|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-523 |
3.21e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLltetSDLKT 355
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 356 KMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEgagqqvcwASTELDKEKA 435
Cdd:COG1196 317 RLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--------AEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 515
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
....*...
gi 1890346197 516 QATTDLRL 523
Cdd:COG1196 467 ELLEEAAL 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
274-517 |
5.55e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.76 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDL 353
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 354 KTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwASTELDKE 433
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA---EEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 434 KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQG 513
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
....
gi 1890346197 514 LEQA 517
Cdd:COG1196 497 LEAE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-517 |
9.96e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 9.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKT 355
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 356 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwasteLDKEKA 435
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-------LEELEE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 515
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
..
gi 1890346197 516 QA 517
Cdd:COG1196 488 EA 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-522 |
4.72e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 4.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQQLLTETSDLKT 355
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----LEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 356 KMATLERELKQQRESTQAVEAKAQQLQEEgerRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKA 435
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 515
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
....*..
gi 1890346197 516 QATTDLR 522
Cdd:COG1196 453 ELEEEEE 459
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
277-522 |
7.64e-14 |
|
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: 75.48 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQagklEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTK 356
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKE----LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 357 MATLERELKQQRESTQAVEAKAQQLQeegERRAAAERQVQQLEEQVQQLEAQVQLLvgrlegagqqvcwaSTELDKEKAR 436
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELE---AQIEQLKEELKALREALDELRAELTLL--------------NEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 437 VDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS---EREQGQCQLRAQQELLQSLQREKQG 513
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSEELRE 905
|
....*....
gi 1890346197 514 LEQATTDLR 522
Cdd:TIGR02168 906 LESKRSELR 914
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-532 |
1.11e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRkdLTRlskhVEALRAQLEeaeGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqCLSEWEH---DKQQLLTETSD 352
Cdd:COG1196 183 ATEEN--LER----LEDILGELE---RQLEPLERQAEKAERYRELKEELKELEAEL---LLLKLREleaELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 353 LKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwASTELDK 432
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE---LEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 433 EKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQEL--------- 503
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELaaqleelee 407
|
250 260 270
....*....|....*....|....*....|
gi 1890346197 504 -LQSLQREKQGLEQATTDLRLTILELEREL 532
Cdd:COG1196 408 aEEALLERLERLEEELEELEEALAELEEEE 437
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-523 |
1.32e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKT 355
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 356 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQqleeqvqqleaqvqllvgRLEGAGQQVcwASTELDKEKA 435
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE------------------RLEEELEEL--EEALAELEEE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 436 RvdsmvrhqESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcQLRAQQELLQSLQREKQGLE 515
Cdd:COG1196 437 E--------EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA-EAAARLLLLLEAEADYEGFL 507
|
....*...
gi 1890346197 516 QATTDLRL 523
Cdd:COG1196 508 EGVKAALL 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
277-517 |
5.05e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQ-------QLLTE 349
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE----ISRLEQQKQilrerlaNLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 350 TSDLKTKMATLERELKQQRESTQAVEAKAQQLQE--EGERRAAAERQVQQLEEQVQQLEAQVQL--LVGRLEGAGQQVCW 425
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEelESLEAELEELEAELEELESRLEELEEQLetLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 426 ASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQER-----EELRGSLDEAEAQRARVEEQLQSEREQ-------- 492
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREEleeaeqal 477
|
250 260 270
....*....|....*....|....*....|
gi 1890346197 493 -----GQCQLRAQQELLQSLQREKQGLEQA 517
Cdd:TIGR02168 478 daaerELAQLQARLDSLERLQENLEGFSEG 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
278-533 |
1.44e-12 |
|
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: 71.63 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQeqgaRRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 358 ATLERELKqqrESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 437
Cdd:TIGR02168 750 AQLSKELT---ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 438 DSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS---EREQGQCQLRAQQELLQSLQREKQGL 514
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSEELREL 906
|
250
....*....|....*....
gi 1890346197 515 EQATTDLRLTILELERELE 533
Cdd:TIGR02168 907 ESKRSELRRELEELREKLA 925
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-520 |
9.94e-12 |
|
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: 68.93 E-value: 9.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRKDLTRLSKHVE------ALRAQLEEAEGQKDGLRKQA--GKLEQALKQEQGARRRQAEEDEQcLSEWEHDKQQLL 347
Cdd:TIGR02168 195 LNELERQLKSLERQAEkaerykELKAELRELELALLVLRLEElrEELEELQEELKEAEEELEELTAE-LQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 348 TETSDLKTKMATLERELKqqrESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAS 427
Cdd:TIGR02168 274 LEVSELEEEIEELQKELY---ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 428 TELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE---EQLQSEREQGQCQLRAQQELL 504
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarlERLEDRRERLQQEIEELLKKL 430
|
250
....*....|....*.
gi 1890346197 505 QSLQREKQGLEQATTD 520
Cdd:TIGR02168 431 EEAELKELQAELEELE 446
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
292-517 |
4.53e-11 |
|
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: 65.17 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 292 ALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQQLLTETSDLKTKMATLERELKQQREST 371
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 372 QAVEAKAQQLQEE-GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwastelDKEKARVDSMVRHQESLQAK 450
Cdd:COG4942 93 AELRAELEAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-------PARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 451 QRALLKQLDSLD---QEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLEQA 517
Cdd:COG4942 166 RAELEAERAELEallAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
284-525 |
9.67e-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: 65.47 E-value: 9.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 284 TRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWE---HDKQQLLTETSDLKTKMATL 360
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 361 ERELKQQRESTQAVEAKAQQLQEE-GERRAAAE----RQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKA 435
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDlHKLEEALNdleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 436 RVDSMVRHqesLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE----------EQLQSEREQGQCQLRAQQELLQ 505
Cdd:TIGR02169 830 YLEKEIQE---LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaalrdlesrlGDLKKERDELEAQLRELERKIE 906
|
250 260
....*....|....*....|
gi 1890346197 506 SLQREKQGLEQATTDLRLTI 525
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKL 926
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
280-530 |
1.08e-10 |
|
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: 65.47 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 280 RKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLE--QALKqeqgARRRQAEEDEQcLSEW---EHDKQQLLTETSDLK 354
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALL----KEKREYEGYEL-LKEKealERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 355 TKMATLERELKQQRESTQAVEAKAQQLQEE-----GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTE 429
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 430 LDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDE--AEAQRARVE--------EQLQSEREQGQCQLRA 499
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdKEFAETRDElkdyreklEKLKREINELKRELDR 410
|
250 260 270
....*....|....*....|....*....|.
gi 1890346197 500 QQELLQSLQREKQGLEQATTDLRLTILELER 530
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
276-516 |
2.16e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRKDLTRLSKHVEALRAQ---LEEAEGQKDGLRKQAGKLEQalkQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSD 352
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQielLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 353 LKTKMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwasteldk 432
Cdd:COG4913 307 LEAELERLEARLDALRE--ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL--------- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 433 ekarvdsmVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSereqgqcqlraqqellqsLQREKQ 512
Cdd:COG4913 376 --------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE------------------LEAEIA 429
|
....
gi 1890346197 513 GLEQ 516
Cdd:COG4913 430 SLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
266-522 |
1.09e-09 |
|
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: 60.93 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 266 PLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgaRRRQAEEDEQclsewehdkQQ 345
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA--RRIRALEQEL---------AA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 346 LLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGErraaaerqvqqleeqvqqleaqVQLLVGRlEGAGQqvcw 425
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPP----------------------LALLLSP-EDFLD---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 426 asteldkekarvdsMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE---QLQSEREQGQCQLRAQQE 502
Cdd:COG4942 134 --------------AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAllaELEEERAALEALKAERQK 199
|
250 260
....*....|....*....|
gi 1890346197 503 LLQSLQREKQGLEQATTDLR 522
Cdd:COG4942 200 LLARLEKELAELAAELAELQ 219
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
276-506 |
1.20e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRKDLT-----RLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQC---LSEWEHDKQQLL 347
Cdd:TIGR02169 277 LNKKIKDLGeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELereIEEERKRRDKLT 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 348 TETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE----GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQV 423
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKleklKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 424 cwasTELDKEKARVDSMVRHQE-----------SLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEqlqsereq 492
Cdd:TIGR02169 437 ----NELEEEKEDKALEIKKQEwkleqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE-------- 504
|
250
....*....|....
