|
Name |
Accession |
Description |
Interval |
E-value |
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
13-248 |
8.24e-120 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 349.51 E-value: 8.24e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 13 QARAEQEEEFISNTLFKKIQALQKEKETLAVNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKL 92
Cdd:pfam09755 69 QAKAEQEEEFISNTLLKKIQALKKEKETLAMNYEQEEEFLTNDLSRKLTQLRQEKVELEQTLEQEQEYQVNKLMRKIEKL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 93 ENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSPENMMRH 172
Cdd:pfam09755 149 EAETLNKQTNLEQLRREKVELENTLEQEQEALVNRLWKRMDKLEAEKRLLQEKLDQPVSAPPSPRDSTSEGDTAQNLTAH 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568968877 173 IRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDERYF 248
Cdd:pfam09755 229 IQYLRKEVERLRRQLATAQQEHTEKMAQYAQEERHIREENLRLQRKLQLEMERREALCRHLSESESSLEMDEERYF 304
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10-241 |
4.61e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 10 QWQQARAEQEEefisntLFKKIQALQKEKETLAVNYEKEEEfltnelSRKLMQLQHEKAELEQHLEQEQEFQVNklmKKI 89
Cdd:COG1196 233 KLRELEAELEE------LEAELEELEAELEELEAELAELEA------ELEELRLELEELELELEEAQAEEYELL---AEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 90 KKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRLwKRMDKLEAEKRILQEKLdqpvsappspRDISMEIDSPENM 169
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELE-EELEELEEELEEAEEEL----------EEAEAELAEAEEA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568968877 170 MRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLE 241
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
29-241 |
3.64e-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: 51.69 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 29 KKIQALQKEKETLAVNYEkeeefltnELSRKLMQLQHEKAELEQHLEQeQEFQVNKLMKKIKKLENDTISKQLTLEQLRR 108
Cdd:COG4942 20 DAAAEAEAELEQLQQEIA--------ELEKELAALKKEEKALLKQLAA-LERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 109 EKIDLENTLEQEQEALVNRLWK--RMDKLEAEKRILqekldqpvsappSPRDISMEIDSPENMMRHIRFLKNEVERLKKQ 186
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRAlyRLGRQPPLALLL------------SPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568968877 187 LRAAQLQHSEKMAQYLEEERhMREENLRLQRKLQREMERREALCRQLSESESSLE 241
Cdd:COG4942 159 LAELAALRAELEAERAELEA-LLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-246 |
1.59e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 12 QQARAEQEEEF-ISNTLFKKIQALQKEKETLAvnyekeeefltnELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIK 90
Cdd:COG1196 281 LELEEAQAEEYeLLAELARLEQDIARLEERRR------------ELEERLEELEEELAELEEELEELEE-ELEELEEELE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 91 KLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRlwkRMDKLEAEKRILQEKLDQpvsappsprdismeidspENMM 170
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL---AEELLEALRAAAELAAQL------------------EELE 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568968877 171 RHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDER 246
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-244 |
2.64e-06 |
|
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: 49.68 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 2 ERQLGSRSQWQQARAEQEEEF--ISNTLFKKIQALQKEKEtlavNYEKEEEFLTNELSRKLMQLQHEKAEL---EQHLEQ 76
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLkeRLEELEEDLSSLEQEIE----NVKSELKELEARIEELEEDLHKLEEALndlEARLSH 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 77 EQEFQVNKLMKKIKK-----------LENDTISKQLTLEQLRREKIDLENTLEqEQEALVNRLWKRMDKLEAEKRILQEK 145
Cdd:TIGR02169 791 SRIPEIQAELSKLEEevsriearlreIEQKLNRLTLEKEYLEKEIQELQEQRI-DLKEQIKSIEKEIENLNGKKEELEEE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 146 LDQpvsappsprdISMEIDSPENMMRHirfLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMER 225
Cdd:TIGR02169 870 LEE----------LEAALRDLESRLGD---LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
250
....*....|....*....
