|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-523 |
3.01e-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: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLltetSDLKT 355
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 356 KMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEgagqqvcwASTELDKEKA 435
Cdd:COG1196 317 RLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--------AEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 515
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
....*...
gi 768025295 516 QATTDLRL 523
Cdd:COG1196 467 ELLEEAAL 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
274-517 |
2.41e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDL 353
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 354 KTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwASTELDKE 433
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA---EEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 434 KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQG 513
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
....
gi 768025295 514 LEQA 517
Cdd:COG1196 497 LEAE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-522 |
2.37e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQQLLTETSDLKT 355
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----LEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 356 KMATLERELKQQRESTQAVEAKAQQLQEEgerRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKA 435
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 436 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 515
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
....*..
gi 768025295 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 |
5.14e-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: 72.40 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQagklEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTK 356
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKE----LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 357 MATLERELKQQRESTQAVEAKAQQLQeegERRAAAERQVQQLEEQVQQLEAQVQLLvgrlegagqqvcwaSTELDKEKAR 436
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELE---AQIEQLKEELKALREALDELRAELTLL--------------NEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 437 VDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS---EREQGQCQLRAQQELLQSLQREKQG 513
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSEELRE 905
|
....*....
gi 768025295 514 LEQATTDLR 522
Cdd:TIGR02168 906 LESKRSELR 914
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
280-532 |
8.54e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 8.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 280 RKDLTRlskhVEALRAQLEeaeGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMAT 359
Cdd:COG1196 185 EENLER----LEDILGELE---RQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 360 LERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwASTELDKEKARVDS 439
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE---LEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 440 MVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQEL----------LQSLQR 509
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELaaqleeleeaEEALLE 414
|
250 260
....*....|....*....|...
gi 768025295 510 EKQGLEQATTDLRLTILELEREL 532
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEE 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
277-517 |
4.69e-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: 69.32 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQ-------QLLTE 349
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE----ISRLEQQKQilrerlaNLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 350 TSDLKTKMATLERELKQQRESTQAVEAKAQQLQE--EGERRAAAERQVQQLEEQVQQLEAQVQL--LVGRLEGAGQQVCW 425
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEelESLEAELEELEAELEELESRLEELEEQLetLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 426 ASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQER-----EELRGSLDEAEAQRARVEEQLQSEREQ-------- 492
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREEleeaeqal 477
|
250 260 270
....*....|....*....|....*....|
gi 768025295 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 |
5.67e-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: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQeqgaRRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 358 ATLERELKqqrESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 437
Cdd:TIGR02168 750 AQLSKELT---ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 438 DSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS---EREQGQCQLRAQQELLQSLQREKQGL 514
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSEELREL 906
|
250
....*....|....*....
gi 768025295 515 EQATTDLRLTILELERELE 533
Cdd:TIGR02168 907 ESKRSELRRELEELREKLA 925
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-507 |
3.05e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKT 355
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 356 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAA----ERQVQQLEEQVQQLEAQVQLLVGRLEgagqqvcwASTELD 431
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALlerlERLEEELEELEEALAELEEEEEEEEE--------ALEEAA 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768025295 432 KEKARVDsmvRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSL 507
Cdd:COG1196 449 EEEAELE---EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-520 |
5.77e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 276 AAEQRKDLTRLSKHVE------ALRAQLEEAEGQKDGLRKQA--GKLEQALKQEQGARRRQAEEDEQcLSEWEHDKQQLL 347
Cdd:TIGR02168 195 LNELERQLKSLERQAEkaerykELKAELRELELALLVLRLEElrEELEELQEELKEAEEELEELTAE-LQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 348 TETSDLKTKMATLERELKqqrESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAS 427
Cdd:TIGR02168 274 LEVSELEEEIEELQKELY---ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 428 TELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE---EQLQSEREQGQCQLRAQQELL 504
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarlERLEDRRERLQQEIEELLKKL 430
|
250
....*....|....*.
gi 768025295 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 |
2.24e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 292 ALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQQLLTETSDLKTKMATLERELKQQREST 371
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 372 QAVEAKAQQLQEE-GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwastelDKEKARVDSMVRHQESLQAK 450
Cdd:COG4942 93 AELRAELEAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-------PARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 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 |
5.65e-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: 62.39 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 284 TRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWE---HDKQQLLTETSDLKTKMATL 360
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 361 ERELKQQRESTQAVEAKAQQLQEE-GERRAAAE----RQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKA 435
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDlHKLEEALNdleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 436 RVDSMVRHqesLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE----------EQLQSEREQGQCQLRAQQELLQ 505
Cdd:TIGR02169 830 YLEKEIQE---LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaalrdlesrlGDLKKERDELEAQLRELERKIE 906
|
250 260
....*....|....*....|
gi 768025295 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 |
6.42e-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: 62.39 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 280 RKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLE--QALKqeqgARRRQAEEDEQcLSEW---EHDKQQLLTETSDLK 354
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALL----KEKREYEGYEL-LKEKealERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 355 TKMATLERELKQQRESTQAVEAKAQQLQEE-----GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTE 429
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 430 LDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDE--AEAQRARVE--------EQLQSEREQGQCQLRA 499
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdKEFAETRDElkdyreklEKLKREINELKRELDR 410
|
250 260 270
....*....|....*....|....*....|.
gi 768025295 500 QQELLQSLQREKQGLEQATTDLRLTILELER 530
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
276-516 |
1.17e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 276 AAEQRKDLTRLSKHVEALRAQ---LEEAEGQKDGLRKQAGKLEQalkQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSD 352
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQielLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 353 LKTKMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwasteldk 432
Cdd:COG4913 307 LEAELERLEARLDALRE--ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL--------- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 433 ekarvdsmVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSereqgqcqlraqqellqsLQREKQ 512
Cdd:COG4913 376 --------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE------------------LEAEIA 429
|
....