gi 1890346197 493 GQCQLRAQQELLQS 506
Cdd:TIGR02169 505 RVRGGRAVEEVLKA 518
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
291-514 |
6.90e-09 |
|
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: 58.75 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 291 EALRAQLEEAegqkdglRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKqqlltetSDLKTKMATLERELKQQRES 370
Cdd:pfam07888 30 ELLQNRLEEC-------LQERAELLQAQEAANRQREKEKERYKRDREQWERQR-------RELESRVAELKEELRQSREK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 371 TQAVEAKAQQLQEEGERRAAAERqvqQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRH------- 443
Cdd:pfam07888 96 HEELEEKYKELSASSEELSEEKD---ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeeeae 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 444 QESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE-------------QLQSEREQGQCQLRAQQELLQSLQRE 510
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDtittltqklttahRKEAENEALLEELRSLQERLNASERK 252
|
....
gi 1890346197 511 KQGL 514
Cdd:pfam07888 253 VEGL 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
277-492 |
1.85e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAlkQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLktk 356
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASSDDL--- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 357 mATLERELKQQRESTQAVEAKAQQLQEEgERRAAAERQvqqleeqvqQLEAQVQLLVGRLEGAGQQVC-WASTELDKEKA 435
Cdd:COG4913 688 -AALEEQLEELEAELEELEEELDELKGE-IGRLEKELE---------QAEEELDELQDRLEAAEDLARlELRALLEERFA 756
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1890346197 436 rvdsmvrhqeslQAKQRALLKQLdsldqeREELRGSLDEAEAQRARVEEQLQSEREQ 492
Cdd:COG4913 757 ------------AALGDAVEREL------RENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
253-475 |
2.39e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 253 QFQQLVQDSMGLRPLpAATVGRWAAEQRKDLtrLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRrqaeed 332
Cdd:COG4913 263 RYAAARERLAELEYL-RAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEARLDALREELDELEAQIR------ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 333 eqclsewEHDKQQLltetSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAerqvqqleeqvqqLEAQVQLL 412
Cdd:COG4913 334 -------GNGGDRL----EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE-------------FAALRAEA 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890346197 413 VGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEA 475
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
291-514 |
5.26e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 291 EALRAQLEEA-EGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWehdkQQLLTETSDLKTKMATLERELKQQRE 369
Cdd:COG4717 41 AFIRAMLLERlEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 370 STQAVEaKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQllvgRLEGAGQQVCWASTELDKEKARVDSMVRhQESLQA 449
Cdd:COG4717 117 ELEKLE-KLLQLLPLYQELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLE-QLSLAT 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890346197 450 KQRA--LLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcqlraQQELLQSLQREKQGL 514
Cdd:COG4717 191 EEELqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE-----AAALEERLKEARLLL 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
275-615 |
8.64e-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: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 275 WAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ---EQGARRRQAEEDEQCLSEWEHDKQQLLTETS 351
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsesENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 352 DLKTKMATLERELKQQRESTQAVEAKAQQLQEEGErraaaerqvqqleeqvqqleaqvqllvgrlegagqqvcwastELD 431
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE------------------------------------------LLE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 432 KEKARVDSMVRHQES----LQAKQRALLKQLDSLDQEREELRGSLDEAEAQRarveEQLQSEREQGQCQLRAQQELLQSL 507
Cdd:TIGR04523 426 KEIERLKETIIKNNSeikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI----NKIKQNLEQKQKELKSKEKELKKL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 508 QREKQGLEQATTDLRLTILELERELEELKERERLLvafpdlhrptETQIhggrsSSVESQITcPTDSGNVTDHMERQVQS 587
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK----------ESKI-----SDLEDELN-KDDFELKKENLEKEIDE 565
|
330 340
....*....|....*....|....*...
gi 1890346197 588 NDIRIRVLQEENGRLQSMLSKIREVAQQ 615
Cdd:TIGR04523 566 KNKEIEELKQTQKSLKKKQEEKQELIDQ 593
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
276-510 |
1.51e-07 |
|
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: 55.34 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALK-------QEQGARRRQAEEDEQC---------LSEW 339
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiQYQQAVQALEKARALCglpdltpenAEDY 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 340 EH---DKQQLLTETS-DLKTKMATLERELKQQRESTQAVEAKAqqlqEEGERRAAAERqvqqlEEQVQQLEAQVQLLVGR 415
Cdd:COG3096 443 LAafrAKEQQATEEVlELEQKLSVADAARRQFEKAYELVCKIA----GEVERSQAWQT-----ARELLRRYRSQQALAQR 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 416 LEGAGQQVcwasTELDKEKARvdsmvrhQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQgQC 495
Cdd:COG3096 514 LQQLRAQL----AELEQRLRQ-------QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ-RS 581
|
250
....*....|....*
gi 1890346197 496 QLRAQQELLQSLQRE 510
Cdd:COG3096 582 ELRQQLEQLRARIKE 596
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
342-532 |
2.17e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 342 DKQQLLTETSDLKTKMATLER------ELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLeaQVQLLVGR 415
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealeDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR--RLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 416 LEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRAL-LKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS------ 488
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAAlglplp 376
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1890346197 489 -EREQGQCQLRAQQELLQSLQREKQGLEQATTDLRLTILELEREL 532
Cdd:COG4913 377 aSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
278-522 |
3.06e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQC-------LSEWEHDKQQLLTET 350
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELeelleqlSLATEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 351 SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAER-------------------QVQQLEEQVQQLEAQVQL 411
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallgLGGSLLSLILTIAGVLFL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 412 LVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLD-SLDQEREELR------GSLDEAEAQRARVEE 484
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLelldriEELQELLREAEELEE 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1890346197 485 QLQSEREQGQCQ-------------LRAQQELLQSLQREKQGLEQATTDLR 522
Cdd:COG4717 362 ELQLEELEQEIAallaeagvedeeeLRAALEQAEEYQELKEELEELEEQLE 412
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
355-523 |
3.54e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 355 TKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQL--LVGRLEGAGQQVCWASTELDK 432
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 433 EKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQ 512
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170
....*....|.
gi 1890346197 513 GLEQATTDLRL 523
Cdd:COG4717 231 QLENELEAAAL 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-525 |
4.80e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 339 WEHDKQQLLTET----SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEG----ERRAAAERQVQQLEEQVQQLEAQVQ 410
Cdd:COG4913 590 HEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELdalqERREALQRLAEYSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 411 L-----LVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAE-----AQRA 480
Cdd:COG4913 670 IaeleaELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdlarlELRA 749
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1890346197 481 RVEEQLQSEREQGQcQLRAQQELLQSLQREKQGLEQATTDLRLTI 525
Cdd:COG4913 750 LLEERFAAALGDAV-ERELRENLEERIDALRARLNRAEEELERAM 793
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
277-522 |
5.84e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDLTRLskhVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSewehdkqqlltETSDLKTK 356
Cdd:PRK02224 515 EERREDLEEL---IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE-----------EVAELNSK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 357 MATLERE---LKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAgqqvcwASTELDKE 433
Cdd:PRK02224 581 LAELKERiesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA------RIEEARED 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 434 KARVDSmvrHQESLQAKqrallkqLDSLDQEREELRGSLDEAEAQRARVEEqLQSEREqgqcQLRAQQELLQSLQREKQG 513
Cdd:PRK02224 655 KERAEE---YLEQVEEK-------LDELREERDDLQAEIGAVENELEELEE-LRERRE----ALENRVEALEALYDEAEE 719
|
....*....
gi 1890346197 514 LEQATTDLR 522
Cdd:PRK02224 720 LESMYGDLR 728
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
277-625 |
7.32e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDLTRlsKHVEALRAQLEEAEGQKDGLRKQAgklEQALKqeqgARRRQAEEDEqclseweHDKQQLLTETSDLKTK 356
Cdd:TIGR02168 177 TERKLERTR--ENLDRLEDILNELERQLKSLERQA---EKAER----YKELKAELRE-------LELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 357 MATLERELKQQRESTQAVEAKAQQLQEEGE--RRAAAERQvqqleeqvqqleAQVQLLVGRLEGAGQqvcwasteldkEK 434
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEelRLEVSELE------------EEIEELQKELYALAN-----------EI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 435 ARVDSMVRHQeslQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQgqcqLRAQQELLQSLQREKQGL 514
Cdd:TIGR02168 298 SRLEQQKQIL---RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE----LESLEAELEELEAELEEL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 515 EQATTDLrltilelereleelkererllvafpdlhrptETQIHGGRSSSVEsqitcptdsgnvtdhMERQVQSNDIRIRV 594
Cdd:TIGR02168 371 ESRLEEL-------------------------------EEQLETLRSKVAQ---------------LELQIASLNNEIER 404
|
330 340 350
....*....|....*....|....*....|.
