|
Name |
Accession |
Description |
Interval |
E-value |
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1-485 |
0e+00 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 657.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 1 MRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILiHHNGGIPANKKLSTTLPEIEYREKGK 80
Cdd:pfam09726 177 MRLRKQREVQKENEFYMQLLQQALPKEQQMLDRQERETSETAKGLSEVDPLAL-NQNGHSLNKKDSTLQLPELEYREKKN 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 81 EKDKDAKKHNLG-INNNNILQPVDSKIQEIEYMENHINSKRLNND-LVGSTENLLKEDSC--------TASSKNYKNAS- 149
Cdd:pfam09726 256 SGTSSGSDSKKShNHNIHNLNHVDSKLQEKEYMENHSNSKRLNIStSPGSEEDLLVRESVssksssssSSSNKNYKNASg 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 150 ---GVVNSSPRSHSATNGSIPSSSS-KNEKKQKC-TSKGPSAHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQASR 224
Cdd:pfam09726 336 gsaNSSNSSPRSHSHNSGSVTSSSSsKNSKKQKGpGGKSGARHKDPAENCIPNNQLSKPDALVRLEQDIKKLKAELQASR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 225 QVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLMEEKKRK 304
Cdd:pfam09726 416 QTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQEARASAEKQLAEEKKRK 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 305 KLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELRKYKENEKDTEVLMSALSAM 384
Cdd:pfam09726 496 KEEEATAARAVALAAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSAM 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 385 QDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSitysaaTSPLSPVSPHYS 464
Cdd:pfam09726 576 QDKNQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEVMAVMPS------TSRITPVTPHYS 649
|
490 500
....*....|....*....|.
gi 1243457555 465 SKFVETSPSGLDPNASVYQPL 485
Cdd:pfam09726 650 SKFMDTSPSMRDPNASVYPPL 670
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-439 |
5.27e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 204 DALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKL 283
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 284 KAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTmdmKVKEEQIRELELKVQE 363
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR---AAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1243457555 364 ---LRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 439
Cdd:COG1196 410 ealLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-439 |
9.40e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 9.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 197 NNQLSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNI 276
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 277 SQLEKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECtETLRSRIRELEAEGKKLTMDMKVKEEQI-- 354
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-KALREALDELRAELTLLNEEAANLRERLes 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 355 --RELELKVQELRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFS----ALGDAKRQLEIAQGQILQKDQ 428
Cdd:TIGR02168 829 leRRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleeALALLRSELEELSEELRELES 908
|
250
....*....|.
gi 1243457555 429 EIKDLKQKIAE 439
Cdd:TIGR02168 909 KRSELRRELEE 919
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
209-439 |
2.86e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 209 LEQDIKKLKADLQASRQVEQELRSQ----------ISALSSTERGIRSEMGQLR---QENELLQNKLHNAVQMKQKDKQN 275
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKekeleevlreINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 276 ISQLEKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASrgECTETLRSRIRELEAEGKKLTMDMKVKEEQIR 355
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS--EFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 356 ELELKVQELR----KYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDlfsALGDAKRQLEIAQGQILQKDQEIK 431
Cdd:PRK03918 332 ELEEKEERLEelkkKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL---TPEKLEKELEELEKAKEEIEEEIS 408
|
....*...
gi 1243457555 432 DLKQKIAE 439
Cdd:PRK03918 409 KITARIGE 416
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1-485 |
0e+00 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 657.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 1 MRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILiHHNGGIPANKKLSTTLPEIEYREKGK 80
Cdd:pfam09726 177 MRLRKQREVQKENEFYMQLLQQALPKEQQMLDRQERETSETAKGLSEVDPLAL-NQNGHSLNKKDSTLQLPELEYREKKN 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 81 EKDKDAKKHNLG-INNNNILQPVDSKIQEIEYMENHINSKRLNND-LVGSTENLLKEDSC--------TASSKNYKNAS- 149
Cdd:pfam09726 256 SGTSSGSDSKKShNHNIHNLNHVDSKLQEKEYMENHSNSKRLNIStSPGSEEDLLVRESVssksssssSSSNKNYKNASg 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 150 ---GVVNSSPRSHSATNGSIPSSSS-KNEKKQKC-TSKGPSAHKDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQASR 224
Cdd:pfam09726 336 gsaNSSNSSPRSHSHNSGSVTSSSSsKNSKKQKGpGGKSGARHKDPAENCIPNNQLSKPDALVRLEQDIKKLKAELQASR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 225 QVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQLMEEKKRK 304
Cdd:pfam09726 416 QTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQEARASAEKQLAEEKKRK 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 305 KLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELRKYKENEKDTEVLMSALSAM 384
Cdd:pfam09726 496 KEEEATAARAVALAAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSAM 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 385 QDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSitysaaTSPLSPVSPHYS 464
Cdd:pfam09726 576 QDKNQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAEVMAVMPS------TSRITPVTPHYS 649
|
490 500
....*....|....*....|.