gi 768025295 513 GLEQ 516
Cdd:COG4913 430 SLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
285-506 |
6.68e-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: 58.93 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 285 RLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQC---LSEWEHDKQQLLTETSDLKTKMATLE 361
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELereIEEERKRRDKLTEEYAELKEELEDLR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 362 RELKQQRESTQAVEAKAQQLQEE----GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwasTELDKEKARV 437
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKleklKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI----NELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 438 DSMVRHQE-----------SLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEqlqsereqGQCQLRAQQELLQS 506
Cdd:TIGR02169 447 ALEIKKQEwkleqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE--------RVRGGRAVEEVLKA 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
266-522 |
8.36e-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: 57.85 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 266 PLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgaRRRQAEEDEQclsewehdkQQ 345
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA--RRIRALEQEL---------AA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 346 LLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGErraaaerqvqqleeqvqqleaqVQLLVGRlEGAGQqvcw 425
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPP----------------------LALLLSP-EDFLD---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 426 asteldkekarvdsMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE---QLQSEREQGQCQLRAQQE 502
Cdd:COG4942 134 --------------AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAllaELEEERAALEALKAERQK 199
|
250 260
....*....|....*....|
gi 768025295 503 LLQSLQREKQGLEQATTDLR 522
Cdd:COG4942 200 LLARLEKELAELAAELAELQ 219
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
291-514 |
2.04e-08 |
|
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: 56.83 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 291 EALRAQLEEAegqkdglRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKqqlltetSDLKTKMATLERELKQQRES 370
Cdd:pfam07888 30 ELLQNRLEEC-------LQERAELLQAQEAANRQREKEKERYKRDREQWERQR-------RELESRVAELKEELRQSREK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 371 TQAVEAKAQQLQEEGERRAAAERqvqQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRH------- 443
Cdd:pfam07888 96 HEELEEKYKELSASSEELSEEKD---ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeeeae 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 444 QESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE-------------QLQSEREQGQCQLRAQQELLQSLQRE 510
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDtittltqklttahRKEAENEALLEELRSLQERLNASERK 252
|
....
gi 768025295 511 KQGL 514
Cdd:pfam07888 253 VEGL 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
276-475 |
1.15e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 276 AAEQRKDLTRLSKHVE---ALRAQLEEAEGQKDGLRKQAGKLEQAL-KQEQGARRRQAEEDEQCLSEWEHDKQQLLTETS 351
Cdd:COG4913 247 AREQIELLEPIRELAEryaAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 352 DLKTKMAT--------LERELKQQRESTQAVEAKAQQLQEegerraAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQV 423
Cdd:COG4913 327 ELEAQIRGnggdrleqLEREIERLERELEERERRRARLEA------LLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 768025295 424 CWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEA 475
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
277-492 |
1.27e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEqcLSEWEHDKQQLLTETSDLktk 356
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE--IAELEAELERLDASSDDL--- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 357 mATLERELKQQRESTQAVEAKAQQLQEEgERRAAAERQvqqleeqvqQLEAQVQLLVGRLEGAGQQVC-WASTELDKEKA 435
Cdd:COG4913 688 -AALEEQLEELEAELEELEEELDELKGE-IGRLEKELE---------QAEEELDELQDRLEAAEDLARlELRALLEERFA 756
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 768025295 436 rvdsmvrhqeslQAKQRALLKQLdsldqeREELRGSLDEAEAQRARVEEQLQSEREQ 492
Cdd:COG4913 757 ------------AALGDAVEREL------RENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
342-532 |
5.12e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 342 DKQQLLTETSDLKTKMATLER------ELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLeaQVQLLVGR 415
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealeDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR--RLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 416 LEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRAL-LKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS------ 488
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAAlglplp 376
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768025295 489 -EREQGQCQLRAQQELLQSLQREKQGLEQATTDLRLTILELEREL 532
Cdd:COG4913 377 aSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
276-510 |
6.38e-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: 52.65 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALK-------QEQGARRRQAEEDEQC---------LSEW 339
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiQYQQAVQALEKARALCglpdltpenAEDY 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 340 EH---DKQQLLTETS-DLKTKMATLERELKQQRESTQAVEAKAqqlqEEGERRAAAERqvqqlEEQVQQLEAQVQLLVGR 415
Cdd:COG3096 443 LAafrAKEQQATEEVlELEQKLSVADAARRQFEKAYELVCKIA----GEVERSQAWQT-----ARELLRRYRSQQALAQR 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 416 LEGAGQQVcwasTELDKEKARvdsmvrhQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQgQC 495
Cdd:COG3096 514 LQQLRAQL----AELEQRLRQ-------QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ-RS 581
|
250
....*....|....*
gi 768025295 496 QLRAQQELLQSLQRE 510
Cdd:COG3096 582 ELRQQLEQLRARIKE 596
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
291-494 |
8.19e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 291 EALRAQLEEA-EGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWehdkQQLLTETSDLKTKMATLERELKQQRE 369
Cdd:COG4717 41 AFIRAMLLERlEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 370 STQAVEaKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVG---RLEGAGQQVCWASTELDKEKARVDSMVRHQ-E 445
Cdd:COG4717 117 ELEKLE-KLLQLLPLYQELEALEAELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEEElQ 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 768025295 446 SLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQ 494
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
275-521 |
1.03e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 275 WAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ---EQGARRRQAEEDEQCLSEWEHDKQQLLTETS 351
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsesENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 352 DLKTKMATLERELKQQRESTQAVEAKAQQLQEEGErraaaerqvqqleeqvqqleaqvqllvgrlegagqqvcwastELD 431
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE------------------------------------------LLE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 432 KEKARVDSMVRHQES----LQAKQRALLKQLDSLDQEREELRGSLDEAEAQRarveEQLQSEREQGQCQLRAQQELLQSL 507
Cdd:TIGR04523 426 KEIERLKETIIKNNSeikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI----NKIKQNLEQKQKELKSKEKELKKL 501
|
250
....*....|....
gi 768025295 508 QREKQGLEQATTDL 521
Cdd:TIGR04523 502 NEEKKELEEKVKDL 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-525 |
1.82e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 339 WEHDKQQLLTET----SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEG----ERRAAAERQVQQLEEQVQQLEAQVQ 410
Cdd:COG4913 590 HEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELdalqERREALQRLAEYSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 411 L-----LVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAE-----AQRA 480
Cdd:COG4913 670 IaeleaELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdlarlELRA 749
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 768025295 481 RVEEQLQSEREQGQcQLRAQQELLQSLQREKQGLEQATTDLRLTI 525
Cdd:COG4913 750 LLEERFAAALGDAV-ERELRENLEERIDALRARLNRAEEELERAM 793
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
355-523 |
1.83e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 355 TKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQL--LVGRLEGAGQQVCWASTELDK 432
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 433 EKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQ 512
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170
....*....|.
