|
Name |
Accession |
Description |
Interval |
E-value |
| NUDE_C |
pfam04880 |
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ... |
135-309 |
1.74e-54 |
|
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.
Pssm-ID: 461464 [Multi-domain] Cd Length: 169 Bit Score: 176.13 E-value: 1.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 135 SLEDFEQRLNQAIERNAFLESEL----DDKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSP---TLDCEKMD 207
Cdd:pfam04880 1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRSPSTPslqTLEIFDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 208 SAVQASlslpATPVG-KGSENSFPSpkAIPNGFGTSPLTPSARISAlnivgDLLRKVGALESKLAACRNFAKDQASRKSY 286
Cdd:pfam04880 81 PAVQAV----SSPVIaTPPEKSFNS--LRTGSETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNASRRG 149
|
170 180
....*....|....*....|...
gi 2201757476 287 isgNANSSMMSSNGTKYPHPGHT 309
Cdd:pfam04880 150 ---NSRSLYGSRPPTKFAHSRHT 169
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-195 |
1.95e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAqsykQVSLLEDDLSQ 103
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 104 TRAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELAV 183
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170
....*....|..
gi 2201757476 184 RERQQEVTRKSA 195
Cdd:COG1196 429 ALAELEEEEEEE 440
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-193 |
5.21e-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: 57.76 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRA 106
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 107 IKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLvsvQRLKDEARDLRQELAVRER 186
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI---EELESELEALLNERASLEE 887
|
....*..
gi 2201757476 187 QQEVTRK 193
Cdd:TIGR02168 888 ALALLRS 894
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
13-189 |
5.58e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 13 KEETAYWKELSLKYKQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEK---LEHQYAQ 89
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 90 SYKQVSLLEDDLSQTRAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQR 169
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180
....*....|....*....|
gi 2201757476 170 LKDEARDLRQELAVRERQQE 189
Cdd:COG1196 380 ELEELAEELLEALRAAAELA 399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
27-192 |
5.52e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVETL-----KEKLEHQYAQSYKQVSLLEDDL 101
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 102 SQTRAIKDQLHKYVRELEQANDDLERAKR----ATIVSLEDFEQRLNQAIERNAFLESELDDKESllvSVQRLKDEARDL 177
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEqlslATEEELQDLAEELEELQQRLAELEEELEEAQE---ELEELEEELEQL 232
|
170
....*....|....*
gi 2201757476 178 RQELAVRERQQEVTR 192
Cdd:COG4717 233 ENELEAAALEERLKE 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
45-192 |
7.13e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 45 RELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHqyAQSYKQVSLLEDDLSQTRAIKDQLHKYVRELEQANDD 124
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA--LQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 125 LERAKR---ATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDL------------RQELAVRERQQE 189
Cdd:COG4913 687 LAALEEqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelralleerFAAALGDAVERE 766
|
...
gi 2201757476 190 VTR 192
Cdd:COG4913 767 LRE 769
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
28-192 |
1.12e-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: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 28 QSFQEAREELAEFQE---------GSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVETLKEK---LEHQYAQS-YKQV 94
Cdd:COG4913 262 ERYAAARERLAELEYlraalrlwfAQRRLE-LLEAELEELRAELARLEAELERLEARLDALREEldeLEAQIRGNgGDRL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 95 SLLEDDLSQTRAIKDQLhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLvsvQRLKDEA 174
Cdd:COG4913 341 EQLEREIERLERELEER---ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAAL 414
|
170
....*....|....*...
gi 2201757476 175 RDLRQELavRERQQEVTR 192
Cdd:COG4913 415 RDLRREL--RELEAEIAS 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
31-188 |
1.17e-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: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADnqrlkyevetlKEKLEHQYAQS-YKQVSLLEDDLSQTRAIKD 109
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREE-----------LDELEAQIRGNgGDRLEQLEREIERLERELE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 110 QLhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKE----SLLVSVQRLKDEARDLRQELAVRE 185
Cdd:COG4913 356 ER---ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELEAEIASLE 432
|
...
gi 2201757476 186 RQQ 188
Cdd:COG4913 433 RRK 435
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
31-258 |
2.12e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYaQSYKQVSLLE------------ 98
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY-RSGGSVSYLDvllgsesfsdfl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 99 DDLSQTRAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLR 178
Cdd:COG3883 119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 179 QELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGSENSFPSPKAIPNGFGTSPLTPSARISALNIVGD 258
Cdd:COG3883 199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-202 |
2.22e-07 |
|
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: 52.76 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 13 KEETAYWkELSLKYKqsfqEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYK 92
Cdd:TIGR02169 220 KREYEGY-ELLKEKE----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 93 QVSLLEDDLSQTRAIKDQLHKYVRELE--QANDDLERakRATIVSLEDFEQRLNQAIERNAFLESELDDK----ESLLVS 166
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEerLAKLEAEI--DKLLAEIEELEREIEEERKRRDKLTEEYAELkeelEDLRAE 372
|
170 180 190
....*....|....*....|....*....|....*..
