|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-436 |
8.23e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 8.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 122 IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQ--AKVTEELAAATA 199
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEelAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 200 QVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELT 279
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 280 DLRAEKTSLEKNLSERKKKSAQERcQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEakcE 359
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEE-EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR---L 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 360 QLLASARDEHLQQYREVCAQRDAHQQK-----LALLQDECLALQAQIAA---------FTEQKEHMQRLEKTKSQAPAGR 425
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRglagaVAVLIGVEAAYEAALEAalaaalqniVVEDDEVAAAAIEYLKAAKAGR 573
|
330
....*....|.
gi 1720409153 426 AAADPSEKVKK 436
Cdd:COG1196 574 ATFLPLDKIRA 584
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-443 |
1.36e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 180 QTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKS 259
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 260 EKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKK---SAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTD 336
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAElaeAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 337 QAAAEQLTLAQAELQsqwEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEK 416
Cdd:COG1196 401 QLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250 260
....*....|....*....|....*..
gi 1720409153 417 TKSQAPAGRAAADPSEKVKKIMNQVFQ 443
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-404 |
4.34e-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: 66.62 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 125 NIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATEntqakVTEELAAATAQVSHL 204
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-----LEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 205 QLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEK--------------QSRRQLELK 270
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErriaaterrledleEQIEELSED 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 271 VTSLEEELTDLRAEKTSLEKNL---SERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQ 347
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELealLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409153 348 AELQSQweakceQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAF 404
Cdd:TIGR02168 934 LEVRID------NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-408 |
7.79e-11 |
|
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: 65.86 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 92 LMTKVEELQKHSSgnsMLLPSMSV-TMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNL 170
Cdd:TIGR02169 693 LQSELRRIENRLD---ELSQELSDaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 171 MMEKRNNsLQTATENTQA--------KVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQAD 242
Cdd:TIGR02169 770 LEEDLHK-LEEALNDLEArlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 243 LSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKsaqeRCQAEAEMDEIRKsHQEELD 322
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK----IEELEAQIEKKRK-RLSELK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 323 RLRQLLKKARVSTDQAAAEQLTLAQAELQ-SQWEAKCEQLLASARD------EHLQQYREVCAQRDAHQQKLALLQDECL 395
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEIPEEELSlEDVQAELQRVEEEIRAlepvnmLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
330
....*....|...
gi 1720409153 396 ALQAQIAAFTEQK 408
Cdd:TIGR02169 1004 AILERIEEYEKKK 1016
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
210-436 |
6.80e-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: 61.70 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 210 AHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLE 289
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 290 KNLSERKKK------SAQERCQAEAEMDEIRKSHQEELDRLRQLLKKArVSTDQAAAEQLTLAQAELQSQWEAKCEQL-- 361
Cdd:COG4942 97 AELEAQKEElaellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-APARREQAEELRADLAELAALRAELEAERae 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409153 362 LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKK 436
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-421 |
1.05e-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: 62.38 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 137 KQELLEKSSRIEEQNDKISDLIERnqryveqsnlmMEKRNNSLQTatentQAKVTEELAAATAQVSHLQL-----KMTAH 211
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNE-----------LERQLKSLER-----QAEKAERYKELKAELRELELallvlRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 212 QKKETELQLQLTDNLKETDLLRGHVTRLQADLSELR-------EASEQTQTKFKS--------------EKQSRRQLELK 270
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRlevseleEEIEELQKELYAlaneisrleqqkqiLRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 271 VTSLEEELTDLRAEKTSLEKNLSERKKK--SAQERCQAEAEMDEIRKSHQEELDRLRQLLKKA--RVSTDQAAAE-QLTL 345
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKleELKEELESLEAELEELEAELEELESRLEELEEQleTLRSKVAQLElQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 346 AQAELQSQwEAKCEQLlaSARDEHLQQYRE------VCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKS 419
Cdd:TIGR02168 398 LNNEIERL-EARLERL--EDRRERLQQEIEellkklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
..
gi 1720409153 420 QA 421
Cdd:TIGR02168 475 QA 476
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
188-382 |
2.61e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 188 AKVTEELAAATAQVSHLQLKMTAHQKKETELQ--LQLTDNLKETDLLRGHVTRLQADLSELREASeqtqTKFKSEKQSRR 265
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASS----DDLAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 266 QLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELD-RLRQLLKKARVstdQAAAEQLT 344
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEeRFAAALGDAVE---RELRENLE 772
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720409153 345 LAQAELQSQwEAKCEQLLASARDEHLQQYREVCAQRDA 382
Cdd:COG4913 773 ERIDALRAR-LNRAEEELERAMRAFNREWPAETADLDA 809
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
212-456 |
4.71e-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: 60.07 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 212 QKKETELQL--------QLTDNLKEtdlLRGHVTRLQA-------------------------DLSELREASEQTQTKFK 258
Cdd:TIGR02168 173 RRKETERKLertrenldRLEDILNE---LERQLKSLERqaekaerykelkaelrelelallvlRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 259 SEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKK-----SAQERCQAEAEMDEIRKSH----QEELDRLRQLLK 329
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaNEISRLEQQKQILRERLANlerqLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 330 KARVsTDQAAAEQLTLAQAELQSQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQ 407
Cdd:TIGR02168 330 SKLD-ELAEELAELEEKLEELKEELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1720409153 408 KEHMQ-RLEKTKSQAPAGRAAADPSEKvKKIMNQVFQSLRGEFELEESYD 456
Cdd:TIGR02168 409 LERLEdRRERLQQEIEELLKKLEEAEL-KELQAELEELEEELEELQEELE 457
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
127-349 |
1.11e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 127 QRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKrnnslqtaTENTQAKVTEELAAATAQVSHLQL 206
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED--------AEERLAKLEAEIDKLLAEIEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 207 KMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTK---FKSEKQS-----------RRQLELKVT 272
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKlekLKREINElkreldrlqeeLQRLSEELA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 273 SLEEELTDLRAEKTSLE---KNLSERKKKSAQERCQAEAEMDEIRKSH---QEELDRLRQLLKKARVSTDQAAAEQLTLA 346
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEeekEDKALEIKKQEWKLEQLAADLSKYEQELydlKEEYDRVEKELSKLQRELAEAEAQARASE 503
|
...
gi 1720409153 347 QAE 349
Cdd:TIGR02169 504 ERV 506
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
177-430 |
2.97e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.61 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 177 NSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETE-LQLQLTDNLKETdllrghvTRLQADLSELReASEQTQT 255
Cdd:PRK11281 43 AQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEqLKQQLAQAPAKL-------RQAQAELEALK-DDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 256 KFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSerKKKSAQERCQaeAEMDEirksHQEELDRLRQLLKKARVST 335
Cdd:PRK11281 115 RETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLV--SLQTQPERAQ--AALYA----NSQRLQQIRNLLKGGKVGG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 336 DQAAAEQLTLAQAELQSqWEAKCE---QLLASArdEHLQQYREvcAQRDAHQQKLALLQDECLALQAQIAA--FTEQKEH 410
Cdd:PRK11281 187 KALRPSQRVLLQAEQAL-LNAQNDlqrKSLEGN--TQLQDLLQ--KQRDYLTARIQRLEHQLQLLQEAINSkrLTLSEKT 261
|
250 260
....*....|....*....|
gi 1720409153 411 MQRLEktkSQAPAGRAAADP 430
Cdd:PRK11281 262 VQEAQ---SQDEAARIQANP 278
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
131-354 |
6.09e-08 |
|
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: 55.54 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 131 QENERLKQELLEKSSRIEEQNDKISDL---IERNQRYVEQSNLMMEKRNNSLQtATENTQAKVTEELAAATAQVSHLQLK 207
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALkkeEKALLKQLAALERRIAALARRIR-ALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 208 MTAHQKKETEL--QLQLTDNLKETDLLRG---------HVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEE 276
Cdd:COG4942 99 LEAQKEELAELlrALYRLGRQPPLALLLSpedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409153 277 ELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEElDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQW 354
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA-EELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
122-315 |
7.62e-08 |
|
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: 55.80 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 122 IMSNIQRIIQENERLKQELLEkssrIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTaTENTQAKVTEELAAATAQV 201
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ-LKDEQNKIKKQLSEKQKEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 202 --SHLQLKMTAHQKKETELQLQLTDNLKETDLLRghvtRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELT 279
Cdd:TIGR04523 277 eqNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK----ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720409153 280 DLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRK 315
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-350 |
9.92e-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: 55.83 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 76 TEIRMAVNKVADKMDHLMTKVEELQKhssgnsmllpsmsvtmETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKIS 155
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALAN----------------EISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 156 DLIERNQRyveqsnlmMEKRNNSLQTATENTQAKVTE---ELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLL 232
Cdd:TIGR02168 334 ELAEELAE--------LEEKLEELKEELESLEAELEEleaELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 233 RGHVTRLQADLSELREasEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEknlsERKKKSAQERCQAEAEMDE 312
Cdd:TIGR02168 406 EARLERLEDRRERLQQ--EIEELLKKLEEAELKELQAELEELEEELEELQEELERLE----EALEELREELEEAEQALDA 479
|
250 260 270
....*....|....*....|....*....|....*....