gi 768025295 513 GLEQATTDLRL 523
Cdd:COG4717 231 QLENELEAAAL 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
253-393 |
2.23e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 253 QFQQLVQDSMGLRPLpAATVGRWAAEQRKDL-----TRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRR 327
Cdd:COG4913 263 RYAAARERLAELEYL-RAALRLWFAQRRLELleaelEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE 341
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768025295 328 QAEED----EQCLSEWEHDKQQLLTETSDLKTKMATLERELK-QQRESTQAVEAKAQQLQEEGERRAAAER 393
Cdd:COG4913 342 QLEREierlERELEERERRRARLEALLAALGLPLPASAEEFAaLRAEAAALLEALEEELEALEEALAEAEA 412
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
277-522 |
4.82e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 277 AEQRKDLTRLskhVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSewehdkqqlltETSDLKTK 356
Cdd:PRK02224 515 EERREDLEEL---IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE-----------EVAELNSK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 357 MATLERE---LKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAgqqvcwASTELDKE 433
Cdd:PRK02224 581 LAELKERiesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA------RIEEARED 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 434 KARVDSmvrHQESLQAKqrallkqLDSLDQEREELRGSLDEAEAQRARVEEqLQSEREqgqcQLRAQQELLQSLQREKQG 513
Cdd:PRK02224 655 KERAEE---YLEQVEEK-------LDELREERDDLQAEIGAVENELEELEE-LRERRE----ALENRVEALEALYDEAEE 719
|
....*....
gi 768025295 514 LEQATTDLR 522
Cdd:PRK02224 720 LESMYGDLR 728
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
278-508 |
5.74e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQC-------LSEWEHDKQQLLTET 350
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELeelleqlSLATEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 351 SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAER-------------------QVQQLEEQVQQLEAQVQL 411
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallgLGGSLLSLILTIAGVLFL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 412 LVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLD-SLDQEREELRGSLDE-AEAQRARVEEQLQSE 489
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRiEELQELLREAEELEE 361
|
250
....*....|....*....
gi 768025295 490 REQGQCQLRAQQELLQSLQ 508
Cdd:COG4717 362 ELQLEELEQEIAALLAEAG 380
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
269-505 |
1.93e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 269 AATVGRWAAEQRKD-LTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLL 347
Cdd:PTZ00121 1344 AAEAAKAEAEAAADeAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 348 TETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwaS 427
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK----A 1499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 428 TELDK---EKARVDSMVRHQESLQAKQRALLKQLDSLDQER--------EELRGSLDEAEAQRARVEEQLQSEREQGQCQ 496
Cdd:PTZ00121 1500 DEAKKaaeAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaeekkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
....*....
gi 768025295 497 LRAQQELLQ 505
Cdd:PTZ00121 1580 LRKAEEAKK 1588
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
277-523 |
1.95e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQclsewehdkQQLLTETSDLKTK 356
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQL---------AEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 357 MATLERELKQQRESTQAVEAkAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwasteLDKEKAR 436
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ-------LQQEAQR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 437 VDSMVRHQ-ESLQAKQRALLKQLDSLDQEREElrgsLDEAEAQRARVEEQLQSEREQgqcqlraQQELLQSLQREKQGLE 515
Cdd:COG3206 314 ILASLEAElEALQAREASLQAQLAQLEARLAE----LPELEAELRRLEREVEVAREL-------YESLLQRLEEARLAEA 382
|
....*...
gi 768025295 516 QATTDLRL 523
Cdd:COG3206 383 LTVGNVRV 390
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
274-392 |
2.30e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRK-----QAGKLEQALKQEQGARR----RQAEEDEQCLSEWEHDKQ 344
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKaeeenKIKAAEEAKKAEEDKKKaeeaKKAEEDEKKAAEALKKEA 1698
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 768025295 345 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQ--EEGERRAAAE 392
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKkeAEEDKKKAEE 1748
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
277-520 |
3.13e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 277 AEQRKDLTRLSKHVEALRA-QLEEAEGQK--DGLRK--------QAGKLEQALKQEQ--GARRRQAEEDEQCLSEWEHDK 343
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKAdEAKKAEEKKkaDELKKaeelkkaeEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEV 1597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 344 QQLLTETSDLKTKMATLERELKqqrestqaveAKAQQLQEEGERRAAAERQVQQLEEQVQQLEaQVQllvgrlegAGQQV 423
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAK----------IKAEELKKAEEEKKKVEQLKKKEAEEKKKAE-ELK--------KAEEE 1658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 424 CWASTELDKEKARVDSmvRHQESLQAKQRALLKQLDSLDQEREELRGS--LDEAEAQRARVEEQLQSEREQGQCQLraqQ 501
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAEELKKAEEENKIKA---E 1733
|
250
....*....|....*....
gi 768025295 502 ELLQSLQREKQGLEQATTD 520
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKD 1752
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
310-582 |
3.39e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 310 QAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE-GERR 388
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 389 AAAERQVQQLEEQVQQLEAQ-VQLLVGRLEGAgqqvcwaSTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREE 467
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSEsFSDFLDRLSAL-------SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 468 LRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLEQATTDLRLTILELERELEELKERERLLVAFPD 547
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
250 260 270
....*....|....*....|....*....|....*
gi 768025295 548 LHRPTETQIHADPAGPALVPFQQGNPGSNTTSPGQ 582
Cdd:COG3883 246 AAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAAS 280
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
278-516 |
4.83e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 278 EQRKDLTRLSKHVEALRAQLEEAEGQkdgLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQlltETSDLKTKM 357
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAY---LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ---ERINRARKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 358 ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVG------RLEGAGQQVCWASTELD 431
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsqeiHIRDAHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 432 KEKARVDSMVRHQESLQA-------------KQRALLKQLDSLDQEREELRGSLDEAEA----QRARVEEQLQSEREQGQ 494
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTltqklqslckeldILQREQATIDTRTSAFRDLQGQLAHAKKqqelQQRYAELCAAAITCTAQ 452
|
250 260
....*....|....*....|....*
gi 768025295 495 CQL---RAQQELLQSLQREKQGLEQ 516
Cdd:TIGR00618 453 CEKlekIHLQESAQSLKEREQQLQT 477
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
267-516 |
6.82e-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: 45.98 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 267 LPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR--RQAEEDeqcLSEWEHDKQ 344
Cdd:pfam12128 587 LKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTalKNARLD---LRRLFDEKQ 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 345 QLltetSDLKTKmaTLERELKQQRESTQAVEAKAQQLqeEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVc 424
Cdd:pfam12128 664 SE----KDKKNK--ALAERKDSANERLNSLEAQLKQL--DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL- 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 425 waSTELDKEKARVDsmvRHQESLQAKQRALLKQLD-------SLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQL 497
Cdd:pfam12128 735 --KAAIAARRSGAK---AELKALETWYKRDLASLGvdpdviaKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRR 809
|
250
....*....|....*....