gi 568968877 226 REALCRQLSESESSLEMDD 244
Cdd:TIGR02169 937 EDPKGEDEEIPEEELSLED 955
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-237 |
2.91e-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: 49.28 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 10 QWQQARAEQEEefisntLFKKIQALQKEKETLAVNYEKEEEfltnelsrKLMQLQHEKAELEQHLEQEQEfQVNKLMKKI 89
Cdd:TIGR02168 233 RLEELREELEE------LQEELKEAEEELEELTAELQELEE--------KLEELRLEVSELEEEIEELQK-ELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 90 KKLENDTISKQLTLEQLRREKIDLENTLEQEQEALvNRLWKRMDKLEAEKRILQEKLDqpvsappsprDISMEIDSPENM 169
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEELAELEEKLEELKEELE----------SLEAELEELEAE 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568968877 170 MRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESE 237
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
29-241 |
4.28e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 29 KKIQALQKEKETLAVNYEKEEEFLTN--------ELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQ 100
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLkelaeqlkELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 101 L---TLEQLRREKIDLENTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSPENMMRHIRFLK 177
Cdd:PRK03918 553 ElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568968877 178 NEVERLKKQLRAAQLQHSEKMAQYLEEE-RHMREENLRLQRKLQREMERREALCRQLSESESSLE 241
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-246 |
6.98e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 29 KKIQALQKEKETlAVNY----EKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENdtiskqlTLE 104
Cdd:COG1196 200 RQLEPLERQAEK-AERYrelkEELKELEAELLLLKLRELEAELEELEAELEELEA-ELEELEAELAELEA-------ELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 105 QLRREKIDLENTLEQEQEALvNRLWKRMDKLEAEKRILQEKLdqpvsappspRDISMEIDSPENMMRHIRF--------- 175
Cdd:COG1196 271 ELRLELEELELELEEAQAEE-YELLAELARLEQDIARLEERR----------RELEERLEELEEELAELEEeleeleeel 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968877 176 --LKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDER 246
Cdd:COG1196 340 eeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
66-214 |
1.33e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 66 EKAELEQHLEQEQEFQVNKLMKKIKKLENdtiskqlTLEQLRREKIDLENTLEqeqealvnrlwkrmdklEAEKRI--LQ 143
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEE-------QVERLEAEVEELEAELE-----------------EKDERIerLE 447
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568968877 144 EKLdqpvsappspRDISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQlQHSEKMAQYLEEERHMREENLR 214
Cdd:COG2433 448 REL----------SEARSEERREIRKDREISRLDREIERLERELEEER-ERIEELKRKLERLKELWKLEHS 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-245 |
4.57e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 2 ERQLGSR-SQWQQARAEQEEEFISNTlfKKIQALQKEKETLAVNYEKEEEfLTNELSRKLMQLQHEKAELEQHLEQEQEF 80
Cdd:COG1196 290 EYELLAElARLEQDIARLEERRRELE--ERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 81 QVNKLMKKIKKLE--NDTISKQLTLEQLRREKIDLENTLEQEQEALVNRLwkrmDKLEAEKRILQEKLDqpvsappsprd 158
Cdd:COG1196 367 LLEAEAELAEAEEelEELAEELLEALRAAAELAAQLEELEEAEEALLERL----ERLEEELEELEEALA----------- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 159 ismeidspenmmrhirflknEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESES 238
Cdd:COG1196 432 --------------------ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
....*..
gi 568968877 239 SLEMDDE 245
Cdd:COG1196 492 RLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-241 |
5.21e-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: 45.43 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 1 MERQLGSRSQWQQARAEQEEEFisNTLFKKIQALQKEKETL-AVNYEKEEEFltNELSRKLMQLQHEKAELEQHLeQEQE 79
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEEL--EELTAELQELEEKLEELrLEVSELEEEI--EELQKELYALANEISRLEQQK-QILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 80 FQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLE---NTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQPvsappsp 156
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEeklEELKEELESLEAELEELEAELEELESRLEELEEQL------- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 157 RDISMEIDSPENMMRHIRflkNEVERLKkqlraAQLQHSEKMAQYLEEERHMREENLRLQRK--LQREMERREALCRQLS 234
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLN---NEIERLE-----ARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQ 453
|
....*..