gi 1720409153 313 IRKSHQEELDRLRQLLK-KARVSTDQAAAEQLTLAQAEL 350
Cdd:TIGR02168 480 AERELAQLQARLDSLERlQENLEGFSEGVKALLKNQSGL 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
184-376 |
2.72e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 184 ENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNlkETDLLrghvTRLQADLSELREASEQTQTKFKSEKQS 263
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRL----EQLEREIERLERELEERERRRARLEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 264 RRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQE---ELDRLRQL-------LKKARv 333
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREleaEIASLERRksniparLLALR- 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409153 334 stdQAAAEQLTLAQAEL------------QSQWEAKCEQLLASAR------DEHLQQYREV 376
Cdd:COG4913 447 ---DALAEALGLDEAELpfvgelievrpeEERWRGAIERVLGGFAltllvpPEHYAAALRW 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
126-379 |
4.02e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 126 IQRIIQENERLKQELLEKSSRIEEQNDKISDLIERnqryveqsnlmmekrnnslqtatentqakvtEELAAATAQVSHLQ 205
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQER-------------------------------REALQRLAEYSWDE 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 206 LKMTAHQKKETELQLQLtDNLKETDllrGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEK 285
Cdd:COG4913 661 IDVASAEREIAELEAEL-ERLDASS---DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 286 TSLEKNLSERKKKSAQERCQAEAEmDEIRKSHQEELDRLRQLLKKARvstdQAAAEQLTLAQAELQSQWEAKCEQLLASA 365
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALG-DAVERELRENLEERIDALRARL----NRAEEELERAMRAFNREWPAETADLDADL 811
|
250
....*....|....
gi 1720409153 366 RDehLQQYREVCAQ 379
Cdd:COG4913 812 ES--LPEYLALLDR 823
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
115-319 |
9.43e-07 |
|
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: 52.33 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 115 VTMETSMIMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIER-NQRYVEQSNLMMEKRnnslqtatENTQAKVTEE 193
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQlNQLKSEISDLNNQKE--------QDWNKELKSE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 194 LaaataqvshlqlkmTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTS 273
Cdd:TIGR04523 316 L--------------KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720409153 274 LEEELTDLRAEKTSLEKNLSERKKKSAQERCQ---AEAEMDEIRKSHQE 319
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQikkLQQEKELLEKEIER 430
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
125-351 |
1.45e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.84 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 125 NIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERN-----QRYVEQSNLMMEKRNNSLQTATENTQakvtEELAAATA 199
Cdd:PRK11281 74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNdeetrETLSTLSLRQLESRLAQTLDQLQNAQ----NDLAEYNS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 200 QVSHLQLK-------MTAHQKKETELQLQLTDNLKETDLLRG-HVTRLQADLS------ELREASEQTQTKFKSEKQSRR 265
Cdd:PRK11281 150 QLVSLQTQperaqaaLYANSQRLQQIRNLLKGGKVGGKALRPsQRVLLQAEQAllnaqnDLQRKSLEGNTQLQDLLQKQR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 266 QL-ELKVTSLEEELTDLRAEKTslEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAaeqlT 344
Cdd:PRK11281 230 DYlTARIQRLEHQLQLLQEAIN--SKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLN----T 303
|
....*..
gi 1720409153 345 LAQAELQ 351
Cdd:PRK11281 304 LTQQNLR 310
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-400 |
1.52e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 192 EELAAATAQVSHLQLKMTAHQK-KETELQLQLTDNLKEtdllRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELK 270
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERyAAARERLAELEYLRA----ALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 271 VTSLEEELTDLRAEktsLEKNLSERKKKSAQERCQAEAEMDEIrkshQEELDRLRQLLKKARVSTDQAAAEQltlaqAEL 350
Cdd:COG4913 318 LDALREELDELEAQ---IRGNGGDRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASAEEF-----AAL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720409153 351 QSQWEAKCEQLlASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQ 400
Cdd:COG4913 386 RAEAAALLEAL-EEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-349 |
3.97e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 134 ERLKQELLEKSSRIEEQNDKisdliernqRYVEQSNLMMEKRNNSLQTATENTQAKvtEELAAATAQVSHLQLKMTAHQK 213
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEKKMKAEEA 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 214 KETELQLQLTDNLKETDLLRGHVTRLQADLSE-------LREASEQT-----QTKFKSEKQSRRQLELKVTSLEEELTDL 281
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekkkaeeLKKAEEENkikaaEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409153 282 RAEKTSLEKNLSER-KKKSAQERCQAEaemdEIRKSHQEELDRLRQLLKKARvsTDQAAAEQLTLAQAE 349
Cdd:PTZ00121 1693 ALKKEAEEAKKAEElKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAE--EDKKKAEEAKKDEEE 1755
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
136-356 |
4.61e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 136 LKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATEnTQAKVTEELAAATAQVSHLQlkmtaHQKKE 215
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELR-----EELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 216 TELQLQLTDNLKETDLLRGHVTRLQADLSELREaseqtqtkfksEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSER 295
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAELPERLEELEE-----------RLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409153 296 KKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEA 356
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
132-435 |
4.62e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 132 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQA---KVTEELAAATAQVSHLQLKM 208
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaekKKEEAKKKADAAKKKAEEKK 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 209 TAHQ-KKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEqtqTKFKSEkQSRRQLELKVTSlEEELTDLRAEKTS 287
Cdd:PTZ00121 1392 KADEaKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE---AKKKAE-EAKKADEAKKKA-EEAKKAEEAKKKA 1466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 288 LEKNLSERKKKSAQERCQAE--AEMDEIRKSHQEELDRLRQLLKKA---RVSTDQAAAEQLTLAQAELQSQWEAKCEQLL 362
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADeaKKKAEEAKKKADEAKKAAEAKKKAdeaKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409153 363 ASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQK--EHMQRLEKTKSQAPAGRAAADPSEKVK 435
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
240-456 |
6.20e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 240 QADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKK--KSAQERCQAEAEMDEIRKSH 317
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 318 QEELDRLRQLLKKARVSTDQAAAE------QLTLAQAELQSQWEAKCEQlLASARDEHLQQYREVCAQR---DAHQQKLA 388
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEaeaeieELEAQIEQLKEELKALREA-LDELRAELTLLNEEAANLRerlESLERRIA 834
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720409153 389 LLQDECLALQAQIAaftEQKEHMQRLEktKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEFELEESYD 456
Cdd:TIGR02168 835 ATERRLEDLEEQIE---ELSEDIESLA--AEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
213-497 |
7.30e-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: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 213 KKETELQLQLT-DNLKE-TDLLRGhvtrLQADLSELREASEQTQtKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEK 290
Cdd:COG1196 174 KEEAERKLEATeENLERlEDILGE----LERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 291 NLSERKKKSAQ-ERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEH 369
Cdd:COG1196 249 EELEAELEELEaELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 370 LQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQkehmqRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEF 449
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-----LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720409153 450 ELEESydggtiLRTIMHTIKMVTLQLLNHQEEEEEEEEEEEEEKKPLR 497
Cdd:COG1196 404 ELEEA------EEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
125-416 |
1.12e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 125 NIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRnNSLQTATENTQAKVTEELAAATAQVSHL 204
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ-EELEELLEQLSLATEEELQDLAEELEEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 205 QLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQAD------------------------------------------ 242
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallallglggsllsliltiagvlflvlg 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 243 -----LSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAeKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSH 317
Cdd:COG4717 285 llallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGL-PPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 318 QEE--LDRLRQLLKKARVSTD-------------QAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDA 382
Cdd:COG4717 364 QLEelEQEIAALLAEAGVEDEeelraaleqaeeyQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEE 443
|
330 340 350
....*....|....*....|....*....|....
