|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
185-432 |
5.34e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 185 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLltetSDLKT 264
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR----RELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 265 KMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEgagqqvcwASTELDKEKA 344
Cdd:COG1196 317 RLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--------AEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 345 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 424
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
....*...
gi 1370482396 425 QATTDLRL 432
Cdd:COG1196 467 ELLEEAAL 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
183-426 |
7.43e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 7.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 183 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDL 262
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 263 KTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwASTELDKE 342
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA---EEALLERL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 343 KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQG 422
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
....
gi 1370482396 423 LEQA 426
Cdd:COG1196 497 LEAE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
185-431 |
6.27e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 185 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQQLLTETSDLKT 264
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----LEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 265 KMATLERELKQQRESTQAVEAKAQQLQEEgerRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKA 344
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 345 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLE 424
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
....*..
gi 1370482396 425 QATTDLR 431
Cdd:COG1196 453 ELEEEEE 459
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-431 |
1.43e-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: 74.32 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 186 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQagklEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTK 265
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKE----LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 266 MATLERELKQQRESTQAVEAKAQQLQeegERRAAAERQVQQLEEQVQQLEAQVQLLvgrlegagqqvcwaSTELDKEKAR 345
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELE---AQIEQLKEELKALREALDELRAELTLL--------------NEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 346 VDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS---EREQGQCQLRAQQELLQSLQREKQG 422
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSEELRE 905
|
....*....
gi 1370482396 423 LEQATTDLR 431
Cdd:TIGR02168 906 LESKRSELR 914
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
189-441 |
1.58e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 189 RKDLTRlskhVEALRAQLEeaeGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqCLSEWEH---DKQQLLTETSDLKTK 265
Cdd:COG1196 185 EENLER----LEDILGELE---RQLEPLERQAEKAERYRELKEELKELEAEL---LLLKLREleaELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 266 MATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwASTELDKEKAR 345
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE---LEEELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 346 VDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQEL----------LQS 415
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELaaqleeleeaEEA 411
|
250 260
....*....|....*....|....*.
gi 1370482396 416 LQREKQGLEQATTDLRLTILELEREL 441
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEE 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-426 |
1.08e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 186 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQ-------QLLTE 258
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE----ISRLEQQKQilrerlaNLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 259 TSDLKTKMATLERELKQQRESTQAVEAKAQQLQE--EGERRAAAERQVQQLEEQVQQLEAQVQL--LVGRLEGAGQQVCW 334
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEelESLEAELEELEAELEELESRLEELEEQLetLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 335 ASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQER-----EELRGSLDEAEAQRARVEEQLQSEREQ-------- 401
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREEleeaeqal 477
|
250 260 270
....*....|....*....|....*....|
gi 1370482396 402 -----GQCQLRAQQELLQSLQREKQGLEQA 426
Cdd:TIGR02168 478 daaerELAQLQARLDSLERLQENLEGFSEG 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-442 |
1.90e-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: 70.86 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 187 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQeqgaRRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 266
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 267 ATLERELKqqrESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 346
Cdd:TIGR02168 750 AQLSKELT---ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 347 DSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS---EREQGQCQLRAQQELLQSLQREKQGL 423
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnERASLEEALALLRSELEELSEELREL 906
|
250
....*....|....*....
gi 1370482396 424 EQATTDLRLTILELERELE 442
Cdd:TIGR02168 907 ESKRSELRRELEELREKLA 925
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
185-416 |
7.69e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 185 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKT 264
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 265 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAA----ERQVQQLEEQVQQLEAQVQLLVGRLEgagqqvcwASTELD 340
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALlerlERLEEELEELEEALAELEEEEEEEEE--------ALEEAA 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370482396 341 KEKARVDsmvRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSL 416
Cdd:COG1196 449 EEEAELE---EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
185-429 |
1.78e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 185 AAEQRKDLTRLSKHVE------ALRAQLEEAEGQKDGLRKQA--GKLEQALKQEQGARRRQAEEDEQcLSEWEHDKQQLL 256
Cdd:TIGR02168 195 LNELERQLKSLERQAEkaerykELKAELRELELALLVLRLEElrEELEELQEELKEAEEELEELTAE-LQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 257 TETSDLKTKMATLERELKqqrESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAS 336
Cdd:TIGR02168 274 LEVSELEEEIEELQKELY---ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 337 TELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE---EQLQSEREQGQCQLRAQQELL 413
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarlERLEDRRERLQQEIEELLKKL 430
|
250
....*....|....*.
gi 1370482396 414 QSLQREKQGLEQATTD 429
Cdd:TIGR02168 431 EEAELKELQAELEELE 446
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
201-426 |
1.55e-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: 63.24 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 201 ALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEdeqcLSEWEHDKQQLLTETSDLKTKMATLERELKQQREST 280
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 281 QAVEAKAQQLQEE-GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwastelDKEKARVDSMVRHQESLQAK 359
Cdd:COG4942 93 AELRAELEAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-------PARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 360 QRALLKQLDSLD---QEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLEQA 426
Cdd:COG4942 166 RAELEAERAELEallAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-425 |
1.80e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 185 AAEQRKDLTRLSKHVEALRAQ---LEEAEGQKDGLRKQAGKLEQalkQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSD 261
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQielLEPIRELAERYAAARERLAE---LEYLRAALRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 262 LKTKMATLERELKQQREstQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwasteldk 341
Cdd:COG4913 307 LEAELERLEARLDALRE--ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL--------- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 342 ekarvdsmVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSereqgqcqlraqqellqsLQREKQ 421
Cdd:COG4913 376 --------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE------------------LEAEIA 429
|
....
gi 1370482396 422 GLEQ 425
Cdd:COG4913 430 SLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
193-434 |
1.83e-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: 64.32 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 193 TRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWE---HDKQQLLTETSDLKTKMATL 269
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 270 ERELKQQRESTQAVEAKAQQLQEE-GERRAAAE----RQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKA 344
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDlHKLEEALNdleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 345 RVDSMVRHqesLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE----------EQLQSEREQGQCQLRAQQELLQ 414
Cdd:TIGR02169 830 YLEKEIQE---LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaalrdlesrlGDLKKERDELEAQLRELERKIE 906
|
250 260
....*....|....*....|
gi 1370482396 415 SLQREKQGLEQATTDLRLTI 434
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKL 926
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
189-439 |
1.96e-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: 64.32 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 189 RKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLE--QALKqeqgARRRQAEEDEQcLSEW---EHDKQQLLTETSDLK 263
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALL----KEKREYEGYEL-LKEKealERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 264 TKMATLERELKQQRESTQAVEAKAQQLQEE-----GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTE 338
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 339 LDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDE--AEAQRARVE--------EQLQSEREQGQCQLRA 408
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdKEFAETRDElkdyreklEKLKREINELKRELDR 410
|
250 260 270
....*....|....*....|....*....|.
