG1196 274 LELEE-------LELELEEAQAEEY----ELLAELARLEQDIAR---LEERRRELEERLEELEEELAELEE---ELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 286 AEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERhnhdLSSYQDTIQQLE 365
Cdd:COG1196 337 EEL------EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA----AAELAAQLEELE 406
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 112363107 366 NELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETR 409
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
121-417 |
5.62e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 121 EQQNKEIEAEIQALRQKQASHAQLGDAYDQ---EIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDT 197
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEEleaELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 198 EAAIRALRKDIEESSMVKVELDKKVQSLQDEVAflrsNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLEc 277
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 278 hsdqnmHQAEEWFKCRYAKLTEAAEQnkEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSY 357
Cdd:COG1196 376 ------EAEEELEELAEELLEALRAA--AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 112363107 358 QDTIQQLENELRGTKWEMARHLRE---YQDLLNVKMALDIEIAAYRKLLEGEETRFSTFSGSI 417
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEaalLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-404 |
4.14e-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: 60.46 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 147 AYDQEIRELRATLEMvnhekaqvqldsdhLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLq 226
Cdd:TIGR02168 674 ERRREIEELEEKIEE--------------LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL- 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 227 devaflrsnhEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLECHsDQNMHQAEEwfkcRYAKLTEAAEQNKE 306
Cdd:TIGR02168 739 ----------EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-EAEIEELEA----QIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 307 AIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERhnhdLSSYQDTIQQLENELRGTKWEMARHLREYQDLL 386
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALL 879
|
250
....*....|....*...
gi 112363107 387 NVKMALDIEIAAYRKLLE 404
Cdd:TIGR02168 880 NERASLEEALALLRSELE 897
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-377 |
9.11e-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: 59.31 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 99 EKEQLQGLNDRFAGYIEKVHY-LEQQNKEIEAEIQALRQKQAshaQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLE 177
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEeISELEKRLEEIEQLLEELNK---KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 178 EDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERK 257
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 258 DYLKTDISTALKEIRSQLEchsdqnmhqaeewfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKE 337
Cdd:TIGR02169 395 EKLKREINELKRELDRLQE----------------ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 112363107 338 SLERQLSDIEERHNHDlssyQDTIQQLENELRGTKWEMAR 377
Cdd:TIGR02169 459 QLAADLSKYEQELYDL----KEEYDRVEKELSKLQRELAE 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
120-387 |
2.17e-08 |
|
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: 58.16 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 120 LEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEE-EARLRD--- 195
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHsri 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 196 ---------------DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFL---RSNHEEEVADLLAQIQASHITVERK 257
Cdd:TIGR02169 794 peiqaelskleeevsRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEEL 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 258 DYLKTDISTALKEIRSQLECHSDQ--NMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIE------L 329
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQlrELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsL 953
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 112363107 330 ESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLeNELRGTKWEMARHLREYQDLLN 387
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILERIE 1010
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-345 |
4.04e-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: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 99 EKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEE 178
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 179 DIHRLKERFEEEARLRDDTEAAIRALRKDIEEssmvkveldkkvqsLQDEVAFLRSNHEEEVADLLAQIQASHITVERKD 258
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEE--------------LAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 259 YLKTDISTALKEIRSQLECHSDQNMHQAEEwfKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKES 338
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEA--AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
....*..