gi 1720409153 383 HQQKLALLQDECLALQAQIAAFTEQKEHMQRLEK 416
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQE 477
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-359 |
1.38e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 124 SNIQRIIQENErlkQELLEKSSRIEEQNDKISDLIERnqryVEqsnlMMEKRNNSLQtatentqaKVTEELAAATAQVSH 203
Cdd:PRK03918 189 ENIEELIKEKE---KELEEVLREINEISSELPELREE----LE----KLEKEVKELE--------ELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 204 LQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQadlsELREASEQTQT--KFKSE-KQSRRQLELKVTSLEEELTD 280
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKlsEFYEEyLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409153 281 LRAEKTSLEKnLSERKKKSAQERCQAEAEMDEIRKSHqEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCE 359
Cdd:PRK03918 326 IEERIKELEE-KEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
185-408 |
1.39e-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: 48.70 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 185 NTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLtdnlketDLLRGHVTRLQADLSELREASEQTQTKFKS----- 259
Cdd:pfam09726 388 NNQLSKPDALVRLEQDIKKLKAELQASRQTEQELRSQI-------SSLTSLERSLKSELGQLRQENDLLQTKLHNavsak 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 260 --EKQSRRQLELKvtsLEEEltdlRAEKTSLEKNLSERKK-------KSAQERCQAEA---EMDEIRKSHQEELD-RLRQ 326
Cdd:pfam09726 461 qkDKQTVQQLEKR---LKAE----QEARASAEKQLAEEKKrkkeeeaTAARAVALAAAsrgECTESLKQRKRELEsEIKK 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 327 LLKKARVSTDQAAaeqltlaqaelqsQWEAKCEQllasardehLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTE 406
Cdd:pfam09726 534 LTHDIKLKEEQIR-------------ELEIKVQE---------LRKYKESEKDTEVLMSALSAMQDKNQHLENSLSAETR 591
|
..
gi 1720409153 407 QK 408
Cdd:pfam09726 592 IK 593
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
127-421 |
1.88e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 127 QRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQsnlMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQL 206
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEE---VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 207 KMTAHQKKET-----ELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDL 281
Cdd:PRK02224 317 EELEDRDEELrdrleECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 282 RaektsleknlsERKKKSAQERCQAEAEMDEIRkshqEELDRLRQLLKKARVSTdQAAAEQLTLAQAELQSQWEAKCEQL 361
Cdd:PRK02224 397 R-----------ERFGDAPVDLGNAEDFLEELR----EERDELREREAELEATL-RTARERVEEAEALLEAGKCPECGQP 460
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409153 362 LA-SARDEHLQQYREvcaQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQA 421
Cdd:PRK02224 461 VEgSPHVETIEEDRE---RVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERR 518
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
127-380 |
2.02e-05 |
|
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: 48.20 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 127 QRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQAKV----TEELAAATAQVS 202
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELerirQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 203 HLQ-LKMTAHQKK----------------ETELQLQLTDNLKETDLLRGHVTRL-QADLSELREASEQTQTKFKSEKQSR 264
Cdd:pfam17380 379 ELErLQMERQQKNervrqeleaarkvkilEEERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMERVRLEEQER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 265 RQlelKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEElDRLRQLLKKARVSTDQAAAEQLT 344
Cdd:pfam17380 459 QQ---QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEE-ERKRKLLEKEMEERQKAIYEEER 534
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720409153 345 LAQAELQSQWEAKCEQllasaRDEHLQQYREVCAQR 380
Cdd:pfam17380 535 RREAEEERRKQQEMEE-----RRRIQEQMRKATEER 565
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
130-433 |
2.08e-05 |
|
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: 48.03 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 130 IQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVE----QSNLMMEKRN---NSLQTATENTQAKVTEELAAATAQVS 202
Cdd:COG5185 231 IEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNenaNNLIKQFENTKEKIAEYTKSIDIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 203 HLQLKmtaHQKKETELQLQLTDNLKETDllrGHVTRLQADLSELREASEQTQTKFKSEKqSRRQLELKVTSLEEELTDLR 282
Cdd:COG5185 311 TESLE---EQLAAAEAEQELEESKRETE---TGIQNLTAEIEQGQESLTENLEAIKEEI-ENIVGEVELSKSSEELDSFK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 283 AEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKArVSTDQAAAEQLTLAQAELQSQWEAKCEQLL 362
Cdd:COG5185 384 DTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQA-TSSNEEVSKLLNELISELNKVMREADEESQ 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409153 363 ASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAaftEQKEHMQR-LEKTKSQAPAGRAAADPSEK 433
Cdd:COG5185 463 SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLE---KLRAKLERqLEGVRSKLDQVAESLKDFMR 531
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
209-387 |
2.13e-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: 46.46 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 209 TAHQKKETELQLQLTDNlkETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSL 288
Cdd:COG1579 1 AMPEDLRALLDLQELDS--ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 289 EKNLSERKKKSAQERCQAEAEMDEIRKSHQEEldrlRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQlLASARDE 368
Cdd:COG1579 79 EEQLGNVRNNKEYEALQKEIESLKRRISDLED----EILELMERIEELEEELAELEAELAELEAELEEKKAE-LDEELAE 153
|
170
....*....|....*....
gi 1720409153 369 HLQQYREVCAQRDAHQQKL 387
Cdd:COG1579 154 LEAELEELEAEREELAAKI 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
221-428 |
2.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 221 QLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLE--LKVTSLEEELTDLRAEKTSLEKNLsERKKK 298
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERL-EELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 299 SAQERCQAEAEMDEIRkshqEELDRLRQLLKKARVSTDQAAAEQLTlaqaelqsqweakceqllasardEHLQQYREVCA 378
Cdd:COG4717 154 RLEELRELEEELEELE----AELAELQEELEELLEQLSLATEEELQ-----------------------DLAEELEELQQ 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720409153 379 QRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAA 428
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
79-420 |
5.11e-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: 46.89 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 79 RMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMETSM--IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISD 156
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKqvLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 157 LIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVtEELAAATAQVSHLQLKMtahQKKETELQLQLTDNLKEtdllRGHV 236
Cdd:TIGR00618 259 QQLLKQLRARIEELRAQEAVLEETQERINRARKA-APLAAHIKAVTQIEQQA---QRIHTELQSKMRSRAKL----LMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 237 TRLQADLSELREASEQTQTKFKSEKQSRRQLELKVtsleeeltdLRAEKTSLEKNLSERKKKSAQERCQAEaemdEIRKS 316
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT---------SIREISCQQHTLTQHIHTLQQQKTTLT----QKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 317 HQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYRevcaQRDAHQQKLALLQDECLA 396
Cdd:TIGR00618 398 LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEK----LEKIHLQESAQSLKEREQ 473
|
330 340
....*....|....*....|....*....