gi 1890346197 595 LQEENGRLQSMLSKIREVAQQGGLKLIPQDR 625
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-519 |
3.00e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 310 QAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE-GERR 388
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 389 AAAERQVQQLEEQVQQLEAQ-VQLLVGRLEGagqqvcwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREE 467
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSEsFSDFLDRLSA-------LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1890346197 468 LRGSLDEAEAQRARVEEQLQSEREqgqcQLRAQQELLQSLQREKQGLEQATT 519
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSA----EEAAAEAQLAELEAELAAAEAAAA 213
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
277-523 |
4.45e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQclsewehdkQQLLTETSDLKTK 356
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQL---------AEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 357 MATLERELKQQRESTQAVEAkAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwasteLDKEKAR 436
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ-------LQQEAQR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 437 VDSMVRHQ-ESLQAKQRALLKQLDSLDQEREElrgsLDEAEAQRARVEEQLQSEREQgqcqlraQQELLQSLQREKQGLE 515
Cdd:COG3206 314 ILASLEAElEALQAREASLQAQLAQLEARLAE----LPELEAELRRLEREVEVAREL-------YESLLQRLEEARLAEA 382
|
....*...
gi 1890346197 516 QATTDLRL 523
Cdd:COG3206 383 LTVGNVRV 390
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
278-516 |
7.78e-06 |
|
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: 49.58 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 278 EQRKDLTRLSKHVEALRAQLEEAEGQkdgLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQlltETSDLKTKM 357
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAY---LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ---ERINRARKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 358 ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVG------RLEGAGQQVCWASTELD 431
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsqeiHIRDAHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 432 KEKARVDSMVRHQESLQA-------------KQRALLKQLDSLDQEREELRGSLDEAEA----QRARVEEQLQSEREQGQ 494
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTltqklqslckeldILQREQATIDTRTSAFRDLQGQLAHAKKqqelQQRYAELCAAAITCTAQ 452
|
250 260
....*....|....*....|....*
gi 1890346197 495 CQL---RAQQELLQSLQREKQGLEQ 516
Cdd:TIGR00618 453 CEKlekIHLQESAQSLKEREQQLQT 477
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
344-517 |
8.46e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 344 QQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERraaaerqvqqleeqvqqLEAQVQLLVGRLEGAGQQV 423
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-----------------LEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 424 CWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQ-GQCQLRAQQE 502
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElAALEQELQAL 176
|
170
....*....|....*
gi 1890346197 503 LLQSLQREKQGLEQA 517
Cdd:COG4372 177 SEAEAEQALDELLKE 191
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
281-474 |
1.14e-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: 47.23 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 281 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEqgarRRQAEEDEQCLSEWEHDK--QQLLTETSDLKTKMA 358
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQLGNVRNNKeyEALQKEIESLKRRIS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 359 TLERELKQQREstqAVEAKAQQLQEEGERRAAAErqvqqleeqvqqleaqvqllvgrlegagqqvcwasTELDKEKARVD 438
Cdd:COG1579 107 DLEDEILELME---RIEELEEELAELEAELAELE-----------------------------------AELEEKKAELD 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 1890346197 439 smvrhqeslqAKQRALLKQLDSLDQEREELRGSLDE 474
Cdd:COG1579 149 ----------EELAELEAELEELEAEREELAAKIPP 174
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
269-524 |
1.22e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 48.84 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSewehDKQQLLT 348
Cdd:COG5281 173 AAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAAS----AAAQALA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 349 ETSDLKTKMATLERELKQQRESTQAVEAKAQQL--QEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwA 426
Cdd:COG5281 249 ALAAAAAAAALALAAAAELALTAQAEAAAAAAAaaAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALR--A 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 427 STELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQS 506
Cdd:COG5281 327 AAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWAAGAKAALAEYADSATNVAAQVAQA 406
|
250
....*....|....*...
gi 1890346197 507 LQREKQGLEQATTDLRLT 524
Cdd:COG5281 407 ATSAFSGLTDALAGAVTT 424
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
277-520 |
1.29e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDLTRLSKHVEALRA-QLEEAEGQK--DGLRK--------QAGKLEQALKQEQ--GARRRQAEEDEQCLSEWEHDK 343
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKAdEAKKAEEKKkaDELKKaeelkkaeEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEV 1597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 344 QQLLTETSDLKTKmatlerELKQQREStqavEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEaQVQllvgrlegAGQQV 423
Cdd:PTZ00121 1598 MKLYEEEKKMKAE------EAKKAEEA----KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE-ELK--------KAEEE 1658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 424 CWASTELDKEKARVDSmvRHQESLQAKQRALLKQLDSLDQEREELRGS--LDEAEAQRARVEEQLQSEREQGQCQLraqQ 501
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAEELKKAEEENKIKA---E 1733
|
250
....*....|....*....
gi 1890346197 502 ELLQSLQREKQGLEQATTD 520
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKD 1752
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
269-505 |
1.50e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 269 AATVGRWAAEQRKD-LTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLL 347
Cdd:PTZ00121 1344 AAEAAKAEAEAAADeAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 348 TETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwaS 427
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK----A 1499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 428 TELDK---EKARVDSMVRHQESLQAKQRALLKQLDSLDQER--------EELRGSLDEAEAQRARVEEQLQSEREQGQCQ 496
Cdd:PTZ00121 1500 DEAKKaaeAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaeekkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
....*....
gi 1890346197 497 LRAQQELLQ 505
Cdd:PTZ00121 1580 LRKAEEAKK 1588
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
252-517 |
1.58e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 252 GQFQQLVQ------DSMGLRPLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAegqkDGLRKQAGKLEQALKQEQGAR 325
Cdd:COG3096 413 IQYQQAVQalekarALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVA----DAARRQFEKAYELVCKIAGEV 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 326 RRQA--EEDEQCLSEWEhDKQQLLTETSDLKTKMATLERELKQQREstqaveakAQQLQEEGERRAAAERqvqqleeqvq 403
Cdd:COG3096 489 ERSQawQTARELLRRYR-SQQALAQRLQQLRAQLAELEQRLRQQQN--------AERLLEEFCQRIGQQL---------- 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 404 QLEAQVQLLVGRLEgagQQVCWASTELDKEKARVDSMVRHQESLQAKQRAL-------LKQLDSLDQEREELRGSLDEAE 476
Cdd:COG3096 550 DAAEELEELLAELE---AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawLAAQDALERLREQSGEALADSQ 626
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1890346197 477 AQRARVEEQLQSERE--QGQCQLRAQQellQSLQREKQGLEQA 517
Cdd:COG3096 627 EVTAAMQQLLEREREatVERDELAARK---QALESQIERLSQP 666
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
274-392 |
1.61e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRK-----QAGKLEQALKQEQGARR----RQAEEDEQCLSEWEHDKQ 344
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKaeeenKIKAAEEAKKAEEDKKKaeeaKKAEEDEKKAAEALKKEA 1698
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1890346197 345 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQ--EEGERRAAAE 392
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKkeAEEDKKKAEE 1748
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
276-490 |
1.61e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALkqeqgARRRQAEEDEQCLSEWEHDKQQLltetSDLKT 355
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERL----EELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 356 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERqvqqleeqvqqleaqvqllvgrlegagqqvcwasteldkekA 435
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATE-----------------------------------------E 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1890346197 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLD--EAEAQRARVEEQLQSER 490
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEAR 249
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
267-516 |
1.79e-05 |
|
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: 48.30 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 267 LPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR--RQAEEDeqcLSEWEHDKQ 344
Cdd:pfam12128 587 LKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTalKNARLD---LRRLFDEKQ 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 345 QLltetSDLKTKmaTLERELKQQRESTQAVEAKAQQLqeEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVc 424
Cdd:pfam12128 664 SE----KDKKNK--ALAERKDSANERLNSLEAQLKQL--DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL- 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 425 waSTELDKEKARVDsmvRHQESLQAKQRALLKQLD-------SLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQL 497
Cdd:pfam12128 735 --KAAIAARRSGAK---AELKALETWYKRDLASLGvdpdviaKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRR 809
|
250
....*....|....*....