gi 2201757476 167 VQRLKDEARDLRQELA-VRERQQEVTRKSAPSSPTLD 202
Cdd:TIGR02169 373 LEEVDKEFAETRDELKdYREKLEKLKREINELKRELD 409
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
27-199 |
2.28e-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: 52.07 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYK-------QVSLLED 99
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRlgrqpplALLLSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 100 DLSQT-------RAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQR--- 169
Cdd:COG4942 130 DFLDAvrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKela 209
|
170 180 190
....*....|....*....|....*....|....*...
gi 2201757476 170 --------LKDEARDLRQELAVRERQQEVTRKSAPSSP 199
Cdd:COG4942 210 elaaelaeLQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-195 |
2.90e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRAIKDQ 110
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 111 LHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELAVRERQQEV 190
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
....*
gi 2201757476 191 TRKSA 195
Cdd:COG1196 482 LLEEL 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-195 |
2.95e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRAI 107
Cdd:COG1196 305 ARLEERRRELEERLEELEEElaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 108 KDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELAVRERQ 187
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
....*...
gi 2201757476 188 QEVTRKSA 195
Cdd:COG1196 465 LAELLEEA 472
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
13-189 |
3.88e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 13 KEETAYWKELSLKYKQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSyK 92
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA-A 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 93 QVSLLEDDLSQTRAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKD 172
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
170
....*....|....*..
gi 2201757476 173 EARDLRQELAVRERQQE 189
Cdd:COG1196 481 ELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-189 |
4.06e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRAIKDQ 110
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201757476 111 LHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELAVRERQQE 189
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-189 |
4.67e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRA 106
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 107 IKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELAVRER 186
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
...
gi 2201757476 187 QQE 189
Cdd:COG1196 471 EAA 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-195 |
5.04e-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: 51.60 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 24 LKYKQSFQEAREELAEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVETLK----------EKLEHQYAQS 90
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAElrkELEELEEELEQLRKELEELSRQISALRkdlarleaevEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 91 YKQVSLLEddlsqtraikDQLHKYVRELEQANDDLERAKRativSLEDFEQRLNQAIERNAFLESELDDKESllvSVQRL 170
Cdd:TIGR02168 753 SKELTELE----------AEIEELEERLEEAEEELAEAEA----EIEELEAQIEQLKEELKALREALDELRA---ELTLL 815
|
170 180
....*....|....*....|....*
gi 2201757476 171 KDEARDLRQELAVRERQQEVTRKSA 195
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRL 840
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
13-189 |
6.68e-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: 51.21 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 13 KEETAYWKELSLKYKQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQAdnqrlkyevetlkekLEHQYAQSYK 92
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ---------------LELQIASLNN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 93 QVSLLEDDLSQtraIKDQLHKYVRELEQANDDLERAKRATIVS-LEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLK 171
Cdd:TIGR02168 401 EIERLEARLER---LEDRRERLQQEIEELLKKLEEAELKELQAeLEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
170 180
....*....|....*....|..
gi 2201757476 172 DEARD----LRQELAVRERQQE 189
Cdd:TIGR02168 478 DAAERelaqLQARLDSLERLQE 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-190 |
7.01e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRAIKDQ 110
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 111 LHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELAVRERQQEV 190
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
25-187 |
2.32e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 25 KYKQSFQEAREELAEFQEGSRELE------------AELEAQLVQAEQRNRDLQAD----NQRLKYEVETLKEKLEHQYA 88
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGLVDlseeaklllqqlSELESQLAEARAELAEAEARlaalRAQLGSGPDALPELLQSPVI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 89 QSYK-QVSLLEDDLSQTRAIKDQLHKYVRELEQANDDLERAKRATIVS-LEDFEQRLNQAIERNAFLESELDDKESLLVS 166
Cdd:COG3206 266 QQLRaQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRiLASLEAELEALQAREASLQAQLAQLEARLAE 345
|
170 180
....*....|....*....|.
gi 2201757476 167 VQRLKDEARDLRQELAVRERQ 187
Cdd:COG3206 346 LPELEAELRRLEREVEVAREL 366
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-189 |
2.94e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRA 106
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 107 IKDQLhkyvRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELAVRER 186
Cdd:COG1196 426 LEEAL----AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
...
gi 2201757476 187 QQE 189
Cdd:COG1196 502 DYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
39-195 |
3.08e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 39 EFQEGSRELEAELeaQLVQAEQRNRDLQADNQRLKyEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRAIKDQLHKYVREL 118
Cdd:COG1196 217 ELKEELKELEAEL--LLLKLRELEAELEELEAELE-ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201757476 119 EQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSA 195
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-194 |
4.58e-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: 48.51 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQEgsreleaELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRA 106
Cdd:TIGR02168 304 KQILRERLANLERQLE-------ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 107 IKDQLHKYVRELEQANDDLERAkRATIVS----LEDFEQRLNQAIERNAFLESELDDKESLLVSVQ--RLKDEARDLRQE 180
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASL-NNEIERlearLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEE 455
|
170
....*....|....
gi 2201757476 181 LAVRERQQEVTRKS 194
Cdd:TIGR02168 456 LERLEEALEELREE 469
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
20-197 |
6.67e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 20 KELSLKYKQSFQEAREELAEFQEGSRELE---------AELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQyaQS 90
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKeaeekeeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--PL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 91 YKQVSLLEDDLSQTRAIKDQLHKYVRELEQANDDLERAKRAtivsLEDFEQRLNQAIERNAF-----LESELDDKESLLV 165
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEELRELEEELEELEAE----LAELQEELEELLEQLSLateeeLQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|..