gi 568968877 235 ESESSLE 241
Cdd:TIGR02168 454 EELERLE 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-259 |
6.82e-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: 45.05 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 12 QQARAEQEEEFISNTLFKKIQALQKEKETLAVNYEKEEEFLTN------ELSRKLMQLQHEKAELEQHLEQEQEfQVNKL 85
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeieELEERLEEAEEELAEAEAEIEELEA-QIEQL 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 86 MKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVnRLWKRMDKLEAEKRILQEKL----DQPVSAPPSPRDISM 161
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIA-ATERRLEDLEEQIEELSEDIeslaAEIEELEELIEELES 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 162 EIDSPEN----MMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALcrqLSESE 237
Cdd:TIGR02168 874 ELEALLNerasLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL---SEEYS 950
|
250 260
....*....|....*....|...
gi 568968877 238 SSLEMDDERYFN-EMSAQGLRPR 259
Cdd:TIGR02168 951 LTLEEAEALENKiEDDEEEARRR 973
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
62-240 |
1.11e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 62 QLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDtiskqltLEQLRREKIDLENTLEQEQEALVNRLWKRMDKLEAEKRI 141
Cdd:COG4913 285 FAQRRLELLEAELEELRA-ELARLEAELERLEAR-------LDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 142 LQEKLDQ--------PVSAPPSPRDIsmeidspENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREE-- 211
Cdd:COG4913 357 RERRRARleallaalGLPLPASAEEF-------AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEia 429
|
170 180 190
....*....|....*....|....*....|.
gi 568968877 212 NLRLQRKL--QREMERREALCRQLSESESSL 240
Cdd:COG4913 430 SLERRKSNipARLLALRDALAEALGLDEAEL 460
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
55-235 |
2.27e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 55 ELSRKLMQLQHEKAELEQHLEqeqefqvnKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEqEALVNRLWKRMDK 134
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELA--------ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-EARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 135 LEAEKRIlqekldqpvsappspRDISMEIDSPENMMR----HIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMRE 210
Cdd:COG1579 85 VRNNKEY---------------EALQKEIESLKRRISdledEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|....*
gi 568968877 211 ENLRLQRKLQREMERREALCRQLSE 235
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
16-144 |
2.44e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 16 AEQEEEFISNTLFKKIQALQKEKETLAvnyeKEEEF-LTNELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLEN 94
Cdd:PRK12704 36 AEEEAKRILEEAKKEAEAIKKEALLEA----KEEIHkLRNEFEKELRERRNELQKLEKRLLQKEE-NLDRKLELLEKREE 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568968877 95 DTISKQLTLEQLRREKIDLENTLEQEQEALVNRLWK--RMDKLEAEKRILQE 144
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisGLTAEEAKEILLEK 162
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-242 |
4.81e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 42 AVNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDtiskqltLEQLRREKIDLENTLEQ-E 120
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-------LEELEAELEELREELEKlE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 121 QEALVNRLWKRMDKLEAEKRILQEKLDQpvsappsprdISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQ 200
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEE----------LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568968877 201 YLE------EERHMREENLRLQRK-LQREMERREALCRQLSESESSLEM 242
Cdd:COG4717 193 ELQdlaeelEELQQRLAELEEELEeAQEELEELEEELEQLENELEAAAL 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-246 |
4.91e-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: 42.36 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 13 QARAEQEEEFISNTLFKKIQALQKEKETLAVNYEKEEEFLTnELSRKLMQLQHEKAELEQHLEQEQ-------EFQVNKL 85
Cdd:TIGR02169 214 QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE-KLTEEISELEKRLEEIEQLLEELNkkikdlgEEEQLRV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 86 MKKIKKLENDTISKQLTLEQLRREKIDLENTLeQEQEALVNRLWKRMDKLEAEKRILQEKLDQpvsappsprdISMEIDS 165
Cdd:TIGR02169 293 KEKIGELEAEIASLERSIAEKERELEDAEERL-AKLEAEIDKLLAEIEELEREIEEERKRRDK----------LTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 166 PENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSL-EMDD 244
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKInELEE 441
|
..