gi 1890346197 498 RAQQELLQSLQREKQGLEQ 516
Cdd:pfam12128 810 PRLATQLSNIERAISELQQ 828
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
278-486 |
2.65e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEqALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKm 357
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 358 atlERELKQQRESTQAVEAKAQQ---LQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAS---TELD 431
Cdd:PRK03918 275 ---IEELEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELE 351
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 432 KEKARVDSMVRHQESLqakqRALLKQLDSLDQER-----EELRGSLDEAEAQRARVEEQL 486
Cdd:PRK03918 352 KRLEELEERHELYEEA----KAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEI 407
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
269-506 |
3.05e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.43 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEgqkDGLRKQAgKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT 348
Cdd:pfam05557 36 ASALKRQLDRESDRNQELQKRIRLLEKREAEAE---EALREQA-ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 349 ETSDLKTKMATLERELKQQRESTQAVEakaQQLQEEGERRAAAERQVQQLEEQVQQLEA---QVQLLVGRLEgagQQVCW 425
Cdd:pfam05557 112 ELSELRRQIQRAELELQSTNSELEELQ---ERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQ---SQEQD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 426 aSTELDKEKARVDSMVRhQESLQAKQRALLKQLDS-------LDQEREELRGSLDEAEAQRARVEEqLQSEREQGQCQLR 498
Cdd:pfam05557 186 -SEIVKNSKSELARIPE-LEKELERLREHNKHLNEnienkllLKEEVEDLKRKLEREEKYREEAAT-LELEKEKLEQELQ 262
|
....*...
gi 1890346197 499 AQQELLQS 506
Cdd:pfam05557 263 SWVKLAQD 270
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
247-517 |
3.65e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 247 LPSSLGQFQQLVQDSMGLRPLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR 326
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 327 RQAEEDEQCLSEWEHDKQQLLTETSDLKT-KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAaERQVQQLEEQVQQL 405
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTlTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-QAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 406 EAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQ---ESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARV 482
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEaenEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1890346197 483 EEQL-QSEREQGQCQLRAQQELLQ------SLQREKQGLEQA 517
Cdd:pfam07888 271 QAELhQARLQAAQLTLQLADASLAlregraRWAQERETLQQS 312
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
277-522 |
4.10e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ------EQGARRRQAEEDEQCLSEWEHD-------- 342
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREleerieELKKEIEELEEKVKELKELKEKaeeyikls 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 343 --KQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEaQVQLLVGRLEGAG 420
Cdd:PRK03918 300 efYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 421 QQVcwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRAR--VEEQLQSEREQGQCqLR 498
Cdd:PRK03918 379 KRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKEL-LE 455
|
250 260
....*....|....*....|....
gi 1890346197 499 AQQELLQSLQREKQGLEQATTDLR 522
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLR 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
432-532 |
4.77e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 432 KEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE---EQLQSEREQGQCQLRAQQELLQSLQ 508
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100
....*....|....*....|....
gi 1890346197 509 REKQGLEQATTDLRLTILELEREL 532
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDL 774
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
278-515 |
4.98e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQA--------------EEDEQCLSEWEHDK 343
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEelerlkkrltgltpEKLEKELEELEKAK 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 344 QQLLTETSDLKTKMATLERELKQQRESTQAVE-AKA------QQLQEEGERRAAAErqvqqleeqvqqLEAQVQLLVGRL 416
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKkAKGkcpvcgRELTEEHRKELLEE------------YTAELKRIEKEL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 417 EGAGQQVcwasTELDKEKARVDsMVRHQESLQAKQRALLKQLDSLD---------------QEREELRGSLDEAEAQRAR 481
Cdd:PRK03918 469 KEIEEKE----RKLRKELRELE-KVLKKESELIKLKELAEQLKELEeklkkynleelekkaEEYEKLKEKLIKLKGEIKS 543
|
250 260 270
....*....|....*....|....*....|....
gi 1890346197 482 VEEQLQSEREQgQCQLRAQQELLQSLQREKQGLE 515
Cdd:PRK03918 544 LKKELEKLEEL-KKKLAELEKKLDELEEELAELL 576
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
269-524 |
5.33e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLE---QALKQEQGARRRQAEEDEQCLSEWEHD--- 342
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEdflEELREERDELREREAELEATLRTARERvee 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 343 KQQLLTE------------------TSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERqvqqleeQVQQ 404
Cdd:PRK02224 445 AEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIER-------LEER 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 405 LEAQVQLLVGRLEGAGQQVCWAStELDKEKARVDSMVRHQESLQAKQR-----------ALLKQLDSLDQEREEL---RG 470
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAE-ELRERAAELEAEAEEKREAAAEAEeeaeeareevaELNSKLAELKERIESLeriRT 596
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1890346197 471 SLDEAEAQRARVEEqLQSEREQGQCQLRAQQELLQSLQREKQGLEQATTDLRLT 524
Cdd:PRK02224 597 LLAAIADAEDEIER-LREKREALAELNDERRERLAEKRERKRELEAEFDEARIE 649
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
288-504 |
6.19e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 288 KHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ-----EQGARRRQAEEDEqcLSEWEHDKQQLLTETSDLKTKMATLER 362
Cdd:pfam00038 54 KEIEDLRRQLDTLTVERARLQLELDNLRLAAEDfrqkyEDELNLRTSAEND--LVGLRKDLDEATLARVDLEAKIESLKE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 363 EL---------------KQQRESTQAVEAKAQQLQEEG----ERRAA----AERQVQQLEEQVQQLEAQVQLLVGRlegA 419
Cdd:pfam00038 132 ELaflkknheeevrelqAQVSDTQVNVEMDAARKLDLTsalaEIRAQyeeiAAKNREEAEEWYQSKLEELQQAAAR---N 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 420 GQQVCWASTELdkekarvdSMVRHQ-ESLQAKQRALLKQLDSLDQEREEL--RGSLDEAEAQR--ARVEEQLQSEREQGQ 494
Cdd:pfam00038 209 GDALRSAKEEI--------TELRRTiQSLEIELQSLKKQKASLERQLAETeeRYELQLADYQEliSELEAELQETRQEMA 280
|
250
....*....|
gi 1890346197 495 CQLRAQQELL 504
Cdd:pfam00038 281 RQLREYQELL 290
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
274-517 |
8.05e-05 |
|
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: 46.32 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALkqeqgarrrqaeedeqclseweHDKQQLLTETSDL 353
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL----------------------QDTQELLQEETRQ 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 354 KTKMATLERELKQQRESTQaveakaQQLQEEGERRAAAERqvqqleeqvqqleaqvqllvgrlegagqQVCWASTELDKE 433
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQ------EQLEEEEEAKRNVER----------------------------QLSTLQAQLSDM 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 434 KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARveeqLQSEREQGQCQLRAQQELLQSLQREKQG 513
Cdd:pfam01576 530 KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR----LQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
....
gi 1890346197 514 LEQA 517
Cdd:pfam01576 606 FDQM 609
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
277-522 |
8.31e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDLTRLSKHVEALRAQ--------------LEEAEGQKDGLRKQAGKLEQALKQEQGARRR--------------- 327
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERfgdapvdlgnaedfLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgq 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 328 ---------QAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLE---------RELKQQRE-STQAVEAKAQQLQEEGERR 388
Cdd:PRK02224 460 pvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlveaedriERLEERREdLEELIAERRETIEEKRERA 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 389 AAAERQVQQLEEQVQQLEAQVQllvgRLEGAGQQVCWASTELDKEKARVDSMVrhqESLqAKQRALLKQLDSLDQEREEL 468
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAA----EAEEEAEEAREEVAELNSKLAELKERI---ESL-ERIRTLLAAIADAEDEIERL 611
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890346197 469 ---RGSLDEAEAQRarvEEQLQSEREQGQcQLRAQ------QELLQSLQREKQGLEQATTDLR 522
Cdd:PRK02224 612 rekREALAELNDER---RERLAEKRERKR-ELEAEfdeariEEAREDKERAEEYLEQVEEKLD 670
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
269-510 |
9.17e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT 348
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 349 EtsDLKTKMATLERELKQqrESTQAVEAKAQQLQeegERRAAAERqvqqleeqvqqleaqVQLLVGRLEGAGQQVCWAST 428
Cdd:COG4717 366 E--ELEQEIAALLAEAGV--EDEEELRAALEQAE---EYQELKEE---------------LEELEEQLEELLGELEELLE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 429 ELDKE--KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELR--GSLDEAEAQRARVEEQLQSEREQGQcQLRAQQELL 504
Cdd:COG4717 424 ALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWA-ALKLALELL 502
|
....*.
