|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-446 |
4.30e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 122 IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNS------LQTATENTQARILHAEQ 195
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerleeLEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 196 EKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRR 275
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 276 QLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERcQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTL 355
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 356 AQAELQSQWEAkcEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQiAAFTEQKEHMQRLEKTKSQAPAGR 435
Cdd:COG1196 497 LEAEADYEGFL--EGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ-NIVVEDDEVAAAAIEYLKAAKAGR 573
|
330
....*....|.
gi 1907156437 436 AAADPSEKVKK 446
Cdd:COG1196 574 ATFLPLDKIRA 584
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-453 |
2.47e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 162 QRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDL 241
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 242 LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKK---SAQERCQAEA 318
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAElaeAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 319 EMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQsqwEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLA 398
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907156437 399 LLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQ 453
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
134-402 |
4.50e-13 |
|
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: 73.17 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 134 ERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLM------MEKRNNSLQTATENTQARILHAEQEKAKVTEELAAA 207
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 208 TAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEE 287
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 288 LTDLRAEKTSLEKNLS---ERKKKSAQERCQAEAEMDEIRKS-HQEELDRLRQLLKKArVSTDQAAAEQLTLAQAELqsq 363
Cdd:TIGR02168 395 IASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEEL-QEELERLEEALEELREEL--- 470
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907156437 364 weAKCEQLLASARDEHLQqyrevcaqrdaHQQKLALLQD 402
Cdd:TIGR02168 471 --EEAEQALDAAERELAQ-----------LQARLDSLER 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
126-382 |
1.35e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 126 IQRIIQENERLKQELLEKSSRIEEQNDKIsDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELA 205
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 206 AATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLE 285
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 286 EELTDLRAEKTSLEKNLSERKKKSAQERcQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWE 365
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLE-EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250
....*....|....*..
gi 1907156437 366 AKCEQLLASARDEHLQQ 382
Cdd:COG1196 472 AALLEAALAELLEELAE 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-418 |
2.62e-12 |
|
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: 70.87 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 92 LMTKVEELQKHSSgnsMLLPSMSV-TMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNL 170
Cdd:TIGR02169 693 LQSELRRIENRLD---ELSQELSDaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 171 MMEKRNNsLQTATENTQARILHA-----EQEKAKVTEELAAATAQVSHLQLKMtahqkKETELQLQLTDNLKETdlLRGH 245
Cdd:TIGR02169 770 LEEDLHK-LEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREIEQKL-----NRLTLEKEYLEKEIQE--LQEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 246 VTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKsaqeRCQAEAEMDEIRK 325
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK----IEELEAQIEKKRK 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 326 sHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ-SQWEAKCEQLLASARD------EHLQQYREVCAQRDAHQQKLA 398
Cdd:TIGR02169 918 -RLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSlEDVQAELQRVEEEIRAlepvnmLAIQEYEEVLKRLDELKEKRA 996
|
330 340
....*....|....*....|
gi 1907156437 399 LLQDECLALQAQIAAFTEQK 418
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKKK 1016
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-392 |
1.47e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 185 NTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQ--LQLTDNLKETDLLRGHVTRLQADLSELREASeq 262
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASS-- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 263 tqTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELD-RLRQLLKKA 341
Cdd:COG4913 685 --DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEeRFAAALGDA 762
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907156437 342 RVstdQAAAEQLTLAQAELQSQwEAKCEQLLASARDEHLQQYREVCAQRDA 392
Cdd:COG4913 763 VE---RELRENLEERIDALRAR-LNRAEEELERAMRAFNREWPAETADLDA 809
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
182-411 |
3.15e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 182 ATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASE 261
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 262 QTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKN---LSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLL 338
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 339 KKARVSTDQAAAEQLTLaqAELQSQWEAKCEQL---------LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQA 409
Cdd:TIGR02168 824 ERLESLERRIAATERRL--EDLEEQIEELSEDIeslaaeieeLEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
..
gi 1907156437 410 QI 411
Cdd:TIGR02168 902 EL 903
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
68-339 |
6.59e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 68 MTEARQHNTEIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSvtMETSMIMSNIQRIIQENERLKQELLEKSSRI 147
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR--KDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 148 EEQNDKISDL----------IERNQRYVEQSNLMMEK------------------------RNNSLQTATENTQARILHA 193
Cdd:TIGR02168 764 EELEERLEEAeeelaeaeaeIEELEAQIEQLKEELKAlrealdelraeltllneeaanlreRLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 194 EQEKAKVTEELAAATAQVSHLQLKMTahqkketELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQS 273
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIE-------ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156437 274 RRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLK 339
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
220-446 |
8.57e-10 |
|
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: 61.32 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 220 AHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLE 299
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 300 KNLSERKKK------SAQERCQAEAEMDEIRKSHQEELDRLRQLLKKArVSTDQAAAEQLTLAQAELQSQWEAKCEQL-- 371
Cdd:COG4942 97 AELEAQKEElaellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEELRADLAELAALRAELEAERae 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156437 372 LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKK 446
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-466 |
3.38e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 184 ENTQARILHAEQEKAKVTEELAAATAQVSHLQLkmtahQKKETELQLQLTDNLKETDLlrghvTRLQADLSELREASEQT 263
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLER-----QAEKAERYKELKAELRELEL-----ALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 264 QTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKK-----SAQERCQAEAEMDEIRKSH----QEELDRL 334
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaNEISRLEQQKQILRERLANlerqLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 335 RQLLKKARVsTDQAAAEQLTLAQAELQSQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIA 412
Cdd:TIGR02168 325 LEELESKLD-ELAEELAELEEKLEELKEELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907156437 413 AFTEQKEHMQ-RLEKTKSQAPAGRAAADPSEKvKKIMNQVFQSLRGEFELEESYD 466
Cdd:TIGR02168 404 RLEARLERLEdRRERLQQEIEELLKKLEEAEL-KELQAELEELEEELEELQEELE 457
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
127-359 |
6.67e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 127 QRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQtateNTQARILHAEQEKAKVTEELAA 206
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA----KLEAEIDKLLAEIEELEREIEE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 207 ATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEE 286
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156437 287 ELTDLRAEKTSLE---KNLSERKKKSAQERCQAEAEMDEIRKSH---QEELDRLRQLLKKARVSTDQAAAEQLTLAQAE 359
Cdd:TIGR02169 428 AIAGIEAKINELEeekEDKALEIKKQEWKLEQLAADLSKYEQELydlKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
134-386 |
8.86e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 134 ERLKQELLekssRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSH 213
Cdd:COG4913 238 ERAHEALE----DAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 214 LQLKMTAHQKKETELQLQLTDNlkETDLLrghvTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRA 293
Cdd:COG4913 314 LEARLDALREELDELEAQIRGN--GGDRL----EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 294 EKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQE---ELDRLRQL-------LKKARvstdQAAAEQLTLAQAEL--- 360
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELREleaEIASLERRksniparLLALR----DALAEALGLDEAELpfv 463
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1907156437 361 ---------QSQWEAKCEQLLASAR------DEHLQQYREV 386
Cdd:COG4913 464 gelievrpeEERWRGAIERVLGGFAltllvpPEHYAAALRW 504
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
123-426 |
1.45e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 123 MSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTE 202
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 203 ELAAATAQVSHLQLKMTAHQKKETELQLQ--------------LTDNLKETDLLRGHVTRLQA-----DLSELREASEQT 263
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLgllalLFLLLAREKASL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 264 QTKFKSEKQSRRQLELKVTSLEEELTDLRAeKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEE--LDRLRQLLKKA 341
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGL-PPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAEA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 342 RVSTD-------------QAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQ 408
Cdd:COG4717 380 GVEDEeelraaleqaeeyQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE 459
|
330
....*....|....*...
gi 1907156437 409 AQIAAFTEQKEHMQRLEK 426
Cdd:COG4717 460 AELEQLEEDGELAELLQE 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-300 |
4.74e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 76 TEIRMAVNKVADKMDHLMTKVEELQKhssgnsmllpsmsvtmETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKIS 155
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALAN----------------EISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 156 DLIERNQRYVEQSNL--------------------MMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQ 215
Cdd:TIGR02168 334 ELAEELAELEEKLEElkeelesleaeleeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 216 lkmtAHQKKETELQLQLTDNLKETDL--LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRA 293
Cdd:TIGR02168 414 ----DRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
....*..