gi 1243457555 465 SKFVETSPSGLDPNASVYQPL 485
Cdd:pfam09726 650 SKFMDTSPSMRDPNASVYPPL 670
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-439 |
5.27e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 204 DALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKL 283
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 284 KAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTmdmKVKEEQIRELELKVQE 363
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR---AAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1243457555 364 ---LRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 439
Cdd:COG1196 410 ealLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-439 |
9.40e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 9.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 197 NNQLSKPDALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNI 276
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 277 SQLEKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECtETLRSRIRELEAEGKKLTMDMKVKEEQI-- 354
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-KALREALDELRAELTLLNEEAANLRERLes 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 355 --RELELKVQELRKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFS----ALGDAKRQLEIAQGQILQKDQ 428
Cdd:TIGR02168 829 leRRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleeALALLRSELEELSEELRELES 908
|
250
....*....|.
gi 1243457555 429 EIKDLKQKIAE 439
Cdd:TIGR02168 909 KRSELRRELEE 919
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
206-447 |
1.68e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 206 LVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAvqmkqkdKQNISQLEKKLKA 285
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-------ANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 286 EQEARSFVEKQLmEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELR 365
Cdd:TIGR02168 307 LRERLANLERQL-EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 366 -KYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAkrQLEIAQGQILQKDQEIKDLKQKIAEVMAVM 444
Cdd:TIGR02168 386 sKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEAL 463
|
...
gi 1243457555 445 PSI 447
Cdd:TIGR02168 464 EEL 466
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
208-439 |
1.17e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 208 RLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAvqmkqkdKQNISQLEKKLKAEQ 287
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL-------LAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 288 EARSFVEKQLMEEKKRKKLEEATAARAVAFAaasrgectETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELRky 367
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEEL--------EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE-- 378
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1243457555 368 KENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLfSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 439
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERL-ERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
208-431 |
3.33e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 208 RLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQ 287
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 288 EARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTmdmKVKEEQIRELELKVQELRKY 367
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE---EEEEEEEALEEAAEEEAELE 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243457555 368 KENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLdLFSALGDAKRQLEIAQGQILQKDQEIK 431
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAA-RLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
204-439 |
9.58e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 204 DALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKL 283
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 284 KAEQEARSFVEKQLmEEKKRKKLEEATAARAVAFAAASRGECTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQE 363
Cdd:TIGR02168 799 KALREALDELRAEL-TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 364 LRK-YKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQK---------------- 426
Cdd:TIGR02168 878 LLNeRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlseeysltleeae 957
|
250 260
....*....|....*....|....*.
gi 1243457555 427 -------------DQEIKDLKQKIAE 439
Cdd:TIGR02168 958 alenkieddeeeaRRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
206-441 |
2.55e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 206 LVRLEQDIKKLKADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNaVQMKQKD------KQNISQL 279
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK-LEEALNDlearlsHSRIPEI 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 280 EKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTEtLRSRIRELEAEGKKLTMDMKVKEEQIRELEL 359
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-LKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 360 KVQELRK-YKENEKDTEVLMSALSAMQDKTQHLENSLSaetriklDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIA 438
Cdd:TIGR02169 876 ALRDLESrLGDLKKERDELEAQLRELERKIEELEAQIE-------KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
...