gi 112363107 339 LERQLSD 345
Cdd:COG1196 496 LLEAEAD 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
120-343 |
5.36e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 120 LEQQNKEIEAEIQALRQKQASHAQLgDAYDQEIRELRATLEMVNHEKAQVQLDS-----DHLEEDIHRLKERFEEEARLR 194
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELleaelEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 195 DDTEAAIRALRKDIEESSMVKVE-LDKKVQSLQDEVAfLRSNHEEEVADLLAQIQASHITVERkdylktdistALKEIRS 273
Cdd:COG4913 319 DALREELDELEAQIRGNGGDRLEqLEREIERLERELE-ERERRRARLEALLAALGLPLPASAE----------EFAALRA 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 274 QLECHSDQnmhqaeewfkcryakLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQL 343
Cdd:COG4913 388 EAAALLEA---------------LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
96-369 |
8.12e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 96 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 175
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 176 LEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFL---RSNHEEEVADLLAQIQASHI 252
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLeeaLALLRSELEELSEELRELES 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 253 TVERKDYLKTDISTALKEIRSQLECHSDQNMHQAEEwFKCRYAKLTEAAEQNKEAI----RSAKEEIAEYRRQLQS---- 324
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQER-LSEEYSLTLEEAEALENKIeddeEEARRRLKRLENKIKElgpv 987
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 112363107 325 --KSI-ELESVRGTKESLERQLSDIEERhnhdLSSYQDTIQQLENELR 369
Cdd:TIGR02168 988 nlAAIeEYEELKERYDFLTAQKEDLTEA----KETLEEAIEEIDREAR 1031
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
10-97 |
1.70e-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: 49.31 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 10 NPSAYRRVTETRSsFSRVSGSPSSGFR---SQSWSRGSPSTVSSSYKRS-ALAPRLAYSSAMLSSAESSldfsQSSSLLN 85
Cdd:pfam04732 2 SSSSYRRMFGDSS-SSRPSYSSSSGSRsvsSRSYSRSSSSSPSSSSRRSsRSSSRSSYPSLAADSLDFS----LADALNQ 76
|
90
....*....|..
gi 112363107 86 ggsggDYKLSRS 97
Cdd:pfam04732 77 -----EFKATRT 83
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
139-421 |
3.76e-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: 53.23 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 139 ASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEssmvkveL 218
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 219 DKKVQSLQDEVAFLRsnheEEVADLLAQIQAShitvERKDYLKTDISTalkeirsqlechsdQNMHQAEEWFKcRYAKLT 298
Cdd:COG4942 89 EKEIAELRAELEAQK----EELAELLRALYRL----GRQPPLALLLSP--------------EDFLDAVRRLQ-YLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 299 EAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHnhdlssyQDTIQQLENELRGTKWEMARH 378
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER-------QKLLARLEKELAELAAELAEL 218
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 112363107 379 LREYQDLLNVKMALDIEIAAYRKLLEGeeTRFSTFSGSITGPL 421
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERTPA--AGFAALKGKLPWPV 259
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
96-386 |
4.02e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 96 RSNEKEQLQGLNDRFAGYIEK-----VHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVnhekaqvq 170
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL-------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 171 ldsDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEessmvkvELDKKVQSLQDEVAfLRSNHEEEVADLLAQIQAS 250
Cdd:PRK02224 254 ---ETLEAEIEDLRETIAETEREREELAEEVRDLRERLE-------ELEEERDDLLAEAG-LDDADAEAVEARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 251 HITVERK-DYLKTDISTALKEIRSQLEchsdqNMHQAEEwfkcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 329
Cdd:PRK02224 323 DEELRDRlEECRVAAQAHNEEAESLRE-----DADDLEE----RAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 112363107 330 ESVRGTKESLERQLSDIEERHNhDLSSYQDTIQQLENELRGTKWEMARHLREYQDLL 386
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEALL 449
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-391 |
5.36e-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: 53.52 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 120 LEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRatLEMVNHEKAQVQLDS---------DHLEEDIHRLKERFEEE 190
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEIEELQKelyalaneiSRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 191 ARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKE 270