gi 2201757476 166 SVQRLKDEARDLRQELAVRERQQEVTRKSAPS 197
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-195 |
1.01e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 20 KELSLkYKQSFQEAREELAEFQEgsreLEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLED 99
Cdd:TIGR02168 225 LELAL-LVLRLEELREELEELQE----ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 100 DLSQTRAIKDQLHKYVRELEQANDDLERAkrativsledfEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQ 179
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEEL-----------ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170
....*....|....*...
gi 2201757476 180 EL--AVRERQQEVTRKSA 195
Cdd:TIGR02168 369 ELesRLEELEEQLETLRS 386
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
13-182 |
1.21e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 13 KEETAYWKELSLKYKQSFQEAREELAEFQEGSRELE---AELEAQLVQAEQRNRDLQADNQRLKYEVE---TLKEKLEHQ 86
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLErriAATERRLEDLEEQIEELSEDIESLAAEIEeleELIEELESE 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 87 YAQSYKQVSLLEDDLSQTRAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQA-IERNAFLES-------ELD 158
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLeVRIDNLQERlseeyslTLE 954
|
170 180
....*....|....*....|....*...
gi 2201757476 159 DKESLLV----SVQRLKDEARDLRQELA 182
Cdd:TIGR02168 955 EAEALENkiedDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-177 |
1.30e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQEGSRELEAELEAQ---LVQAEQRNRDLQADNQRLKYEVETLK--------EKLEHQYAQSYKQVS 95
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLrskVAQLELQIASLNNEIERLEARLERLEdrrerlqqEIEELLKKLEEAELK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 96 LLEDDLSQTRAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEAR 175
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
..
gi 2201757476 176 DL 177
Cdd:TIGR02168 517 GL 518
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
27-183 |
2.39e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQEGSRELEAELEA-----QLVQAEQRnrdLQADNQRLKYEVETLKEKLEHQ---YAQSYKQVSLLE 98
Cdd:COG3096 305 QYRLVEMARELEELSARESDLEQDYQAasdhlNLVQTALR---QQEKIERYQEDLEELTERLEEQeevVEEAAEQLAEAE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 99 DDLSQTRA----IKDQLHKYVRELE----------QANDDLERAKR---ATIVSLEDFEQRLnqaiernafleSELDDKE 161
Cdd:COG3096 382 ARLEAAEEevdsLKSQLADYQQALDvqqtraiqyqQAVQALEKARAlcgLPDLTPENAEDYL-----------AAFRAKE 450
|
170 180
....*....|....*....|..
gi 2201757476 162 sllvsvQRLKDEARDLRQELAV 183
Cdd:COG3096 451 ------QQATEEVLELEQKLSV 466
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
31-196 |
2.43e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHqyaqsykqvslLEDDLSQTRAi 107
Cdd:COG1579 20 DRLEHRLKELPAELAELEDElaaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-----------YEEQLGNVRN- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 108 kdqlhkyVRELEQANDDLERAKRAtIVSLEDFEQRLNQAIERN----AFLESELDDKESLLVSVQ-RLKDEARDLRQELA 182
Cdd:COG1579 88 -------NKEYEALQKEIESLKRR-ISDLEDEILELMERIEELeeelAELEAELAELEAELEEKKaELDEELAELEAELE 159
|
170
....*....|....
gi 2201757476 183 VRERQQEVTRKSAP 196
Cdd:COG1579 160 ELEAEREELAAKIP 173
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
31-196 |
5.96e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEAELEAQLVQ-AEQRNRDLQADNQRLKYEVETL---KEKLEHQYAQSYKQVSLLEDDLSQTRA 106
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQeLQEQRIDLKEQIKSIEKEIENLngkKEELEEELEELEAALRDLESRLGDLKK 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 107 IKDQLHKYVRELEQANDDLErakratiVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELAVRER 186
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELE-------AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR 962
|
170
....*....|
gi 2201757476 187 QQEVTRKSAP 196
Cdd:TIGR02169 963 VEEEIRALEP 972
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
31-148 |
6.75e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLqadnQRLKYEVETLKEKLEHQYA--QSYKQVSLLEDDLSQTRAIK 108
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEA----EALLKEAEKLKEELEEKKEklQEEEDKLLEEAEKEAQQAIK 580
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2201757476 109 ------DQLHKYVRELEQANDDLERAKRativsLEDFEQRLNQAIE 148
Cdd:PRK00409 581 eakkeaDEIIKELRQLQKGGYASVKAHE-----LIEARKRLNKANE 621
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
31-190 |
8.79e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEAELEAQlvqaeQRNRDLQADNQRLKYEVETLKEKLEH----------QYAQSYKQVSLLEDD 100
Cdd:PRK02224 568 EEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREAlaelnderreRLAEKRERKRELEAE 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 101 -----LSQTRAIKDQLHKYVRELEQANDDLERAK---RATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKD 172
Cdd:PRK02224 643 fdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERREALENRVEALEALYDEAEELES 722
|
170
....*....|....*...