gi 1890346197 505 QSLQRE 510
Cdd:COG4717 503 EEAREE 508
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
282-387 |
1.01e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.82 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 282 DLTRLSKHVEALRAQLEEAEGQKDGLRKQAgkleQALKQEQGarrrQAEEDEQCLSE----WEHDKQQLLTETSDLKTKM 357
Cdd:pfam05911 703 ELASCTENLESTKSQLQESEQLIAELRSEL----ASLKESNS----LAETQLKCMAEsyedLETRLTELEAELNELRQKF 774
|
90 100 110
....*....|....*....|....*....|
gi 1890346197 358 ATLERELKQQRESTQAVEAKAQQLQEEGER 387
Cdd:pfam05911 775 EALEVELEEEKNCHEELEAKCLELQEQLER 804
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
326-503 |
1.01e-04 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 44.27 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 326 RRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMAtlERELKQQRESTQAVEAKAQQLQEegERRAAAERqvqqleeqvQQL 405
Cdd:pfam15665 52 KRRIQTLEESLEQHERMKRQALTEFEQYKRRVE--ERELKAEAEHRQRVVELSREVEE--AKRAFEEK---------LES 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 406 EAQVQllvgrlegagqqvcwASTELDKEKARVDSMVRHQ---ESLQAKQRAL--------LKQLDSLDQEREELRGSLDE 474
Cdd:pfam15665 119 FEQLQ---------------AQFEQEKRKALEELRAKHRqeiQELLTTQRAQsasslaeqEKLEELHKAELESLRKEVED 183
|
170 180
....*....|....*....|....*....
gi 1890346197 475 AEAQRARVEEqlQSEREQGQCQLRAQQEL 503
Cdd:pfam15665 184 LRKEKKKLAE--EYEQKLSKAQAFYEREL 210
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
343-521 |
1.01e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 343 KQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleEQVQQLEAQVQLLVGRLEGAGQQ 422
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK---------------NGLVDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 423 VCWASTELDKEKARVDSMVRHQESLQAKQ---------RALLKQLDSLDQEREELRGSLDE-------AEAQRARVEEQL 486
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQL 307
|
170 180 190
....*....|....*....|....*....|....*....
gi 1890346197 487 QSEREQGQCQLRAQQELLQ----SLQREKQGLEQATTDL 521
Cdd:COG3206 308 QQEAQRILASLEAELEALQareaSLQAQLAQLEARLAEL 346
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
276-516 |
1.06e-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: 45.94 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRK-------QAGKLEQALKQEQGARRRqAEEDEQCLSEwehDKQQLLT 348
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALARLEEETAQKNNALKkireleaQISELQEDLESERAARNK-AEKQRRDLGE---ELEALKT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 349 ETSDLKTKMATlERELKQQRES---------------------------TQAVEAKAQQLQEEGERRAAAERQVQQLEEQ 401
Cdd:pfam01576 307 ELEDTLDTTAA-QQELRSKREQevtelkkaleeetrsheaqlqemrqkhTQALEELTEQLEQAKRNKANLEKAKQALESE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 402 VQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRAR 481
Cdd:pfam01576 386 NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
250 260 270
....*....|....*....|....*....|....*...
gi 1890346197 482 VEEQLQSEREQGQCQLRAQQEL---LQSLQREKQGLEQ 516
Cdd:pfam01576 466 LESQLQDTQELLQEETRQKLNLstrLRQLEDERNSLQE 503
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
281-525 |
1.49e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 281 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRqaeeDEQCLSEWEHDKQ---QLLTETSDLKTKM 357
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK----LELLLSNLKKKIQknkSLESQISELKKQN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 358 ATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleeqVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 437
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQ-----------------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 438 DSMVRHQESL-QAKQRALLK----QLDSLDQEREELRGSLDEAEAQRARVEEQ----------LQSEREQGQCQLRAQQE 502
Cdd:TIGR04523 291 NQLKSEISDLnNQKEQDWNKelksELKNQEKKLEEIQNQISQNNKIISQLNEQisqlkkeltnSESENSEKQRELEEKQN 370
|
250 260 270
....*....|....*....|....*....|
gi 1890346197 503 LLQSLQREKQG-------LEQATTDLRLTI 525
Cdd:TIGR04523 371 EIEKLKKENQSykqeiknLESQINDLESKI 400
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
277-383 |
1.53e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEqclsewehdkqqlltETSDLKTK 356
Cdd:COG2433 409 TEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR---------------EISRLDRE 473
|
90 100
....*....|....*....|....*..
gi 1890346197 357 MATLERELKQQRESTQAVEAKAQQLQE 383
Cdd:COG2433 474 IERLERELEEERERIEELKRKLERLKE 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
277-484 |
2.45e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDL-TRLSKH-VEALRAQLEEAEGQK---DGLRKQAGKLEQALKQEQGARRRQAEEDEQcLSEWEHDKQQLLTETS 351
Cdd:PRK03918 502 AEQLKELeEKLKKYnLEELEKKAEEYEKLKeklIKLKGEIKSLKKELEKLEELKKKLAELEKK-LDELEEELAELLKELE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 352 DLKTK-MATLERELKQ----QRESTQAVEAKaQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQ----- 421
Cdd:PRK03918 581 ELGFEsVEELEERLKElepfYNEYLELKDAE-KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkysee 659
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890346197 422 ---QVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE 484
Cdd:PRK03918 660 eyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
278-520 |
2.57e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAgkleQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEEL----EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 358 ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 437
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 438 DSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLEQA 517
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
...
gi 1890346197 518 TTD 520
Cdd:COG4372 320 ALL 322
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
341-515 |
2.78e-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: 42.99 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 341 HDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAG 420
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 421 QQVcwaSTEldKEkarVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQ 500
Cdd:COG1579 83 GNV---RNN--KE---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170
....*....|....*
gi 1890346197 501 QELLQSLQREKQGLE 515
Cdd:COG1579 155 EAELEELEAEREELA 169
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
270-514 |
2.80e-04 |
|
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: 44.12 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 270 ATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAL----KQEQGARRRQAEEDEQC--LSEWEHDK 343
Cdd:pfam07888 139 KTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslsKEFQELRNSLAQRDTQVlqLQDTITTL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 344 QQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLlvgrlegagqQV 423
Cdd:pfam07888 219 TQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTL----------QL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 424 CWASTELDKEKARvdsMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQL----RA 499
Cdd:pfam07888 289 ADASLALREGRAR---WAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLsesrRE 365
|
250
....*....|....*...
gi 1890346197 500 QQEL---LQSLQREKQGL 514
Cdd:pfam07888 366 LQELkasLRVAQKEKEQL 383
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
630-751 |
2.94e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 630 SSKGTQGATPPVQAKSTSPgPLGRQHLPSSRTGRTLLGQPCTSPPRQPCTSPPRQPCTSPPRQPCTSPSRQPCSQP-SKS 708
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARP-PVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPrPQP 2941
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1890346197 709 LLEGVTHLDTCTQNPIKVLVRLRKRLSPGRGQASSAHQPQERP 751
Cdd:PHA03247 2942 PLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
279-489 |
3.10e-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: 42.99 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 279 QRKD--LTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT-----ETS 351
Cdd:COG1579 13 QELDseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 352 DLKTKMATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleeqvqqleaqvqllvgrlegagqqvcwasteLD 431
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEE---------------------------------------------LA 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1890346197 432 KEKARVDSMVRHQESLQAKqrallkqldsLDQEREELRGSLDEAEAQRARVEEQLQSE 489
Cdd:COG1579 128 ELEAELAELEAELEEKKAE----------LDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
299-512 |
3.99e-04 |
|
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: 43.96 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 299 EAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEA-- 376
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEIsr 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 377 --KAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTE--------LDKEKARVDSMVRHQES 446
Cdd:pfam17380 377 mrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEarqrevrrLEEERAREMERVRLEEQ 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890346197 447 LQAKQRALLKQlDSLDQEREELRGSLDE-----AEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQ 512
Cdd:pfam17380 457 ERQQQVERLRQ-QEEERKRKKLELEKEKrdrkrAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
267-526 |
4.00e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 267 LPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEG--QKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQ 344
Cdd:COG1196 540 LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 345 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVC 424
Cdd:COG1196 620 DTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 425 WASTELDKE-KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEA-----------EAQRARVEEqLQSEREQ 492
Cdd:COG1196 700 LAEEEEERElAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdlEELERELER-LEREIEA 778
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1890346197 493 -GQCQLRAQQEL------LQSLQREKQGLEQATTDLRLTIL 526
Cdd:COG1196 779 lGPVNLLAIEEYeeleerYDFLSEQREDLEEARETLEEAIE 819
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
272-373 |
4.17e-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: 43.21 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 272 VGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETS 351
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
90 100
....*....|....*....|..