gi 768025295 498 RAQQELLQSLQREKQGLEQ 516
Cdd:pfam12128 810 PRLATQLSNIERAISELQQ 828
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
252-506 |
7.10e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 252 GQFQQLVQ------DSMGLRPLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAegqkDGLRKQAGKLEQALKQEQGAR 325
Cdd:COG3096 413 IQYQQAVQalekarALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVA----DAARRQFEKAYELVCKIAGEV 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 326 RRQA--EEDEQCLSEWEhDKQQLLTETSDLKTKMATLERELKQQREstqaveakAQQLQEEGERRAAAERqvqqleeqvq 403
Cdd:COG3096 489 ERSQawQTARELLRRYR-SQQALAQRLQQLRAQLAELEQRLRQQQN--------AERLLEEFCQRIGQQL---------- 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 404 QLEAQVQLLVGRLEgagQQVCWASTELDKEKARVDSMVRHQESLQAKQRAL-------LKQLDSLDQEREELRGSLDEAE 476
Cdd:COG3096 550 DAAEELEELLAELE---AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawLAAQDALERLREQSGEALADSQ 626
|
250 260 270
....*....|....*....|....*....|..
gi 768025295 477 AQRARVEEQLQSERE--QGQCQLRAQQELLQS 506
Cdd:COG3096 627 EVTAAMQQLLEREREatVERDELAARKQALES 658
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
247-517 |
8.21e-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: 45.27 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 247 LPSSLGQFQQLVQDSMGLRPLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR 326
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 327 RQAEEDEQCLSEWEHDKQQLLTETSDLKT-KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAaERQVQQLEEQVQQL 405
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTlTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-QAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 406 EAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQ---ESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARV 482
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEaenEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 768025295 483 EEQL-QSEREQGQCQLRAQQELLQ------SLQREKQGLEQA 517
Cdd:pfam07888 271 QAELhQARLQAAQLTLQLADASLAlregraRWAQERETLQQS 312
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
432-532 |
9.61e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 432 KEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE---EQLQSEREQGQCQLRAQQELLQSLQ 508
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100
....*....|....*....|....
gi 768025295 509 REKQGLEQATTDLRLTILELEREL 532
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDL 774
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
278-486 |
1.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEqALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKm 357
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 358 atlERELKQQRESTQAVEAKAQQ---LQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAS---TELD 431
Cdd:PRK03918 275 ---IEELEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELE 351
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 432 KEKARVDSMVRHQESLqakqRALLKQLDSLDQER-----EELRGSLDEAEAQRARVEEQL 486
Cdd:PRK03918 352 KRLEELEERHELYEEA----KAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEI 407
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
277-476 |
1.19e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ----------------EQGARRRQAEEDEQCLSEWE 340
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREleerieelkkeieeleEKVKELKELKEKAEEYIKLS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 341 HDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEaQVQLLVGRLEGAG 420
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLK 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 768025295 421 QQVcwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAE 476
Cdd:PRK03918 379 KRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
269-506 |
1.23e-04 |
|
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: 45.12 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEgqkDGLRKQAgKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT 348
Cdd:pfam05557 36 ASALKRQLDRESDRNQELQKRIRLLEKREAEAE---EALREQA-ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 349 ETSDLKTKMATLERELKQQRESTQAVEakaQQLQEEGERRAAAERQVQQLEEQVQQLEA---QVQLLVGRLEgagQQVCW 425
Cdd:pfam05557 112 ELSELRRQIQRAELELQSTNSELEELQ---ERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQ---SQEQD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 426 aSTELDKEKARVDSMVRhQESLQAKQRALLKQLDS-------LDQEREELRGSLDEAEAQRARVEEqLQSEREQGQCQLR 498
Cdd:pfam05557 186 -SEIVKNSKSELARIPE-LEKELERLREHNKHLNEnienkllLKEEVEDLKRKLEREEKYREEAAT-LELEKEKLEQELQ 262
|
....*...
gi 768025295 499 AQQELLQS 506
Cdd:pfam05557 263 SWVKLAQD 270
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
282-387 |
1.32e-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: 45.05 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 282 DLTRLSKHVEALRAQLEEAEGQKDGLRKQAgkleQALKQEQGarrrQAEEDEQCLSE----WEHDKQQLLTETSDLKTKM 357
Cdd:pfam05911 703 ELASCTENLESTKSQLQESEQLIAELRSEL----ASLKESNS----LAETQLKCMAEsyedLETRLTELEAELNELRQKF 774
|
90 100 110
....*....|....*....|....*....|
gi 768025295 358 ATLERELKQQRESTQAVEAKAQQLQEEGER 387
Cdd:pfam05911 775 EALEVELEEEKNCHEELEAKCLELQEQLER 804
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
281-474 |
1.79e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 281 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEqgarRRQAEEDEQCLSEWEHDK--QQLLTETSDLKTKMA 358
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQLGNVRNNKeyEALQKEIESLKRRIS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 359 TLERELKQQREstqAVEAKAQQLQEEGERRAAAErqvqqleeqvqqleaqvqllvgrlegagqqvcwasTELDKEKARVD 438
Cdd:COG1579 107 DLEDEILELME---RIEELEEELAELEAELAELE-----------------------------------AELEEKKAELD 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 768025295 439 smvrhqeslqAKQRALLKQLDSLDQEREELRGSLDE 474
Cdd:COG1579 149 ----------EELAELEAELEELEAEREELAAKIPP 174
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
299-512 |
1.79e-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: 44.73 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 299 EAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEA-- 376
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEIsr 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 377 --KAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTE--------LDKEKARVDSMVRHQES 446
Cdd:pfam17380 377 mrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEarqrevrrLEEERAREMERVRLEEQ 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768025295 447 LQAKQRALLKQlDSLDQEREELRGSLDE-----AEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQ 512
Cdd:pfam17380 457 ERQQQVERLRQ-QEEERKRKKLELEKEKrdrkrAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
277-383 |
1.81e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 277 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEqclsewehdkqqlltETSDLKTK 356
Cdd:COG2433 409 TEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR---------------EISRLDRE 473
|
90 100
....*....|....*....|....*..