gi 2201757476 173 EARDLRQELavreRQQEV 190
Cdd:PRK02224 723 MYGDLRAEL----RQRNV 736
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
31-174 |
9.07e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.90 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEA---ELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKL---EHQYAQSYKQVSLLEDDLSQT 104
Cdd:pfam19220 100 REAEAAKEELRIELRDKTAqaeALERQLAAETEQNRALEEENKALREEAQAAEKALqraEGELATARERLALLEQENRRL 179
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2201757476 105 RAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLL---VSVQRLKDEA 174
Cdd:pfam19220 180 QALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHraeRASLRMKLEA 252
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
22-149 |
9.91e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 22 LSLKyKQSFQEAREELAEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVETLKekleHQYAQSYKQVSLLE 98
Cdd:PRK09039 69 LSLE-RQGNQDLQDSVANLRASLSAAEAErsrLQALLAELAGAGAAAEGRAGELAQELDSEK----QVSARALAQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2201757476 99 DDLSQTRAikdQLHKyvreLEQANDDLERAKRATIVSLEDFEQRLNQAIER 149
Cdd:PRK09039 144 QQIAALRR---QLAA----LEAALDASEKRDRESQAKIADLGRRLNVALAQ 187
|
|
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
29-154 |
1.41e-04 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 43.15 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 29 SFQEAREELAEFQEGSREleaeleAQLVQAeqrnrdlQADNQR--LKYEVETLKEKLEHqyaqsykqvslLEDDLSQTRa 106
Cdd:pfam09738 87 SLRDIKHELKEVEEKYRK------AMISNA-------QLDNEKsnLMYQVDLLKDKLEE-----------MEESLAELQ- 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2201757476 107 ikdqlhkyvRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLE 154
Cdd:pfam09738 142 ---------RELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-195 |
1.58e-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: 43.52 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 10 SSPKEETAYWKELSLKYKQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQ------ADNQRLKYEVETLKEKL 83
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqeiENVKSELKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 84 EHQYAQSYKQVSLLEDDLSQTRaikdqlhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESL 163
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLSHSR---------IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190
....*....|....*....|....*....|....
gi 2201757476 164 LVSVQRLKDEARDLRQEL--AVRERQQEVTRKSA 195
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLngKKEELEEELEELEA 875
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
20-182 |
1.87e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 20 KELSLKYKQSF---QEAREELAEFQEGSRELEAELE-----------AQLVQAEQrnRDLQADNQRLKYeVETLKEKLEH 85
Cdd:COG0497 154 EELLEEYREAYrawRALKKELEELRADEAERARELDllrfqleeleaAALQPGEE--EELEEERRRLSN-AEKLREALQE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 86 QYAqsykqvsLLEDD----LSQTRAIKDQLHKYVRELEQANDDLERAKRATIvSLEDFEQRLNQAIERNAFLESELDDKE 161
Cdd:COG0497 231 ALE-------ALSGGeggaLDLLGQALRALERLAEYDPSLAELAERLESALI-ELEEAASELRRYLDSLEFDPERLEEVE 302
|
170 180
....*....|....*....|....*...
gi 2201757476 162 SLLVSVQRLK-------DEARDLRQELA 182
Cdd:COG0497 303 ERLALLRRLArkygvtvEELLAYAEELR 330
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
27-193 |
3.03e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRA 106
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE-QLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 107 IKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELAVRER 186
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
....*..
gi 2201757476 187 QQEVTRK 193
Cdd:COG4372 189 LKEANRN 195
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
31-182 |
3.13e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEA-------------ELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEH-QYAQSYKQVSL 96
Cdd:COG4913 671 AELEAELERLDASSDDLAAleeqleeleaeleELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRAL 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 97 LEDDLSQ----------TRAIKDQLHKYVRELEQANDDLERAKR--------------ATIVSLEDFEQRLNQAIE---- 148
Cdd:COG4913 751 LEERFAAalgdaverelRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldADLESLPEYLALLDRLEEdglp 830
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2201757476 149 ------RNAFLESELDDKESLLvsvQRLKDEARDLRQELA 182
Cdd:COG4913 831 eyeerfKELLNENSIEFVADLL---SKLRRAIREIKERID 867
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
14-211 |
3.55e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 14 EETAYWKELSLKYKQSFQEAREELAEFQEGSRELE-----AELEAQLVQAEQRNRDLQADNQRLKyEVETLKEKLEHQYA 88
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEQQAQRIHTELQ-SKMRSRAKLLMKRA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 89 QSYKQvsllEDDLSQTRAIKDQLHKYVRELEQANDD----LERAKRATIVS--LEDFEQRLNQAIERNAFLESELDDKES 162
Cdd:TIGR00618 332 AHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEVatsiREISCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDILQR 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2201757476 163 LLVSVQRLKDEARDLRQELAVRERQQEVTRKSAP-----SSPTLDCEKMDSAVQ 211
Cdd:TIGR00618 408 EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAElcaaaITCTAQCEKLEKIHL 461
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
20-193 |
4.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 20 KELSLKYKQSFQEAREELAEFQEGSRELEAEL---------EAQLVQAEQRNRDLQADNQRLK-YEVETLK------EKL 83
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELrelekvlkkESELIKLKELAEQLKELEEKLKkYNLEELEkkaeeyEKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 84 EHQYAQSYKQVSLLEDDL-------SQTRAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELekleelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA 610
|
170 180 190
....*....|....*....|....*....|....*..