gi 1720409153 397 LQAQIAAFTEQ-----KEHMQRLEKTKSQ 420
Cdd:TIGR00618 474 QLQTKEQIHLQetrkkAVVLARLLELQEE 502
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
184-330 |
9.49e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 184 ENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQT--QTKFKSEK 261
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409153 262 QSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKK 330
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
495-680 |
1.10e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 495 PLRPSLEQPGPATPGMPPAPPSGETQEAPEvlpeqvvgettPLPLQALPTPENGAQTrkgePAEAEVPSEIKDSSLPPQP 574
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPRPQPPLAPTTDPAGA-----------GEPSGAVPQPWLGALV----PGRVAVPRFRVPQPAPSRE 2987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 575 AGIPA-HRVLGPPTSIPPKPPGPVTMDSESEEMLAADQRTVQPNgllgeEHVREVATDGLLQGNSRRLSL-TPDPEKGEP 652
Cdd:PHA03247 2988 APASStPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPP-----DDTEDSDADSLFDSDSERSDLeALDPLPPEP 3062
|
170 180
....*....|....*....|....*....
gi 1720409153 653 PalDPESQGGEAQPPECKQAEDVSSS-GP 680
Cdd:PHA03247 3063 H--DPFAHEPDPATPEAGARESPSSQfGP 3089
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
135-421 |
1.34e-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: 45.49 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 135 RLKQELLEKSSRIEEQNDKISDL---IERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEE--LAAATAQVSHLQLKMt 209
Cdd:pfam15921 479 KVVEELTAKKMTLESSERTVSDLtasLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhLRNVQTECEALKLQM- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 210 AHQKKETELQLQLTDNLkeTDLLRGH---VTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKT 286
Cdd:pfam15921 558 AEKDKVIEILRQQIENM--TQLVGQHgrtAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKV 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 287 SLEKNLSERKKKSAQERCQAEAEMDEIRKSHQE--ELDRLRQLLKKarvsTDQAAAEQLTLAQAELQSQweakceqlLAS 364
Cdd:pfam15921 636 KLVNAGSERLRAVKDIKQERDQLLNEVKTSRNElnSLSEDYEVLKR----NFRNKSEEMETTTNKLKMQ--------LKS 703
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720409153 365 ARDEhLQQYREVCAQ---RDAHQQKLAL-LQDECLALQAQIAAFTEQkehMQRLEKTKSQA 421
Cdd:pfam15921 704 AQSE-LEQTRNTLKSmegSDGHAMKVAMgMQKQITAKRGQIDALQSK---IQFLEEAMTNA 760
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
127-354 |
1.36e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 127 QRIIQENERLkqelLEKSSRIEEQNDK---ISDLIerNQRYVEQSnlmmEKRNnSLQTATENTQAKVTEELAAATAQVSH 203
Cdd:PRK10929 109 QEILQVSSQL----LEKSRQAQQEQDRareISDSL--SQLPQQQT----EARR-QLNEIERRLQTLGTPNTPLAQAQLTA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 204 LQLKMTAHQKKETELQL-QLTDNLKE------TDLLRGHVTRLQADLSELReaseqTQTKFKSEKQSRRQLElKVTSLEE 276
Cdd:PRK10929 178 LQAESAALKALVDELELaQLSANNRQelarlrSELAKKRSQQLDAYLQALR-----NQLNSQRQREAERALE-STELLAE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 277 ELTDLRAEKTS-LEKN--LSERKKKSAQercqaeaEMDEIrKSHQEeldrlrqllkkarvstdQAAAEQLTLAQA----E 349
Cdd:PRK10929 252 QSGDLPKSIVAqFKINreLSQALNQQAQ-------RMDLI-ASQQR-----------------QAASQTLQVRQAlntlR 306
|
....*
gi 1720409153 350 LQSQW 354
Cdd:PRK10929 307 EQSQW 311
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-419 |
1.50e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 182 ATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTK----- 256
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaell 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 257 ---FKSEKQSRRQLELKVTSLEEELTDLRAektsLEKNLSERKKksaqercqaeaEMDEIRKShQEELDRLRQLLKKARv 333
Cdd:COG4942 111 ralYRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARRE-----------QAEELRAD-LAELAALRAELEAER- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 334 stdqaaaEQLTLAQAELQSQweakcEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQR 413
Cdd:COG4942 174 -------AELEALLAELEEE-----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....*.
gi 1720409153 414 LEKTKS 419
Cdd:COG4942 242 RTPAAG 247
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
182-367 |
1.53e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 45.23 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 182 ATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEK 261
Cdd:COG5283 32 ALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLSAAQRRLRSSLEQTNRQLERQQQRLARLG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 262 QSRRQLelkvTSLEEELTDLRAEKTSLEkNLSERKKKSAQERCQAEAEMDEIRKSHQ-----EELDRLRQLLKKA----R 332
Cdd:COG5283 112 ARQDRL----KAARARLQRLAGAGAAAA-AIGAALAASVKPAIDFEDAMADVAATVDldkssEQFKALGKQARELsaqtP 186
|
170 180 190
....*....|....*....|....*....|....*
gi 1720409153 333 VSTDQAAAEQLTLAQAELQSQweakceQLLASARD 367
Cdd:COG5283 187 QSADDIAAGQAALAQAGVSAE------DILAFTPT 215
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-332 |
1.75e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 124 SNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSlQTATENTQAKVTEELAAAtaqvsh 203
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLK-KRLTGLTPEKLEKELEEL------ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 204 lqlkmtahQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTkfksekqSRRQLElkvtslEEELTDLRA 283
Cdd:PRK03918 397 --------EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPV-------CGRELT------EEHRKELLE 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1720409153 284 EKTSLEKNLSERKKKSAQERCQAEAEMDEIRK--SHQEELDRLRQLLKKAR 332
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKvlKKESELIKLKELAEQLK 506
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
132-413 |
2.07e-04 |
|
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: 44.63 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 132 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAH 211
Cdd:pfam05667 223 EEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTH 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 212 QKKET---ELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSL 288
Cdd:pfam05667 303 TEKLQftnEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEEL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 289 EKNLsERKKKSAQERCQAEAEMDEirkshqeeldrLRQLLkkarvstdQAAAEQLtlaqAELQSQWEAKCEQLLasardE 368
Cdd:pfam05667 383 EKQY-KVKKKTLDLLPDAEENIAK-----------LQALV--------DASAQRL----VELAGQWEKHRVPLI-----E 433
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720409153 369 HLQQYREVCA-QRDAHQQKLA---LLQDECLalqaQIAAFTEQKEHMQR 413
Cdd:pfam05667 434 EYRALKEAKSnKEDESQRKLEeikELREKIK----EVAEEAKQKEELYK 478
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
212-502 |
2.22e-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: 45.06 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 212 QKKETELQLQLTDNLKETDLLRGHVTRLQadlSELREASEQTqtkfkSEKQSRRQ-LELKVTSLEEELTDL--------- 281
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELS---QELSDASRKI-----GEIEKEIEqLEQEEEKLKERLEELeedlssleq 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 282 -----RAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEqltlAQAELQSqwEA 356
Cdd:TIGR02169 752 eienvKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE----IEQKLNR--LT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 357 KCEQLLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAaftEQKEHMQRLEKTKSqapagraaaDPSEKVKK 436
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE---ELEAALRDLESRLG---------DLKKERDE 893
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409153 437 IMNQVFQSLRGEFELEESYDggtILRTIMHTIKmVTLQLLNHQEEEEEEEEEEEEEKKPLRPSLEQ 502
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIE---KKRKRLSELK-AKLEALEEELSEIEDPKGEDEEIPEEELSLED 955
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
82-285 |