gi 1370482396 409 QQELLQSLQREKQGLEQATTDLRLTILELER 439
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
194-415 |
2.11e-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: 60.85 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 194 RLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQC---LSEWEHDKQQLLTETSDLKTKMATLE 270
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELereIEEERKRRDKLTEEYAELKEELEDLR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 271 RELKQQRESTQAVEAKAQQLQEE----GERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwasTELDKEKARV 346
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKleklKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI----NELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 347 DSMVRHQE-----------SLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEqlqsereqGQCQLRAQQELLQS 415
Cdd:TIGR02169 447 ALEIKKQEwkleqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE--------RVRGGRAVEEVLKA 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
175-431 |
4.81e-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: 58.62 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 175 PLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgaRRRQAEEDEQclsewehdkQQ 254
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA--RRIRALEQEL---------AA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 255 LLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGErraaaerqvqqleeqvqqleaqVQLLVGRlEGAGQqvcw 334
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPP----------------------LALLLSP-EDFLD---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 335 asteldkekarvdsMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE---QLQSEREQGQCQLRAQQE 411
Cdd:COG4942 134 --------------AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAllaELEEERAALEALKAERQK 199
|
250 260
....*....|....*....|
gi 1370482396 412 LLQSLQREKQGLEQATTDLR 431
Cdd:COG4942 200 LLARLEKELAELAAELAELQ 219
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-401 |
1.94e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 186 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAlkQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLktk 265
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASSDDL--- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 266 mATLERELKQQRESTQAVEAKAQQLQEEgERRAAAERQvqqleeqvqQLEAQVQLLVGRLEGAGQQVC-WASTELDKEKA 344
Cdd:COG4913 688 -AALEEQLEELEAELEELEEELDELKGE-IGRLEKELE---------QAEEELDELQDRLEAAEDLARlELRALLEERFA 756
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370482396 345 rvdsmvrhqeslQAKQRALLKQLdsldqeREELRGSLDEAEAQRARVEEQLQSEREQ 401
Cdd:COG4913 757 ------------AALGDAVEREL------RENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
162-384 |
2.68e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 162 QFQQLVQDSMGLRPLpAATVGRWAAEQRKDLtrLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRrqaeed 241
Cdd:COG4913 263 RYAAARERLAELEYL-RAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEARLDALREELDELEAQIR------ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 242 eqclsewEHDKQQLltetSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAerqvqqleeqvqqLEAQVQLL 321
Cdd:COG4913 334 -------GNGGDRL----EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE-------------FAALRAEA 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370482396 322 VGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEA 384
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
200-423 |
3.22e-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: 56.44 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 200 EALRAQLEEAegqkdglRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKqqlltetSDLKTKMATLERELKQQRES 279
Cdd:pfam07888 30 ELLQNRLEEC-------LQERAELLQAQEAANRQREKEKERYKRDREQWERQR-------RELESRVAELKEELRQSREK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 280 TQAVEAKAQQLQEEGERRAAAERqvqQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRH------- 352
Cdd:pfam07888 96 HEELEEKYKELSASSEELSEEKD---ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQrkeeeae 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 353 QESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE-------------QLQSEREQGQCQLRAQQELLQSLQRE 419
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDtittltqklttahRKEAENEALLEELRSLQERLNASERK 252
|
....
gi 1370482396 420 KQGL 423
Cdd:pfam07888 253 VEGL 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-403 |
9.13e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 200 EALRAQLEEA-EGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWehdkQQLLTETSDLKTKMATLERELKQQRE 278
Cdd:COG4717 41 AFIRAMLLERlEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 279 STQAVEaKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVG---RLEGAGQQVCWASTELDKEKARVDSMVRHQ-E 354
Cdd:COG4717 117 ELEKLE-KLLQLLPLYQELEALEAELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEEElQ 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1370482396 355 SLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQ 403
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
251-441 |
1.93e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 251 DKQQLLTETSDLKTKMATLER------ELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLeaQVQLLVGR 324
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahealeDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR--RLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 325 LEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRAL-LKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS------ 397
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAAlglplp 376
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1370482396 398 -EREQGQCQLRAQQELLQSLQREKQGLEQATTDLRLTILELEREL 441
Cdd:COG4913 377 aSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
185-419 |
2.35e-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: 54.19 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 185 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALK-------QEQGARRRQAEEDEQC---------LSEW 248
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiQYQQAVQALEKARALCglpdltpenAEDY 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 249 EH---DKQQLLTETS-DLKTKMATLERELKQQRESTQAVEAKAqqlqEEGERRAAAERqvqqlEEQVQQLEAQVQLLVGR 324
Cdd:COG3096 443 LAafrAKEQQATEEVlELEQKLSVADAARRQFEKAYELVCKIA----GEVERSQAWQT-----ARELLRRYRSQQALAQR 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 325 LEGAGQQVcwasTELDKEKARvdsmvrhQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQgQC 404
Cdd:COG3096 514 LQQLRAQL----AELEQRLRQ-------QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ-RS 581
|
250
....*....|....*
gi 1370482396 405 QLRAQQELLQSLQRE 419
Cdd:COG3096 582 ELRQQLEQLRARIKE 596
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
264-432 |
4.26e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 264 TKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQL--LVGRLEGAGQQVCWASTELDK 341
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 342 EKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQ 421
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170
....*....|.
gi 1370482396 422 GLEQATTDLRL 432
Cdd:COG4717 231 QLENELEAAAL 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
248-434 |
5.01e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 248 WEHDKQQLLTET----SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEG----ERRAAAERQVQQLEEQVQQLEAQVQ 319
Cdd:COG4913 590 HEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELdalqERREALQRLAEYSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 320 LL-----VGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAE-----AQRA 389
Cdd:COG4913 670 IAeleaeLERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdlarlELRA 749
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1370482396 390 RVEEQLQSEREQGQcQLRAQQELLQSLQREKQGLEQATTDLRLTI 434
Cdd:COG4913 750 LLEERFAAALGDAV-ERELRENLEERIDALRARLNRAEEELERAM 793
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
187-431 |
6.11e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 187 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQC-------LSEWEHDKQQLLTET 259
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELeelleqlSLATEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 260 SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAER-------------------QVQQLEEQVQQLEAQVQL 320
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallgLGGSLLSLILTIAGVLFL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 321 LVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLD-SLDQEREELR------GSLDEAEAQRARVEE 393
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLelldriEELQELLREAEELEE 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1370482396 394 QLQSEREQGQCQ-------------LRAQQELLQSLQREKQGLEQATTDLR 431
Cdd:COG4717 362 ELQLEELEQEIAallaeagvedeeeLRAALEQAEEYQELKEELEELEEQLE 412
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
186-431 |
6.95e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 186 AEQRKDLTRLskhVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSewehdkqqlltETSDLKTK 265
Cdd:PRK02224 515 EERREDLEEL---IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE-----------EVAELNSK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 266 MATLERE---LKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAgqqvcwASTELDKE 342
Cdd:PRK02224 581 LAELKERiesLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA------RIEEARED 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 343 KARVDSmvrHQESLQAKqrallkqLDSLDQEREELRGSLDEAEAQRARVEEqLQSEREqgqcQLRAQQELLQSLQREKQG 422
Cdd:PRK02224 655 KERAEE---YLEQVEEK-------LDELREERDDLQAEIGAVENELEELEE-LRERRE----ALENRVEALEALYDEAEE 719
|
....*....
gi 1370482396 423 LEQATTDLR 431
Cdd:PRK02224 720 LESMYGDLR 728
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
184-430 |
1.12e-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: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 184 WAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ---EQGARRRQAEEDEQCLSEWEHDKQQLLTETS 260
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNsesENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 261 DLKTKMATLERELKQQRESTQAVEAKAQQLQEEGErraaaerqvqqleeqvqqleaqvqllvgrlegagqqvcwastELD 340
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE------------------------------------------LLE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 341 KEKARVDSMVRHQES----LQAKQRALLKQLDSLDQEREELRGSLDEAEAQRarveEQLQSEREQGQCQLRAQQELLQSL 416
Cdd:TIGR04523 426 KEIERLKETIIKNNSeikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI----NKIKQNLEQKQKELKSKEKELKKL 501
|
250
....*....|....
gi 1370482396 417 QREKQGLEQATTDL 430
Cdd:TIGR04523 502 NEEKKELEEKVKDL 515
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
186-432 |
6.56e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 186 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQclsewehdkQQLLTETSDLKTK 265
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQL---------AEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 266 MATLERELKQQRESTQAVEAkAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwasteLDKEKAR 345
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ-------LQQEAQR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 346 VDSMVRHQ-ESLQAKQRALLKQLDSLDQEREElrgsLDEAEAQRARVEEQLQSEREQgqcqlraQQELLQSLQREKQGLE 424
Cdd:COG3206 314 ILASLEAElEALQAREASLQAQLAQLEARLAE----LPELEAELRRLEREVEVAREL-------YESLLQRLEEARLAEA 382
|
....*...