gi 768025295 357 MATLERELKQQRESTQAVEAKAQQLQE 383
Cdd:COG2433 474 IERLERELEEERERIEELKRKLERLKE 500
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
276-452 |
2.35e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQA--EEDEQCLSEWEHDKQQLltetsdl 353
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleAELAELPERLEELEERL------- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 354 ktkmatleRELKQQRESTQAVEAKAQQLQEegERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKE 433
Cdd:COG4717 156 --------EELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170
....*....|....*....
gi 768025295 434 KARVDSMVRHQESLQAKQR 452
Cdd:COG4717 226 EEELEQLENELEAAALEER 244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
278-392 |
2.63e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKqeqgARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE----DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
90 100 110
....*....|....*....|....*....|....*
gi 768025295 358 ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAE 392
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERVRGGRAVE 513
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
278-515 |
3.81e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQA--------------EEDEQCLSEWEHDK 343
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEelerlkkrltgltpEKLEKELEELEKAK 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 344 QQLLTETSDLKTKMATLERELKQQRESTQAVE-AKA------QQLQEEGERRAAAErqvqqleeqvqqLEAQVQLLVGRL 416
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKkAKGkcpvcgRELTEEHRKELLEE------------YTAELKRIEKEL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 417 EGAGQQVcwasTELDKEKARVDsMVRHQESLQAKQRALLKQLDSLD---------------QEREELRGSLDEAEAQRAR 481
Cdd:PRK03918 469 KEIEEKE----RKLRKELRELE-KVLKKESELIKLKELAEQLKELEeklkkynleelekkaEEYEKLKEKLIKLKGEIKS 543
|
250 260 270
....*....|....*....|....*....|....
gi 768025295 482 VEEQLQSEREQgQCQLRAQQELLQSLQREKQGLE 515
Cdd:PRK03918 544 LKKELEKLEEL-KKKLAELEKKLDELEEELAELL 576
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
344-517 |
4.18e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 344 QQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERraaaerqvqqleeqvqqLEAQVQLLVGRLEGAGQQV 423
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-----------------LEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 424 CWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQ-GQCQLRAQQE 502
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElAALEQELQAL 176
|
170
....*....|....*
gi 768025295 503 LLQSLQREKQGLEQA 517
Cdd:COG4372 177 SEAEAEQALDELLKE 191
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
269-524 |
4.32e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLE---QALKQEQGARRRQAEEDEQCLSEWEHD--- 342
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEdflEELREERDELREREAELEATLRTARERvee 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 343 KQQLLTE------------------TSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERqvqqleeQVQQ 404
Cdd:PRK02224 445 AEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIER-------LEER 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 405 LEAQVQLLVGRLEGAGQQVCWAStELDKEKARVDSMVRHQESLQAKQR-----------ALLKQLDSLDQEREEL---RG 470
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAE-ELRERAAELEAEAEEKREAAAEAEeeaeeareevaELNSKLAELKERIESLeriRT 596
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 768025295 471 SLDEAEAQRARVEEqLQSEREQGQCQLRAQQELLQSLQREKQGLEQATTDLRLT 524
Cdd:PRK02224 597 LLAAIADAEDEIER-LREKREALAELNDERRERLAEKRERKRELEAEFDEARIE 649
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
343-521 |
4.41e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 343 KQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleEQVQQLEAQVQLLVGRLEGAGQQ 422
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK---------------NGLVDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 423 VCWASTELDKEKARVDSMVRHQESLQAKQ---------RALLKQLDSLDQEREELRGSLDE-------AEAQRARVEEQL 486
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQL 307
|
170 180 190
....*....|....*....|....*....|....*....
gi 768025295 487 QSEREQGQCQLRAQQELLQ----SLQREKQGLEQATTDL 521
Cdd:COG3206 308 QQEAQRILASLEAELEALQareaSLQAQLAQLEARLAEL 346
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
288-504 |
6.11e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 288 KHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ-----EQGARRRQAEEDEqcLSEWEHDKQQLLTETSDLKTKMATLER 362
Cdd:pfam00038 54 KEIEDLRRQLDTLTVERARLQLELDNLRLAAEDfrqkyEDELNLRTSAEND--LVGLRKDLDEATLARVDLEAKIESLKE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 363 EL---------------KQQRESTQAVEAKAQQLQEEG----ERRAA----AERQVQQLEEQVQQLEAQVQLLVGRlegA 419
Cdd:pfam00038 132 ELaflkknheeevrelqAQVSDTQVNVEMDAARKLDLTsalaEIRAQyeeiAAKNREEAEEWYQSKLEELQQAAAR---N 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 420 GQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLdsldQEREElRGSLDEAEAQR--ARVEEQLQSEREQGQCQL 497
Cdd:pfam00038 209 GDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQL----AETEE-RYELQLADYQEliSELEAELQETRQEMARQL 283
|
....*..
gi 768025295 498 RAQQELL 504
Cdd:pfam00038 284 REYQELL 290
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
281-525 |
6.80e-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: 42.70 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 281 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRqaeeDEQCLSEWEHDKQ---QLLTETSDLKTKM 357
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK----LELLLSNLKKKIQknkSLESQISELKKQN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 358 ATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleeqVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 437
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQ-----------------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 438 DSMVRHQESL-QAKQRALLK----QLDSLDQEREELRGSLDEAEAQRARVEEQ----------LQSEREQGQCQLRAQQE 502
Cdd:TIGR04523 291 NQLKSEISDLnNQKEQDWNKelksELKNQEKKLEEIQNQISQNNKIISQLNEQisqlkkeltnSESENSEKQRELEEKQN 370
|
250 260 270
....*....|....*....|....*....|
gi 768025295 503 LLQSLQREKQG-------LEQATTDLRLTI 525
Cdd:TIGR04523 371 EIEKLKKENQSykqeiknLESQINDLESKI 400
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
274-517 |
6.97e-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: 42.85 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 274 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALkqeqgarrrqaeedeqclseweHDKQQLLTETSDL 353
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL----------------------QDTQELLQEETRQ 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 354 KTKMATLERELKQQRESTQaveakaQQLQEEGERRAAAERqvqqleeqvqqleaqvqllvgrlegagqQVCWASTELDKE 433
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQ------EQLEEEEEAKRNVER----------------------------QLSTLQAQLSDM 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 434 KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARveeqLQSEREQGQCQLRAQQELLQSLQREKQG 513
Cdd:pfam01576 530 KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR----LQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
....