gi 2201757476 157 LDDKESLLVSVQRLKDEARDLRQELAVRERQQEVTRK 193
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
27-223 |
4.80e-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: 41.98 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRA 106
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 107 IKDQLHKY-----------------------VRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESElddKESL 163
Cdd:TIGR02169 929 LEEELSEIedpkgedeeipeeelsledvqaeLQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE---RKAI 1005
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2201757476 164 LVSVQRLKDEARDLRQEL--AVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGK 223
Cdd:TIGR02169 1006 LERIEEYEKKKREVFMEAfeAINENFNEIFAELSGGTGELILENPDDPFAGGLELSAKPKGK 1067
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
13-183 |
5.99e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 13 KEETAYWKELSLKYKQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYK 92
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 93 QVSLLeddLSQTRAIKDQLHKYVRELEQANDDLERAKRATIVSLEDfeqrLNQAIERNAFLESELDDkesLLVSVQRLKD 172
Cdd:pfam05483 241 QVSLL---LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN----LKELIEKKDHLTKELED---IKMSLQRSMS 310
|
170
....*....|.
gi 2201757476 173 EARDLRQELAV 183
Cdd:pfam05483 311 TQKALEEDLQI 321
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
21-192 |
8.51e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 21 ELSLKYKQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEK---LEHQYAQSYKQVSLL 97
Cdd:pfam17045 74 ELVAKYEQQLQKLQEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKsleWEQQRLQYQQQVASL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 98 EddlSQTRAIKDQL-----HKYVRELEQANDDLErAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQR-LK 171
Cdd:pfam17045 154 E---AQRKALAEQSsliqsAAYQVQLEGRKQCLE-ASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGDSNRkLL 229
|
170 180
....*....|....*....|.
gi 2201757476 172 DEARDLRQELAVRERQQEVTR 192
Cdd:pfam17045 230 EEQQRLLEELRMSQRQLQVLQ 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-196 |
9.98e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 24 LKYKQSFQEAREELAEFQEGSRELE---AELEAQLV----QAE--QRNRDLQADNQRLK-----YEVETLKEKLEH---Q 86
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENLDRLEdilNELERQLKslerQAEkaERYKELKAELRELElallvLRLEELREELEElqeE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 87 YAQSYKQVSLLEDDLSQTRAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVS 166
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190
....*....|....*....|....*....|
gi 2201757476 167 VQRLKDEARDLRQELAVRERQQEVTRKSAP 196
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLE 357
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
34-157 |
1.04e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 34 REELAEfqegSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQyaQSYKQvslledDLSQTRAIKDQLHK 113
Cdd:pfam13851 32 KEEIAE----LKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY--EKDKQ------SLKNLKARLKVLEK 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2201757476 114 YVRELEQANDDLERAKRATIVSLEDFEQRLNQAIE--------RNAFLESEL 157
Cdd:pfam13851 100 ELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQdvqqktglKNLLLEKKL 151
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
49-184 |
1.08e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.42 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 49 AELEAQLVQAEQRNRDLQADNQRLKYEVETLKEK--LEHQYAQSYKQVSLLEDDLSQTRAIKDQlhKYV--RELEQANDD 124
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIaaAEAQLAAAQAQLDLAQRELERYQALYKK--GAVsqQELDEARAA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 125 LERAKRAtivsLEDFEQRLNQAiERNAFLESELDDKESLLVSVQRLKDEARDLRQELAVR 184
Cdd:COG1566 157 LDAAQAQ----LEAAQAQLAQA-QAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIR 211
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
32-195 |
1.13e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 32 EAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRAIKDQL 111
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 112 hKYVRELEQANDDLERAKRATIVSledfEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELAVRERQQEVT 191
Cdd:pfam02463 233 -KLNEERIDLLQELLRDEQEEIES----SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
....
gi 2201757476 192 RKSA 195
Cdd:pfam02463 308 RKVD 311
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-177 |
1.14e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRA 106
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 107 IKDQLHKYVRELEQANDDLERAKRAtIVSL--------EDFEqrlnQAIERNAFLESELDD----KESLLVSVQRLKDEA 174
Cdd:COG1196 751 EALEELPEPPDLEELERELERLERE-IEALgpvnllaiEEYE----ELEERYDFLSEQREDleeaRETLEEAIEEIDRET 825
|
...
gi 2201757476 175 RDL 177
Cdd:COG1196 826 RER 828
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
21-251 |
1.16e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.89 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 21 ELSLKYKQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQ----------S 90
Cdd:pfam07111 478 DLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQlevarqgqqeS 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 91 YKQVSLLEDDLSQTRAIKDQ-LHKYVRELE-----QANDDLERAKRA------TIVSLEDFEQRLNQAIERNAFLeseld 158
Cdd:pfam07111 558 TEEAASLRQELTQQQEIYGQaLQEKVAEVEtrlreQLSDTKRRLNEArreqakAVVSLRQIQHRATQEKERNQEL----- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 159 dkesllvsvQRLKDEARDLRQELAVReRQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGSENSFPSPKAIPNG 238
Cdd:pfam07111 633 ---------RRLQDEARKEEGQRLAR-RVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSA 702
|
250
....*....|...