gi 1370482396 425 QATTDLRL 432
Cdd:COG3206 383 LTVGNVRV 390
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
219-428 |
1.71e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 219 QAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE-GERR 297
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 298 AAAERQVQQLEEQVQQLEAQ-VQLLVGRLEGAgqqvcwaSTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREE 376
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSEsFSDFLDRLSAL-------SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1370482396 377 LRGSLDEAEAQRARVEEQLQSEREqgqcQLRAQQELLQSLQREKQGLEQATT 428
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSA----EEAAAEAQLAELEAELAAAEAAAA 213
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
190-383 |
2.36e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 190 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEqgarRRQAEEDEQCLSEWEHDK--QQLLTETSDLKTKMA 267
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQLGNVRNNKeyEALQKEIESLKRRIS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 268 TLERELKQQREstqAVEAKAQQLQEEGERRAAAErqvqqleeqvqqleaqvqllvgrlegagqqvcwasTELDKEKARVD 347
Cdd:COG1579 107 DLEDEILELME---RIEELEEELAELEAELAELE-----------------------------------AELEEKKAELD 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 1370482396 348 smvrhqeslqAKQRALLKQLDSLDQEREELRGSLDE 383
Cdd:COG1579 149 ----------EELAELEAELEELEAEREELAAKIPP 174
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
176-425 |
2.50e-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: 47.53 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 176 LPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR--RQAEEDeqcLSEWEHDKQ 253
Cdd:pfam12128 587 LKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTalKNARLD---LRRLFDEKQ 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 254 QLltetSDLKTKmaTLERELKQQRESTQAVEAKAQQLqeEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVc 333
Cdd:pfam12128 664 SE----KDKKNK--ALAERKDSANERLNSLEAQLKQL--DKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL- 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 334 waSTELDKEKARVDsmvRHQESLQAKQRALLKQLD-------SLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQL 406
Cdd:pfam12128 735 --KAAIAARRSGAK---AELKALETWYKRDLASLGvdpdviaKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRR 809
|
250
....*....|....*....
gi 1370482396 407 RAQQELLQSLQREKQGLEQ 425
Cdd:pfam12128 810 PRLATQLSNIERAISELQQ 828
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
178-414 |
2.54e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 178 AATVGRWAAEQRKD-LTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLL 256
Cdd:PTZ00121 1344 AAEAAKAEAEAAADeAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 257 TETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQvcwaS 336
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK----A 1499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 337 TELDK---EKARVDSMVRHQESLQAKQRALLKQLDSLDQER--------EELRGSLDEAEAQRARVEEQLQSEREQGQCQ 405
Cdd:PTZ00121 1500 DEAKKaaeAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaeekkkaDELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
....*....
gi 1370482396 406 LRAQQELLQ 414
Cdd:PTZ00121 1580 LRKAEEAKK 1588
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
161-426 |
2.69e-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: 47.64 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 161 GQFQQLVQ------DSMGLRPLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAegqkDGLRKQAGKLEQALKQEQGAR 234
Cdd:COG3096 413 IQYQQAVQalekarALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVA----DAARRQFEKAYELVCKIAGEV 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 235 RRQA--EEDEQCLSEWEhDKQQLLTETSDLKTKMATLERELKQQREstqaveakAQQLQEEGERRAAAERqvqqleeqvq 312
Cdd:COG3096 489 ERSQawQTARELLRRYR-SQQALAQRLQQLRAQLAELEQRLRQQQN--------AERLLEEFCQRIGQQL---------- 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 313 QLEAQVQLLVGRLEgagQQVCWASTELDKEKARVDSMVRHQESLQAKQRAL-------LKQLDSLDQEREELRGSLDEAE 385
Cdd:COG3096 550 DAAEELEELLAELE---AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawLAAQDALERLREQSGEALADSQ 626
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1370482396 386 AQRARVEEQLQSERE--QGQCQLRAQQellQSLQREKQGLEQA 426
Cdd:COG3096 627 EVTAAMQQLLEREREatVERDELAARK---QALESQIERLSQP 666
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
185-399 |
3.10e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 185 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALkqeqgARRRQAEEDEQCLSEWEHDKQQLltetSDLKT 264
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERL----EELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 265 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERqvqqleeqvqqleaqvqllvgrlegagqqvcwasteldkekA 344
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATE-----------------------------------------E 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370482396 345 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLD--EAEAQRARVEEQLQSER 399
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEAR 249
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
183-301 |
3.14e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 183 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRK-----QAGKLEQALKQEQGARR----RQAEEDEQCLSEWEHDKQ 253
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKaeeenKIKAAEEAKKAEEDKKKaeeaKKAEEDEKKAAEALKKEA 1698
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1370482396 254 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQ--EEGERRAAAE 301
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKkeAEEDKKKAEE 1748
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
187-425 |
3.74e-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: 47.27 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 187 EQRKDLTRLSKHVEALRAQLEEAEGQkdgLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQlltETSDLKTKM 266
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAY---LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ---ERINRARKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 267 ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVG------RLEGAGQQVCWASTELD 340
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsqeiHIRDAHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 341 KEKARVDSMVRHQESLQA-------------KQRALLKQLDSLDQEREELRGSLDEAEA----QRARVEEQLQSEREQGQ 403
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTltqklqslckeldILQREQATIDTRTSAFRDLQGQLAHAKKqqelQQRYAELCAAAITCTAQ 452
|
250 260
....*....|....*....|....*
gi 1370482396 404 CQL---RAQQELLQSLQREKQGLEQ 425
Cdd:TIGR00618 453 CEKlekIHLQESAQSLKEREQQLQT 477
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
186-429 |
4.05e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 186 AEQRKDLTRLSKHVEALRA-QLEEAEGQK--DGLRK--------QAGKLEQALKQEQ--GARRRQAEEDEQCLSEWEHDK 252
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKAdEAKKAEEKKkaDELKKaeelkkaeEKKKAEEAKKAEEdkNMALRKAEEAKKAEEARIEEV 1597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 253 QQLLTETSDLKTKMATLERELKqqrestqaveAKAQQLQEEGERRAAAERQVQQLEEQVQQLEaQVQllvgrlegAGQQV 332
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAK----------IKAEELKKAEEEKKKVEQLKKKEAEEKKKAE-ELK--------KAEEE 1658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 333 CWASTELDKEKARVDSmvRHQESLQAKQRALLKQLDSLDQEREELRGS--LDEAEAQRARVEEQLQSEREQGQCQLraqQ 410
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAEELKKAEEENKIKA---E 1733
|
250
....*....|....*....
gi 1370482396 411 ELLQSLQREKQGLEQATTD 429
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKD 1752
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
187-395 |
5.13e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 187 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEqALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKm 266
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 267 atlERELKQQRESTQAVEAKAQQ---LQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWAS---TELD 340
Cdd:PRK03918 275 ---IEELEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKkklKELE 351
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 341 KEKARVDSMVRHQESLqakqRALLKQLDSLDQER-----EELRGSLDEAEAQRARVEEQL 395
Cdd:PRK03918 352 KRLEELEERHELYEEA----KAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEI 407
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
341-441 |
5.91e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 341 KEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVE---EQLQSEREQGQCQLRAQQELLQSLQ 417
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100
....*....|....*....|....
gi 1370482396 418 REKQGLEQATTDLRLTILELEREL 441
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDL 774
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
178-433 |
6.71e-05 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 46.14 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 178 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSewehDKQQLLT 257
Cdd:COG5281 173 AAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAAS----AAAQALA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 258 ETSDLKTKMATLERELKQQRESTQAVEAKAQQL--QEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwA 335
Cdd:COG5281 249 ALAAAAAAAALALAAAAELALTAQAEAAAAAAAaaAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALR--A 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 336 STELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQS 415
Cdd:COG5281 327 AAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWAAGAKAALAEYADSATNVAAQVAQA 406
|
250
....*....|....*...