gi 1907156437 294 EKTSLEK 300
Cdd:TIGR02168 490 RLDSLER 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
123-364 |
1.17e-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: 54.77 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 123 MSNIQRIIQENERLKQELLEKssrIEEQNDKISDLIERNQRYVEQSNLmMEKRNNSLQTATENTQARIlhaEQEKAKVTE 202
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQ---LAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAEL---EAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 203 ELAAATAQVSHLQLKMTAHQKketelqlQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKfksekqsRRQLELKVT 282
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPE-------DFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-------RAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 283 SLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEElDRLRQLLKKARVSTDQAAAEQLTLAQAELQS 362
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
..
gi 1907156437 363 QW 364
Cdd:COG4942 254 KL 255
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
132-445 |
4.49e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 132 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATaqv 211
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE--- 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 212 shlQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEqtqTKFKSEkQSRRQLELKVTSlEEELTDL 291
Cdd:PTZ00121 1389 ---EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE---AKKKAE-EAKKADEAKKKA-EEAKKAE 1460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 292 RAEKTSLEKNLSERKKKSAQERCQAE--AEMDEIRKSHQEELDRLRQLLKKA---RVSTDQAAAEQLTLAQAELQSQWEA 366
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADeaKKKAEEAKKKADEAKKAAEAKKKAdeaKKAEEAKKADEAKKAEEAKKADEAK 1540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 367 KCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQK--EHMQRLEKTKSQAPAGRAAADPSEKV 444
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
.
gi 1907156437 445 K 445
Cdd:PTZ00121 1621 K 1621
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
193-440 |
1.27e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.22 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 193 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETE-LQLQLTDNLKETdllrghvTRLQADLSELReASEQTQTKFKSEK 271
Cdd:PRK11281 49 NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEqLKQQLAQAPAKL-------RQAQAELEALK-DDNDEETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 272 QSRRQLELKVTSLEEELTDLRAEKTSLEKNLSerKKKSAQERCQAEaeMDEirksHQEELDRLRQLLKKARVSTDQAAAE 351
Cdd:PRK11281 121 LSLRQLESRLAQTLDQLQNAQNDLAEYNSQLV--SLQTQPERAQAA--LYA----NSQRLQQIRNLLKGGKVGGKALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 352 QLTLAQAELQSqWEAKCE---QLLASArdEHLQQYREvcAQRDAHQQKLALLQDECLALQAQIAA--FTEQKEHMQRLEk 426
Cdd:PRK11281 193 QRVLLQAEQAL-LNAQNDlqrKSLEGN--TQLQDLLQ--KQRDYLTARIQRLEHQLQLLQEAINSkrLTLSEKTVQEAQ- 266
|
250
....*....|....
gi 1907156437 427 tkSQAPAGRAAADP 440
Cdd:PRK11281 267 --SQDEAARIQANP 278
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
231-438 |
1.36e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 231 QLTDNLKETDLLRGHVTRLQADLSELREASEQtqtkfksekqsrrqlelkvtsLEEELTDLRAEKTSLEKNLseRKKKSA 310
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEE---------------------LEAELEELREELEKLEKLL--QLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 311 QERCQAEAEMDEIrkshQEELDRLRQllKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDE---HLQQYREVC 387
Cdd:COG4717 132 QELEALEAELAEL----PERLEELEE--RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEELQ 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907156437 388 AQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAA 438
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
202-410 |
1.93e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 202 EELAAATAQVSHLQLKMTAHQK-KETELQLQLTDNLKEtdllRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELK 280
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERyAAARERLAELEYLRA----ALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 281 VTSLEEELTDLRAEktsLEKNLSERKKKSAQERCQAEAEMDEIrkshQEELDRLRQLLKKARVSTDQAAAEQltlaqAEL 360
Cdd:COG4913 318 LDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASAEEF-----AAL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907156437 361 QSQWEAKCEQLlASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQ 410
Cdd:COG4913 386 RAEAAALLEAL-EEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
184-366 |
3.27e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 184 ENTQARILHAEQEKAKVTEELAAATAQVSHLQlkmtaHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREaseqt 263
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELR-----EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEE----- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 264 qtkfksEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARV 343
Cdd:COG4717 154 ------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180
....*....|....*....|...
gi 1907156437 344 STDQAAAEQLTLAQAELQSQWEA 366
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARL 250
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-429 |
5.73e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 180 QTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREA 259
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 260 SEQTQTK--------FKSEKQSRRQLELKVTSLEEELTDLRAektsLEKNLSERKKksaqercqaeaEMDEIRKShQEEL 331
Cdd:COG4942 99 LEAQKEElaellralYRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARRE-----------QAEELRAD-LAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 332 DRLRQLLKKARvstdqaaaEQLTLAQAELQSQweakcEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQI 411
Cdd:COG4942 163 AALRAELEAER--------AELEALLAELEEE-----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|....*...
gi 1907156437 412 AAFTEQKEHMQRLEKTKS 429
Cdd:COG4942 230 ARLEAEAAAAAERTPAAG 247
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
127-390 |
6.09e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 127 QRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEkRNNSLQTATENTQARilhaEQEKAKvTEELAA 206
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-RERELERIRQEERKR----ELERIR-QEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 207 ATAQVSHLQ-LKMTAHQKK----------------ETELQLQLTDNLKETDLLRGHVTRL-QADLSELREASEQTQTKFK 268
Cdd:pfam17380 373 EISRMRELErLQMERQQKNervrqeleaarkvkilEEERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMERVR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 269 SEKQSRRQlelKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEElDRLRQLLKKARVSTDQA 348
Cdd:pfam17380 453 LEEQERQQ---QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEE-ERKRKLLEKEMEERQKA 528
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907156437 349 AAEQLTLAQAELQSQWEAKCEQllasaRDEHLQQYREVCAQR 390
Cdd:pfam17380 529 IYEEERRREAEEERRKQQEMEE-----RRRIQEQMRKATEER 565
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-369 |
6.72e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 124 SNIQRIIQENErlkQELLEKSSRIEEQNDKISDLIERnqryVEqsnlMMEKRNNSLqtatENTQARILHAEQEKAKVTEE 203
Cdd:PRK03918 189 ENIEELIKEKE---KELEEVLREINEISSELPELREE----LE----KLEKEVKEL----EELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 204 LAAATAQVSHLQlKMTAHQKKETElqlQLTDNLKETDLLRGHVTRLQAdLSELREaseqtqtKFKSEKqsrRQLELKVTS 283
Cdd:PRK03918 254 KRKLEEKIRELE-ERIEELKKEIE---ELEEKVKELKELKEKAEEYIK-LSEFYE-------EYLDEL---REIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 284 LEEELTDLRAEKTSLEKnLSERKKKSAQERCQAEAEMDEIRKSHqEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQ 363
Cdd:PRK03918 319 LEEEINGIEERIKELEE-KEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEEL 396
|
....*.