gi 1890346197 352 DLKTKMATLERELKQQRESTQA 373
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPA 245
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
285-510 |
5.02e-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: 43.63 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 285 RLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAL----------KQEQGARRRQAEEDEQCLSE-------WEHDKQQLL 347
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELddllvdldhqRQLVSNLEKKQKKFDQMLAEekaisarYAEERDRAE 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 348 TETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAA-----------ERQVQQLEEQVQQLEAQVQLLVGRL 416
Cdd:pfam01576 629 AEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknvhelERSKRALEQQVEEMKTQLEELEDEL 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 417 EGAGQQVCWASTELDKEKARVDSMVRHQESL-QAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS------- 488
Cdd:pfam01576 709 QATEDAKLRLEVNMQALKAQFERDLQARDEQgEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKEleaqida 788
|
250 260
....*....|....*....|....*
gi 1890346197 489 ---EREQGQCQLRAQQELLQSLQRE 510
Cdd:pfam01576 789 ankGREEAVKQLKKLQAQMKDLQRE 813
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
278-525 |
5.05e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 278 EQRKDLTRLS-------KHVEaLRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTET 350
Cdd:TIGR04523 195 KLLKLELLLSnlkkkiqKNKS-LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 351 SDL---KTKMATLERELKQqrestqaVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQL-----LVGRLEgagQQ 422
Cdd:TIGR04523 274 KELeqnNKKIKELEKQLNQ-------LKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIsqnnkIISQLN---EQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 423 VcwasTELDKEKARVDSM-VRHQESLQAKQrallKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcQLraqQ 501
Cdd:TIGR04523 344 I----SQLKKELTNSESEnSEKQRELEEKQ----NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ-QK---D 411
|
250 260
....*....|....*....|....
gi 1890346197 502 ELLQSLQREKQGLEQATTDLRLTI 525
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETI 435
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
445-524 |
5.55e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 445 ESLQAKQRALLKQLDSLDQEREELRgSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQS---------LQREKQGLE 515
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEkaaetsqerKQKRKEITD 223
|
....*....
gi 1890346197 516 QATTDLRLT 524
Cdd:PRK11448 224 QAAKRLELS 232
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
276-519 |
5.58e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.13 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRKDLTRLSKHVEALRAQLEEA-------EGQKDGLRKQAGKLEQALkQEQGARRRQAEEDEQcLSEWEHDKQQLLT 348
Cdd:pfam19220 106 KEELRIELRDKTAQAEALERQLAAEteqnralEEENKALREEAQAAEKAL-QRAEGELATARERLA-LLEQENRRLQALS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 349 E-----TSDLKTKMATLERELKQQRESTQAVEAkaqQLQEEgerRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQV 423
Cdd:pfam19220 184 EeqaaeLAELTRRLAELETQLDATRARLRALEG---QLAAE---QAERERAEAQLEEAVEAHRAERASLRMKLEALTARA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 424 cwASTEldkekaRVDSMVRHQ-ESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQsEREQGQCQLRAQQE 502
Cdd:pfam19220 258 --AATE------QLLAEARNQlRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQ-EMQRARAELEERAE 328
|
250
....*....|....*...
gi 1890346197 503 LL-QSLQREKQGLEQATT 519
Cdd:pfam19220 329 MLtKALAAKDAALERAEE 346
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
277-492 |
6.01e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDLTRLSKHVEALRA-----QLEEAEGQKDGLRKQAGKLE---QALKQEQGAR--RRQAEEDE-----QCLSEWEH 341
Cdd:TIGR02169 768 EELEEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEVSRIEarlREIEQKLNRLtlEKEYLEKEiqelqEQRIDLKE 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 342 DKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQ 421
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 422 QVCWASTELDKEKARVDSMVRHQ---ESLQAKQRALLKQLDSLD-------QEREELRGSLDEAEAQRARVEEqlqsERE 491
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEE----ERK 1003
|
.
gi 1890346197 492 Q 492
Cdd:TIGR02169 1004 A 1004
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
426-524 |
7.24e-04 |
|
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like proteins. TelA and KlA are associated with tellurite resistance and plasmid fertility inhibition.
Pssm-ID: 461748 Cd Length: 330 Bit Score: 42.50 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 426 ASTELDKEKARVDSMVRH----QESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQ-----------RARVEEQLQSER 490
Cdd:pfam05816 79 AGNKIEKYFAKYQTAGAQidkiVVELEKGQDELLKDNAMLDQMYEKNLEYFKELEKYiaagelkleelDAELLPELEAKA 158
|
90 100 110
....*....|....*....|....*....|....*.
gi 1890346197 491 EQGQCQLRAQ--QELLQSLQRekqgLEQATTDLRLT 524
Cdd:pfam05816 159 AASGDPEDAQalRDLRQALFR----LEQRIHDLELQ 190
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
286-522 |
7.37e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 286 LSKHVEALRAQLEEAEGQKDGLRKQAGKLEQaLKQEQGARRrqaeEDEQCLSEWEHDKQQLLTETSDLKTKMATLErELK 365
Cdd:PRK04863 892 LADRVEEIREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQ----SDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVV 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 366 QQR-----ESTQAVEAKAQQLQEegerraaaerqvqqleeqvqqleaqvqLLVGRLEGAGQQVCWASTELDKEKARVDSM 440
Cdd:PRK04863 966 QRRahfsyEDAAEMLAKNSDLNE---------------------------KLRQRLEQAEQERTRAREQLRQAQAQLAQY 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 441 VRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARV-EEQL-------QSEREQGQCQLRAQQELLQSLQREKQ 512
Cdd:PRK04863 1019 NQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARArRDELharlsanRSRRNQLEKQLTFCEAEMDNLTKKLR 1098
|
250
....*....|
gi 1890346197 513 GLEQATTDLR 522
Cdd:PRK04863 1099 KLERDYHEMR 1108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
274-517 |
8.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 274 RWAAEQRKDLTRlSKHVEALR-----AQLEEAEGQKDGLRKQAGKLEQALKQEQgarRRQAEE----DEQCLSEwEHDKQ 344
Cdd:PTZ00121 1230 KKAEEAKKDAEE-AKKAEEERnneeiRKFEEARMAHFARRQAAIKAEEARKADE---LKKAEEkkkaDEAKKAE-EKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 345 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQleeqvqqleaqvqllvgRLEGAGQQVC 424
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-----------------EAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 425 WASTELDKEKARVDSM------VRHQESLQAKQRALLKQLDSLDQEREELRgsldEAEAQRARVEEQLQSEREQGQCQLR 498
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAkkkaeeKKKADEAKKKAEEDKKKADELKKAAAAKK----KADEAKKKAEEKKKADEAKKKAEEA 1443
|
250
....*....|....*....
gi 1890346197 499 AQQELLQSLQREKQGLEQA 517
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEA 1462
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
290-512 |
9.02e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 290 VEALRAQLEEAEGQKDGLRKQAGKLEQalkqeqgaRRRQAEEDeqcLSEWEHDKQQLLTETSDLKTKMATLE-------- 361
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKE--------KRDELNEE---LKELAEKRDELNAQVKELREEAQELRekrdelne 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 362 --RELKQQRESTQaveAKAQQLQEEgerrAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAgQQVcwASTELDKEKARVDS 439
Cdd:COG1340 72 kvKELKEERDELN---EKLNELREE----LDELRKELAELNKAGGSIDKLRKEIERLEWR-QQT--EVLSPEEEKELVEK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 440 MVRHQESLQAKQRA---------LLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcQLRAQQELLQSLQRE 510
Cdd:COG1340 142 IKELEKELEKAKKAlekneklkeLRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD-ELRKEADELHKEIVE 220
|
..
gi 1890346197 511 KQ 512
Cdd:COG1340 221 AQ 222
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
290-517 |
9.19e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 290 VEALRAQLEEAEGQKDGLRKQAGKLEQALK-------QEQGARRRQAEEDEQC-LSEWEHDKQQLLTETSDLKTKMATLE 361
Cdd:PRK04863 378 QEENEARAEAAEEEVDELKSQLADYQQALDvqqtraiQYQQAVQALERAKQLCgLPDLTADNAEDWLEEFQAKEQEATEE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 362 -RELKQQRESTQAVE---AKAQQLQeegeRRAAAERQVQQLEEQVQQLEAQV---QLLVGRLEGAGQQVcwasTELDKEk 434
Cdd:PRK04863 458 lLSLEQKLSVAQAAHsqfEQAYQLV----RKIAGEVSRSEAWDVARELLRRLreqRHLAEQLQQLRMRL----SELEQR- 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 435 arvdsmVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQgQCQLRAQQELLQSLQREKQGL 514
Cdd:PRK04863 529 ------LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER-RMALRQQLEQLQARIQRLAAR 601
|
...