gi 1370482396 416 LQREKQGLEQATTDLRLT 433
Cdd:COG5281 407 ATSAFSGLTDALAGAVTT 424
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
178-433 |
7.09e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 178 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLE---QALKQEQGARRRQAEEDEQCLSEWEHD--- 251
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEdflEELREERDELREREAELEATLRTARERvee 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 252 KQQLLTE------------------TSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERqvqqleeQVQQ 313
Cdd:PRK02224 445 AEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIER-------LEER 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 314 LEAQVQLLVGRLEGAGQQVCWAStELDKEKARVDSMVRHQESLQAKQR-----------ALLKQLDSLDQEREEL---RG 379
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAE-ELRERAAELEAEAEEKREAAAEAEeeaeeareevaELNSKLAELKERIESLeriRT 596
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1370482396 380 SLDEAEAQRARVEEqLQSEREQGQCQLRAQQELLQSLQREKQGLEQATTDLRLT 433
Cdd:PRK02224 597 LLAAIADAEDEIER-LREKREALAELNDERRERLAEKRERKRELEAEFDEARIE 649
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
253-426 |
7.18e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 253 QQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERraaaerqvqqleeqvqqLEAQVQLLVGRLEGAGQQV 332
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ-----------------LEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 333 CWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQ-GQCQLRAQQE 411
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElAALEQELQAL 176
|
170
....*....|....*
gi 1370482396 412 LLQSLQREKQGLEQA 426
Cdd:COG4372 177 SEAEAEQALDELLKE 191
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
186-431 |
7.41e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 186 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ----------------EQGARRRQAEEDEQCLSEWE 249
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREleerieelkkeieeleEKVKELKELKEKAEEYIKLS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 250 HDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEaQVQLLVGRLEGAG 329
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 330 QQVcwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRAR--VEEQLQSEREQGQCqLR 407
Cdd:PRK03918 379 KRL--TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKEL-LE 455
|
250 260
....*....|....*....|....
gi 1370482396 408 AQQELLQSLQREKQGLEQATTDLR 431
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLR 479
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
178-415 |
7.67e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 178 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEgqkDGLRKQAgKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT 257
Cdd:pfam05557 36 ASALKRQLDRESDRNQELQKRIRLLEKREAEAE---EALREQA-ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 258 ETSDLKTKMATLERELKQQRESTQAVEakaQQLQEEGERRAAAERQVQQLEEQVQQLEA---QVQLLVGRLEgagQQVCW 334
Cdd:pfam05557 112 ELSELRRQIQRAELELQSTNSELEELQ---ERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQ---SQEQD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 335 aSTELDKEKARVDSMVRhQESLQAKQRALLKQLDS-------LDQEREELRGSLDEAEAQRARVEEqLQSEREQGQCQLR 407
Cdd:pfam05557 186 -SEIVKNSKSELARIPE-LEKELERLREHNKHLNEnienkllLKEEVEDLKRKLEREEKYREEAAT-LELEKEKLEQELQ 262
|
....*...
gi 1370482396 408 AQQELLQS 415
Cdd:pfam05557 263 SWVKLAQD 270
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-541 |
8.84e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 186 AEQRKDLTRlsKHVEALRAQLEEAEGQKDGLRKQAgklEQALKqeqgARRRQAEEDEqclseweHDKQQLLTETSDLKTK 265
Cdd:TIGR02168 177 TERKLERTR--ENLDRLEDILNELERQLKSLERQA---EKAER----YKELKAELRE-------LELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 266 MATLERELKQQRESTQAVEAKAQQLQEEGE--RRAAAERQvqqleeqvqqleAQVQLLVGRLEGAGQqvcwasteldkEK 343
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEelRLEVSELE------------EEIEELQKELYALAN-----------EI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 344 ARVDSMVRHQeslQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQgqcqLRAQQELLQSLQREKQGL 423
Cdd:TIGR02168 298 SRLEQQKQIL---RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE----LESLEAELEELEAELEEL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 424 EQATTDLRLTIlelereleelkererllvafpdlhrptETQihgpvplgtggRSSSVEsqitcptdsgnvtdhMERQVQS 503
Cdd:TIGR02168 371 ESRLEELEEQL---------------------------ETL-----------RSKVAQ---------------LELQIAS 397
|
330 340 350
....*....|....*....|....*....|....*...
gi 1370482396 504 NDIRIRVLQEENGRLQSMLSKIREVAQQGGLKLIPQDR 541
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
156-426 |
1.06e-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: 45.27 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 156 LPSSLGQFQQLVQDSMGLRPLPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR 235
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 236 RQAEEDEQCLSEWEHDKQQLLTETSDLKT-KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAaERQVQQLEEQVQQL 314
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTlTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-QAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 315 EAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQ---ESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARV 391
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEaenEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1370482396 392 EEQL-QSEREQGQCQLRAQQELLQ------SLQREKQGLEQA 426
Cdd:pfam07888 271 QAELhQARLQAAQLTLQLADASLAlregraRWAQERETLQQS 312
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
191-296 |
1.13e-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: 45.44 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 191 DLTRLSKHVEALRAQLEEAEGQKDGLRKQAgkleQALKQEQGarrrQAEEDEQCLSE----WEHDKQQLLTETSDLKTKM 266
Cdd:pfam05911 703 ELASCTENLESTKSQLQESEQLIAELRSEL----ASLKESNS----LAETQLKCMAEsyedLETRLTELEAELNELRQKF 774
|
90 100 110
....*....|....*....|....*....|
gi 1370482396 267 ATLERELKQQRESTQAVEAKAQQLQEEGER 296
Cdd:pfam05911 775 EALEVELEEEKNCHEELEAKCLELQEQLER 804
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
186-431 |
1.17e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 186 AEQRKDLTRLSKHVEALRAQ--------------LEEAEGQKDGLRKQAGKLEQALKQEQGARRR--------------- 236
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERfgdapvdlgnaedfLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgq 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 237 ---------QAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLE---------RELKQQRE-STQAVEAKAQQLQEEGERR 297
Cdd:PRK02224 460 pvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlveaedriERLEERREdLEELIAERRETIEEKRERA 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 298 AAAERQVQQLEEQVQQLEAQVQllvgRLEGAGQQVCWASTELDKEKARVDSMVrhqESLqAKQRALLKQLDSLDQEREEL 377
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAA----EAEEEAEEAREEVAELNSKLAELKERI---ESL-ERIRTLLAAIADAEDEIERL 611
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370482396 378 ---RGSLDEAEAQRarvEEQLQSEREQGQcQLRAQ------QELLQSLQREKQGLEQATTDLR 431
Cdd:PRK02224 612 rekREALAELNDER---RERLAEKRERKR-ELEAEfdeariEEAREDKERAEEYLEQVEEKLD 670
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
197-413 |
1.23e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 197 KHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQ-----EQGARRRQAEEDEqcLSEWEHDKQQLLTETSDLKTKMATLER 271
Cdd:pfam00038 54 KEIEDLRRQLDTLTVERARLQLELDNLRLAAEDfrqkyEDELNLRTSAEND--LVGLRKDLDEATLARVDLEAKIESLKE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 272 EL---------------KQQRESTQAVEAKAQQLQEEG----ERRAA----AERQVQQLEEQVQQLEAQVQLLVGRlegA 328
Cdd:pfam00038 132 ELaflkknheeevrelqAQVSDTQVNVEMDAARKLDLTsalaEIRAQyeeiAAKNREEAEEWYQSKLEELQQAAAR---N 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 329 GQQVCWASTELdkekarvdSMVRHQ-ESLQAKQRALLKQLDSLDQEREEL--RGSLDEAEAQR--ARVEEQLQSEREQGQ 403
Cdd:pfam00038 209 GDALRSAKEEI--------TELRRTiQSLEIELQSLKKQKASLERQLAETeeRYELQLADYQEliSELEAELQETRQEMA 280
|
250
....*....|
gi 1370482396 404 CQLRAQQELL 413
Cdd:pfam00038 281 RQLREYQELL 290
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
187-424 |
1.32e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 187 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQA--------------EEDEQCLSEWEHDK 252
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEelerlkkrltgltpEKLEKELEELEKAK 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 253 QQLLTETSDLKTKMATLERELKQQRESTQAVE-AKA------QQLQEEGERRAAAErqvqqleeqvqqLEAQVQLLVGRL 325
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKkAKGkcpvcgRELTEEHRKELLEE------------YTAELKRIEKEL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 326 EGAGQQVcwasTELDKEKARVDsMVRHQESLQAKQRALLKQLDSLD---------------QEREELRGSLDEAEAQRAR 390
Cdd:PRK03918 469 KEIEEKE----RKLRKELRELE-KVLKKESELIKLKELAEQLKELEeklkkynleelekkaEEYEKLKEKLIKLKGEIKS 543
|
250 260 270
....*....|....*....|....*....|....