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 271 ---IRSQLECHSDQnMHQAEEwfkcRYAKLTEAAEQNKEAIRSAkeEIAEYRRQLQSKSIELESVRGTKESLERQLSDIE 347
Cdd:TIGR02168 395 iasLNNEIERLEAR-LERLED----RRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 112363107 348 ER---HNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMA 391
Cdd:TIGR02168 468 EEleeAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
114-367 |
9.18e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 114 IEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMvnhekAQVQLDSDHLEEDIHRLKERFEeeaRL 193
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY-----SWDEIDVASAEREIAELEAELE---RL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 194 RDDTeAAIRALRKDIEESSMVKVELDKKVQSLQDEvaflRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRS 273
Cdd:COG4913 681 DASS-DDLAALEEQLEELEAELEELEEELDELKGE----IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 274 QLEChSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEE-IAEYRRQLQSKSIELESVrgtkESLERQLSDIEerhNH 352
Cdd:COG4913 756 AAAL-GDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESL----PEYLALLDRLE---ED 827
|
250
....*....|....*
gi 112363107 353 DLSSYQDTIQQLENE 367
Cdd:COG4913 828 GLPEYEERFKELLNE 842
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
94-406 |
1.63e-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: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 94 LSRSNEKEQLQGlndRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS 173
Cdd:TIGR02168 673 LERRREIEELEE---KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 174 DHLEEDIHR------------------LKERFEEEARLRDDTEAAIRALRKDIEESSmvkvELDKKVQSLQDEVAFLRSN 235
Cdd:TIGR02168 750 AQLSKELTEleaeieeleerleeaeeeLAEAEAEIEELEAQIEQLKEELKALREALD----ELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 236 HEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLEchsdqnmhqaeewfkcRYAKLTEAAEQNKEAIRSAKEEI 315
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE----------------LIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 316 AEYRRQLQSKSIELESVRGTKESLERQLsdieERHNHDLSSYQDTIQQLENELRGTKwemARHLREYQDLLNVKMALDIE 395
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRREL----EELREKLAQLELRLEGLEVRIDNLQ---ERLSEEYSLTLEEAEALENK 962
|
330
....*....|.
gi 112363107 396 IAAYRKLLEGE 406
Cdd:TIGR02168 963 IEDDEEEARRR 973
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
121-301 |
1.92e-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: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 121 EQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS-DHLEEDIHRLKERFEEEARLRDDTEA 199
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 200 AIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQAshitverkdyLKTDISTALKEIRSQLECHS 279
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD----------LRRELRELEAEIASLERRKS 436
|
170 180
....*....|....*....|....
gi 112363107 280 --DQNMHQAEEWFkCRYAKLTEAA 301
Cdd:COG4913 437 niPARLLALRDAL-AEALGLDEAE 459
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
100-403 |
5.33e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 100 KEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEI--RELRATLEMVNHEKAQVQLDSDHLE 177
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 178 EdihrLKERFEEEARLRDDTEAAIRALRKDIEessmvkvELDKKVQSLQDEVAFLRSNHeEEVADLLAQIQASHITverK 257
Cdd:COG4913 689 A----LEEQLEELEAELEELEEELDELKGEIG-------RLEKELEQAEEELDELQDRL-EAAEDLARLELRALLE---E 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 258 DYLKTDISTALKEIRSQLEchsDQNMHQAEEWFKCRyAKLTEAAEQNKEAIRSAK-------EEIAEYRRQLQS-KSIEL 329
Cdd:COG4913 754 RFAAALGDAVERELRENLE---ERIDALRARLNRAE-EELERAMRAFNREWPAETadldadlESLPEYLALLDRlEEDGL 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 330 ----------------ESVRGTKESLERQLSDIEERhnhdlssyqdtIQQLENELRGTKWEMARHLReyqdlLNVKMALD 393
Cdd:COG4913 830 peyeerfkellnensiEFVADLLSKLRRAIREIKER-----------IDPLNDSLKRIPFGPGRYLR-----LEARPRPD 893
|
330
....*....|
gi 112363107 394 IEIAAYRKLL 403
Cdd:COG4913 894 PEVREFRQEL 903
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
99-246 |
7.53e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 99 EKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYD--QEIRELRATLEMVNH----------EK 166
Cdd:COG4717 79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPErleeleerleEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 167 AQVQLDSDHLEEDIHRLKERFEEEARLRD-DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLA 245
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
.