gi 2201757476 239 FGTSPLTPSARIS 251
Cdd:pfam07111 703 SAPIPAAVPTRES 715
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
143-189 |
1.40e-03 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 39.96 E-value: 1.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2201757476 143 LNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELAVRERQQE 189
Cdd:PRK13922 71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNLKESLDY 117
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
44-200 |
1.60e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 39.71 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 44 SRELEAELEAQLVQAEQRNRDLQADNQRLKyEVETLKEKLEHQYAQSYkqvslleddlSQTRAIKDQLHKYVRELEQAND 123
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQ-ALESELAISRQDYDGAT----------AQLRAAQAAVKAAQAQLAQAQI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 124 DLERAK-RATI--VSLEDF-EQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQELA-----VRERQQEVTRKS 194
Cdd:pfam00529 125 DLARRRvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlqIAEAEAELKLAK 204
|
....*.
gi 2201757476 195 APSSPT 200
Cdd:pfam00529 205 LDLERT 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
41-194 |
1.94e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 41 QEGSRELEAELEaQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRA----IKDQLHKYVR 116
Cdd:COG4942 19 ADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAelaeLEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 117 ELEQANDDLERAKRAT-----------IVSLEDFEQ--RLNQAIER-NAFLESELDDKESLLVSVQRLKDEARDLRQELA 182
Cdd:COG4942 98 ELEAQKEELAELLRALyrlgrqpplalLLSPEDFLDavRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170
....*....|..
gi 2201757476 183 VRERQQEVTRKS 194
Cdd:COG4942 178 ALLAELEEERAA 189
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
27-189 |
2.04e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEARE--ELAEF-QEGSRELEAELEAQLVQAEQRNRDLQadnQRLkyeveTLKEKLEHQYAQSYKQVSLLEDDLSQ 103
Cdd:PRK04863 420 VQALERAKQlcGLPDLtADNAEDWLEEFQAKEQEATEELLSLE---QKL-----SVAQAAHSQFEQAYQLVRKIAGEVSR 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 104 TRA-------IKD------------QLHKYVRELEQANDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDDKESLL 164
Cdd:PRK04863 492 SEAwdvarelLRRlreqrhlaeqlqQLRMRLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARL 567
|
170 180
....*....|....*....|....*
gi 2201757476 165 VSvqrLKDEARDLRQELAVRERQQE 189
Cdd:PRK04863 568 ES---LSESVSEARERRMALRQQLE 589
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
27-142 |
2.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 27 KQSFQEAREELAEFQE-----GSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDL 101
Cdd:COG4913 315 EARLDALREELDELEAqirgnGGDRLE-QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2201757476 102 SQTRAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQR 142
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
42-187 |
2.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 42 EGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLK--EKLEHQYAQSYKQVSLLEDDLSQTRAIKDQLHKYVRELE 119
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201757476 120 --------QANDDLERA--KRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLkdeaRDLRQELAVRERQ 187
Cdd:PRK02224 551 aeaeekreAAAEAEEEAeeAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERL----REKREALAELNDE 624
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
23-131 |
2.37e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 23 SLKYKQSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLLEDDLS 102
Cdd:COG4942 137 RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
90 100
....*....|....*....|....*....
gi 2201757476 103 QTRAIKDQLHKYVRELEQANDDLERAKRA 131
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| FtsB |
COG2919 |
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning]; |
49-84 |
2.43e-03 |
|
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442163 [Multi-domain] Cd Length: 96 Bit Score: 36.78 E-value: 2.43e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2201757476 49 AELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLE 84
Cdd:COG2919 32 RELRQEIAELEAENAKLKARNAELEAEVADLKDGPD 67
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
32-174 |
2.47e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 32 EAREELAEFQEGSRELEAELEAQlVQAEQRNRDLQADNQRL----------KYEVETLKEKLEHQYAQSYKQVSLLEDDL 101
Cdd:pfam01576 630 EAREKETRALSLARALEEALEAK-EELERTNKQLRAEMEDLvsskddvgknVHELERSKRALEQQVEEMKTQLEELEDEL 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 102 SQTRAIKDQLH--------KYVRELeQANDDLERAKRATIVS--------LEDFEQRLNQAIERNAFLESELDDKESLLV 165
Cdd:pfam01576 709 QATEDAKLRLEvnmqalkaQFERDL-QARDEQGEEKRRQLVKqvreleaeLEDERKQRAQAVAAKKKLELDLKELEAQID 787
|
....*....