gi 1370482396 391 VEEQLQSEREQgQCQLRAQQELLQSLQREKQGLE 424
Cdd:PRK03918 544 LKKELEKLEEL-KKKLAELEKKLDELEEELAELL 576
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
186-292 |
1.45e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 186 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEqclsewehdkqqlltETSDLKTK 265
Cdd:COG2433 409 TEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR---------------EISRLDRE 473
|
90 100
....*....|....*....|....*..
gi 1370482396 266 MATLERELKQQRESTQAVEAKAQQLQE 292
Cdd:COG2433 474 IERLERELEEERERIEELKRKLERLKE 500
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
252-430 |
1.54e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 252 KQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleEQVQQLEAQVQLLVGRLEGAGQQ 331
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK---------------NGLVDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 332 VCWASTELDKEKARVDSMVRHQESLQAKQ---------RALLKQLDSLDQEREELRGSLDE-------AEAQRARVEEQL 395
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQL 307
|
170 180 190
....*....|....*....|....*....|....*....
gi 1370482396 396 QSEREQGQCQLRAQQELLQ----SLQREKQGLEQATTDL 430
Cdd:COG3206 308 QQEAQRILASLEAELEALQareaSLQAQLAQLEARLAEL 346
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
187-301 |
1.58e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 187 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKqeqgARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 266
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE----DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
90 100 110
....*....|....*....|....*....|....*
gi 1370482396 267 ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAE 301
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERVRGGRAVE 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
178-419 |
1.67e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 178 AATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT 257
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 258 EtsDLKTKMATLERELKQqrESTQAVEAKAQQLQeegERRAAAERqvqqleeqvqqleaqVQLLVGRLEGAGQQVCWAST 337
Cdd:COG4717 366 E--ELEQEIAALLAEAGV--EDEEELRAALEQAE---EYQELKEE---------------LEELEEQLEELLGELEELLE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 338 ELDKE--KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELR--GSLDEAEAQRARVEEQLQSEREQGQcQLRAQQELL 413
Cdd:COG4717 424 ALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWA-ALKLALELL 502
|
....*.
gi 1370482396 414 QSLQRE 419
Cdd:COG4717 503 EEAREE 508
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
183-426 |
2.88e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 183 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALkqeqgarrrqaeedeqclseweHDKQQLLTETSDL 262
Cdd:pfam01576 426 RQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL----------------------QDTQELLQEETRQ 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 263 KTKMATLERELKQQRESTQaveakaQQLQEEGERRAAAERqvqqleeqvqqleaqvqllvgrlegagqQVCWASTELDKE 342
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQ------EQLEEEEEAKRNVER----------------------------QLSTLQAQLSDM 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 343 KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARveeqLQSEREQGQCQLRAQQELLQSLQREKQG 422
Cdd:pfam01576 530 KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR----LQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
....
gi 1370482396 423 LEQA 426
Cdd:pfam01576 606 FDQM 609
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
235-412 |
3.27e-04 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 42.34 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 235 RRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMAtlERELKQQRESTQAVEAKAQQLQEegERRAAAERqvqqleeqvQQL 314
Cdd:pfam15665 52 KRRIQTLEESLEQHERMKRQALTEFEQYKRRVE--ERELKAEAEHRQRVVELSREVEE--AKRAFEEK---------LES 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 315 EAQVQllvgrlegagqqvcwASTELDKEKARVDSMVRHQ---ESLQAKQRAL--------LKQLDSLDQEREELRGSLDE 383
Cdd:pfam15665 119 FEQLQ---------------AQFEQEKRKALEELRAKHRqeiQELLTTQRAQsasslaeqEKLEELHKAELESLRKEVED 183
|
170 180
....*....|....*....|....*....
gi 1370482396 384 AEAQRARVEEqlQSEREQGQCQLRAQQEL 412
Cdd:pfam15665 184 LRKEKKKLAE--EYEQKLSKAQAFYEREL 210
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
185-425 |
3.27e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 185 AAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRK-------QAGKLEQALKQEQGARRRqAEEDEQCLSEwehDKQQLLT 257
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALARLEEETAQKNNALKkireleaQISELQEDLESERAARNK-AEKQRRDLGE---ELEALKT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 258 ETSDLKTKMATlERELKQQRES---------------------------TQAVEAKAQQLQEEGERRAAAERQVQQLEEQ 310
Cdd:pfam01576 307 ELEDTLDTTAA-QQELRSKREQevtelkkaleeetrsheaqlqemrqkhTQALEELTEQLEQAKRNKANLEKAKQALESE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 311 VQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRAR 390
Cdd:pfam01576 386 NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
250 260 270
....*....|....*....|....*....|....*...
gi 1370482396 391 VEEQLQSEREQGQCQLRAQQEL---LQSLQREKQGLEQ 425
Cdd:pfam01576 466 LESQLQDTQELLQEETRQKLNLstrLRQLEDERNSLQE 503
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
250-424 |
3.73e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 250 HDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAG 329
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 330 QQVcwaSTEldKEkarVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQ 409
Cdd:COG1579 83 GNV---RNN--KE---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170
....*....|....*
gi 1370482396 410 QELLQSLQREKQGLE 424
Cdd:COG1579 155 EAELEELEAEREELA 169
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
546-667 |
3.75e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 546 SSKGTQGATPPVQAKSTSPgPLGRQHLPSSRTGRTLLGQPCTSPPRQPCTSPPRQPCTSPPRQPCTSPSRQPCSQP-SKS 624
Cdd:PHA03247 2863 RRRPPSRSPAAKPAAPARP-PVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPrPQP 2941
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1370482396 625 LLEGVTHLDTCTQNPIKVLVRLRKRLSPGRGQASSAHQPQERP 667
Cdd:PHA03247 2942 PLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
176-435 |
4.98e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 176 LPAATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEG--QKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQ 253
Cdd:COG1196 540 LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 254 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVC 333
Cdd:COG1196 620 DTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 334 WASTELDKE-KARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEA-----------EAQRARVEEqLQSEREQ 401
Cdd:COG1196 700 LAEEEEERElAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdlEELERELER-LEREIEA 778
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1370482396 402 -GQCQLRAQQEL------LQSLQREKQGLEQATTDLRLTIL 435
Cdd:COG1196 779 lGPVNLLAIEEYeeleerYDFLSEQREDLEEARETLEEAIE 819
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
354-433 |
5.18e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 354 ESLQAKQRALLKQLDSLDQEREELRgSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQS---------LQREKQGLE 424
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQ-ALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEkaaetsqerKQKRKEITD 223
|
....*....