gi 568968877 245 ER 246
Cdd:TIGR02169 442 EK 443
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
29-148 |
4.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 29 KKIQALQKEKETLAVNYEKEEEFLTNElsrKLMQLQHEkaelEQHLEQEQEFQVNKLMKKIKKLENDTISKQltlEQLRR 108
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKE---ALLEAKEE----IHKLRNEFEKELRERRNELQKLEKRLLQKE---ENLDR 100
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568968877 109 EKIDLENtLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQ 148
Cdd:PRK12704 101 KLELLEK-REEELEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
16-149 |
5.53e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 16 AEQEEEFISNTLFKKIQALQKEKEtlAVNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEqefqVNKLMKKIKKlEND 95
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEE--AEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE----AQQAIKEAKK-EAD 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568968877 96 TISKQLtleQLRREKIDLENTLEQEQEALvNRLWKRMDKLEAEKRILQEKLDQP 149
Cdd:PRK00409 588 EIIKEL---RQLQKGGYASVKAHELIEAR-KRLNKANEKKEKKKKKQKEKQEEL 637
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
107-243 |
5.66e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 107 RREKIDLENTLEQEQEaLVNRLWKRMDKLEAEKRILQEKLDQpvsappsprdismeidspenmmrhirfLKNEVERLKKQ 186
Cdd:COG2433 398 EREKEHEERELTEEEE-EIRRLEEQVERLEAEVEELEAELEE---------------------------KDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568968877 187 LRAAQLQHSEKmAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMD 243
Cdd:COG2433 450 LSEARSEERRE-IRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLE 505
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
13-247 |
5.98e-04 |
|
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: 42.27 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 13 QARAEQEEEFISNTLFKKiqalqkEKETLAVNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEF--QVNKLMKKIK 90
Cdd:pfam02463 205 QAKKALEYYQLKEKLELE------EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKlaQVLKENKEEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 91 KLENDTISKQLTL----EQLRREKIDLE---NTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAppSPRDISMEI 163
Cdd:pfam02463 279 KEKKLQEEELKLLakeeEELKSELLKLErrkVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL--EIKREAEEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 164 DSPENMMRHIRFLKNEVERLKKQLRAAQL------QHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESE 237
Cdd:pfam02463 357 EEEELEKLQEKLEQLEEELLAKKKLESERlssaakLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE 436
|
250
....*....|
gi 568968877 238 SSLEMDDERY 247
Cdd:pfam02463 437 ESIELKQGKL 446
|
|
| PRK14644 |
PRK14644 |
hypothetical protein; Provisional |
29-118 |
6.02e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 184779 [Multi-domain] Cd Length: 136 Bit Score: 39.82 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 29 KKIQALQKEKETLAVNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQ---LTLE- 104
Cdd:PRK14644 39 KDIEELTKEISDFIDNLSVEFDFDSLDISSPGFDMDYETDELENHIGEIIDVSLNKEVNKTDFITGELLENNpetITLKw 118
|
90
....*....|....*...
gi 568968877 105 ----QLRREKIDLENTLE 118
Cdd:PRK14644 119 nckgQFRKVEINKENIKK 136
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
54-254 |
6.14e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 54 NELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRL----- 128
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQA-ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 129 -WKRMDKLEA--EKRILQEKLDQpVSAppsprdISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQlqhsekmaqylEEE 205
Cdd:COG3883 98 sGGSVSYLDVllGSESFSDFLDR-LSA------LSKIADADADLLEELKADKAELEAKKAELEAKL-----------AEL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568968877 206 RHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDERYFNEMSAQ 254
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
12-250 |
7.56e-04 |
|
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: 41.88 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 12 QQARAEQEEEFISNTLFKKIQALQKEKETLAVNYEKEEEFLTNELSRKLMQLQHEKAELEQ--HLEQEQEFQVNKLMKKI 89
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKleRRKVDDEEKLKESEKEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 90 KKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQpvsappsPRDISMEIDSPENM 169
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE-------SERLSSAAKLKEEE 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 170 MRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEErhmrEENLRLQRKLQREMERREALCRQLSESESSLEMDDERYFN 249
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL----EEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
.
gi 568968877 250 E 250
Cdd:pfam02463 473 L 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-246 |
8.78e-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: 41.58 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 74 LEQEQEfqVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQ------EQEALVNRLWKRMDKLEAEKRILQEKLD 147
Cdd:TIGR02168 673 LERRRE--IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQlrkeleELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 148 QPVSAPPSPRDISMEIDSPENmmrHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERRE 227
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLE---EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170
....*....|....*....