gi 768025295 514 LEQA 517
Cdd:pfam01576 606 FDQM 609
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
270-514 |
7.08e-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: 42.57 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 270 ATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAL----KQEQGARRRQAEEDEQC--LSEWEHDK 343
Cdd:pfam07888 139 KTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslsKEFQELRNSLAQRDTQVlqLQDTITTL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 344 QQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLlvgrlegagqQV 423
Cdd:pfam07888 219 TQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTL----------QL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 424 CWASTELDKEKARvdsMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQL----RA 499
Cdd:pfam07888 289 ADASLALREGRAR---WAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLsesrRE 365
|
250
....*....|....*...
gi 768025295 500 QQEL---LQSLQREKQGL 514
Cdd:pfam07888 366 LQELkasLRVAQKEKEQL 383
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
445-524 |
7.26e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 445 ESLQAKQRALLKQLDSLDQEREELRgSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQS---------LQREKQGLE 515
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEkaaetsqerKQKRKEITD 223
|
....*....
gi 768025295 516 QATTDLRLT 524
Cdd:PRK11448 224 QAAKRLELS 232
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
276-516 |
7.52e-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: 42.47 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 276 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRK-------QAGKLEQALKQEQGARRRqAEEDEQCLSEwehDKQQLLT 348
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALARLEEETAQKNNALKkireleaQISELQEDLESERAARNK-AEKQRRDLGE---ELEALKT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 349 ETSDLKTKMATlERELKQQRES---------------------------TQAVEAKAQQLQEEGERRAAAERQVQQLEEQ 401
Cdd:pfam01576 307 ELEDTLDTTAA-QQELRSKREQevtelkkaleeetrsheaqlqemrqkhTQALEELTEQLEQAKRNKANLEKAKQALESE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 402 VQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRAR 481
Cdd:pfam01576 386 NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
250 260 270
....*....|....*....|....*....|....*...
gi 768025295 482 VEEQLQSEREQGQCQLRAQQEL---LQSLQREKQGLEQ 516
Cdd:pfam01576 466 LESQLQDTQELLQEETRQKLNLstrLRQLEDERNSLQE 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
272-373 |
7.91e-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: 42.06 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 272 VGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETS 351
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
90 100
....*....|....*....|..
gi 768025295 352 DLKTKMATLERELKQQRESTQA 373
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPA 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
277-522 |
8.36e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 277 AEQRKDLTRLSKHVEALRAQ--------------LEEAEGQKDGLRKQAGKLEQALKQEQGARRR--------------- 327
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERfgdapvdlgnaedfLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgq 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 328 ---------QAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLE---------RELKQQRE-STQAVEAKAQQLQEEGERR 388
Cdd:PRK02224 460 pvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlveaedriERLEERREdLEELIAERRETIEEKRERA 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 389 AAAERQVQQLEEQVQQLEAQVQllvgRLEGAGQQVCWASTELDKEKARVDSMVrhqESLqAKQRALLKQLDSLDQEREEL 468
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAA----EAEEEAEEAREEVAELNSKLAELKERI---ESL-ERIRTLLAAIADAEDEIERL 611
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768025295 469 ---RGSLDEAEAQRarvEEQLQSEREQGQcQLRAQ------QELLQSLQREKQGLEQATTDLR 522
Cdd:PRK02224 612 rekREALAELNDER---RERLAEKRERKR-ELEAEfdeariEEAREDKERAEEYLEQVEEKLD 670
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
341-515 |
8.92e-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: 41.06 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 341 HDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAG 420
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 421 QQVcwaSTEldKEkarVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQ 500
Cdd:COG1579 83 GNV---RNN--KE---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170
....*....|....*
gi 768025295 501 QELLQSLQREKQGLE 515
Cdd:COG1579 155 EAELEELEAEREELA 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
277-484 |
9.76e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 277 AEQRKDL-TRLSKH-VEALRAQLEEAEGQK---DGLRKQAGKLEQALKQEQGARRRQAEEDEQcLSEWEHDKQQLLTETS 351
Cdd:PRK03918 502 AEQLKELeEKLKKYnLEELEKKAEEYEKLKeklIKLKGEIKSLKKELEKLEELKKKLAELEKK-LDELEEELAELLKELE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 352 DLKTK-MATLERELKQ----QRESTQAVEAKaQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQ----- 421
Cdd:PRK03918 581 ELGFEsVEELEERLKElepfYNEYLELKDAE-KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkysee 659
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768025295 422 ---QVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE 484
Cdd:PRK03918 660 eyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
274-517 |
1.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 274 RWAAEQRKDLTRlSKHVEALR-----AQLEEAEGQKDGLRKQAGKLEQALKQEQgarRRQAEE----DEQCLSEwEHDKQ 344
Cdd:PTZ00121 1230 KKAEEAKKDAEE-AKKAEEERnneeiRKFEEARMAHFARRQAAIKAEEARKADE---LKKAEEkkkaDEAKKAE-EKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 345 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQleeqvqqleaqvqllvgRLEGAGQQVC 424
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-----------------EAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 425 WASTELDKEKARVDSM------VRHQESLQAKQRALLKQLDSLDQEREELRgsldEAEAQRARVEEQLQSEREQGQCQLR 498
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAkkkaeeKKKADEAKKKAEEDKKKADELKKAAAAKK----KADEAKKKAEEKKKADEAKKKAEEA 1443
|
250
....*....|....*....
gi 768025295 499 AQQELLQSLQREKQGLEQA 517
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEA 1462
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
269-524 |
1.67e-03 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 41.52 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSewehDKQQLLT 348
Cdd:COG5281 173 AAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAAS----AAAQALA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 349 ETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAST 428
Cdd:COG5281 249 ALAAAAAAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALRAAA 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 429 ELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQ 508
Cdd:COG5281 329 QALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWAAGAKAALAEYADSATNVAAQVAQAAT 408
|
250
....*....|....*.
gi 768025295 509 REKQGLEQATTDLRLT 524
Cdd:COG5281 409 SAFSGLTDALAGAVTT 424
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
326-503 |
1.69e-03 |
|
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: 40.03 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 326 RRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMAtlERELKQQRESTQAVEAKAQQLQEegERRAAAERqvqqleeqvQQL 405
Cdd:pfam15665 52 KRRIQTLEESLEQHERMKRQALTEFEQYKRRVE--ERELKAEAEHRQRVVELSREVEE--AKRAFEEK---------LES 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 406 EAQVQllvgrlegagqqvcwASTELDKEKARVDSMVRHQ---ESLQAKQRAL--------LKQLDSLDQEREELRGSLDE 474
Cdd:pfam15665 119 FEQLQ---------------AQFEQEKRKALEELRAKHRqeiQELLTTQRAQsasslaeqEKLEELHKAELESLRKEVED 183
|
170 180
....*....|....*....|....*....