gi 112363107 246 Q 246
Cdd:COG4717 239 A 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
92-351 |
1.96e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 92 YKLSRSNEKEQLQGLNDRFAGYIEKVHYLEqqnkEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQL 171
Cdd:PRK02224 225 YEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 172 DSDHLEEDIHRLKERfeeearlRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHE---EEVADLLAQIQ 248
Cdd:PRK02224 301 EAGLDDADAEAVEAR-------REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEelrEEAAELESELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 249 ASHITVERKDYLKTDISTALKEIRSQLEcHSDQNMHQAEEWFKCRYAKLTEAAEQNKE---AIRSAKEEIAEYRRQLQS- 324
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFG-DAPVDLGNAEDFLEELREERDELREREAEleaTLRTARERVEEAEALLEAg 452
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 112363107 325 ------KSIE-------LESVRGTKESLERQLSDIEERHN 351
Cdd:PRK02224 453 kcpecgQPVEgsphvetIEEDRERVEELEAELEDLEEEVE 492
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
96-386 |
2.99e-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: 47.58 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 96 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 175
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 176 LEEDIHRL-KERFEEEARLRD------DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLR------SNHEEEVAD 242
Cdd:pfam07888 155 MKERAKKAgAQRKEEEAERKQlqaklqQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklttaHRKEAENEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 243 LLAQIQAS----HITVERKDYLKTDI-STALKEIRSQLECH-------------SDQNMHQAEEwfKCRYAKLTEAAEQN 304
Cdd:pfam07888 235 LLEELRSLqerlNASERKVEGLGEELsSMAAQRDRTQAELHqarlqaaqltlqlADASLALREG--RARWAQERETLQQS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 305 KEAirsAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQD 384
Cdd:pfam07888 313 AEA---DKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQE 389
|
..
gi 112363107 385 LL 386
Cdd:pfam07888 390 LL 391
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
95-328 |
4.65e-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: 46.68 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 95 SRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQAS-HAQLGDAYDQEIRELRATLEMVNHEKAQVQLDS 173
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAElRAELEAQKEELAELLRALYRLGRQPPLALLLSP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 174 DHLEEDIHRLkERFEEEARLRddtEAAIRALRKDIEESSMVKVELDKKVQSLQDevafLRSNHEEEVADLLAQIQashit 253
Cdd:COG4942 129 EDFLDAVRRL-QYLKYLAPAR---REQAEELRADLAELAALRAELEAERAELEA----LLAELEEERAALEALKA----- 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 112363107 254 vERKDYLKtDISTALKEIRSQLechsdqnmhqaeewfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIE 328
Cdd:COG4942 196 -ERQKLLA-RLEKELAELAAEL-------------------AELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
100-364 |
4.94e-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: 47.37 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 100 KEQLQGLNDRFAgyiEKVHYLEQQNKEIEA----EIQALRQKQAS-HAQLGDAYDQeIRELRATLEMVNHEKAQVQLDSD 174
Cdd:TIGR02169 257 TEEISELEKRLE---EIEQLLEELNKKIKDlgeeEQLRVKEKIGElEAEIASLERS-IAEKERELEDAEERLAKLEAEID 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 175 HLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRsnheEEVADLLAQIQASHITV 254
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR----EKLEKLKREINELKREL 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 255 ERKDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYA--KLTEAAEQNKE-------AIRSAKEEIAEY---RRQL 322
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEikKQEWKLEQLAAdlskyeqELYDLKEEYDRVekeLSKL 488
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 112363107 323 QSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQL 364
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
125-331 |
8.34e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 125 KEIEAEIQALRQKQASHAQLgdaYDQEIRELRATLEMVNHEKAQVQLdsdhLEEDIHRLKERFEEEARLRDDTEAAIRAL 204
Cdd:COG4717 49 ERLEKEADELFKPQGRKPEL---NLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 205 RKDIEessmvKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLECHSDQNMH 284
Cdd:COG4717 122 EKLLQ-----LLPLYQELEALEAELAEL----PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 112363107 285 QAEEWFKcRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELES 331
Cdd:COG4717 193 ELQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
132-373 |
4.87e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 132 QALRQKQASHAQLGDAYDQEIRELRATLE---------MVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIR 202
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEeaeaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 203 ALRKDIEESSMVKVEL--DKKVQSLQDEVAFLRSnheeEVADLLAQIQASHITVERkdyLKTDISTALKEIRSQLEchsd 280
Cdd:COG3206 244 ALRAQLGSGPDALPELlqSPVIQQLRAQLAELEA----ELAELSARYTPNHPDVIA---LRAQIAALRAQLQQEAQ---- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 281 qnmhqaeewfkcryaKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDT 360
Cdd:COG3206 313 ---------------RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
250
....*....|...