gi 1890346197 515 EQA 517
Cdd:PRK04863 602 APA 604
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
272-525 |
9.84e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 272 VGRWAAEQRKDLTRLSKHVEA-----LRAQLEEAEGQKDGLRKQAGKLEQalKQEQGARRRqaEEDEQCLSEWEHDKQQL 346
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEkeekdLHERLNGLESELAELDEEIERYEE--QREQARETR--DEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 347 LT---ETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE-GERRAAAERQVQQL---EEQVQQLEAQVQLLVGRLEGA 419
Cdd:PRK02224 254 ETleaEIEDLRETIAETEREREELAEEVRDLRERLEELEEErDDLLAEAGLDDADAeavEARREELEDRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 420 GQQVCWASTELDKEKARVDSmvRHQESLQAKQRAllkqlDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQ---GQCQ 496
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADD--LEERAEELREEA-----AELESELEEAREAVEDRREEIEELEEEIEELRERfgdAPVD 406
|
250 260
....*....|....*....|....*....
gi 1890346197 497 LRAQQELLQSLQREKQGLEQATTDLRLTI 525
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATL 435
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
328-517 |
1.04e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 328 QAEED-EQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLE 406
Cdd:PRK03918 186 KRTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 407 AQVQLLVGRLEGAGQQVCwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEqL 486
Cdd:PRK03918 266 ERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE-L 343
|
170 180 190
....*....|....*....|....*....|.
gi 1890346197 487 QSEREQGQCQLRAQQELLQSLQREKQGLEQA 517
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
343-479 |
1.13e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 40.71 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 343 KQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERqvqqleeqvQQLEAQVQLLVGRLEGAgqq 422
Cdd:PRK07352 52 REAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIR---------AEIEKQAIEDMARLKQT--- 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1890346197 423 vcwASTELDKEKARVDSMVRHQESLQAKQRALlkqldsldqerEELRGSLDEAEAQR 479
Cdd:PRK07352 120 ---AAADLSAEQERVIAQLRREAAELAIAKAE-----------SQLPGRLDEDAQQR 162
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
286-384 |
1.42e-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: 40.66 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 286 LSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgarrRQAEEDEQCLSEWEHDKQQLLTetsdLKTKMATLERELK 365
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQ----EEVEELRKQLENYEKDKQSLKN----LKARLKVLEKELK 102
|
90
....*....|....*....
gi 1890346197 366 QQRESTQAVEAKAQQLQEE 384
Cdd:pfam13851 103 DLKWEHEVLEQRFEKVERE 121
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-502 |
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 1890346197 281 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQ---GARRRQAEEDEQCLSEWEhdkqQLL--TETSDLKT 355
Cdd:COG3883 44 AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelGERARALYRSGGSVSYLD----VLLgsESFSDFLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 356 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAErqvqqleeqvQQLEAQVQLLVGRLEgagqqvcwastELDKEKA 435
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKL----------AELEALKAELEAAKA-----------ELEAQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890346197 436 RVDSMVrhqESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQE 502
Cdd:COG3883 179 EQEALL---AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
294-388 |
1.59e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 294 RAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEED---EQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRES 370
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELvalEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220
|
90
....*....|....*...
gi 1890346197 371 TQAVEAKAQQLQEEGERR 388
Cdd:PRK11448 221 ITDQAAKRLELSEEETRI 238
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
290-524 |
2.06e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 290 VEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRE 369
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKE 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 370 STQAVEAKAQQLQE-EGERRAAAE-----RQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRH 443
Cdd:pfam10174 532 ECSKLENQLKKAHNaEEAVRTNPEindriRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLR 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 444 QESLQAKQRALLKQLdsldqEREELRGSLDEAEAQRARVEEqlqSEREQGQCQLraqQELLQSLQREKQGLEQatTDLRL 523
Cdd:pfam10174 612 QMKEQNKKVANIKHG-----QQEMKKKGAQLLEEARRREDN---LADNSQQLQL---EELMGALEKTRQELDA--TKARL 678
|
.
gi 1890346197 524 T 524
Cdd:pfam10174 679 S 679
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
274-523 |
2.18e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgaRRRQAEEDEQCLSEWE------------- 340
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE--NELEAAALEERLKEARlllliaaallall 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 341 --HDKQQLLTET----------------SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQV 402
Cdd:COG4717 263 glGGSLLSLILTiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 403 QQLEAQVQLLVGRLEGAGQQVCWASTELDKE----KARVDS---------MVRHQESLQAKQRALLKQLDSLDQEREEL- 468
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAallaEAGVEDeeelraaleQAEEYQELKEELEELEEQLEELLGELEELl 422
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1890346197 469 -RGSLDEAEAQRARVEEQLQSEREQgqcqlraQQELLQSLQREKQGLEQATTDLRL 523
Cdd:COG4717 423 eALDEEELEEELEELEEELEELEEE-------LEELREELAELEAELEQLEEDGEL 471
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
281-384 |
2.21e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.73 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 281 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKqeqgARRRQAEEDEQCLSEW-EHDKQQLLTETSdlktkmAT 359
Cdd:pfam02841 197 QALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMME----AQERSYQEHVKQLIEKmEAEREQLLAEQE------RM 266
|
90 100
....*....|....*....|....*.
gi 1890346197 360 LERELKQQRE-STQAVEAKAQQLQEE 384
Cdd:pfam02841 267 LEHKLQEQEElLKEGFKTEAESLQKE 292
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
294-509 |
2.36e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 294 RAQLEEAEGQKDGLRKQAGKLEQALKQEQgarRRQAEEdeqclsEWEHDKQQLltetsdlktkmatlERELKQQRESTQA 373
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEA---LLEAKE------EIHKLRNEF--------------EKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 374 VEAKAQQLQEEGERRAAAerqvqqleeqvqqleaqvqllvgrLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRA 453
Cdd:PRK12704 87 LEKRLLQKEENLDRKLEL------------------------LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890346197 454 LLKQLDSLDQE--REELRGSL-DEAEAQRA----RVEEQLQSEREQgqcqlRAQQELLQSLQR 509
Cdd:PRK12704 143 ELERISGLTAEeaKEILLEKVeEEARHEAAvlikEIEEEAKEEADK-----KAKEILAQAIQR 200
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
276-521 |
2.50e-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: 41.31 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 276 AAEQRKDLTRLSKhveALRAQLEEAEGQKDGLRKQAGKLEQ---ALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSD 352
Cdd:pfam01576 648 ALEAKEELERTNK---QLRAEMEDLVSSKDDVGKNVHELERskrALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 353 LKtkmATLERELKQQREstQAVEAKAQ----------QLQEEGERRAAAerqvqqlEEQVQQLEAQVQLLVGRLEGAGQQ 422
Cdd:pfam01576 725 LK---AQFERDLQARDE--QGEEKRRQlvkqvreleaELEDERKQRAQA-------VAAKKKLELDLKELEAQIDAANKG 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 423 VCWASTELDKEKARVDSMVRHQESLQAKQRALL-------KQLDSLdqEREELRGSLDEAEAQRARveEQLQSEREQGQC 495
Cdd:pfam01576 793 REEAVKQLKKLQAQMKDLQRELEEARASRDEILaqskeseKKLKNL--EAELLQLQEDLAASERAR--RQAQQERDELAD 868
|
250 260
....*....|....*....|....*.
gi 1890346197 496 QLRAQQELLQSLQREKQGLEQATTDL 521
Cdd:pfam01576 869 EIASGASGKSALQDEKRRLEARIAQL 894
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
278-517 |
2.97e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 278 EQRKDlTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR----RQAEEDEQC--LSEWEHDKQQLLTETS 351
Cdd:PTZ00121 1082 DAKED-NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaeeaRKAEDARKAeeARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 352 D--LKTKMATLERELKQQRESTQAVEA-KAQQLQE-------EGERRAAAERQVQQLEEQVQQLEAQVqllVGRLEGAGQ 421
Cdd:PTZ00121 1161 EdaRKAEEARKAEDAKKAEAARKAEEVrKAEELRKaedarkaEAARKAEEERKAEEARKAEDAKKAEA---VKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 422 QvcwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQER--EELRGSLDEAEAQRARVEEQLQ--SEREQGQCQL 497
Cdd:PTZ00121 1238 D---AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkaDELKKAEEKKKADEAKKAEEKKkaDEAKKKAEEA 1314
|
250 260
....*....|....*....|
gi 1890346197 498 RAQQELLQSLQREKQGLEQA 517
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAA 1334
|
|
| Cornifin |
pfam02389 |
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ... |
668-702 |
3.23e-03 |
|
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.