gi 1907156437 364 WEAKCE 369
Cdd:PRK03918 397 EKAKEE 402
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
188-340 |
7.48e-06 |
|
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: 48.00 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 188 ARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQT--QT 265
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156437 266 KFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKK 340
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
122-329 |
8.79e-06 |
|
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: 49.25 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 122 IMSNIQRIIQENERLKQELLEkssrIEEQNDKISD-LIERNQRYVEQSNLMMEKRNNSLQTATENT------QARILHAE 194
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISE----LKKQNNQLKDnIEKKQQEINEKTTEISNTQTQLNQLKDEQNkikkqlSEKQKELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 195 QEKAKVTE-------------ELAAATAQVSHLQLK--MTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREA 259
Cdd:TIGR04523 278 QNNKKIKElekqlnqlkseisDLNNQKEQDWNKELKseLKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156437 260 SEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQ---AEAEMDEIRKSHQE 329
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQikkLQQEKELLEKEIER 430
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
223-507 |
9.03e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 223 KKETELQLQLT-DNLKE-TDLLRGhvtrLQADLSELREASEQTQtKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEK 300
Cdd:COG1196 174 KEEAERKLEATeENLERlEDILGE----LERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 301 NLSERKKKSAQ-ERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEH 379
Cdd:COG1196 249 EELEAELEELEaELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 380 LQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQkehmqRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEF 459
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-----LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907156437 460 ELEESydggtiLRTIMHTIKMVTLQLLNHQEEEEEEEEEEEEEKKPLR 507
Cdd:COG1196 404 ELEEA------EEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-359 |
9.18e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 134 ERLKQELLEKSSRIEEQNDKisdliernqRYVEQSNLMMEKRNNSLQTATENTQArilhaeqEKAKVTEELaaataQVSH 213
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKA-------EEARIEEVM-----KLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 214 LQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSE-------LREASEQT-----QTKFKSEKQSRRQLELKV 281
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkkaeeLKKAEEENkikaaEEAKKAEEDKKKAEEAKK 1682
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156437 282 TSLEEELTDLRAEKTSLEKNLSER-KKKSAQERCQAEaemdEIRKSHQEELDRLRQLLKKARvsTDQAAAEQLTLAQAE 359
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEElKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAE--EDKKKAEEAKKDEEE 1755
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
82-295 |
2.21e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 82 VNKVADKMDHLMTKVEELQKHSSGNSML---LPSMSVTMETSM---IMSNIQRIIQ-ENERLKQELLEKSSRIEEQNDKI 154
Cdd:COG5022 894 ISSLKLVNLELESEIIELKKSLSSDLIEnleFKTELIARLKKLlnnIDLEEGPSIEyVKLPELNKLHEVESKLKETSEEY 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 155 SDLIERNQRYVEQSNLMMEKRNNSLQTATE-NTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLT 233
Cdd:COG5022 974 EDLLKKSTILVREGNKANSELKNFKKELAElSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKG 1053
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156437 234 DNLKEtdllrghVTRLQADLSELREASEQTQTKFKSEKQSRRQ--LELKVTSLEEELTDLRAEK 295
Cdd:COG5022 1054 LLLLE-------NNQLQARYKALKLRRENSLLDDKQLYQLESTenLLKTINVKDLEVTNRNLVK 1110
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
125-361 |
2.25e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 125 NIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERN-----QRYVEQSNLMMEKRNNSLQTATENTQarilhaeqekak 199
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetrETLSTLSLRQLESRLAQTLDQLQNAQ------------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 200 vtEELAAATAQVSHLQLK-------MTAHQKKETELQLQLTDNLKETDLLRG-HVTRLQADLS------ELREASEQTQT 265
Cdd:PRK11281 142 --NDLAEYNSQLVSLQTQperaqaaLYANSQRLQQIRNLLKGGKVGGKALRPsQRVLLQAEQAllnaqnDLQRKSLEGNT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 266 KFKSEKQSRRQL-ELKVTSLEEELTDLRAEKTslEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVS 344
Cdd:PRK11281 220 QLQDLLQKQRDYlTARIQRLEHQLQLLQEAIN--SKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKA 297
|
250
....*....|....*..
gi 1907156437 345 TDQAAaeqlTLAQAELQ 361
Cdd:PRK11281 298 TEKLN----TLTQQNLR 310
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
219-397 |
3.17e-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: 46.07 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 219 TAHQKKETELQLQLTDNlkETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSL 298
Cdd:COG1579 1 AMPEDLRALLDLQELDS--ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 299 EKNLSERKKKSAQERCQAEAEMDEIRKSHQEEldrlRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQlLASARDE 378
Cdd:COG1579 79 EEQLGNVRNNKEYEALQKEIESLKRRISDLED----EILELMERIEELEEELAELEAELAELEAELEEKKAE-LDEELAE 153
|
170
....*....|....*....
gi 1907156437 379 HLQQYREVCAQRDAHQQKL 397
Cdd:COG1579 154 LEAELEELEAEREELAAKI 172
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
194-430 |
3.89e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 194 EQEKAKVTEELAAATAQVSHLQLKmtahqkkETELQLQLtDNLKETdllRGHVTRLQADLSELR--EASEQTQTKFKSEK 271
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLI-------IDEKRQQL-ERLRRE---REKAERYQALLKEKReyEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 272 QsRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAE 351
Cdd:TIGR02169 238 Q-KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 352 QLTLA--QAELQSQWEAKCEQLLASARDehLQQYRevcAQRDAHQQKLALLQDECLALQAQI--------AAFTEQKEHM 421
Cdd:TIGR02169 317 LEDAEerLAKLEAEIDKLLAEIEELERE--IEEER---KRRDKLTEEYAELKEELEDLRAELeevdkefaETRDELKDYR 391
|
....*....
gi 1907156437 422 QRLEKTKSQ 430
Cdd:TIGR02169 392 EKLEKLKRE 400
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
209-418 |
6.23e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 46.38 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 209 AQVSHLQLKMTAHQKKETELQLQLtdnlketDLLRGHVTRLQADLSELREASEQTQTKFKS-------EKQSRRQLELKv 281
Cdd:pfam09726 402 QDIKKLKAELQASRQTEQELRSQI-------SSLTSLERSLKSELGQLRQENDLLQTKLHNavsakqkDKQTVQQLEKR- 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 282 tsLEEEltdlRAEKTSLEKNLSERKK-------KSAQERCQAEA---EMDEIRKSHQEELD-RLRQLLKKARVSTDQAAa 350
Cdd:pfam09726 474 --LKAE----QEARASAEKQLAEEKKrkkeeeaTAARAVALAAAsrgECTESLKQRKRELEsEIKKLTHDIKLKEEQIR- 546
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156437 351 eqltlaqaelqsQWEAKCEQllasardehLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQK 418
Cdd:pfam09726 547 ------------ELEIKVQE---------LRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETRIK 593
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
79-430 |
7.62e-05 |
|
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: 46.50 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 79 RMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMETSMimSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLI 158
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERK--QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 159 ERNQRYVEQSNLMMEKRNnsLQTATENTQARIlhaeqEKAKVTEELAAATAQVSHLQLKMtahQKKETELQLQLTDNLKE 238
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRA--QEAVLEETQERI-----NRARKAAPLAAHIKAVTQIEQQA---QRIHTELQSKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 239 tdllRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVtsleeeltdLRAEKTSLEKNLSERKKKSAQERCQAEa 318
Cdd:TIGR00618 327 ----LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT---------SIREISCQQHTLTQHIHTLQQQKTTLT- 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 319 emdEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYRevcaQRDAHQQKLA 398
Cdd:TIGR00618 393 ---QKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEK----LEKIHLQESA 465
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907156437 399 LLQDECLALQAQIAAFTEQ-----KEHMQRLEKTKSQ 430
Cdd:TIGR00618 466 QSLKEREQQLQTKEQIHLQetrkkAVVLARLLELQEE 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-459 |
7.90e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 124 SNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTA---TENTQARILHAEQEKAKV 200
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgltPEKLEKELEELEKAKEEI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 201 TEELAAATAQVS------------------------------------------HLQLKMTAHQKKETELQL-QLTDNLK 237
Cdd:PRK03918 404 EEEISKITARIGelkkeikelkkaieelkkakgkcpvcgrelteehrkelleeyTAELKRIEKELKEIEEKErKLRKELR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 238 ETDLLRGHVTRLQA------------------DLSELREASEQTQT-------------KFKSEKQSRRQLELKVTSLEE 286
Cdd:PRK03918 484 ELEKVLKKESELIKlkelaeqlkeleeklkkyNLEELEKKAEEYEKlkekliklkgeikSLKKELEKLEELKKKLAELEK 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 287 ELTDLRAEKTSLEKNLSERKKKSAQErcqAEAEMDEIRKSHQE---------ELDRLRQLLKKARVSTDQAAAEqLTLAQ 357
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESVEE---LEERLKELEPFYNEylelkdaekELEREEKELKKLEEELDKAFEE-LAETE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 358 AELQSQwEAKCEQLLASARDEhlqQYREVcaqrdahQQKLALLQDECLALQAQIAAFTEQKEHMQR-LEKTKSQAPAGRA 436
Cdd:PRK03918 640 KRLEEL-RKELEELEKKYSEE---EYEEL-------REEYLELSRELAGLRAELEELEKRREEIKKtLEKLKEELEEREK 708
|
410 420
....*....|....*....|...