gi 768025295 475 AEAQRARVEEqlQSEREQGQCQLRAQQEL 503
Cdd:pfam15665 184 LRKEKKKLAE--EYEQKLSKAQAFYEREL 210
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
288-492 |
1.80e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 288 KHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARrrqaEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQ 367
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI----QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 368 RESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQ--- 444
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsl 953
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 768025295 445 ESLQAKQRALLKQLDSLD-------QEREELRGSLDEAEAQRARVEEqlqsEREQ 492
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEE----ERKA 1004
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
294-388 |
1.87e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 294 RAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEED---EQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRES 370
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELvalEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220
|
90
....*....|....*...
gi 768025295 371 TQAVEAKAQQLQEEGERR 388
Cdd:PRK11448 221 ITDQAAKRLELSEEETRI 238
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
269-526 |
1.93e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 269 AATVGRWAAEQRK-DLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLL 347
Cdd:COG1196 559 AAAAIEYLKAAKAgRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 348 TETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAS 427
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 428 TELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELrGSLDEAEAQRARVEEQLQS--------EREqgqcqLRA 499
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELERELERLEREIEAlgpvnllaIEE-----YEE 792
|
250 260
....*....|....*....|....*..
gi 768025295 500 QQELLQSLQREKQGLEQATTDLRLTIL 526
Cdd:COG1196 793 LEERYDFLSEQREDLEEARETLEEAIE 819
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
269-510 |
1.98e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 269 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT 348
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 349 EtsDLKTKMATLERELKQqrESTQAVEAKAQQLQEEGERRaaaerqvqqleeqvqqleAQVQLLVGRLEGAGQQVCWAST 428
Cdd:COG4717 366 E--ELEQEIAALLAEAGV--EDEEELRAALEQAEEYQELK------------------EELEELEEQLEELLGELEELLE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 429 ELDKE--KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELR--GSLDEAEAQRARVEEQLQSEREQGQcQLRAQQELL 504
Cdd:COG4717 424 ALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWA-ALKLALELL 502
|
....*.
gi 768025295 505 QSLQRE 510
Cdd:COG4717 503 EEAREE 508
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
426-524 |
2.06e-03 |
|
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: 40.58 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 426 ASTELDKEKARVDSMVRH----QESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQ-----------RARVEEQLQSER 490
Cdd:pfam05816 79 AGNKIEKYFAKYQTAGAQidkiVVELEKGQDELLKDNAMLDQMYEKNLEYFKELEKYiaagelkleelDAELLPELEAKA 158
|
90 100 110
....*....|....*....|....*....|....*.
gi 768025295 491 EQGQCQLRAQ--QELLQSLQRekqgLEQATTDLRLT 524
Cdd:pfam05816 159 AASGDPEDAQalRDLRQALFR----LEQRIHDLELQ 190
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
328-517 |
2.32e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 328 QAEED-EQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLE 406
Cdd:PRK03918 186 KRTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 407 AQVQLLVGRLEGAGQQVCwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEqL 486
Cdd:PRK03918 266 ERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE-L 343
|
170 180 190
....*....|....*....|....*....|.
gi 768025295 487 QSEREQGQCQLRAQQELLQSLQREKQGLEQA 517
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
286-522 |
2.38e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 286 LSKHVEALRAQLEEAEGQKDGLRKQAGKLEQaLKQEQGARRrqaeEDEQCLSEWEHDKQQLLTETSDLKTKMATLErELK 365
Cdd:PRK04863 892 LADRVEEIREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQ----SDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVV 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 366 QQR-----ESTQAVEAKAQQLQEegerraaaerqvqqleeqvqqleaqvqLLVGRLEGAGQQVCWASTELDKEKARVDSM 440
Cdd:PRK04863 966 QRRahfsyEDAAEMLAKNSDLNE---------------------------KLRQRLEQAEQERTRAREQLRQAQAQLAQY 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 441 VRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARV-EEQL-------QSEREQGQCQLRAQQELLQSLQREKQ 512
Cdd:PRK04863 1019 NQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARArRDELharlsanRSRRNQLEKQLTFCEAEMDNLTKKLR 1098
|
250
....*....|
gi 768025295 513 GLEQATTDLR 522
Cdd:PRK04863 1099 KLERDYHEMR 1108
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
278-525 |
2.68e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 278 EQRKDLTRLS-------KHVEaLRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTET 350
Cdd:TIGR04523 195 KLLKLELLLSnlkkkiqKNKS-LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 351 SDL---KTKMATLERELKQqrestqaVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQL-----LVGRLEgagQQ 422
Cdd:TIGR04523 274 KELeqnNKKIKELEKQLNQ-------LKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIsqnnkIISQLN---EQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 423 VcwasTELDKEKARVDSM-VRHQESLQAKQrallKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcQLraqQ 501
Cdd:TIGR04523 344 I----SQLKKELTNSESEnSEKQRELEEKQ----NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ-QK---D 411
|
250 260
....*....|....*....|....
gi 768025295 502 ELLQSLQREKQGLEQATTDLRLTI 525
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETI 435
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
290-517 |
2.79e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 290 VEALRAQLEEAEGQKDGLRKQAGKLEQALK-------QEQGARRRQAEEDEQC-LSEWEHDKQQLLTETSDLKTKMATLE 361
Cdd:PRK04863 378 QEENEARAEAAEEEVDELKSQLADYQQALDvqqtraiQYQQAVQALERAKQLCgLPDLTADNAEDWLEEFQAKEQEATEE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 362 -RELKQQRESTQAVE---AKAQQLQeegeRRAAAERQVQQLEEQVQQLEAQV---QLLVGRLEGAGQQVcwasTELDKEk 434
Cdd:PRK04863 458 lLSLEQKLSVAQAAHsqfEQAYQLV----RKIAGEVSRSEAWDVARELLRRLreqRHLAEQLQQLRMRL----SELEQR- 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 435 arvdsmVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQgQCQLRAQQELLQSLQREKQGL 514
Cdd:PRK04863 529 ------LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER-RMALRQQLEQLQARIQRLAAR 601
|
...