Pssm-ID: 280537 [Multi-domain] Cd Length: 135 Bit Score: 38.50 E-value: 3.23e-03
10 20 30
....*....|....*....|....*....|....*
gi 1890346197 668 QPCTSPPRQPCTSPPRQPCTSPPRQPCTSPSRQPC 702
Cdd:pfam02389 7 QPCQPPPQEPCVPTTKEPCHSKVPEPCNPKVPEPC 41
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
262-468 |
3.27e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 262 MGLRPLPAATVGRWAAEQRKDLTRLSK---HVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSE 338
Cdd:COG4372 16 FGLRPKTGILIAALSEQLRKALFELDKlqeELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 339 WEHDKQQLLT---ETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEgerRAAAERQVQQLEEQVQQLEAQVQLLVGR 415
Cdd:COG4372 96 LAQAQEELESlqeEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE---IAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1890346197 416 LEGAGQQVcwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREEL 468
Cdd:COG4372 173 LQALSEAE--AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEA 223
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
277-532 |
4.33e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGA------------------------RRRQAEED 332
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvligveaayeaaleaalaaalqniVVEDDEVA 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 333 EQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLL 412
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 413 VGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS-ERE 491
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEErLEE 719
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1890346197 492 QGQCQLRAQQELLQSLQREKQGLEQATTDLRLTILELEREL 532
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
241-516 |
4.77e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 241 LCQSQNLPSSLGQFQQLVQDSMGLRPLPAATVGRWAAEQRKDLTRLSKHvEALRAQLEEAEGQkdglrkqagkleQALKQ 320
Cdd:TIGR00618 371 SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKKQ------------QELQQ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 321 EQGARRRQAEEDE-QCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE------GERRAAAER 393
Cdd:TIGR00618 438 RYAELCAAAITCTaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgSCIHPNPAR 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 394 QVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDS---MVRHQESLQAKQRALLKQ-LDSLDQEREELR 469
Cdd:TIGR00618 518 QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEqmqEIQQSFSILTQCDNRSKEdIPNLQNITVRLQ 597
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890346197 470 GSLD-EAEAQRARVEEQLQSERE-------------QGQCQLRAQQELLqSLQREKQGLEQ 516
Cdd:TIGR00618 598 DLTEkLSEAEDMLACEQHALLRKlqpeqdlqdvrlhLQQCSQELALKLT-ALHALQLTLTQ 657
|
|
| CDC37_N |
smart01071 |
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ... |
278-367 |
5.89e-03 |
|
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.
Pssm-ID: 198139 [Multi-domain] Cd Length: 154 Bit Score: 38.17 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAgKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:smart01071 53 YELIMNDHLNKRIDKLLKGLREEELSPETPTYNE-MLAELQDQLKKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKL 131
|
90
....*....|
gi 1890346197 358 ATLERELKQQ 367
Cdd:smart01071 132 DELEKEEKKK 141
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
243-521 |
6.02e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 243 QSQNLPSSLGQFQQLVQDSMGLRplpaATVGRWAAEQR---KDLTRLSKHV----EALRAQLEEAEGQKDG-------LR 308
Cdd:pfam05483 280 QDENLKELIEKKDHLTKELEDIK----MSLQRSMSTQKaleEDLQIATKTIcqltEEKEAQMEELNKAKAAhsfvvteFE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 309 KQAGKLEQALKQEQgaRRRQAEEDEQCLSEWE-HDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGER 387
Cdd:pfam05483 356 ATTCSLEELLRTEQ--QRLEKNEDQLKIITMElQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 388 RAAAERQV----QQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKAR-------------------------VD 438
Cdd:pfam05483 434 LKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnieltahcdklllenkeltqeasdmTL 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 439 SMVRHQESL---QAKQRALLKQLDSLDQEREELRGSLDEaeaqrarVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 515
Cdd:pfam05483 514 ELKKHQEDIincKKQEERMLKQIENLEEKEMNLRDELES-------VREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE 586
|
....*.
gi 1890346197 516 QATTDL 521
Cdd:pfam05483 587 KQMKIL 592
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
444-516 |
6.23e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.56 E-value: 6.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890346197 444 QESLQAKQRALLKQLDS----LDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcqlRAQQELLQSLQREKQGLEQ 516
Cdd:pfam03938 21 QAQLEKKFKKRQAELEAkqkeLQKLYEELQKDGALLEEEREEKEQELQKKEQELQ---QLQQKAQQELQKKQQELLQ 94
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
624-751 |
6.35e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.31 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 624 DRLWSPSSKGTQGATPPVQAKSTSPG-PlgrqhlPSSRTGRTLlGQPCTSPPRQPCTSPPrQPCTSPPRQPCTSPSRQPc 702
Cdd:PHA03247 2565 DRSVPPPRPAPRPSEPAVTSRARRPDaP------PQSARPRAP-VDDRGDPRGPAPPSPL-PPDTHAPDPPPPSPSPAA- 2635
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1890346197 703 SQPSKSLLEGVTHLDTCTQNPIKVLVRLRKRLSpGRGQASSAHQPQERP 751
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRAR-RLGRAAQASSPPQRP 2683
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
347-517 |
6.51e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 347 LTETSDLKTKMATLERELKQQRESTQAVEAKAQ--------------------QLQEEGERRA----------------- 389
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELKLKEQAKKALeyyqlkekleleeeyllyldYLKLNEERIDllqellrdeqeeiessk 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 390 ----AAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQER 465
Cdd:pfam02463 258 qeieKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1890346197 466 EELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLEQA 517
Cdd:pfam02463 338 EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
297-512 |
6.80e-03 |
|
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: 39.94 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 297 LEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMA------TLERELKQQRES 370
Cdd:COG5185 238 FQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAeytksiDIKKATESLEEQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 371 TQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEG--AGQQVCWASTELDKEKARVDSMVrhqESLQ 448
Cdd:COG5185 318 LAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENivGEVELSKSSEELDSFKDTIESTK---ESLD 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890346197 449 AKQRALLKQLDSL-----------DQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQ 512
Cdd:COG5185 395 EIPQNQRGYAQEIlatledtlkaaDRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAY 469
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
271-514 |
7.17e-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: 39.82 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 271 TVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQclsewehdkQQLLTET 350
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQ---------AYWQVVE 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 351 SDLKTKMATLERELKQQREstqAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwastel 430
Cdd:pfam12128 725 GALDAQLALLKAAIAARRS---GAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEV------- 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 431 dkekARVDSMVRHQESLQAKQRALlkQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQRE 510
Cdd:pfam12128 795 ----LRYFDWYQETWLQRRPRLAT--QLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCE 868
|
....
gi 1890346197 511 KQGL 514
Cdd:pfam12128 869 MSKL 872
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
293-517 |
8.23e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 293 LRAQLEEAE-------GQKDGLRKQAGKLEQALKQEQGARRR-------------QAEED----EQCLSEWEHDKQQLLT 348
Cdd:pfam01576 80 LESRLEEEEersqqlqNEKKKMQQHIQDLEEQLDEEEAARQKlqlekvtteakikKLEEDilllEDQNSKLSKERKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 349 ETSDLKTKMATLERELKQQRESTQAVEAKAQQLQE----EGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVC 424
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEErlkkEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 425 WASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQ---SEREQGQCQLRAQQ 501
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEalkTELEDTLDTTAAQQ 319
|
250
....*....|....*.
gi 1890346197 502 ELLQSLQREKQGLEQA 517
Cdd:pfam01576 320 ELRSKREQEVTELKKA 335
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
428-522 |
8.90e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.85 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890346197 428 TELDKEKARVDSMVrhqESLQAKQRALLKQLDSLDQEREELRgSLDEAEAQRARveEQLQSEREQGQCQLRAQQELlqsl 507
Cdd:smart00787 161 KLLMKELELLNSIK---PKLRDRKDALEEELRQLKQLEDELE-DCDPTELDRAK--EKLKKLLQEIMIKVKKLEEL---- 230
|
90
....*....|....*
gi 1890346197 508 QREKQGLEQATTDLR 522
Cdd:smart00787 231 EEELQELESKIEDLT 245
|
|
| |