gi 1907156437 437 AADPSEKVKKIMNQVfQSLRGEF 459
Cdd:PRK03918 709 AKKELEKLEKALERV-EELREKV 730
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-341 |
9.44e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 130 IQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLM---------MEKRNNSLQTATENTQARILHAEQEKAKV 200
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYeeyldelreIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 201 tEELaaataqvshlqlkmtahQKKETELQLQLTDnLKETDLLRGHVTRLQADLSELR-EASEQTQTKFKSEKQSrrqLEL 279
Cdd:PRK03918 341 -EEL-----------------KKKLKELEKRLEE-LEERHELYEEAKAKKEELERLKkRLTGLTPEKLEKELEE---LEK 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156437 280 KVTSLEEELTDLRAEKTSLEKNLSERKK-----KSAQERCQ------AEAEMDEIRKSHQEELDRLRQLLKKA 341
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKaieelKKAKGKCPvcgrelTEEHRKELLEEYTAELKRIEKELKEI 471
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
176-377 |
1.06e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 45.62 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 176 NNSLQTATENTQA---RILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQAD 252
Cdd:COG5283 13 KSALESAKQRVAAlaqALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLSAAQRRLRSS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 253 LSELREASEQTQTKFKSEKQSRRQLelkvTSLEEELTDLRAEKTSLEkNLSERKKKSAQERCQAEAEMDEIRKSHQ---- 328
Cdd:COG5283 93 LEQTNRQLERQQQRLARLGARQDRL----KAARARLQRLAGAGAAAA-AIGAALAASVKPAIDFEDAMADVAATVDldks 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907156437 329 -EELDRLRQLLKKA----RVSTDQAAAEQLTLAQAELQSQweakceQLLASARD 377
Cdd:COG5283 168 sEQFKALGKQARELsaqtPQSADDIAAGQAALAQAGVSAE------DILAFTPT 215
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
135-431 |
1.09e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 135 RLKQELLEKSSRIEEQNDKIsdliERNQRYVEQSNLMM----EKRN--NSLQTATENTQARILHAEQEKAKVTEELAAAT 208
Cdd:PRK02224 210 GLESELAELDEEIERYEEQR----EQARETRDEADEVLeeheERREelETLEAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 209 AQVSHLQ---------------------LKMTAHQKKETELQ-------LQLTDNLKETDLLRGHVTRLQADLSELREAS 260
Cdd:PRK02224 286 ERLEELEeerddllaeaglddadaeaveARREELEDRDEELRdrleecrVAAQAHNEEAESLREDADDLEERAEELREEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 261 EQTQTKFKSEKQSRRQLELKVTSLEEELTDLRaektsleknlsERKKKSAQERCQAEAEMDEIRkshqEELDRLRQLLKK 340
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELR-----------ERFGDAPVDLGNAEDFLEELR----EERDELREREAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 341 ARVSTdQAAAEQLTLAQAELQSQWEAKCEQLLA-SARDEHLQQYREvcaQRDAHQQKLALLQDECLALQAQIAAFTEQKE 419
Cdd:PRK02224 431 LEATL-RTARERVEEAEALLEAGKCPECGQPVEgSPHVETIEEDRE---RVEELEAELEDLEEEVEEVEERLERAEDLVE 506
|
330
....*....|..
gi 1907156437 420 HMQRLEKTKSQA 431
Cdd:PRK02224 507 AEDRIERLEERR 518
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
505-690 |
1.13e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 505 PLRPSLEQPGPATPGMPPAPPSGETQEAPEvlpeqvvgettPLPLQALPTPENGAQTrkgePAEAEVPSEIKDSSLPPQP 584
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPRPQPPLAPTTDPAGA-----------GEPSGAVPQPWLGALV----PGRVAVPRFRVPQPAPSRE 2987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 585 AGIPA-HRVLGPPTSIPPKPPGPVTMDSESEEMLAADQRTVQPNgllgeEHVREVATDGLLQGNSRRLSL-TPDPEKGEP 662
Cdd:PHA03247 2988 APASStPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPP-----DDTEDSDADSLFDSDSERSDLeALDPLPPEP 3062
|
170 180
....*....|....*....|....*....
gi 1907156437 663 PalDPESQGGEAQPPECKQAEDVSSS-GP 690
Cdd:PHA03247 3063 H--DPFAHEPDPATPEAGARESPSSQfGP 3089
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
70-308 |
1.22e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 70 EARQHNTEIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMetsmiMSNIQRIIQENERLKQELLEKSSRIEE 149
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDEL-----VEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 150 QNDKISDLierNQRYVEQSNLM--------MEKRNNSLQTATENtqariLHAEQEK-AKVTEELAAATAQVShlqlKMTA 220
Cdd:PHA02562 253 PSAALNKL---NTAAAKIKSKIeqfqkvikMYEKGGVCPTCTQQ-----ISEGPDRiTKIKDKLKELQHSLE----KLDT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 221 HQKKETELQLQLTDNLKEtdllrghVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEK 300
Cdd:PHA02562 321 AIDELEEIMDEFNEQSKK-------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
....*...
gi 1907156437 301 NLSERKKK 308
Cdd:PHA02562 394 TKSELVKE 401
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
126-364 |
1.37e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 126 IQRIIQENERLKQELLEKSS-----RIEEQNDKISDLIERNQRYVEQSNLMmekrnnSLQTATENTQARILHAEQEKAKV 200
Cdd:COG3206 158 AEAYLEQNLELRREEARKALefleeQLPELRKELEEAEAALEEFRQKNGLV------DLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 201 TEELAAATAQVSHLQlkmtahqkKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASE----------QTQTKFKS- 269
Cdd:COG3206 232 RAELAEAEARLAALR--------AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSArytpnhpdviALRAQIAAl 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 270 EKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERcQAEAEMDEIrkshQEELDRLRQLLKKArvstdQAA 349
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP-ELEAELRRL----EREVEVARELYESL-----LQR 373
|
250
....*....|....*
gi 1907156437 350 AEQLTLAQAELQSQW 364
Cdd:COG3206 374 LEEARLAEALTVGNV 388
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
172-361 |
1.51e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 172 MEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQA 251
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 252 DLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEEL 331
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180 190
....*....|....*....|....*....|
gi 1907156437 332 DRLRQLLKKARVSTDQAAAEQLTLAQAELQ 361
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-446 |
1.88e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 134 ERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMME--KRNNSLQTATENTQARILHAEQEKAKvTEELAAATAQV 211
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKKAEEAKK-ADEAKKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 212 SHLQLKMTAHQKKETELQLQLTDNLKETDllRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKvtslEEELTDL 291
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEED--KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK----KAEEAKI 1620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 292 RAEKtsLEKNLSERKKKSAQERCQAEA--EMDEIRKSHQEELDRLRQLLKKARvsTDQAAAEQLTLAQAELQSQWEAKCE 369
Cdd:PTZ00121 1621 KAEE--LKKAEEEKKKVEQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAE--EDKKKAEEAKKAEEDEKKAAEALKK 1696
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156437 370 QLLASARDEHLQQYREVcAQRDAHQQKLAllqDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKK 446
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAE-EKKKAEELKKA---EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
120-372 |
1.90e-04 |
|
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: 45.01 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 120 SMIMSNIQRIIQENER---LKQEL-------LEKSSRIEEQNDKISDLIERNQRYVEQS-NLMMEKR--NNSLQTATE-- 184
Cdd:TIGR04523 328 NQISQNNKIISQLNEQisqLKKELtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIkNLESQINdlESKIQNQEKln 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 185 -NTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQT 263
Cdd:TIGR04523 408 qQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 264 QTKFKSE-------KQSRRQLELKV-------TSLEEELTDLRAEKTSLEKNLSERKKK-----SAQERCQAEAEMDEIr 324
Cdd:TIGR04523 488 QKELKSKekelkklNEEKKELEEKVkdltkkiSSLKEKIEKLESEKKEKESKISDLEDElnkddFELKKENLEKEIDEK- 566
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907156437 325 kshQEELDRLRQLLKKARVSTDQAA--AEQLTLAQAELQSQWEAKCEQLL 372
Cdd:TIGR04523 567 ---NKEIEELKQTQKSLKKKQEEKQelIDQKEKEKKDLIKEIEEKEKKIS 613
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
130-443 |
2.11e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 130 IQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVE----QSNLMMEKRN---NSLQTATENTQARILHAEQE--KAKV 200
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNenaNNLIKQFENTKEKIAEYTKSidIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 201 TEE----LAAATAQVSHLQLKMtahqKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQT--KFKSEKQsr 274
Cdd:COG5185 311 TESleeqLAAAEAEQELEESKR----ETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSseELDSFKD-- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 275 rQLELKVTSLEEELTDLRAEKTSLEKNLSERKkksaqercqaeaemdeirKSHQEELDRLRQLLKKArVSTDQAAAEQLT 354
Cdd:COG5185 385 -TIESTKESLDEIPQNQRGYAQEILATLEDTL------------------KAADRQIEELQRQIEQA-TSSNEEVSKLLN 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 355 LAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAaftEQKEHMQR-LEKTKSQAPA 433
Cdd:COG5185 445 ELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLE---KLRAKLERqLEGVRSKLDQ 521
|
330
....*....|
gi 1907156437 434 GRAAADPSEK 443
Cdd:COG5185 522 VAESLKDFMR 531
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
122-305 |
2.41e-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: 43.37 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 122 IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIErnqryvEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVT 201
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKT------ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 202 EELAAATAQVSHLQLKMTAHQKKETELQLQLtdnlketdllrghvTRLQADLSELREASEQTQTKFKSEKQsrrQLELKV 281
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERI--------------EELEEELAELEAELAELEAELEEKKA---ELDEEL 151
|
170 180
....*....|....*....|....