gi 1370482396 425 QATTDLRLT 433
Cdd:PRK11448 224 QAAKRLELS 232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
186-393 |
5.71e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 186 AEQRKDL-TRLSKH-VEALRAQLEEAEGQK---DGLRKQAGKLEQALKQEQGARRRQAEEDEQcLSEWEHDKQQLLTETS 260
Cdd:PRK03918 502 AEQLKELeEKLKKYnLEELEKKAEEYEKLKeklIKLKGEIKSLKKELEKLEELKKKLAELEKK-LDELEEELAELLKELE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 261 DLKTK-MATLERELKQ----QRESTQAVEAKaQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQ----- 330
Cdd:PRK03918 581 ELGFEsVEELEERLKElepfYNEYLELKDAE-KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkysee 659
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370482396 331 ---QVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEE 393
Cdd:PRK03918 660 eyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
188-398 |
6.03e-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: 41.83 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 188 QRKD--LTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLT-----ETS 260
Cdd:COG1579 13 QELDseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 261 DLKTKMATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleeqvqqleaqvqllvgrlegagqqvcwasteLD 340
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEE---------------------------------------------LA 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370482396 341 KEKARVDSMVRHQESLQAKqrallkqldsLDQEREELRGSLDEAEAQRARVEEQLQSE 398
Cdd:COG1579 128 ELEAELAELEAELEEKKAE----------LDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
181-282 |
6.84e-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: 42.44 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 181 VGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETS 260
Cdd:COG4942 144 LAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
90 100
....*....|....*....|..
gi 1370482396 261 DLKTKMATLERELKQQRESTQA 282
Cdd:COG4942 224 ELEALIARLEAEAAAAAERTPA 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
190-434 |
7.17e-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: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 190 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRqaeeDEQCLSEWEHDKQ---QLLTETSDLKTKM 266
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK----LELLLSNLKKKIQknkSLESQISELKKQN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 267 ATLERELKQQRESTQAVEAKAQQLQEEgerraaaerqvqqleeqVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 346
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQ-----------------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 347 DSMVRHQESL-QAKQRALLK----QLDSLDQEREELRGSLDEAEAQRARVEEQ----------LQSEREQGQCQLRAQQE 411
Cdd:TIGR04523 291 NQLKSEISDLnNQKEQDWNKelksELKNQEKKLEEIQNQISQNNKIISQLNEQisqlkkeltnSESENSEKQRELEEKQN 370
|
250 260 270
....*....|....*....|....*....|
gi 1370482396 412 LLQSLQREKQG-------LEQATTDLRLTI 434
Cdd:TIGR04523 371 EIEKLKKENQSykqeiknLESQINDLESKI 400
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-401 |
8.88e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 199 VEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGAR---RRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQ 275
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKeylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 276 QRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRHQ-- 353
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEls 952
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370482396 354 -ESLQAKQRALLKQLDSLD-------QEREELRGSLDEAEAQRARVEEqlqsEREQ 401
Cdd:TIGR02169 953 lEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEE----ERKA 1004
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
179-423 |
9.07e-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: 42.19 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 179 ATVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAL----KQEQGARRRQAEEDEQC--LSEWEHDK 252
Cdd:pfam07888 139 KTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslsKEFQELRNSLAQRDTQVlqLQDTITTL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 253 QQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLlvgrlegagqQV 332
Cdd:pfam07888 219 TQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTL----------QL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 333 CWASTELDKEKARvdsMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQL----RA 408
Cdd:pfam07888 289 ADASLALREGRAR---WAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLsesrRE 365
|
250
....*....|....*...
gi 1370482396 409 QQEL---LQSLQREKQGL 423
Cdd:pfam07888 366 LQELkasLRVAQKEKEQL 383
|
|
| TelA |
pfam05816 |
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ... |
335-433 |
9.11e-04 |
|
Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like proteins. TelA and KlA are associated with tellurite resistance and plasmid fertility inhibition.
Pssm-ID: 461748 Cd Length: 330 Bit Score: 41.73 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 335 ASTELDKEKARVDSMVRH----QESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQ-----------RARVEEQLQSER 399
Cdd:pfam05816 79 AGNKIEKYFAKYQTAGAQidkiVVELEKGQDELLKDNAMLDQMYEKNLEYFKELEKYiaagelkleelDAELLPELEAKA 158
|
90 100 110
....*....|....*....|....*....|....*.
gi 1370482396 400 EQGQCQLRAQ--QELLQSLQRekqgLEQATTDLRLT 433
Cdd:pfam05816 159 AASGDPEDAQalRDLRQALFR----LEQRIHDLELQ 190
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
195-431 |
1.16e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 195 LSKHVEALRAQLEEAEGQKDGLRKQAGKLEQaLKQEQGARRrqaeEDEQCLSEWEHDKQQLLTETSDLKTKMATLErELK 274
Cdd:PRK04863 892 LADRVEEIREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQ----SDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVV 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 275 QQR-----ESTQAVEAKAQQLQEegerraaaerqvqqleeqvqqleaqvqLLVGRLEGAGQQVCWASTELDKEKARVDSM 349
Cdd:PRK04863 966 QRRahfsyEDAAEMLAKNSDLNE---------------------------KLRQRLEQAEQERTRAREQLRQAQAQLAQY 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 350 VRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARV-EEQL-------QSEREQGQCQLRAQQELLQSLQREKQ 421
Cdd:PRK04863 1019 NQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARArRDELharlsanRSRRNQLEKQLTFCEAEMDNLTKKLR 1098
|
250
....*....|
gi 1370482396 422 GLEQATTDLR 431
Cdd:PRK04863 1099 KLERDYHEMR 1108
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
187-429 |
1.18e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 187 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAgkleQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 266
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEEL----EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 267 ATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARV 346
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 347 DSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQGLEQA 426
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
...
gi 1370482396 427 TTD 429
Cdd:COG4372 320 ALL 322
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
199-426 |
1.28e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 199 VEALRAQLEEAEGQKDGLRKQAGKLEQALK-------QEQGARRRQAEEDEQC-LSEWEHDKQQLLTETSDLKTKMATLE 270
Cdd:PRK04863 378 QEENEARAEAAEEEVDELKSQLADYQQALDvqqtraiQYQQAVQALERAKQLCgLPDLTADNAEDWLEEFQAKEQEATEE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 271 -RELKQQRESTQAVE---AKAQQLQeegeRRAAAERQVQQLEEQVQQLEAQV---QLLVGRLEGAGQQVcwasTELDKEk 343
Cdd:PRK04863 458 lLSLEQKLSVAQAAHsqfEQAYQLV----RKIAGEVSRSEAWDVARELLRRLreqRHLAEQLQQLRMRL----SELEQR- 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 344 arvdsmVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQgQCQLRAQQELLQSLQREKQGL 423
Cdd:PRK04863 529 ------LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER-RMALRQQLEQLQARIQRLAAR 601
|
...
gi 1370482396 424 EQA 426
Cdd:PRK04863 602 APA 604
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
208-421 |
1.30e-03 |
|
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: 42.03 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 208 EAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEA-- 285
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEIsr 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 286 --KAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTE--------LDKEKARVDSMVRHQES 355
Cdd:pfam17380 377 mrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEarqrevrrLEEERAREMERVRLEEQ 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370482396 356 LQAKQRALLKQlDSLDQEREELRGSLDE-----AEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQREKQ 421
Cdd:pfam17380 457 ERQQQVERLRQ-QEEERKRKKLELEKEKrdrkrAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
181-434 |
1.40e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 181 VGRWAAEQRKDLTRLSKHVEA-----LRAQLEEAEGQKDGLRKQAGKLEQalKQEQGARRRqaEEDEQCLSEWEHDKQQL 255
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEkeekdLHERLNGLESELAELDEEIERYEE--QREQARETR--DEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 256 LT---ETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEE-GERRAAAERQVQQL---EEQVQQLEAQVQLLVGRLEGA 328
Cdd:PRK02224 254 ETleaEIEDLRETIAETEREREELAEEVRDLRERLEELEEErDDLLAEAGLDDADAeavEARREELEDRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 329 GQQVCWASTELDKEKARVDSmvRHQESLQAKQRAllkqlDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQ---GQCQ 405
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADD--LEERAEELREEA-----AELESELEEAREAVEDRREEIEELEEEIEELRERfgdAPVD 406
|
250 260
....*....|....*....|....*....