gi 768025295 515 EQA 517
Cdd:PRK04863 602 APA 604
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
285-510 |
3.11e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 285 RLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAL----------KQEQGARRRQAEEDEQCLSE-------WEHDKQQLL 347
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELddllvdldhqRQLVSNLEKKQKKFDQMLAEekaisarYAEERDRAE 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 348 TETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAA-----------ERQVQQLEEQVQQLEAQVQLLVGRL 416
Cdd:pfam01576 629 AEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknvhelERSKRALEQQVEEMKTQLEELEDEL 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 417 EGAGQQVCWASTELDKEKARVDSMVRHQESL-QAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS------- 488
Cdd:pfam01576 709 QATEDAKLRLEVNMQALKAQFERDLQARDEQgEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKEleaqida 788
|
250 260
....*....|....*....|....*
gi 768025295 489 ---EREQGQCQLRAQQELLQSLQRE 510
Cdd:pfam01576 789 ankGREEAVKQLKKLQAQMKDLQRE 813
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
290-524 |
3.70e-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: 40.19 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 290 VEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRE 369
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKE 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 370 STQAVEAKAQQLQE-EGERRAAAE-----RQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRH 443
Cdd:pfam10174 532 ECSKLENQLKKAHNaEEAVRTNPEindriRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLR 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 444 QESLQAKQRALLKQLdsldqEREELRGSLDEAEAQRARVEEQLQSEREQgqcQLraqQELLQSLQREKQGLEqaTTDLRL 523
Cdd:pfam10174 612 QMKEQNKKVANIKHG-----QQEMKKKGAQLLEEARRREDNLADNSQQL---QL---EELMGALEKTRQELD--ATKARL 678
|
.
gi 768025295 524 T 524
Cdd:pfam10174 679 S 679
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
278-520 |
4.04e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAgkleQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEEL----EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 358 ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 437
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 438 DSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLEQA 517
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
...
gi 768025295 518 TTD 520
Cdd:COG4372 320 ALL 322
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
286-384 |
5.09e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.73 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 286 LSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgarrRQAEEDEQCLSEWEHDKQQLLTetsdLKTKMATLERELK 365
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQ----EEVEELRKQLENYEKDKQSLKN----LKARLKVLEKELK 102
|
90
....*....|....*....
gi 768025295 366 QQRESTQAVEAKAQQLQEE 384
Cdd:pfam13851 103 DLKWEHEVLEQRFEKVERE 121
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
272-525 |
5.22e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 272 VGRWAAEQRKDLTRLSKHVEA-----LRAQLEEAEGQKDGLRKQAGKLEQalKQEQGARRRqaEEDEQCLSEWEHDKQQL 346
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEkeekdLHERLNGLESELAELDEEIERYEE--QREQARETR--DEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 347 LT---ETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE-GERRAAAERQVQQL---EEQVQQLEAQVQLLVGRLEGA 419
Cdd:PRK02224 254 ETleaEIEDLRETIAETEREREELAEEVRDLRERLEELEEErDDLLAEAGLDDADAeavEARREELEDRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 420 GQQVCWASTELDKEKARVDSmvRHQESLQAKQRAllkqlDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQ---GQCQ 496
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADD--LEERAEELREEA-----AELESELEEAREAVEDRREEIEELEEEIEELRERfgdAPVD 406
|
250 260
....*....|....*....|....*....
gi 768025295 497 LRAQQELLQSLQREKQGLEQATTDLRLTI 525
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATL 435
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
343-479 |
5.64e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 38.01 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 343 KQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERqvqqleeqvQQLEAQVQLLVGRLEGAgqq 422
Cdd:PRK07352 52 REAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIR---------AEIEKQAIEDMARLKQT--- 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 768025295 423 vcwASTELDKEKARVDSMVRHQESLQAKQRALlkqldsldqerEELRGSLDEAEAQR 479
Cdd:PRK07352 120 ---AAADLSAEQERVIAQLRREAAELAIAKAE-----------SQLPGRLDEDAQQR 162
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
278-517 |
6.18e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 278 EQRKDlTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR----RQAEEDEQC--LSEWEHDKQQLLTETS 351
Cdd:PTZ00121 1082 DAKED-NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaeeaRKAEDARKAeeARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 352 D--LKTKMATLERELKQQRESTQAVEA-KAQQLQE-------EGERRAAAERQVQQLEEQVQQLEAQVqllVGRLEGAGQ 421
Cdd:PTZ00121 1161 EdaRKAEEARKAEDAKKAEAARKAEEVrKAEELRKaedarkaEAARKAEEERKAEEARKAEDAKKAEA---VKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 422 QvcwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQER--EELRGSLDEAEAQRARVEEQLQ--SEREQGQCQL 497
Cdd:PTZ00121 1238 D---AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkaDELKKAEEKKKADEAKKAEEKKkaDEAKKKAEEA 1314
|
250 260
....*....|....*....|
gi 768025295 498 RAQQELLQSLQREKQGLEQA 517
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAA 1334
|
|
| CDC37_N |
smart01071 |
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ... |
278-367 |
7.68e-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: 37.40 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 278 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAgKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 357
Cdd:smart01071 53 YELIMNDHLNKRIDKLLKGLREEELSPETPTYNE-MLAELQDQLKKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKL 131
|
90
....*....|
gi 768025295 358 ATLERELKQQ 367
Cdd:smart01071 132 DELEKEEKKK 141
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
281-384 |
7.69e-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: 38.81 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 281 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKqeqgARRRQAEEDEQCLSEW-EHDKQQLLTETSdlktkmAT 359
Cdd:pfam02841 197 QALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMME----AQERSYQEHVKQLIEKmEAEREQLLAEQE------RM 266
|
90 100
....*....|....*....|....*.
gi 768025295 360 LERELKQQRE-STQAVEAKAQQLQEE 384
Cdd:pfam02841 267 LEHKLQEQEElLKEGFKTEAESLQKE 292
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
294-509 |
8.40e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 294 RAQLEEAEGQKDGLRKQAGKLEQALKQEQgarRRQAEEdeqclsEWEHDKQQLltetsdlktkmatlERELKQQRESTQA 373
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEA---LLEAKE------EIHKLRNEF--------------EKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768025295 374 VEAKAQQLQEEGERRAAAerqvqqleeqvqqleaqvqllvgrLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRA 453
Cdd:PRK12704 87 LEKRLLQKEENLDRKLEL------------------------LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768025295 454 LLKQLDSLDQE--REELRGSL-DEAEAQRA----RVEEQLQSEREQgqcqlRAQQELLQSLQR 509
Cdd:PRK12704 143 ELERISGLTAEeaKEILLEKVeEEARHEAAvlikEIEEEAKEEADK-----KAKEILAQAIQR 200
|
|
| |