gi 1907156437 282 TSLEEELTDLRAEKTSLEKNLSER 305
Cdd:COG1579 152 AELEAELEELEAEREELAAKIPPE 175
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
222-512 |
3.02e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 222 QKKETELQLQLTDNLKETDLLRGHVTRLQadlSELREASEQTqtkfkSEKQSRRQ-LELKVTSLEEELTDL--------- 291
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELS---QELSDASRKI-----GEIEKEIEqLEQEEEKLKERLEELeedlssleq 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 292 -----RAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEqltlAQAELQSqwEA 366
Cdd:TIGR02169 752 eienvKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE----IEQKLNR--LT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 367 KCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAaftEQKEHMQRLEKTKSqapagraaaDPSEKVKK 446
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE---ELEAALRDLESRLG---------DLKKERDE 893
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156437 447 IMNQVFQSLRGEFELEESYDggtILRTIMHTIKmVTLQLLNHQEEEEEEEEEEEEEKKPLRPSLEQ 512
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIE---KKRKRLSELK-AKLEALEEELSEIEDPKGEDEEIPEEELSLED 955
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
135-385 |
3.17e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.65 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 135 RLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAataqvshl 214
Cdd:pfam15905 55 KVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAS-------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 215 qlkmtahqkketeLQLQLTDNLKETDLLR------GHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEEL 288
Cdd:pfam15905 127 -------------LEKQLLELTRVNELLKakfsedGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 289 TDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQ--EELDRLRQLLKKARVSTDQAAAEQLTLAQA------EL 360
Cdd:pfam15905 194 EHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCvsEQVEKYKLDIAQLEELLKEKNDEIESLKQSleekeqEL 273
|
250 260
....*....|....*....|....*...
gi 1907156437 361 QSQWE---AKCeQLLASARDEHLQQYRE 385
Cdd:pfam15905 274 SKQIKdlnEKC-KLLESEKEELLREYEE 300
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
159-369 |
4.16e-04 |
|
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: 44.01 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 159 ERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDnlke 238
Cdd:pfam01576 200 EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE---- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 239 tdllrghvtrLQADLSELREASEqtqtkfKSEKQSR---RQLELKVTSLEEELTDLRAE---KTSLEKNLSERKKKSAQE 312
Cdd:pfam01576 276 ----------LQEDLESERAARN------KAEKQRRdlgEELEALKTELEDTLDTTAAQqelRSKREQEVTELKKALEEE 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156437 313 RCQAEAEMDEIRKSHQEELDRLRQLLKKARVS------TDQAAAEQLTLAQAELQSQWEAKCE 369
Cdd:pfam01576 340 TRSHEAQLQEMRQKHTQALEELTEQLEQAKRNkanlekAKQALESENAELQAELRTLQQAKQD 402
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
202-442 |
5.76e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 202 EELAAATAQVSHLQLKMTAHQKKETELQLQLtDNLKET-DLLRGHVTR--------LQADLSELREASEQTQTKFKSEKQ 272
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQL-EQAKEGlSALNRLLPRlnlladetLADRVEEIREQLDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 273 SRRQLELkvtsLEEELTDLRAEktsleknlserkkksaqercqaEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAA--- 349
Cdd:PRK04863 916 HGNALAQ----LEPIVSVLQSD----------------------PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrra 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 350 ------AEQLTLAQAELQSQWEAKCEQlLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFteqkehMQR 423
Cdd:PRK04863 970 hfsyedAAEMLAKNSDLNEKLRQRLEQ-AEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL------KQE 1042
|
250 260
....*....|....*....|..
gi 1907156437 424 LEKTKSQAPAG---RAAADPSE 442
Cdd:PRK04863 1043 LQDLGVPADSGaeeRARARRDE 1064
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
150-425 |
5.77e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 150 QNDKISDLIERNQRYVeQSNLMM---EKRNNSLQTAT-ENTQA---RILHAEQEK-AKVTEELAAATAQVSHLQlkmTAH 221
Cdd:COG3096 254 DRDLFKHLITEATNYV-AADYMRhanERRELSERALElRRELFgarRQLAEEQYRlVEMARELEELSARESDLE---QDY 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 222 QKKETELQLQLTdNLKetdlLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKN 301
Cdd:COG3096 330 QAASDHLNLVQT-ALR----QQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 302 LSE------------RKKKSAQERCQ--------AEAEMDEIRKSHQEELDRLRQLlkKARVSTDQAAAEQLTLAQAELQ 361
Cdd:COG3096 405 LDVqqtraiqyqqavQALEKARALCGlpdltpenAEDYLAAFRAKEQQATEEVLEL--EQKLSVADAARRQFEKAYELVC 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 362 S---------QWEAKCEQLLASARDEHL--------QQYREvcAQRDAHQQKLA--LLQDECLALQAQIAAFTEQKEHMQ 422
Cdd:COG3096 483 KiageversqAWQTARELLRRYRSQQALaqrlqqlrAQLAE--LEQRLRQQQNAerLLEEFCQRIGQQLDAAEELEELLA 560
|
...
gi 1907156437 423 RLE 425
Cdd:COG3096 561 ELE 563
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
137-431 |
6.03e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 137 KQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTE---ELAAATAQVSH 213
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsRVDLKLQELQH 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 214 LQLKMTAHQKKETE---LQLQLTDNLKETDLLRGHVTRLQADLSEL-REASEQTQTKFKSEKQ-SRRQLEL--------- 279
Cdd:pfam15921 536 LKNEGDHLRNVQTEceaLKLQMAEKDKVIEILRQQIENMTQLVGQHgRTAGAMQVEKAQLEKEiNDRRLELqefkilkdk 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 280 ---KVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQE--ELDRLRQLLKKarvsTDQAAAEQLT 354
Cdd:pfam15921 616 kdaKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNElnSLSEDYEVLKR----NFRNKSEEME 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 355 LAQAELQSQweakceqlLASARDEhLQQYREVCAQ---RDAHQQKLAL-LQDECLALQAQIAAFTEQkehMQRLEKTKSQ 430
Cdd:pfam15921 692 TTTNKLKMQ--------LKSAQSE-LEQTRNTLKSmegSDGHAMKVAMgMQKQITAKRGQIDALQSK---IQFLEEAMTN 759
|
.
gi 1907156437 431 A 431
Cdd:pfam15921 760 A 760
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
125-420 |
6.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 125 NIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRN---NSLQTATENTQARILHAEQEKAKVT 201
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEeleELLEQLSLATEEELQDLAEELEELQ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 202 EELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKV 281
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 282 TSLEeeLTDLRAEKTSLEKNLSERKKKSAQERCQAE---AEMDEIRKSHQEELDRLRQLLKKARvSTDQAAAEQLTLAQA 358
Cdd:COG4717 286 LALL--FLLLAREKASLGKEAEELQALPALEELEEEeleELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELEEE 362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907156437 359 ELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDeclaLQAQIAAFTEQKEH 420
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEE----LEEQLEELLGELEE 420
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
147-313 |
1.14e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 42.13 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 147 IEEQNDKISDLIErnqryvEQSNLMMEKR--NNSLQTATE---NTQARILHAEQEKAKVTEELAAATAQVSHLQLK-MTA 220
Cdd:pfam15066 365 INKLKENVEELIE------DKYNVILEKNdiNKTLQNLQEilaNTQKHLQESRKEKETLQLELKKIKVNYVHLQERyITE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 221 HQKKETE----LQLQLTDNLKEtdllrGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELkvtSLEEELTdlRAEKt 296
Cdd:pfam15066 439 MQQKNKSvsqcLEMDKTLSKKE-----EEVERLQQLKGELEKATTSALDLLKREKETREQEFL---SLQEEFQ--KHEK- 507
|
170
....*....|....*...
gi 1907156437 297 sleKNLSERKK-KSAQER 313
Cdd:pfam15066 508 ---ENLEERQKlKSRLEK 522
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
242-409 |
1.16e-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: 42.63 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 242 LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSlEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMD 321
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 322 EIRKshqeeldRLRQLLKKARV-STDQAAAEQLtlaqaELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALL 400
Cdd:COG3096 589 QLRA-------RIKELAARAPAwLAAQDALERL-----REQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQAL 656
|
....*....