2.66e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.68 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 82 VNKVADKMDHLMTKVEELQKHSSGNSML---LPSMSVTMETSM---IMSNIQRIIQ-ENERLKQELLEKSSRIEEQNDKI 154
Cdd:COG5022 894 ISSLKLVNLELESEIIELKKSLSSDLIEnleFKTELIARLKKLlnnIDLEEGPSIEyVKLPELNKLHEVESKLKETSEEY 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 155 SDLIERNQRYVEQSNLMMEKRNNSLQTATEntQAKVTEELAAATAQVSHLQLKMTAHQK--------KETELQLQLTDNL 226
Cdd:COG5022 974 EDLLKKSTILVREGNKANSELKNFKKELAE--LSKQYGALQESTKQLKELPVEVAELQSaskiisseSTELSILKPLQKL 1051
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409153 227 KETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEK 285
Cdd:COG5022 1052 KGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVK 1110
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
70-298 |
2.95e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 70 EARQHNTEIRMAVNKVADKMDHLMTKVEELQKHSSGNSMLLPSMSVTMetsmiMSNIQRIIQENERLKQELLEKSSRIEE 149
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDEL-----VEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 150 QNDKISDLierNQRYVEQSNLM--------MEKRNNSLQTATEN---TQAKVTEelaaATAQVSHLQLKMTA---HQKKE 215
Cdd:PHA02562 253 PSAALNKL---NTAAAKIKSKIeqfqkvikMYEKGGVCPTCTQQiseGPDRITK----IKDKLKELQHSLEKldtAIDEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 216 TELQLQLTDNLKEtdllrghVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSER 295
Cdd:PHA02562 326 EEIMDEFNEQSKK-------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 1720409153 296 KKK 298
Cdd:PHA02562 399 VKE 401
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
300-448 |
3.12e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 300 AQERCQAEAEMDEIRKS---HQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARD-EHL-QQYR 374
Cdd:COG4913 616 EAELAELEEELAEAEERleaLEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDlAALeEQLE 695
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409153 375 EVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRL--EKTKSQAPAGRAAADP---SEKVKKIMNQVFQSLRGE 448
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleAAEDLARLELRALLEErfaAALGDAVERELRENLEER 774
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
188-420 |
3.34e-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: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 188 AKVTEELAAATAQVSHLQLKmtahqkkETELQLQLtDNLKETdllRGHVTRLQADLSELR--EASEQTQTKFKSEKQsRR 265
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLI-------IDEKRQQL-ERLRRE---REKAERYQALLKEKReyEGYELLKEKEALERQ-KE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 266 QLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTL 345
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 346 A--QAELQSQWEAKCEQLLASARDehLQQYRevcAQRDAHQQKLALLQDECLALQAQI--------AAFTEQKEHMQRLE 415
Cdd:TIGR02169 321 EerLAKLEAEIDKLLAEIEELERE--IEEER---KRRDKLTEEYAELKEELEDLRAELeevdkefaETRDELKDYREKLE 395
|
....*
gi 1720409153 416 KTKSQ 420
Cdd:TIGR02169 396 KLKRE 400
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
126-354 |
3.65e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 126 IQRIIQENERLKQELLEKSSR-IEEQNDKISDLIERNQRYVEQsnlmMEKRNNSLQTATENTQakVTEELAAATAQVSHL 204
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEE----FRQKNGLVDLSEEAKL--LLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 205 QLKMTAHQKKETELQLQLTDNLKETDLLRGH--VTRLQADLSELREASEQTQTKFKS---------------EKQSRRQL 267
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPnhpdvialraqiaalRAQLQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 268 ELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERcQAEAEMDEIrkshQEELDRLRQLLKKArvstdQAAAEQLTLAQ 347
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELP-ELEAELRRL----EREVEVARELYESL-----LQRLEEARLAE 381
|
....*..
gi 1720409153 348 AELQSQW 354
Cdd:COG3206 382 ALTVGNV 388
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
192-432 |
4.50e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 192 EELAAATAQVSHLQLKMTAHQKKETELQLQLtDNLKET-DLLRGHVTR--------LQADLSELREASEQTQTKFKSEKQ 262
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQL-EQAKEGlSALNRLLPRlnlladetLADRVEEIREQLDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 263 SRRQLELkvtsLEEELTDLRAEktsleknlserkkksaqercqaEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAA--- 339
Cdd:PRK04863 916 HGNALAQ----LEPIVSVLQSD----------------------PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrra 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 340 ------AEQLTLAQAELQSQWEAKCEQlLASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFteqkehMQR 413
Cdd:PRK04863 970 hfsyedAAEMLAKNSDLNEKLRQRLEQ-AEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL------KQE 1042
|
250 260
....*....|....*....|..
gi 1720409153 414 LEKTKSQAPAG---RAAADPSE 432
Cdd:PRK04863 1043 LQDLGVPADSGaeeRARARRDE 1064
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
122-295 |
4.74e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 122 IMSNIQRIIQENERLKQELLEKSSRIEEQNDKISDL----------IERNQRYVEQSNLMMEKRNNSLQTATENtqakvt 191
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAkteledlekeIKRLELEIEEVEARIKKYEEQLGNVRNN------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 192 EELAAATAQVSHLQLKMTAHQKKETELQLQLtdnlketdllrghvTRLQADLSELREASEQTQTKFKSEKQsrrQLELKV 271
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERI--------------EELEEELAELEAELAELEAELEEKKA---ELDEEL 151
|
170 180
....*....|....*....|....
gi 1720409153 272 TSLEEELTDLRAEKTSLEKNLSER 295
Cdd:COG1579 152 AELEAELEELEAEREELAAKIPPE 175
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
56-414 |
5.74e-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: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 56 HFQGSGDMMSFLMteaRQHNTEIRMAVNKVADKMDHLmtkvEELQKHSSGNSMLLPSMSvtmetsmiMSNIQRIIQENER 135
Cdd:pfam15921 214 HFRSLGSAISKIL---RELDTEISYLKGRIFPVEDQL----EALKSESQNKIELLLQQH--------QDRIEQLISEHEV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 136 LKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKE 215
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 216 TELQLQLTDNLKETDLLRGHVTRLQADL----SELREASEQTQTKFKSEKQS-------RRQLE---LKVTSLEEELTDL 281
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADLhkreKELSLEKEQNKRLWDRDTGNsitidhlRRELDdrnMEVQRLEALLKAM 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 282 RAE-KTSLEKNLS--ERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQllKKARVSTDQAAAEQLTLAQAELQSQWEAKC 358
Cdd:pfam15921 439 KSEcQGQMERQMAaiQGKNESLEKVSSLTAQLESTKEMLRKVVEELTA--KKMTLESSERTVSDLTASLQEKERAIEATN 516
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409153 359 EQL--LASARDEHLQQYREVCAQRDAHQQklalLQDECLALQAQIAA-------FTEQKEHMQRL 414
Cdd:pfam15921 517 AEItkLRSRVDLKLQELQHLKNEGDHLRN----VQTECEALKLQMAEkdkvieiLRQQIENMTQL 577
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
131-367 |
6.53e-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: 43.24 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 131 QENERLKQELLEKSSRIEEQNDKISDLIERnqryVEQSNLMMEKRNNSLQTATENTQAKVTEElaaaTAQVSHLQLKMTA 210
Cdd:pfam01576 422 SESERQRAELAEKLSKLQSELESVSSLLNE----AEGKNIKLSKDVSSLESQLQDTQELLQEE----TRQKLNLSTRLRQ 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 211 HQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELR----------EASEQTQTKFKSEKQSRRQ-----------LEL 269
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKkkleedagtlEALEEGKKRLQRELEALTQqleekaaaydkLEK 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 270 KVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERcQAEAEMDEIRKSHQEELDRLRQLL--KKARVSTDQAAAEQLTLAQ 347
Cdd:pfam01576 574 TKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFD-QMLAEEKAISARYAEERDRAEAEAreKETRALSLARALEEALEAK 652
|
250 260
....*....|....*....|...