gi 2201757476 166 SVQRLKDEA 174
Cdd:pfam01576 788 AANKGREEA 796
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-180 |
2.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 28 QSFQEAREELAEFQEGSR--------------ELEAELEAQLVQAEQRNRDLQADNQRLKYEVETLKEK---LEHQYAQS 90
Cdd:PRK02224 282 RDLRERLEELEEERDDLLaeaglddadaeaveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDaddLEERAEEL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 91 YKQVSLLEDDLSQTRAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRL 170
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER 441
|
170
....*....|
gi 2201757476 171 KDEARDLRQE 180
Cdd:PRK02224 442 VEEAEALLEA 451
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-192 |
2.74e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 28 QSFQEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKY-EVETLKEKLEHQYAQSYKQVSLLEDDLSQTRA 106
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 107 IKDQLHKYVRELEQANDDLERAK---RATIVSL----EDFEQRL-------NQAIERNAFLESELDDKESLLVSVQRLKD 172
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIksiEKEIENLngkkEELEEELeeleaalRDLESRLGDLKKERDELEAQLRELERKIE 906
|
170 180
....*....|....*....|
gi 2201757476 173 EARDLRQELAVRERQQEVTR 192
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKL 926
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
13-183 |
2.80e-03 |
|
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: 39.49 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 13 KEETAYWKELSLKYKQSFQEAREELAEFQEgSRELEAELEAQLVQAEQRNRDLQ----------ADNQRLKYEVETLKEK 82
Cdd:pfam07888 167 KEEEAERKQLQAKLQQTEEELRSLSKEFQE-LRNSLAQRDTQVLQLQDTITTLTqklttahrkeAENEALLEELRSLQER 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 83 LehqyAQSYKQVSLLEDDLSQTRAIKDQ----LHKYVRELEQANDDLERAkrativSLEDFEQRLNQAIERNAFLESELD 158
Cdd:pfam07888 246 L----NASERKVEGLGEELSSMAAQRDRtqaeLHQARLQAAQLTLQLADA------SLALREGRARWAQERETLQQSAEA 315
|
170 180 190
....*....|....*....|....*....|.
gi 2201757476 159 DKESLL---VSVQRLKD---EARDLRQELAV 183
Cdd:pfam07888 316 DKDRIEklsAELQRLEErlqEERMEREKLEV 346
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
22-194 |
2.98e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 22 LSLKYKQSFQ-EAREELAEFQEGSRELEAELE---AQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKQVSLL 97
Cdd:TIGR02169 660 RAPRGGILFSrSEPAELQRLRERLEGLKRELSslqSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 98 EDDLSQTRAIKDQLHKYVRELEQANDDLERaKRATIV----SLEDFEQRLNQAI------------ERNAFLESELDDKE 161
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEE-LEEDLHkleeALNDLEARLSHSRipeiqaelskleEEVSRIEARLREIE 818
|
170 180 190
....*....|....*....|....*....|...
gi 2201757476 162 SLLVSVQRLKDEARDLRQELAVRERQQEVTRKS 194
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
71-182 |
3.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 71 RLKYEVETLKEKLEH-----QYAQSYKQvslLEDDLSQTRAIKDQLHKYVRE-----LEQANDDLERAKRATIVSLEDFE 140
Cdd:COG4913 239 RAHEALEDAREQIELlepirELAERYAA---ARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELERLE 315
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2201757476 141 QRLNQAIE-----RNAFLESELDDKESLLVSVQRLKDEARDLRQELA 182
Cdd:COG4913 316 ARLDALREeldelEAQIRGNGGDRLEQLEREIERLERELEERERRRA 362
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
13-193 |
3.57e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 13 KEETAYwkELSLKYKQSFQEAREELAEFQEGSRELE---AELEAQLVQAEQRNRDLQADNQRLKYEVETLK------EKL 83
Cdd:PRK03918 159 DYENAY--KNLGEVIKEIKRRIERLEKFIKRTENIEeliKEKEKELEEVLREINEISSELPELREELEKLEkevkelEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 84 EHQYAQSYKQVSLLEDDLSQTRAIKDQLHKYVRELEQANDDLERaKRATIVSLEDFEQR-------LNQAIERNAFLESE 156
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE-KVKELKELKEKAEEyiklsefYEEYLDELREIEKR 315
|
170 180 190
....*....|....*....|....*....|....*...