gi 1907156437 401 QDECLALQA 409
Cdd:COG3096 657 ESQIERLSQ 665
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
122-318 |
1.19e-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: 42.63 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 122 IMSNIQRIIQENERLKQELLEKSSRIEEQNDKI---SDLIERNQRYVEQSNLMMEKRNNSLqtaTENTQARILHAEQEKA 198
Cdd:COG3096 925 LVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalSEVVQRRPHFSYEDAVGLLGENSDL---NEKLRARLEQAEEARR 1001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 199 KVTEELAAATAQV-----------SHLQLKMTAHQKKETELQ---LQLTDNLKETdlLRGHVTRLQADLSELReaseqtq 264
Cdd:COG3096 1002 EAREQLRQAQAQYsqynqvlaslkSSRDAKQQTLQELEQELEelgVQADAEAEER--ARIRRDELHEELSQNR------- 1072
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907156437 265 tkfksekqSRRqlelkvTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEA 318
Cdd:COG3096 1073 --------SRR------SQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
204-441 |
1.22e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 204 LAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTkfksekqsrrqlelKVTS 283
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA--------------EIDK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 284 LEEELTDLRAEKTSLEKNLSERkKKSAQERCQAEAEMDEI--RKSHQEELDRLrQLLKKArVSTDQAAAEQLTLAQAELQ 361
Cdd:COG3883 70 LQAEIAEAEAEIEERREELGER-ARALYRSGGSVSYLDVLlgSESFSDFLDRL-SALSKI-ADADADLLEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 362 SQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAAD 439
Cdd:COG3883 147 AKKAELEAKLaeLEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
..
gi 1907156437 440 PS 441
Cdd:COG3883 227 AA 228
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
89-423 |
1.23e-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: 42.19 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 89 MDHLMTKVEELQKHSSGNSMLLPSMSVTMetsmimsnIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQS 168
Cdd:pfam07888 3 LDELVTLEEESHGEEGGTDMLLVVPRAEL--------LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 169 NLMMEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQlQLTDNLKETDLLRghvtr 248
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELE-EDIKTLTQRVLER----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 249 lQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQ 328
Cdd:pfam07888 149 -ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 329 EELDrLRQLLKKARVSTDQAAAEQLTLA----------------QAEL-QSQWEAKCEQLLASARDEHLQQYREVCAQ-R 390
Cdd:pfam07888 228 KEAE-NEALLEELRSLQERLNASERKVEglgeelssmaaqrdrtQAELhQARLQAAQLTLQLADASLALREGRARWAQeR 306
|
330 340 350
....*....|....*....|....*....|....*
gi 1907156437 391 DAHQQKLALLQDECLALQAQIAAFTE--QKEHMQR 423
Cdd:pfam07888 307 ETLQQSAEADKDRIEKLSAELQRLEErlQEERMER 341
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
202-385 |
1.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 202 EELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTrlqaDLSELREASEQTQtKFKSEKQSRRQLELKV 281
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE----DEEELRAALEQAE-EYQELKEELEELEEQL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 282 TSLEEELTDLRAEKTslEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ 361
Cdd:COG4717 412 EELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
170 180
....*....|....*....|....
gi 1907156437 362 SQWEAKceQLLASARDEHLQQYRE 385
Cdd:COG4717 490 EEWAAL--KLALELLEEAREEYRE 511
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
202-425 |
1.49e-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: 42.25 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 202 EELAAATAQVSHLQLKMTAHQKKETELQLQLtDNLKET-DLLRGHVTRL----QADLSELREASEQTQTKFKSEKQSRRQ 276
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQL-DQLKEQlQLLNKLLPQAnllaDETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 277 LELKVTSLEEELTDLRAEKTS---LEKNLSERKKKSAQERCQAEAeMDEI--RKSH-------------QEELDRLRQLL 338
Cdd:COG3096 915 HGKALAQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFA-LSEVvqRRPHfsyedavgllgenSDLNEKLRARL 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 339 KKArvstdQAAAEQLTLAQAELQSQWeAKCEQLLASARdehlqqyrevcAQRDAHQQKLALLQDECLALQAQIAAFTEQK 418
Cdd:COG3096 994 EQA-----EEARREAREQLRQAQAQY-SQYNQVLASLK-----------SSRDAKQQTLQELEQELEELGVQADAEAEER 1056
|
....*....
gi 1907156437 419 --EHMQRLE 425
Cdd:COG3096 1057 arIRRDELH 1065
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
191-382 |
1.69e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.67 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 191 LHAEQEKAKVTE--ELAAATAQVSHLQLKmtahqKKETELQLQLT-DNLKETDLLRGHVTRLQADLSELreaSEQTQTKF 267
Cdd:pfam09731 236 EKAQSLAKLVDQykELVASERIVFQQELV-----SIFPDIIPVLKeDNLLSNDDLNSLIAHAHREIDQL---SKKLAELK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 268 KSEKQsrrQLELKVTSLEEELTDLRAEktsLEKNLSE-RKKKSAQERCQAEAEMDEIRKSHQEEldrLRQLLKKARVSTD 346
Cdd:pfam09731 308 KREEK---HIERALEKQKEELDKLAEE---LSARLEEvRAADEAQLRLEFEREREEIRESYEEK---LRTELERQAEAHE 378
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907156437 347 QAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQ 382
Cdd:pfam09731 379 EHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLK 414
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
132-423 |
1.86e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.55 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 132 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLmmekrnnslqtATENTQARILHAEQEKAKVTEEL-AAATAQ 210
Cdd:pfam05667 223 EEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAAL-----------AGTEATSGASRSAQDLAELLSSFsGSSTTD 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 211 VSHLQLKMTAHQKKET---ELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEE 287
Cdd:pfam05667 292 TGLTKGSRFTHTEKLQftnEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 288 LTDLRAEKTSLEKNLsERKKKSAQERCQAEAEMDEirkshqeeldrLRQLLkkarvstdQAAAEQLtlaqAELQSQWEAK 367
Cdd:pfam05667 372 LEELKEQNEELEKQY-KVKKKTLDLLPDAEENIAK-----------LQALV--------DASAQRL----VELAGQWEKH 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 368 CEQLLasardEHLQQYREVCA-QRDAHQQKLA---LLQDECLalqaQIAAFTEQKEHMQR 423
Cdd:pfam05667 428 RVPLI-----EEYRALKEAKSnKEDESQRKLEeikELREKIK----EVAEEAKQKEELYK 478
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
145-363 |
1.86e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 145 SRIEEQNDKISDLIERNQRYVEQSNLMMEKRNnSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQ--LKMTAHQ 222
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELE-ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReeLGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 223 KKETELQLQLTDNLKETDLLRGHVTRLQA-------------DLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELT 289
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDFLDRLSAlskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156437 290 DLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQ 363
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
240-431 |
1.89e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 240 DLLRGHVTRLQADLSELREASEQTQTKFKSE----KQSRRQLE-----LKVTSLEEELTDLRAEKTSLEKNLSERKKKSA 310
Cdd:PRK04778 201 DQLEEELAALEQIMEEIPELLKELQTELPDQlqelKAGYRELVeegyhLDHLDIEKEIQDLKEQIDENLALLEELDLDEA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 311 QERCQA-EAEMDEI----------RKSHQEELDRLRQLLKKARVSTDQAAAE--------QLTLAQAELQSQWEAKCEQL 371
Cdd:PRK04778 281 EEKNEEiQERIDQLydilerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEidrvkqsyTLNESELESVRQLEKQLESL 360
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156437 372 LAsardehlqQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQ----KEHMQRLEKTKSQA 431
Cdd:PRK04778 361 EK--------QYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEqeklSEMLQGLRKDELEA 416
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
173-336 |
1.97e-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: 40.68 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 173 EKRNNSLQTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTD--NLKETDLLRGHVTRLQ 250
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 251 ADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEktsleknLSERKKKSAQERCQAEAEMDEIRKSHQEE 330
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE-------LDEELAELEAELEELEAEREELAAKIPPE 175
|
170
....*....|
gi 1907156437 331 L----DRLRQ 336
Cdd:COG1579 176 LlalyERIRK 185
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
220-413 |
2.12e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.36 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 220 AHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSElreaseqtQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLE 299
Cdd:pfam12795 34 ASKQRAAAYQKALDDAPAELRELRQELAALQAKAEA--------APKEILASLSLEELEQRLLQTSAQLQELQNQLAQLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 300 KNLSERKKKSAQercqAEAEMDEIRKshqeELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQW----EAKCEQLLASA 375
Cdd:pfam12795 106 SQLIELQTRPER----AQQQLSEARQ----RLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKaqidMLEQELLSNNN 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907156437 376 RDEHLQqyrevcAQRDAHQQKLALLQDECLALQAQIAA 413
Cdd:pfam12795 178 RQDLLK------ARRDLLTLRIQRLEQQLQALQELLNE 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
247-506 |
2.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 247 TRLQADLSELREASEQTQtKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLseRKKKSAQERCQAEAEMDEIrks 326
Cdd:COG4717 71 KELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLL--QLLPLYQELEALEAELAEL--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 327 hQEELDRLRQllKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDE---HLQQYREVCAQRDAHQQKLALLQDE 403
Cdd:COG4717 145 -PERLEELEE--RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 404 CLALQAQIAAFTEQKEHMQRLE---------------------------------------------------KTKSQAP 432
Cdd:COG4717 222 LEELEEELEQLENELEAAALEErlkearlllliaaallallglggsllsliltiagvlflvlgllallflllaREKASLG 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907156437 433 AGRAAADPSEKVKKIMNQVFQSLRGEFELEESYDGGTILRTIMHTIKMVTLQLLNHQEEEEEEEEEEEEEKKPL 506
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
182-339 |
2.33e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 182 ATENTQARILHAEQEKAKVTEELAaataqvshlqlkmtahqkketelqlQLTDNLKETDLLRGHVTRLQADLSELREASE 261
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREIN-------------------------EISSELPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 262 QTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERK--KKSAQERCQAEAEMDEIRKSHQE---ELDRLRQ 336
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREiekRLSRLEE 321
|
...