gi 568968877 228 ALCRQLSESESSLEMDDER 246
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQ 846
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
17-241 |
1.33e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 17 EQEEEFIS-----NTLFKKIQALQKEKETLAVNYEKEEEF--LTNELSRKLMQLQHEKAELEQHLEQEQEfQVNKLMKKI 89
Cdd:PRK03918 197 EKEKELEEvlreiNEISSELPELREELEKLEKEVKELEELkeEIEELEKELESLEGSKRKLEEKIRELEE-RIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 90 KKLEnDTISKQLTLEQLRREKIDLENTLEQEQEALvNRLWKRMDKLEAEKRILQEKLDqpvsappsprdismEIDSPENM 169
Cdd:PRK03918 276 EELE-EKVKELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEINGIEERIK--------------ELEEKEER 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568968877 170 MRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLE 241
Cdd:PRK03918 340 LEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
25-232 |
1.38e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 25 NTLFKKIQALQKEKETLAVNYEKEEEFLTNE------LSRKLMQLQHEKAELEQHLEQEQEFQVN----------KLMKK 88
Cdd:pfam01576 450 NEAEGKNIKLSKDVSSLESQLQDTQELLQEEtrqklnLSTRLRQLEDERNSLQEQLEEEEEAKRNverqlstlqaQLSDM 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 89 IKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALvnrlwKRMDKLEAEKRILQEKLDqpvsappsprDISMEIDspen 168
Cdd:pfam01576 530 KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKA-----AAYDKLEKTKNRLQQELD----------DLLVDLD---- 590
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968877 169 mmrHIRFLKNEVErlKKQLRAAQLQHSEKM--AQYLEE----ERHMREENLR---LQRKLQREMERREALCRQ 232
Cdd:pfam01576 591 ---HQRQLVSNLE--KKQKKFDQMLAEEKAisARYAEErdraEAEAREKETRalsLARALEEALEAKEELERT 658
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
18-144 |
2.49e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 18 QEEEFISNTLFKKIQALQKEKETLAVNYEKEEEfLTNELSRKLMQLQHEKAELEQHlEQEQEFQVNKLMKKIKKLENDTI 97
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNK-IISQLNEQISQLKKELTNSESE-NSEKQRELEEKQNEIEKLKKENQ 380
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568968877 98 SKQLTLEQLRREKIDLENTLeQEQEALVNRLWKRMDKLEAEKRILQE 144
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKI-QNQEKLNQQKDEQIKKLQQEKELLEK 426
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
27-228 |
4.21e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 27 LFKKIQALQKEKETLAVNYEKEEEfltnelsrKLMQLQHEKAELEQHLEQEQEfqVNKLMKKIKKLENDTISKQLTLEQL 106
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEE--------KIRELEERIEELKKEIEELEE--KVKELKELKEKAEEYIKLSEFYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 107 RREKIDLENTLEQeQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAppspRDISMEIDSPENMMRHIRFLKNEVERLKKQ 186
Cdd:PRK03918 306 LDELREIEKRLSR-LEEEINGIEERIKELEEKEERLEELKKKLKEL----EKRLEELEERHELYEEAKAKKEELERLKKR 380
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568968877 187 LRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREA 228
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
10-91 |
6.40e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 37.12 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 10 QWQQARAEQEEEFisNTLFKKIQALQKEKETLAVNYEKEEEFLT--------NELSRKLMQLQHEKAELEQHLEQEQEFQ 81
Cdd:COG2825 40 EGKAAQKKLEKEF--KKRQAELQKLEKELQALQEKLQKEAATLSeeerqkkeRELQKKQQELQRKQQEAQQDLQKRQQEL 117
|
90
....*....|
gi 568968877 82 VNKLMKKIKK 91
Cdd:COG2825 118 LQPILEKIQK 127
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
67-205 |
9.94e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 38.12 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568968877 67 KAELEQHLEQEQEFQVNKLMKKIKKLENDTISkqlTLEQLrrEKIDLENTLEQEQEALVNRLWKRMDKLEAEKRILQEKL 146
Cdd:pfam13166 270 KAALEAHFDDEFTEFQNRLQKLIEKVESAISS---LLAQL--PAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRAL 344
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568968877 147 DQPVSAPPSPRDISMEIDSPENMM--------------RHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEE 205
Cdd:pfam13166 345 EAKRKDPFKSIELDSVDAKIESINdlvasineliakhnEITDNFEEEKNKAKKKLRLHLVEEFKSEIDEYKDK 417
|
|
| |