gi 1370482396 406 LRAQQELLQSLQREKQGLEQATTDLRLTI 434
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATL 435
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
237-426 |
1.42e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 237 QAEED-EQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLE 315
Cdd:PRK03918 186 KRTENiEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 316 AQVQLLVGRLEGAGQQVCwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEqL 395
Cdd:PRK03918 266 ERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE-L 343
|
170 180 190
....*....|....*....|....*....|.
gi 1370482396 396 QSEREQGQCQLRAQQELLQSLQREKQGLEQA 426
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
203-297 |
1.43e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 203 RAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEED---EQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRES 279
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELvalEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220
|
90
....*....|....*...
gi 1370482396 280 TQAVEAKAQQLQEEGERR 297
Cdd:PRK11448 221 ITDQAAKRLELSEEETRI 238
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
194-419 |
1.44e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 194 RLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQAL----------KQEQGARRRQAEEDEQCLSE-------WEHDKQQLL 256
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELddllvdldhqRQLVSNLEKKQKKFDQMLAEekaisarYAEERDRAE 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 257 TETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAA-----------ERQVQQLEEQVQQLEAQVQLLVGRL 325
Cdd:pfam01576 629 AEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknvhelERSKRALEQQVEEMKTQLEELEDEL 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 326 EGAGQQVCWASTELDKEKARVDSMVRHQESL-QAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS------- 397
Cdd:pfam01576 709 QATEDAKLRLEVNMQALKAQFERDLQARDEQgEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKEleaqida 788
|
250 260
....*....|....*....|....*
gi 1370482396 398 ---EREQGQCQLRAQQELLQSLQRE 419
Cdd:pfam01576 789 ankGREEAVKQLKKLQAQMKDLQRE 813
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
185-428 |
1.47e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 185 AAEQRKDLTRLSKHVEALRAQLEEA-------EGQKDGLRKQAGKLEQALkQEQGARRRQAEEDEQcLSEWEHDKQQLLT 257
Cdd:pfam19220 106 KEELRIELRDKTAQAEALERQLAAEteqnralEEENKALREEAQAAEKAL-QRAEGELATARERLA-LLEQENRRLQALS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 258 E-----TSDLKTKMATLERELKQQRESTQAVEAkaqQLQEEgerRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQV 332
Cdd:pfam19220 184 EeqaaeLAELTRRLAELETQLDATRARLRALEG---QLAAE---QAERERAEAQLEEAVEAHRAERASLRMKLEALTARA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 333 cwASTEldkekaRVDSMVRHQ-ESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQsEREQGQCQLRAQQE 411
Cdd:pfam19220 258 --AATE------QLLAEARNQlRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQ-EMQRARAELEERAE 328
|
250
....*....|....*...
gi 1370482396 412 LL-QSLQREKQGLEQATT 428
Cdd:pfam19220 329 MLtKALAAKDAALERAEE 346
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
252-388 |
1.88e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 39.55 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 252 KQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERqvqqleeqvQQLEAQVQLLVGRLEGAgqq 331
Cdd:PRK07352 52 REAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIR---------AEIEKQAIEDMARLKQT--- 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370482396 332 vcwASTELDKEKARVDSMVRHQESLQAKQRALlkqldsldqerEELRGSLDEAEAQR 388
Cdd:PRK07352 120 ---AAADLSAEQERVIAQLRREAAELAIAKAE-----------SQLPGRLDEDAQQR 162
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
195-293 |
2.07e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 195 LSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgarrRQAEEDEQCLSEWEHDKQQLLTetsdLKTKMATLERELK 274
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQ----EEVEELRKQLENYEKDKQSLKN----LKARLKVLEKELK 102
|
90
....*....|....*....
gi 1370482396 275 QQRESTQAVEAKAQQLQEE 293
Cdd:pfam13851 103 DLKWEHEVLEQRFEKVERE 121
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
183-426 |
2.27e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 183 RWAAEQRKDLTRlSKHVEALR-----AQLEEAEGQKDGLRKQAGKLEQALKQEQgarRRQAEE----DEQCLSEwEHDKQ 253
Cdd:PTZ00121 1230 KKAEEAKKDAEE-AKKAEEERnneeiRKFEEARMAHFARRQAAIKAEEARKADE---LKKAEEkkkaDEAKKAE-EKKKA 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 254 QLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQleeqvqqleaqvqllvgRLEGAGQQVC 333
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-----------------EAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 334 WASTELDKEKARVDSM------VRHQESLQAKQRALLKQLDSLDQEREELRgsldEAEAQRARVEEQLQSEREQGQCQLR 407
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAkkkaeeKKKADEAKKKAEEDKKKADELKKAAAAKK----KADEAKKKAEEKKKADEAKKKAEEA 1443
|
250
....*....|....*....
gi 1370482396 408 AQQELLQSLQREKQGLEQA 426
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEA 1462
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
187-434 |
2.40e-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: 41.16 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 187 EQRKDLTRLS-------KHVEaLRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTET 259
Cdd:TIGR04523 195 KLLKLELLLSnlkkkiqKNKS-LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 260 SDL---KTKMATLERELKQqrestqaVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQL-----LVGRLEgagQQ 331
Cdd:TIGR04523 274 KELeqnNKKIKELEKQLNQ-------LKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQIsqnnkIISQLN---EQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 332 VcwasTELDKEKARVDSM-VRHQESLQAKQrallKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcQLraqQ 410
Cdd:TIGR04523 344 I----SQLKKELTNSESEnSEKQRELEEKQ----NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ-QK---D 411
|
250 260
....*....|....*....|....
gi 1370482396 411 ELLQSLQREKQGLEQATTDLRLTI 434
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETI 435
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
199-421 |
2.78e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 199 VEALRAQLEEAEGQKDGLRKQAGKLEQalkqeqgaRRRQAEEDeqcLSEWEHDKQQLLTETSDLKTKMATLE-------- 270
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKE--------KRDELNEE---LKELAEKRDELNAQVKELREEAQELRekrdelne 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 271 --RELKQQRESTQaveAKAQQLQEEgerrAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAgQQVcwASTELDKEKARVDS 348
Cdd:COG1340 72 kvKELKEERDELN---EKLNELREE----LDELRKELAELNKAGGSIDKLRKEIERLEWR-QQT--EVLSPEEEKELVEK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 349 MVRHQESLQAKQRA---------LLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQcQLRAQQELLQSLQRE 419
Cdd:COG1340 142 IKELEKELEKAKKAlekneklkeLRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD-ELRKEADELHKEIVE 220
|
..
gi 1370482396 420 KQ 421
Cdd:COG1340 221 AQ 222
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
203-418 |
2.80e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 203 RAQLEEAEGQKDGLRKQAGKLEQALKQEQgarRRQAEEdeqclsEWEHDKQQLltetsdlktkmatlERELKQQRESTQA 282
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEA---LLEAKE------EIHKLRNEF--------------EKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 283 VEAKAQQLQEEGERRAAAerqvqqleeqvqqleaqvqllvgrLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRA 362
Cdd:PRK12704 87 LEKRLLQKEENLDRKLEL------------------------LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370482396 363 LLKQLDSLDQE--REELRGSL-DEAEAQRA----RVEEQLQSEREQgqcqlRAQQELLQSLQR 418
Cdd:PRK12704 143 ELERISGLTAEeaKEILLEKVeEEARHEAAvlikEIEEEAKEEADK-----KAKEILAQAIQR 200
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
190-293 |
3.84e-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: 39.96 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 190 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKqeqgARRRQAEEDEQCLSEW-EHDKQQLLTETSdlktkmAT 268
Cdd:pfam02841 197 QALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMME----AQERSYQEHVKQLIEKmEAEREQLLAEQE------RM 266
|
90 100
....*....|....*....|....*.