gi 2201757476 157 LDDKESLLVSVQRLKDEARDLRQELA-VRERQQEVTRK 193
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEeLKKKLKELEKR 353
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
25-149 |
3.58e-03 |
|
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: 38.37 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 25 KYKQSFQEAREELAEFQEGSRELEAELE---AQLVQAEQR------NRDLQAdnqrLKYEVETLKeklehqyaqsyKQVS 95
Cdd:COG1579 42 ALEARLEAAKTELEDLEKEIKRLELEIEeveARIKKYEEQlgnvrnNKEYEA----LQKEIESLK-----------RRIS 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2201757476 96 LLEDDLSQTRAIKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIER 149
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
28-181 |
4.13e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.17 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 28 QSFQEAREELAEFQEGSRELeAELEAQLVQAEQRNRDLQAD---NQRLKYEVETLKEKLEHQYAQSYKQVSLLE------ 98
Cdd:COG3096 893 DRLEELREELDAAQEAQAFI-QQHGKALAQLEPLVAVLQSDpeqFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfs 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 99 -----DDLSQTRAIKDQLHkyvRELEQANDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDDKESLLVSV-QRLKD 172
Cdd:COG3096 972 yedavGLLGENSDLNEKLR---ARLEQAEEARREAREQ----LRQAQAQYSQYNQVLASLKSSRDAKQQTLQELeQELEE 1044
|
170 180
....*....|....*....|
gi 2201757476 173 -----------EARDLRQEL 181
Cdd:COG3096 1045 lgvqadaeaeeRARIRRDEL 1064
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
49-196 |
4.30e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 37.63 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 49 AELEAQLVQAEQR-----NRDLQADNQRLKYEVETLKEKLEhQYAQSYKQVslLEDDLSQTRAikdQLHKYVREL-EQAN 122
Cdd:pfam01442 14 EELQEQLGPVAQElvdrlEKETEALRERLQKDLEEVRAKLE-PYLEELQAK--LGQNVEELRQ---RLEPYTEELrKRLN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201757476 123 DDLERAKRATIVSLEDFEQRLNQAIER-NAFLESELDD-KESLLVSVQRLKDEARDLRQEL--AVRERQQEVTRKSAP 196
Cdd:pfam01442 88 ADAEELQEKLAPYGEELRERLEQNVDAlRARLAPYAEElRQKLAERLEELKESLAPYAEEVqaQLSQRLQELREKLEP 165
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
41-195 |
4.70e-03 |
|
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: 38.72 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 41 QEGSRELEAELEAQLVQAEQRNRDlqadnqrlKYEVETLKEKLEHQYAQSYKQVSLLEDDLSQTRAIKDQLHKYVRELEQ 120
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKE--------KERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201757476 121 ANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLvsvQRLKDeardlRQELAVRERQQEVTRKSA 195
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL---ERMKE-----RAKKAGAQRKEEEAERKQ 175
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
30-189 |
6.16e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 38.62 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 30 FQEAREELAEFQEGSRELEA---ELEAQLVQAEQRNRDLQADNQRLKYEVETLKEKLEHQYAQSYKqvslLEDDLSQTRA 106
Cdd:pfam01576 56 CAEAEEMRARLAARKQELEEilhELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQK----LQLEKVTTEA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 107 IKDQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQ-RLKDEARdLRQELAVRE 185
Cdd:pfam01576 132 KIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEeRLKKEEK-GRQELEKAK 210
|
....
gi 2201757476 186 RQQE 189
Cdd:pfam01576 211 RKLE 214
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
35-182 |
6.87e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 38.28 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 35 EELAEFQEGSRELEAELEAQLVQAEQRNRD-LQADNQRLKYEVETLKEKLEHQYAQsYKQVSLLEDDLSQTRAIKDQLHK 113
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESELREqLEAGKLEFNEEEYRLKSRLGELKLR-LNQATATPELLLQLENFDERIER 475
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2201757476 114 YVRELEQANDDLERAKRA----------TIVSLEDFEQRLNQAIERNAFLESELDDKESLLVSVqrLKDEARDLRQELA 182
Cdd:pfam12128 476 AREEQEAANAEVERLQSElrqarkrrdqASEALRQASRRLEERQSALDELELQLFPQAGTLLHF--LRKEAPDWEQSIG 552
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
8-181 |
7.12e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 38.18 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 8 TFSSPKEETAYWKELSLKYKQSFQEAREELAEFQEGSRELEAELEaqlvQAEQRNRDLQADNQRLKYEVETLKEkLEhqy 87
Cdd:pfam05557 105 VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS----EAEQLRQNLEKQQSSLAEAEQRIKE-LE--- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 88 aqsyKQVSLLEDDLSQTRAIKDQLHKYvreleqanDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDDKESLLVSV 167
Cdd:pfam05557 177 ----FEIQSQEQDSEIVKNSKSELARI--------PELEKELER----LREHNKHLNENIENKLLLKEEVEDLKRKLERE 240
|
170
....*....|....
gi 2201757476 168 QRLKDEARDLRQEL 181
Cdd:pfam05557 241 EKYREEAATLELEK 254
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
31-131 |
7.96e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.40 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 31 QEAREELAEFQEGSRELEAELEAQLVQAEQRNRDLQADNQrlkyEVETLKEKLEHQYAQSYKQvslLEDDLSQTRAIKDQ 110
Cdd:PRK04863 564 EARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAP----AWLAAQDALARLREQSGEE---FEDSQDVTEYMQQL 636
|
90 100
....*....|....*....|.
gi 2201757476 111 LHKyVRELEQANDDLERAKRA 131
Cdd:PRK04863 637 LER-ERELTVERDELAARKQA 656
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
35-181 |
9.33e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 38.01 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201757476 35 EELAEFQEGSRELEAELEAQlvqaeqrnrdlQADNQRLKYEVETLKEKLEhQYAQSYKQVSLLEDDLSQTRaikdqlhky 114
Cdd:COG3096 836 AELAALRQRRSELERELAQH-----------RAQEQQLRQQLDQLKEQLQ-LLNKLLPQANLLADETLADR--------- 894
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2201757476 115 VRELEQANDDLERAKRativSLEDFEQRLNQAIERNAFLESELDDKESLLVSVQRLKDEARDLRQEL 181
Cdd:COG3096 895 LEELREELDAAQEAQA----FIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQI 957
|
|
| |