gi 112363107 361 iqQLENELRGTKW 373
Cdd:COG3206 378 --RLAEALTVGNV 388
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
98-472 |
6.66e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 98 NEKEQLQGLNDRFAGYIEKVhylEQQNKEIEAEiqalrqkQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLE 177
Cdd:PRK01156 353 NQILELEGYEMDYNSYLKSI---ESLKKKIEEY-------SKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 178 EDIHRLKERfeeearlrddteaaIRALRKDIEESSMVKVEL--------------DKKVQSLQDEVAFLRSNHEEEVADL 243
Cdd:PRK01156 423 SKVSSLNQR--------------IRALRENLDELSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREI 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 244 laQIQASHITVERKDYLKTDISTALKEIRSQLECHSDQNMHQAE-EWFKCRYAKLTEA---AEQNKEAIRSAKEEIAEYR 319
Cdd:PRK01156 489 --EIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADlEDIKIKINELKDKhdkYEEIKNRYKSLKLEDLDSK 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 320 RQ------LQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRgtkwEMARHLREYQDLLNVKMALD 393
Cdd:PRK01156 567 RTswlnalAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIR----EIENEANNLNNKYNEIQENK 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 394 IEIAAYRKLLEGEETRFSTFSG------SITGPLYTHRQPSVTISSKIQKTKVEAPKLKVQHKFVEEIIEEtkVEDEKSE 467
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAEIDSiipdlkEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE--LSDRIND 720
|
....*
gi 112363107 468 MEETL 472
Cdd:PRK01156 721 INETL 725
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
120-262 |
7.66e-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: 41.83 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 120 LEQQNKEIEAEIQALRQKQAshaqlgdAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKER------------- 186
Cdd:COG1579 22 LEHRLKELPAELAELEDELA-------ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyeal 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 112363107 187 ---FEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQAshITVERKDYLKT 262
Cdd:COG1579 95 qkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE--LEAEREELAAK 171
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
120-349 |
1.62e-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: 41.67 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 120 LEQQNKEIEAEIQALRQKQASHAQLGDAY---DQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEearLRDD 196
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLaalERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 197 TEAAIRALRKdieessmvkveldkkvQSLQDEVAFLRSNheEEVADLLAQIQA-SHITVERKDYLKT--DISTALKEIRS 273
Cdd:COG4942 106 LAELLRALYR----------------LGRQPPLALLLSP--EDFLDAVRRLQYlKYLAPARREQAEElrADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 112363107 274 QLECHSDQNMHQAEEWFKCRyAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEER 349
Cdd:COG4942 168 ELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
196-404 |
1.91e-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: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 196 DTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVaflrsnheeevaDLLAQIQASHITVERKDYLKTDISTALKEIRSQl 275
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAEL------------DALQERREALQRLAEYSWDEIDVASAEREIAEL- 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 276 echsdQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERH----- 350
Cdd:COG4913 674 -----EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelr 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 351 -----------------------NHDLSSYQDTIQQLENELRGTkweMARHLREYQDLLNvkmALDIEIAA---YRKLLE 404
Cdd:COG4913 749 alleerfaaalgdaverelrenlEERIDALRARLNRAEEELERA---MRAFNREWPAETA---DLDADLESlpeYLALLD 822
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
120-247 |
3.82e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 120 LEQQNKEIEAEIQALRQKQAshaqlgDAYDQEIRELRATLEMvnhekaqvqldsdhLEEDIHRLKERFEEEarlrDDTEA 199
Cdd:COG0542 416 LERRLEQLEIEKEALKKEQD------EASFERLAELRDELAE--------------LEEELEALKARWEAE----KELIE 471
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 112363107 200 AIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEV-ADLLAQI 247
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVtEEDIAEV 520
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
98-349 |
4.59e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 98 NEKEQLQGLnDRFAG---YIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELratlemvnhEKAQVQLDSD 174
Cdd:COG0497 139 DPDAQRELL-DAFAGleeLLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL---------EAAALQPGEE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 175 -HLEEDIHRLkERFEEearLRDDTEAAIRALrkDIEESSMVKVeLDKKVQSLQDevaflRSNHEEEVADLLAQIQASHIT 253
Cdd:COG0497 209 eELEEERRRL-SNAEK---LREALQEALEAL--SGGEGGALDL-LGQALRALER-----LAEYDPSLAELAERLESALIE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 254 VErkdylktDISTALKEIRSQLEcHSDQNMHQAEEwfkcRYAklteaaeqnkeAIRSAK-------EEIAEYRRQLQSKS 326
Cdd:COG0497 277 LE-------EAASELRRYLDSLE-FDPERLEEVEE----RLA-----------LLRRLArkygvtvEELLAYAEELRAEL 333
|
250 260
....*....|....*....|...