gi 1907156437 337 LLK 339
Cdd:PRK03918 322 EIN 324
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
130-409 |
3.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 130 IQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQsnlmmEKRNNSLQTATENTQARILHAEQEKAKVTEELAAATA 209
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-----EDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 210 QVSHLQLKMTAHQKKETELQLqltdnlkETDLLRGHVTRLQADLSELreaseqtqtkfkseKQSRRQLElKVTSLEEELT 289
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEE-------EAEEAREEVAELNSKLAEL--------------KERIESLE-RIRTLLAAIA 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 290 DLRAEKTSLeknlserkkksaQERCQAEAEMDEIRKSHQEEL-DRLRQL---LKKARVSTDQAAAEQLTLAQAELQSQWE 365
Cdd:PRK02224 603 DAEDEIERL------------REKREALAELNDERRERLAEKrERKRELeaeFDEARIEEAREDKERAEEYLEQVEEKLD 670
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907156437 366 AKCEQ---LLAS-----ARDEHLQQYREVCAQRDAHQQKLALLQDECLALQA 409
Cdd:PRK02224 671 ELREErddLQAEigaveNELEELEELRERREALENRVEALEALYDEAEELES 722
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
180-366 |
3.48e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 180 QTATENTQARILHAEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSE---- 255
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 256 -----------------------------LREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERK 306
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 307 KKSAQERcQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEA 366
Cdd:COG3883 175 AQQAEQE-ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
127-364 |
3.52e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 127 QRIIQENERLKQELLEKssrIEEQNDKISDL------IERNQRYVEQSNLMMEKRN-------------NSL-QTATENT 186
Cdd:PRK10929 71 QQVIDNFPKLSAELRQQ---LNNERDEPRSVppnmstDALEQEILQVSSQLLEKSRqaqqeqdrareisDSLsQLPQQQT 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 187 QARILHAEQE---KAKVTEELAAATAQVSHLQLKMTAHQKKETELQL-QLTDNLKE------TDLLRGHVTRLQADLSEL 256
Cdd:PRK10929 148 EARRQLNEIErrlQTLGTPNTPLAQAQLTALQAESAALKALVDELELaQLSANNRQelarlrSELAKKRSQQLDAYLQAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 257 ReaseqTQTKFKSEKQSRRQLElKVTSLEEELTDLRAEKTS-LEKN--LSERKKKSAQercqaeaEMDEIrKSHQEeldr 333
Cdd:PRK10929 228 R-----NQLNSQRQREAERALE-STELLAEQSGDLPKSIVAqFKINreLSQALNQQAQ-------RMDLI-ASQQR---- 289
|
250 260 270
....*....|....*....|....*....|....*
gi 1907156437 334 lrqllkkarvstdQAAAEQLTLAQA----ELQSQW 364
Cdd:PRK10929 290 -------------QAASQTLQVRQAlntlREQSQW 311
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
217-362 |
4.02e-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: 39.12 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 217 KMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQtqtkFKSEKQSRRQLELKVTSLEEELTDLRAEKt 296
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN----YEKDKQSLKNLKARLKVLEKELKDLKWEH- 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156437 297 sleKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKaRVstdQAAAEQLTLAQAELQS 362
Cdd:pfam13851 109 ---EVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEK-KL---QALGETLEKKEAQLNE 167
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
137-457 |
4.03e-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: 40.71 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 137 KQELLEKSSRIEEQNDKISDLIERnQRYVEQSNLMMEKRNNSLQTATENtQARILHAEQEKAKVTEELAAATAQVSHLQL 216
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSAR-ESDLEQDYQAASDHLNLVQTALRQ-QEKIERYQEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 217 kmtahQKKETELQLQLTDnlKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQL---ELKVTSLEEELTDLRA 293
Cdd:COG3096 376 -----QLAEAEARLEAAE--EEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCglpDLTPENAEDYLAAFRA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 294 EKTSLEKNLSERKKK---SAQERCQAEAEMDEIRK-----SHQEELDRLRQLLKKARVSTDQAA-----------AEQLT 354
Cdd:COG3096 449 KEQQATEEVLELEQKlsvADAARRQFEKAYELVCKiagevERSQAWQTARELLRRYRSQQALAQrlqqlraqlaeLEQRL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 355 LAQAELQSQWEAKC-------------EQLLASA---RDEHLQQYREVCAQRDAHQQKLAllqdeclALQAQIAAFTeqk 418
Cdd:COG3096 529 RQQQNAERLLEEFCqrigqqldaaeelEELLAELeaqLEELEEQAAEAVEQRSELRQQLE-------QLRARIKELA--- 598
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907156437 419 ehmqrlektkSQAPAGRAAADPSEKVKKIMNQVFQSLRG 457
Cdd:COG3096 599 ----------ARAPAWLAAQDALERLREQSGEALADSQE 627
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
122-378 |
4.19e-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: 40.59 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 122 IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIER-NQRYVEQSNLMMEKR-------NNSLQTATENTQARILHA 193
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDElNGELSAADAAVAKDRselealeDQHGAFLDADIETAAADQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 194 EQ------EKAKVTEELAAATAQVSHLQLKMTA-HQKKETELQLQLTDNLKETDLLRGHVTR--------LQADLSELRE 258
Cdd:pfam12128 347 EQlpswqsELENLEERLKALTGKHQDVTAKYNRrRSKIKEQNNRDIAGIKDKLAKIREARDRqlavaeddLQALESELRE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 259 ASEQTQTKFKSEKQ--SRRQLELK-----VTSLEEELTDLRAEKTSLEknlserKKKSAQERCQAEAEmdeirkSHQEEL 331
Cdd:pfam12128 427 QLEAGKLEFNEEEYrlKSRLGELKlrlnqATATPELLLQLENFDERIE------RAREEQEAANAEVE------RLQSEL 494
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907156437 332 DRLRQLLKKARVSTDQA--AAEQLTLAQAELQSQWEAKCEQLLASARDE 378
Cdd:pfam12128 495 RQARKRRDQASEALRQAsrRLEERQSALDELELQLFPQAGTLLHFLRKE 543
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
126-426 |
5.09e-03 |
|
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: 40.34 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 126 IQRIIQENERLKQ---ELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQARILHAEQEKAKVTE 202
Cdd:TIGR00618 565 MQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 203 ELAAATAQVSHLQLKMTAHQKKETELQLQLTD-NLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKV 281
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKELLAsRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 282 TSLEEELTDLRAEKTSLEKNLSERKKKsAQERCQAEAEMDEiRKSHQE-----ELDRLRQLLKKARVSTDQAAAEQLTLA 356
Cdd:TIGR00618 725 NASSSLGSDLAAREDALNQSLKELMHQ-ARTVLKARTEAHF-NNNEEVtaalqTGAELSHLAAEIQFFNRLREEDTHLLK 802
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156437 357 QAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDA------HQQKLALLQD-ECLALQAQiaAFTEQKEHMQRLEK 426
Cdd:TIGR00618 803 TLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEeksatlGEITHQLLKYeECSKQLAQ--LTQEQAKIIQLSDK 877
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
250-438 |
5.19e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.79 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 250 QADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEmdEIRKSHQE 329
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAA--AAKAKAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 330 ELDRLRQLLKKARVSTD-QAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLAllqdecLALQ 408
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKkKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA------EAKA 225
|
170 180 190
....*....|....*....|....*....|
gi 1907156437 409 AQIAAFTEQKEHMQRLEKTKSQAPAGRAAA 438
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
517-760 |
5.33e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.54 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 517 TPGMPPAPPSGETQEAP--EVLPEQVVGETTPLPLQALPT--PENGAQTRKGEPAEAEVPSEIKDSSLPPQPAGIPAHRV 592
Cdd:PHA03307 64 RFEPPTGPPPGPGTEAPanESRSTPTWSLSTLAPASPAREgsPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 593 LGPPTSIPPKPPGpvtmdsESEEMLAADQRTVQPNGLL---GEEHVRevatdgllqgnsrrlsltPDPEKGEPPALDPES 669
Cdd:PHA03307 144 PGPPPAASPPAAG------ASPAAVASDAASSRQAALPlssPEETAR------------------APSSPPAEPPPSTPP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 670 QGGEAQPPECKQAEDVSSSGPRETLLDTELASAAAGTSLRHNQDSQHCSLSGDEEdelfkgATLKVPRPTAQPEEEDEDE 749
Cdd:PHA03307 200 AAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENE------CPLPRPAPITLPTRIWEAS 273
|
250
....*....|.