gi 1720409153 348 AELQ---SQWEAKCEQLLASARD 367
Cdd:pfam01576 653 EELErtnKQLRAEMEDLVSSKDD 675
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
132-436 |
8.06e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 132 ENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATEntqAKVTEELAAATAQVSHLQLKMTAH 211
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKADELKKAEE 1556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 212 QKKETELQLQLTDNLKETDllRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKvtslEEELTDLRAEKtsLEKN 291
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEED--KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK----KAEEAKIKAEE--LKKA 1628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 292 LSERKKKSAQERCQAEA--EMDEIRKSHQEELDRLRQLLKKARvsTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEH 369
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAE--EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720409153 370 LQQYREVcAQRDAHQQKLAllqDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAADPSEKVKK 436
Cdd:PTZ00121 1707 LKKKEAE-EKKKAEELKKA---EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
232-399 |
9.45e-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: 43.02 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 232 LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSlEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMD 311
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 312 EIRKshqeeldRLRQLLKKARV-STDQAAAEQLtlaqaELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLALL 390
Cdd:COG3096 589 QLRA-------RIKELAARAPAwLAAQDALERL-----REQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQAL 656
|
....*....
gi 1720409153 391 QDECLALQA 399
Cdd:COG3096 657 ESQIERLSQ 665
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
194-431 |
9.55e-04 |
|
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: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 194 LAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTkfksekqsrrqlelKVTS 273
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA--------------EIDK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 274 LEEELTDLRAEKTSLEKNLSERkKKSAQERCQAEAEMDEI--RKSHQEELDRLrQLLKKArVSTDQAAAEQLTLAQAELQ 351
Cdd:COG3883 70 LQAEIAEAEAEIEERREELGER-ARALYRSGGSVSYLDVLlgSESFSDFLDRL-SALSKI-ADADADLLEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 352 SQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLEKTKSQAPAGRAAAD 429
Cdd:COG3883 147 AKKAELEAKLaeLEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
..
gi 1720409153 430 PS 431
Cdd:COG3883 227 AA 228
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
141-372 |
1.07e-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: 42.44 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 141 LEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQAKvteELAAATAQVSHLQLKmtahqKKETELQL 220
Cdd:pfam09731 201 LAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYK---ELVASERIVFQQELV-----SIFPDIIP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 221 QLT-DNLKETDLLRGHVTRLQADLSELreaSEQTQTKFKSEKQsrrQLELKVTSLEEELTDLRAEktsLEKNLSE-RKKK 298
Cdd:pfam09731 273 VLKeDNLLSNDDLNSLIAHAHREIDQL---SKKLAELKKREEK---HIERALEKQKEELDKLAEE---LSARLEEvRAAD 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409153 299 SAQERCQAEAEMDEIRKSHQEEldrLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQ 372
Cdd:pfam09731 344 EAQLRLEFEREREEIRESYEEK---LRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLK 414
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
126-314 |
1.16e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 126 IQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRN--NSLQTATENTQAKVTEELaaataqvsh 203
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEklESEKKEKESKISDLEDEL--------- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 204 lqLKMTAHQKKEtELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRA 283
Cdd:TIGR04523 548 --NKDDFELKKE-NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
170 180 190
....*....|....*....|....*....|....
gi 1720409153 284 EKTSLE---KNLSERKKKSAQERCQAEAEMDEIR 314
Cdd:TIGR04523 625 ENEKLSsiiKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
192-375 |
1.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 192 EELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTrlqaDLSELREASEQTQtKFKSEKQSRRQLELKV 271
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE----DEEELRAALEQAE-EYQELKEELEELEEQL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 272 TSLEEELTDLRAEKTslEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ 351
Cdd:COG4717 412 EELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
170 180
....*....|....*....|....
gi 1720409153 352 SQWEAKceQLLASARDEHLQQYRE 375
Cdd:COG4717 490 EEWAAL--KLALELLEEAREEYRE 511
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
154-359 |
1.20e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 154 ISDLIERNQRYvEQSNLMMEKrnnsLQTATENTQAKVTEELAAATAQVSHLQLKMtahQKKETELQLQLTDNLKET---D 230
Cdd:pfam01576 189 ISDLEERLKKE-EKGRQELEK----AKRKLEGESTDLQEQIAELQAQIAELRAQL---AKKEEELQAALARLEEETaqkN 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 231 LLRGHVTRLQADLSELREASEQT-QTKFKSEKQSR---RQLELKVTSLEEELTDLRAE---KTSLEKNLSERKKKSAQER 303
Cdd:pfam01576 261 NALKKIRELEAQISELQEDLESErAARNKAEKQRRdlgEELEALKTELEDTLDTTAAQqelRSKREQEVTELKKALEEET 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720409153 304 CQAEAEMDEIRKSHQEELDRLRQLLKKARVS------TDQAAAEQLTLAQAELQSQWEAKCE 359
Cdd:pfam01576 341 RSHEAQLQEMRQKHTQALEELTEQLEQAKRNkanlekAKQALESENAELQAELRTLQQAKQD 402
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
192-415 |
1.21e-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: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 192 EELAAATAQVSHLQLKMTAHQKKETELQLQLtDNLKET-DLLRGHVTRL----QADLSELREASEQTQTKFKSEKQSRRQ 266
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQL-DQLKEQlQLLNKLLPQAnllaDETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 267 LELKVTSLEEELTDLRAEKTS---LEKNLSERKKKSAQERCQAEAeMDEI--RKSH-------------QEELDRLRQLL 328
Cdd:COG3096 915 HGKALAQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFA-LSEVvqRRPHfsyedavgllgenSDLNEKLRARL 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 329 KKArvstdQAAAEQLTLAQAELQSQWeAKCEQLLASARdehlqqyrevcAQRDAHQQKLALLQDECLALQAQIAAFTEQK 408
Cdd:COG3096 994 EQA-----EEARREAREQLRQAQAQY-SQYNQVLASLK-----------SSRDAKQQTLQELEQELEELGVQADAEAEER 1056
|
....*....
gi 1720409153 409 --EHMQRLE 415
Cdd:COG3096 1057 arIRRDELH 1065
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
124-368 |
1.45e-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: 42.13 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 124 SNIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERnqryVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVSh 203
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQEQLPSWQSELEN----LEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 204 lqlKMTAHQKKETELQLQLTDNLketdllrghvtrLQADLSELREASEQTQTKFKSEKQ--SRRQLELK-----VTSLEE 276
Cdd:pfam12128 397 ---DKLAKIREARDRQLAVAEDD------------LQALESELREQLEAGKLEFNEEEYrlKSRLGELKlrlnqATATPE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 277 ELTDLRAEKTSLEknlserKKKSAQERCQAEAEmdeirkSHQEELDRLRQLLKKARVSTDQA--AAEQLTLAQAELQSQW 354
Cdd:pfam12128 462 LLLQLENFDERIE------RAREEQEAANAEVE------RLQSELRQARKRRDQASEALRQAsrRLEERQSALDELELQL 529
|
250
....*....|....