gi 1243457555 439 EVM 441
Cdd:TIGR02169 949 EEL 951
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-439 |
4.57e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 204 DALVRLEQDIKKLKADLQASR----QVEQELRSQISALSSTERgirsEMGQLRQENELLQNKLHNAVQMKQKDKQNISQL 279
Cdd:COG1196 274 LELEELELELEEAQAEEYELLaelaRLEQDIARLEERRRELEE----RLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 280 EKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASRGECTEtLRSRIRELEAEGKKLTMDMKVKEEQIRELEL 359
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 360 KVQELRKYKENEKDtevlmsALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 439
Cdd:COG1196 429 ALAELEEEEEEEEE------ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
204-436 |
1.58e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 204 DALVRLEQDIKKLkADLQASRQVEQELRSQISALSSTERGIRSEMGQLRQEneLLQNKLHNAVQMKQKDKQNISQLEKKL 283
Cdd:COG4913 242 EALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 284 KAEQEARSFVEKQLMEEKkrkkleeataaravafaaasrGECTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQE 363
Cdd:COG4913 319 DALREELDELEAQIRGNG---------------------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1243457555 364 LRKykenekdtevlmsALSAMQDKTQHLENSLSAETRiklDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQK 436
Cdd:COG4913 378 SAE-------------EFAALRAEAAALLEALEEELE---ALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
205-461 |
1.80e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 205 ALVRLEQDIKKLKADLQASRQVEQELRSQISALSSTErgirsEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLK 284
Cdd:COG3206 176 ALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSE-----EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 285 AEQEARSFVekqlmeekkrkkleeataaravafaaaSRGECTETLRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQEL 364
Cdd:COG3206 251 SGPDALPEL---------------------------LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 365 RKYKENEKDTEV--LMSALSAMQDKTQHLENSLsAETRIKLDLFSA----LGDAKRQLEIAQG---QILQKDQEIkdlkq 435
Cdd:COG3206 304 RAQLQQEAQRILasLEAELEALQAREASLQAQL-AQLEARLAELPEleaeLRRLEREVEVARElyeSLLQRLEEA----- 377
|
250 260
....*....|....*....|....*.
gi 1243457555 436 KIAEVMAVMPSITYSAATSPLSPVSP 461
Cdd:COG3206 378 RLAEALTVGNVRVIDPAVVPLKPVSP 403
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
218-474 |
2.29e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 218 ADLQASRQVE-QELRSQISALSSTERGIRSEMGQLRQENELLQNKLHNAVQMKQKDKQNISQLEKKLKAEQEARSFVEKQ 296
Cdd:COG4942 19 ADAAAEAEAElEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 297 LMEEKKRKKLEEATAARAVAFAAA----SRGECTETLRSRIREleaegKKLTMDMKVKEEQIRELELKVQELRKYKENEK 372
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLalllSPEDFLDAVRRLQYL-----KYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 373 DTevLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSITYSAA 452
Cdd:COG4942 174 AE--LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
250 260
....*....|....*....|...
gi 1243457555 453 TSPLS-PVSPHYSSKFVETSPSG 474
Cdd:COG4942 252 KGKLPwPVSGRVVRRFGERDGGG 274
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
209-439 |
2.86e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 209 LEQDIKKLKADLQASRQVEQELRSQ----------ISALSSTERGIRSEMGQLR---QENELLQNKLHNAVQMKQKDKQN 275
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKekeleevlreINEISSELPELREELEKLEkevKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 276 ISQLEKKLKAEQEARSFVEKQLMEEKKRKKLEEATAARAVAFAAASrgECTETLRSRIRELEAEGKKLTMDMKVKEEQIR 355
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS--EFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 356 ELELKVQELR----KYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDlfsALGDAKRQLEIAQGQILQKDQEIK 431
Cdd:PRK03918 332 ELEEKEERLEelkkKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL---TPEKLEKELEELEKAKEEIEEEIS 408
|
....*...
gi 1243457555 432 DLKQKIAE 439
Cdd:PRK03918 409 KITARIGE 416
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
329-398 |
4.00e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 4.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1243457555 329 LRSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELRK--YKENEKDTEVlmsalSAMQDKTQHLENSLSAE 398
Cdd:COG2433 418 LEEQVERLEAEVEELEAELEEKDERIERLERELSEARSeeRREIRKDREI-----SRLDREIERLERELEEE 484
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
330-439 |
7.96e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243457555 330 RSRIRELEAEGKKLTMDMKVKEEQIRELELKVQELRK----------YKENEKDTEVLMSALSAMQDKTQHLENSLSAET 399
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeYSWDEIDVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1243457555 400 RIKldlfSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAE 439
Cdd:COG4913 689 ALE----EQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
|
| |