gi 1907156437 750 VSMKGRPPPTP 760
Cdd:PHA03307 274 GWNGPSSRPGP 284
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
193-359 |
5.81e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 39.85 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 193 AEQEKAKVTEELAAATAQvshlQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTrLQADlSELREASEQTQTKFKSEKQ 272
Cdd:PRK00106 24 IKMKSAKEAAELTLLNAE----QEAVNLRGKAERDAEHIKKTAKRESKALKKELL-LEAK-EEARKYREEIEQEFKSERQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 273 SRRQLELKVTSLEEELtDLRAEKTSLEKNLSERKKKSAQERC----QAEAEMDEIRKSHQEELDRLRQLlkkarvstDQA 348
Cdd:PRK00106 98 ELKQIESRLTERATSL-DRKDENLSSKEKTLESKEQSLTDKSkhidEREEQVEKLEEQKKAELERVAAL--------SQA 168
|
170
....*....|.
gi 1907156437 349 AAEQLTLAQAE 359
Cdd:PRK00106 169 EAREIILAETE 179
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
274-423 |
6.55e-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: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 274 RRQLELKVTSLEEELTDLRAEKTSLEKnlserkkksAQERCQAEAEMDEIRKSHQE---ELDRLRQLLKKARVSTDQAAA 350
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALED---------AREQIELLEPIRELAERYAAareRLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156437 351 EQLTLAQAELQSQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQ-QKLAllqdeclALQAQIAAFTEQKEHMQR 423
Cdd:COG4913 291 ELLEAELEELRAELARLEAELerLEARLDALREELDELEAQIRGNGgDRLE-------QLEREIERLERELEERER 359
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
223-458 |
6.79e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.06 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 223 KKETELQLQLTDNLKETDLLRGHVtrLQADLSElreaSEQTQTKFKSEKQS--RRQLELKVTSLEEELTDLRAEKTSLE- 299
Cdd:COG5022 823 QKTIKREKKLRETEEVEFSLKAEV--LIQKFGR----SLKAKKRFSLLKKEtiYLQSAQRVELAERQLQELKIDVKSISs 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 300 -KNLSERKKKSAQE-RCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQ---WEAKCEQL--L 372
Cdd:COG5022 897 lKLVNLELESEIIElKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVeskLKETSEEYedL 976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 373 ASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLE---KTKSQAPAGRAAADPSEKVKKIMN 449
Cdd:COG5022 977 LKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQsasKIISSESTELSILKPLQKLKGLLL 1056
|
....*....
gi 1907156437 450 QVFQSLRGE 458
Cdd:COG5022 1057 LENNQLQAR 1065
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
134-417 |
6.91e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 134 ERLKQELLEKSSRIEEQN---DKISDLIERNQRYVEQSNLMMEKRNNSL---QTATENTQARIL---HAEQ--EKAKVTE 202
Cdd:PRK04863 351 ERYQADLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVQQTRAIqyqQAVQalERAKQLC 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 203 ELAAATA-QVSHLQLKMTAHQKKETELQLQLTDNLKETD-----------LLR---GHVTR------------------- 248
Cdd:PRK04863 431 GLPDLTAdNAEDWLEEFQAKEQEATEELLSLEQKLSVAQaahsqfeqayqLVRkiaGEVSRseawdvarellrrlreqrh 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 249 -------LQADLSELREASEQTQTKFKSEKQSRRQLELKVTSlEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAemd 321
Cdd:PRK04863 511 laeqlqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEARERRMALRQ--- 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 322 eirksHQEELD-RLRQLLKKARV-STDQAAAEQLtlaqaELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLAL 399
Cdd:PRK04863 587 -----QLEQLQaRIQRLAARAPAwLAAQDALARL-----REQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
330
....*....|....*...
gi 1907156437 400 LQDECLALQAQIAAFTEQ 417
Cdd:PRK04863 657 LDEEIERLSQPGGSEDPR 674
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
56-424 |
6.97e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 56 HFQGSGDMMSFLMteaRQHNTEIRMAVNKVADKMDHLmtkvEELQKHSSGNSMLLPSMSvtmetsmiMSNIQRIIQENER 135
Cdd:pfam15921 214 HFRSLGSAISKIL---RELDTEISYLKGRIFPVEDQL----EALKSESQNKIELLLQQH--------QDRIEQLISEHEV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 136 LKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENtqariLHAEQEKAKVTEElaaatAQVSHLQ 215
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQ-----LRSELREAKRMYE-----DKIEELE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 216 LKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADL----SELREASEQTQTKFKSEKQS-------RRQLE---LKV 281
Cdd:pfam15921 349 KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLhkreKELSLEKEQNKRLWDRDTGNsitidhlRRELDdrnMEV 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 282 TSLEEELTDLRAE-KTSLEKNLS--ERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQllKKARVSTDQAAAEQLTLAQA 358
Cdd:pfam15921 429 QRLEALLKAMKSEcQGQMERQMAaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTA--KKMTLESSERTVSDLTASLQ 506
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156437 359 ELQSQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQQklalLQDECLALQAQIAA-------FTEQKEHMQRL 424
Cdd:pfam15921 507 EKERAIEATNAEItkLRSRVDLKLQELQHLKNEGDHLRN----VQTECEALKLQMAEkdkvieiLRQQIENMTQL 577
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
193-418 |
8.79e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 39.63 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 193 AEQEKAKVTEELAAATAQVSHLQLKMTAHQKKETELQlqltdnlKETDLLRGHVTRLQADLSElrEASEQTQTKFKSEKQ 272
Cdd:pfam05701 61 AEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAK-------QDSELAKLRVEEMEQGIAD--EASVAAKAQLEVAKA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 273 SRRQLELKVTSLEEELTDLRAEKTSLeknLSERkKKSAQERCQAEAEMDEIRKSHQE---ELDRLRQLLKKARVSTDQAA 349
Cdd:pfam05701 132 RHAAAVAELKSVKEELESLRKEYASL---VSER-DIAIKRAEEAVSASKEIEKTVEEltiELIATKESLESAHAAHLEAE 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907156437 350 AEQLTLAQAELQ--SQWEAKCEQLlasarDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQK 418
Cdd:pfam05701 208 EHRIGAALAREQdkLNWEKELKQA-----EEELQRLNQQLLSAKDLKSKLETASALLLDLKAELAAYMESK 273
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
131-302 |
9.72e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 131 QENERLKQELLEKSSRIEEQNDKISDLIERNQRYveqsnlmmekrnnslqtateNTQARILHAEQEKAKVTEELAAATAQ 210
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKL--------------------EKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156437 211 VSHLQLKMTAHQKKETELQlQLTDNLKEtdlLRGHVTRLQADLS-ELREASEQTQTKFKSEKQSRRQLELKVTSLEEELT 289
Cdd:COG4717 148 LEELEERLEELRELEEELE-ELEAELAE---LQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|...
gi 1907156437 290 DLRAEKTSLEKNL 302
Cdd:COG4717 224 ELEEELEQLENEL 236
|
|
| |