gi 1720409153 355 EAKCEQLLASARDE 368
Cdd:pfam12128 530 FPQAGTLLHFLRKE 543
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
237-496 |
1.47e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 237 TRLQADLSELREASEQTQtKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLseRKKKSAQERCQAEAEMDEIrks 316
Cdd:COG4717 71 KELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLL--QLLPLYQELEALEAELAEL--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 317 hQEELDRLRQllKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDE---HLQQYREVCAQRDAHQQKLALLQDE 393
Cdd:COG4717 145 -PERLEELEE--RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 394 CLALQAQIAAFTEQKEHMQRLE---------------------------------------------------KTKSQAP 422
Cdd:COG4717 222 LEELEEELEQLENELEAAALEErlkearlllliaaallallglggsllsliltiagvlflvlgllallflllaREKASLG 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409153 423 AGRAAADPSEKVKKIMNQVFQSLRGEFELEESYDGGTILRTIMHTIKMVTLQLLNHQEEEEEEEEEEEEEKKPL 496
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
178-356 |
1.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 178 SLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREA-------- 249
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeraral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 250 --------------------------------SEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKK 297
Cdd:COG3883 96 yrsggsvsyldvllgsesfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720409153 298 KSAQERcQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQWEA 356
Cdd:COG3883 176 QQAEQE-ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
230-421 |
1.57e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 230 DLLRGHVTRLQADLSELREASEQTQTKFKSE----KQSRRQLE-----LKVTSLEEELTDLRAEKTSLEKNLSERKKKSA 300
Cdd:PRK04778 201 DQLEEELAALEQIMEEIPELLKELQTELPDQlqelKAGYRELVeegyhLDHLDIEKEIQDLKEQIDENLALLEELDLDEA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 301 QERCQA-EAEMDEI----------RKSHQEELDRLRQLLKKARVSTDQAAAE--------QLTLAQAELQSQWEAKCEQL 361
Cdd:PRK04778 281 EEKNEEiQERIDQLydilerevkaRKYVEKNSDTLPDFLEHAKEQNKELKEEidrvkqsyTLNESELESVRQLEKQLESL 360
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720409153 362 LAsardehlqQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQ----KEHMQRLEKTKSQA 421
Cdd:PRK04778 361 EK--------QYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEqeklSEMLQGLRKDELEA 416
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
210-403 |
1.62e-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: 40.75 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 210 AHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSElreaseqtQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLE 289
Cdd:pfam12795 34 ASKQRAAAYQKALDDAPAELRELRQELAALQAKAEA--------APKEILASLSLEELEQRLLQTSAQLQELQNQLAQLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 290 KNLSERKKKSAQercqAEAEMDEIRKshqeELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQW----EAKCEQLLASA 365
Cdd:pfam12795 106 SQLIELQTRPER----AQQQLSEARQ----RLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKaqidMLEQELLSNNN 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720409153 366 RDEHLQqyrevcAQRDAHQQKLALLQDECLALQAQIAA 403
Cdd:pfam12795 178 RQDLLK------ARRDLLTLRIQRLEQQLQALQELLNE 209
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
150-415 |
1.85e-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: 41.86 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 150 QNDKISDLIERNQRYVeQSNLMM---EKRNNSLQTAT-ENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTD- 224
Cdd:COG3096 254 DRDLFKHLITEATNYV-AADYMRhanERRELSERALElRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAa 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 225 ----NLKETDL-LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSE----- 294
Cdd:COG3096 333 sdhlNLVQTALrQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVqqtra 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 295 -------RKKKSAQERCQ--------AEAEMDEIRKSHQEELDRLRQLlkKARVSTDQAAAEQLTLAQAELQS------- 352
Cdd:COG3096 413 iqyqqavQALEKARALCGlpdltpenAEDYLAAFRAKEQQATEEVLEL--EQKLSVADAARRQFEKAYELVCKiagever 490
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720409153 353 --QWEAKCEQLLASARDEHL--------QQYREvcAQRDAHQQKLA--LLQDECLALQAQIAAFTEQKEHMQRLE 415
Cdd:COG3096 491 sqAWQTARELLRRYRSQQALaqrlqqlrAQLAE--LEQRLRQQQNAerLLEEFCQRIGQQLDAAEELEELLAELE 563
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
136-351 |
2.04e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 136 LKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQtATENTQAKVTEELAAATAQVSHLQLKMTAHQKKE 215
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE-QLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 216 TELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSER 295
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409153 296 KKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQ 351
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
89-413 |
2.08e-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: 41.42 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 89 MDHLMTKVEELQKHSSGNSMLLPSMSVTMetsmimsnIQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQS 168
Cdd:pfam07888 3 LDELVTLEEESHGEEGGTDMLLVVPRAEL--------LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 169 NLMMEKRNNSLQTATENTQAKVTE------ELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKetdLLRGHVTRLQAD 242
Cdd:pfam07888 75 RRELESRVAELKEELRQSREKHEEleekykELSASSEELSEEKDALLAQRAAHEARIRELEEDIK---TLTQRVLERETE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 243 LSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELD 322
Cdd:pfam07888 152 LERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 323 rLRQLLKKARVSTDQAAAEQLTLA----------------QAEL-QSQWEAKCEQLLASARDEHLQQYREVCAQ-RDAHQ 384
Cdd:pfam07888 232 -NEALLEELRSLQERLNASERKVEglgeelssmaaqrdrtQAELhQARLQAAQLTLQLADASLALREGRARWAQeRETLQ 310
|
330 340 350
....*....|....*....|....*....|.
gi 1720409153 385 QKLALLQDECLALQAQIAAFTE--QKEHMQR 413
Cdd:pfam07888 311 QSAEADKDRIEKLSAELQRLEErlQEERMER 341
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
126-290 |
2.12e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 126 IQRIIQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMMEKRNNSLQTATENTQ--AKVTEELAAATAQVSH 203
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 204 LQLKMTAHQKKETELQLQLTDNLKETDLLRghvTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRA 283
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEER---AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....*..
gi 1720409153 284 EKTSLEK 290
Cdd:COG4942 235 EAAAAAE 241
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
173-353 |
2.25e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 173 EKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQ 252
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 253 TQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLE---KNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLK 329
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180
....*....|....*....|....
gi 1720409153 330 KARVSTDQAAAEQLTLAQAELQSQ 353
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRN 195
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
131-417 |
3.01e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 131 QENERLKQELLEKSSRIEEQNDKISDLIERNQRY-VEQSNLMMEKRNNSLQTATENTQAKVtEELAAATAQVSHLQLKMT 209
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLeKLLQLLPLYQELEALEAELAELPERL-EELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 210 AHQKKETELQLQLTDNLKETDL-LRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKT-- 286
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlk 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 287 ----------------------------------------SLEKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDR--- 323
Cdd:COG4717 247 earlllliaaallallglggsllsliltiagvlflvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEElla 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 324 ---------------LRQLLKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQLLASARDE------HLQQYREVCAQRDA 382
Cdd:COG4717 327 alglppdlspeelleLLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElraaleQAEEYQELKEELEE 406
|
330 340 350
....*....|....*....|....*....|....*
gi 1720409153 383 HQQKLALLQDECLALqAQIAAFTEQKEHMQRLEKT 417
Cdd:COG4717 407 LEEQLEELLGELEEL-LEALDEEELEEELEELEEE 440
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
207-352 |
3.09e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 207 KMTAHQKKETELQLQLTDNLKETDLLRGHVTRLQADLSELREASEQtqtkFKSEKQSRRQLELKVTSLEEELTDLRAEKt 286
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN----YEKDKQSLKNLKARLKVLEKELKDLKWEH- 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409153 287 sleKNLSERKKKSAQERCQAEAEMDEIRKSHQEELDRLRQLLKKaRVstdQAAAEQLTLAQAELQS 352
Cdd:pfam13851 109 ---EVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEK-KL---QALGETLEKKEAQLNE 167
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
134-447 |
3.23e-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: 41.09 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 134 ERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQSNLMmEKRNNSLQTATENTQAkvteelAAATAQVSHLQLKMTAHQK 213
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAA-EEEVDSLKSQLADYQQ------ALDVQQTRAIQYQQAVQAL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 214 KETELQLQLTDnlKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQ----LELkVTSLEEELTDLRAEKTSLE 289
Cdd:COG3096 423 EKARALCGLPD--LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQfekaYEL-VCKIAGEVERSQAWQTARE 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 290 KNLSERKKKSAQERCQA-EAEMDEIRK--SHQEELDRLRQLLKKaRVSTDQAAAEQLTLAQAELQSQweakceqllasaR 366
Cdd:COG3096 500 LLRRYRSQQALAQRLQQlRAQLAELEQrlRQQQNAERLLEEFCQ-RIGQQLDAAEELEELLAELEAQ------------L 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 367 DEHLQQYREVCAQRDAHQQKLAllqdeclALQAQIAAFTeqkehmqrlektkSQAPAGRAAADPSEKVKKIMNQVFQSLR 446
Cdd:COG3096 567 EELEEQAAEAVEQRSELRQQLE-------QLRARIKELA-------------ARAPAWLAAQDALERLREQSGEALADSQ 626
|
.