gi 1370482396 269 LERELKQQRE-STQAVEAKAQQLQEE 293
Cdd:pfam02841 267 LEHKLQEQEElLKEGFKTEAESLQKE 292
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
183-432 |
4.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 183 RWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQgaRRRQAEEDEQCLSEWE------------- 249
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE--NELEAAALEERLKEARlllliaaallall 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 250 --HDKQQLLTET----------------SDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQV 311
Cdd:COG4717 263 glGGSLLSLILTiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 312 QQLEAQVQLLVGRLEGAGQQVCWASTELDKE----KARVDS---------MVRHQESLQAKQRALLKQLDSLDQEREEL- 377
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQEIAallaEAGVEDeeelraaleQAEEYQELKEELEELEEQLEELLGELEELl 422
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370482396 378 -RGSLDEAEAQRARVEEQLQSEREQgqcqlraQQELLQSLQREKQGLEQATTDLRL 432
Cdd:COG4717 423 eALDEEELEEELEELEEELEELEEE-------LEELREELAELEAELEQLEEDGEL 471
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
199-433 |
4.20e-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: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 199 VEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRE 278
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKE 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 279 STQAVEAKAQQLQE-EGERRAAAE-----RQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKARVDSMVRH 352
Cdd:pfam10174 532 ECSKLENQLKKAHNaEEAVRTNPEindriRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLR 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 353 QESLQAKQRALLKQLdsldqEREELRGSLDEAEAQRARVEEqlqSEREQGQCQLraqQELLQSLQREKQGLEqaTTDLRL 432
Cdd:pfam10174 612 QMKEQNKKVANIKHG-----QQEMKKKGAQLLEEARRREDN---LADNSQQLQL---EELMGALEKTRQELD--ATKARL 678
|
.
gi 1370482396 433 T 433
Cdd:pfam10174 679 S 679
|
|
| CDC37_N |
smart01071 |
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ... |
187-276 |
5.31e-03 |
|
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.
Pssm-ID: 198139 [Multi-domain] Cd Length: 154 Bit Score: 38.17 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 187 EQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAgKLEQALKQEQGARRRQAEEDEQCLSEWEHDKQQLLTETSDLKTKM 266
Cdd:smart01071 53 YELIMNDHLNKRIDKLLKGLREEELSPETPTYNE-MLAELQDQLKKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKL 131
|
90
....*....|
gi 1370482396 267 ATLERELKQQ 276
Cdd:smart01071 132 DELEKEEKKK 141
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
186-441 |
5.61e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 186 AEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGA------------------------RRRQAEED 241
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvligveaayeaaleaalaaalqniVVEDDEVA 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 242 EQCLSEWEHDKQQLLTETSDLKTKMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLL 321
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 322 VGRLEGAGQQVCWASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARVEEQLQS-ERE 400
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEErLEE 719
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1370482396 401 QGQCQLRAQQELLQSLQREKQGLEQATTDLRLTILELEREL 441
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
190-391 |
6.71e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 190 KDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQ---GARRRQAEEDEQCLSEWEhdkqQLL--TETSDLKT 264
Cdd:COG3883 44 AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelGERARALYRSGGSVSYLD----VLLgsESFSDFLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 265 KMATLERELKQQRESTQAVEAKAQQLQEEGERRAAAErqvqqleeqvQQLEAQVQLLVGRLEGAGQQVCWASTELDKEKA 344
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAELEAKKAELEAKL----------AELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1370482396 345 RVDSMVRHQESLQAKQRALLKQLDSLDQEREELRGSLDEAEAQRARV 391
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
180-423 |
8.04e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.44 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 180 TVGRWAAEQRKDLTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARRRQAEEDEQclsewehdkQQLLTET 259
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQ---------AYWQVVE 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 260 SDLKTKMATLERELKQQREstqAVEAKAQQLQEEGERRAAAERQVQQLEEQVQQLEAQVQLLVGRLEGAGQQVcwastel 339
Cdd:pfam12128 725 GALDAQLALLKAAIAARRS---GAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEV------- 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 340 dkekARVDSMVRHQESLQAKQRALlkQLDSLDQEREELRGSLDEAEAQRARVEEQLQSEREQGQCQLRAQQELLQSLQRE 419
Cdd:pfam12128 795 ----LRYFDWYQETWLQRRPRLAT--QLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCE 868
|
....
gi 1370482396 420 KQGL 423
Cdd:pfam12128 869 MSKL 872
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
187-426 |
8.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 187 EQRKDlTRLSKHVEALRAQLEEAEGQKDGLRKQAGKLEQALKQEQGARR----RQAEEDEQC--LSEWEHDKQQLLTETS 260
Cdd:PTZ00121 1082 DAKED-NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaeeaRKAEDARKAeeARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 261 D--LKTKMATLERELKQQRESTQAVEA-KAQQLQE-------EGERRAAAERQVQQLEEQVQQLEAQVqllVGRLEGAGQ 330
Cdd:PTZ00121 1161 EdaRKAEEARKAEDAKKAEAARKAEEVrKAEELRKaedarkaEAARKAEEERKAEEARKAEDAKKAEA---VKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 331 QvcwASTELDKEKARVDSMVRHQESLQAKQRALLKQLDSLDQER--EELRGSLDEAEAQRARVEEQLQ--SEREQGQCQL 406
Cdd:PTZ00121 1238 D---AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkaDELKKAEEKKKADEAKKAEEKKkaDEAKKKAEEA 1314
|
250 260
....*....|....*....|
gi 1370482396 407 RAQQELLQSLQREKQGLEQA 426
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAA 1334
|
|
| Cornifin |
pfam02389 |
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ... |
584-618 |
8.50e-03 |
|
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.
Pssm-ID: 280537 [Multi-domain] Cd Length: 135 Bit Score: 36.95 E-value: 8.50e-03
10 20 30
....*....|....*....|....*....|....*
gi 1370482396 584 QPCTSPPRQPCTSPPRQPCTSPPRQPCTSPSRQPC 618
Cdd:pfam02389 7 QPCQPPPQEPCVPTTKEPCHSKVPEPCNPKVPEPC 41
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
337-431 |
9.76e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.46 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 337 TELDKEKARVDSMVrhqESLQAKQRALLKQLDSLDQEREELRgSLDEAEAQRARveEQLQSEREQGQCQLRAQQELlqsl 416
Cdd:smart00787 161 KLLMKELELLNSIK---PKLRDRKDALEEELRQLKQLEDELE-DCDPTELDRAK--EKLKKLLQEIMIKVKKLEEL---- 230
|
90
....*....|....*
gi 1370482396 417 QREKQGLEQATTDLR 431
Cdd:smart00787 231 EEELQELESKIEDLT 245
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
540-667 |
9.97e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 39.54 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370482396 540 DRLWSPSSKGTQGATPPVQAKSTSPGPLgrqhlPSSRTGRTLlGQPCTSPPRQPCTSPPrQPCTSPPRQPCTSPSRQPcS 619
Cdd:PHA03247 2565 DRSVPPPRPAPRPSEPAVTSRARRPDAP-----PQSARPRAP-VDDRGDPRGPAPPSPL-PPDTHAPDPPPPSPSPAA-N 2636
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1370482396 620 QPSKSLLEGVTHLDTCTQNPIKVLVRLRKRLSpGRGQASSAHQPQERP 667
Cdd:PHA03247 2637 EPDPHPPPTVPPPERPRDDPAPGRVSRPRRAR-RLGRAAQASSPPQRP 2683
|
|
| |