gi 112363107 327 IELESVRGTKESLERQLSDIEER 349
Cdd:COG0497 334 AELENSDERLEELEAELAEAEAE 356
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
214-405 |
6.97e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 214 VKVELDK-KVQSLQDEVAFLRSNHEEEVADLLAQIQASHitvERKDYLKTDISTA---LKEIRSQLECHSDQNMHQAEEw 289
Cdd:PRK11281 41 VQAQLDAlNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK---EETEQLKQQLAQApakLRQAQAELEALKDDNDEETRE- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 290 fkcRYAKLTEAAEQNK-----EAIRSAKEEIAEYRRQLQSksielesvrgtkeslerqLSDIEERHNHDLSSYQDTIQQL 364
Cdd:PRK11281 117 ---TLSTLSLRQLESRlaqtlDQLQNAQNDLAEYNSQLVS------------------LQTQPERAQAALYANSQRLQQI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 112363107 365 ENELRGTKWEMARHLREYQDLLNVKMA-LDIEIAAYRKLLEG 405
Cdd:PRK11281 176 RNLLKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEG 217
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
238-491 |
7.00e-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: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 238 EEVADLLAQI--QASHITVERKDYLK-TDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEE 314
Cdd:COG1196 189 ERLEDILGELerQLEPLERQAEKAERyRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 315 IAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNH---DLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMA 391
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 392 LDIEIAAYRKLLEGEETRFSTFSGSItgplythrqpsVTISSKIQKTKVEApkLKVQHKFVEEIIEETKVEDEKSEMEET 471
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAEL-----------AEAEEELEELAEEL--LEALRAAAELAAQLEELEEAEEALLER 415
|
250 260
....*....|....*....|
gi 112363107 472 LTAIAEELAASAKEEKEEAE 491
Cdd:COG1196 416 LERLEEELEELEEALAELEE 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
96-479 |
9.80e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 96 RSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDH 175
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 176 LEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLrsnhEEEVADLLAQIQASHITVE 255
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL----ELQIASLNNEIERLEARLE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 256 ----RKDYLKTDISTALKEIRSQ--LECHSDQNMHQAEEwfkcryAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIEL 329
Cdd:TIGR02168 411 rledRRERLQQEIEELLKKLEEAelKELQAELEELEEEL------EELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 330 ESVRGTKESLERQLSDIEERHNH----------------------------------------------DLSSYQDTIQQ 363
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGvkallknqsglsgilgvlselisvdegyeaaieaalggrlqavvveNLNAAKKAIAF 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 112363107 364 LE-----------------NELRGTKWEMARHLREYQDLL-------------------NVKMALDIEIAAYRKLLEGEE 407
Cdd:TIGR02168 565 LKqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAkdlvkfdpklrkalsyllgGVLVVDDLDNALELAKKLRPG 644
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 112363107 408 TRFSTFSGSITGPLYTHRQPSVTISSKIQKTKVEapklkvqhkfveeiIEEtkVEDEKSEMEETLTAIAEEL 479
Cdd:TIGR02168 645 YRIVTLDGDLVRPGGVITGGSAKTNSSILERRRE--------------IEE--LEEKIEELEEKIAELEKAL 700
|
|
| |