gi 1720409153 447 G 447
Cdd:COG3096 627 E 627
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
240-428 |
4.30e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 240 QADLSELREASEQTQTKFKSEKQSRRQLELKVTSLEEELTDLRAEKTSLEKNLSERKKKSAQERCQAEAEmdEIRKSHQE 319
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAA--AAKAKAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 320 ELDRLRQLLKKARVSTD-QAAAEQLTLAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRDAHQQKLAllqdecLALQ 398
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKkKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA------EAKA 225
|
170 180 190
....*....|....*....|....*....|
gi 1720409153 399 AQIAAFTEQKEHMQRLEKTKSQAPAGRAAA 428
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
507-750 |
5.38e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.54 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 507 TPGMPPAPPSGETQEAP--EVLPEQVVGETTPLPLQALPT--PENGAQTRKGEPAEAEVPSEIKDSSLPPQPAGIPAHRV 582
Cdd:PHA03307 64 RFEPPTGPPPGPGTEAPanESRSTPTWSLSTLAPASPAREgsPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 583 LGPPTSIPPKPPGpvtmdsESEEMLAADQRTVQPNGLL---GEEHVRevatdgllqgnsrrlsltPDPEKGEPPALDPES 659
Cdd:PHA03307 144 PGPPPAASPPAAG------ASPAAVASDAASSRQAALPlssPEETAR------------------APSSPPAEPPPSTPP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 660 QGGEAQPPECKQAEDVSSSGPRETLLDTELASAAAGTSLRHNQDSQHCSLSGDEEdelfkgATLKVPRPTAQPEEEDEDE 739
Cdd:PHA03307 200 AAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENE------CPLPRPAPITLPTRIWEAS 273
|
250
....*....|.
gi 1720409153 740 VSMKGRPPPTP 750
Cdd:PHA03307 274 GWNGPSSRPGP 284
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
264-413 |
5.48e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 264 RRQLELKVTSLEEELTDLRAEKTSLEKnlserkkksAQERCQAEAEMDEIRKSHQE---ELDRLRQLLKKARVSTDQAAA 340
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALED---------AREQIELLEPIRELAERYAAareRLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720409153 341 EQLTLAQAELQSQWEAKCEQL--LASARDEHLQQYREVCAQRDAHQ-QKLAllqdeclALQAQIAAFTEQKEHMQR 413
Cdd:COG4913 291 ELLEAELEELRAELARLEAELerLEARLDALREELDELEAQIRGNGgDRLE-------QLEREIERLERELEERER 359
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
130-399 |
5.55e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 130 IQENERLKQELLEKSSRIEEQNDKISDLIERNQRYVEQsnlmmEKRNNSLQTATENTQAKVTEELAAATAQVSHLQLKMT 209
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-----EDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 210 AHQKKETELQLQltdnlketdllrghvtrlQADLSELREASEQTQTKFKSEKQSRRQLELKVTSLeEELTDLRAEKTSLE 289
Cdd:PRK02224 545 RAAELEAEAEEK------------------REAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 290 KNLSERkkksaQERCQAEAEMDEIRKSHQEEL-DRLRQL---LKKARVSTDQAAAEQLTLAQAELQSQWEAKCEQ---LL 362
Cdd:PRK02224 606 DEIERL-----REKREALAELNDERRERLAEKrERKRELeaeFDEARIEEAREDKERAEEYLEQVEEKLDELREErddLQ 680
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720409153 363 AS-----ARDEHLQQYREVCAQRDAHQQKLALLQDECLALQA 399
Cdd:PRK02224 681 AEigaveNELEELEELRERREALENRVEALEALYDEAEELES 722
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
245-349 |
5.72e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 39.85 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 245 ELREASEQTQTKFKSEKQSRRQLELKVTSLEEELtDLRAEKTSLEKNLSERKKKSAQERC----QAEAEMDEIRKSHQEE 320
Cdd:PRK00106 80 EARKYREEIEQEFKSERQELKQIESRLTERATSL-DRKDENLSSKEKTLESKEQSLTDKSkhidEREEQVEKLEEQKKAE 158
|
90 100
....*....|....*....|....*....
gi 1720409153 321 LDRLRQLlkkarvstDQAAAEQLTLAQAE 349
Cdd:PRK00106 159 LERVAAL--------SQAEAREIILAETE 179
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
213-448 |
6.04e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.06 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 213 KKETELQLQLTDNLKETDLLRGHVtrLQADLSElreaSEQTQTKFKSEKQS--RRQLELKVTSLEEELTDLRAEKTSLE- 289
Cdd:COG5022 823 QKTIKREKKLRETEEVEFSLKAEV--LIQKFGR----SLKAKKRFSLLKKEtiYLQSAQRVELAERQLQELKIDVKSISs 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 290 -KNLSERKKKSAQE-RCQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTLAQAELQSQ---WEAKCEQL--L 362
Cdd:COG5022 897 lKLVNLELESEIIElKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVeskLKETSEEYedL 976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 363 ASARDEHLQQYREVCAQRDAHQQKLALLQDECLALQAQIAAFTEQKEHMQRLE---KTKSQAPAGRAAADPSEKVKKIMN 439
Cdd:COG5022 977 LKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQsasKIISSESTELSILKPLQKLKGLLL 1056
|
....*....
gi 1720409153 440 QVFQSLRGE 448
Cdd:COG5022 1057 LENNQLQAR 1065
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
135-455 |
7.47e-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: 39.95 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 135 RLKQELLEKSsriEEQNDKISDLIERNQryVEQSNLMMEKRNNSLQTATENTQAKVTEELAAATAQVShlqlkmTAHQKK 214
Cdd:TIGR00618 153 EFAQFLKAKS---KEKKELLMNLFPLDQ--YTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPD------TYHERK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 215 ETelqlqLTDNLKETDLLRGHVTRLQADLSELREASEQTQTKFKSEKQSRRQLElKVTSLEEELtdlraEKTSLEKNLSE 294
Cdd:TIGR00618 222 QV-----LEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVL-----EETQERINRAR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 295 RKKKSAQERcQAEAEMDEIRKSHQEELDRLRQLLKKARVSTDQAAAEQLTL-AQAELQSQWEAKCeqllasardEHLQQY 373
Cdd:TIGR00618 291 KAAPLAAHI-KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIeEQRRLLQTLHSQE---------IHIRDA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 374 REVCAQRDAHQQKLALLQDECLALQAQIAAFTEQkehMQRLEKTKSQAPAGRAAADPSEKVKKIMNQVFQSLRGEFELEE 453
Cdd:TIGR00618 361 HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQK---LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQ 437
|
..
gi 1720409153 454 SY 455
Cdd:TIGR00618 438 RY 439
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
302-421 |
9.45e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720409153 302 ERCQAEAEMDEIrKSHQEELDRLRQLLKKARvstdqaaaeqltlAQAELQSQWEAKCEQLLASARDEHLQQYREVCAQRD 381
Cdd:COG4913 219 EEPDTFEAADAL-VEHFDDLERAHEALEDAR-------------EQIELLEPIRELAERYAAARERLAELEYLRAALRLW 284
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1720409153 382 AHQQKLALLQDECLALQAQIAAFTEQKEhmqRLEKTKSQA 421
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELE---RLEARLDAL 321
|
|
| |
