|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
107-415 |
7.56e-126 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 368.09 E-value: 7.56e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1843657965 343 DSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESR 415
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
9-106 |
1.48e-13 |
|
Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.
Pssm-ID: 461414 [Multi-domain] Cd Length: 83 Bit Score: 65.88 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732 1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65
|
90
....*....|....*...
gi 1843657965 89 LDFSLADAVNQEFLTTRT 106
Cdd:pfam04732 66 LDFSLADALNQEFKATRT 83
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-421 |
4.72e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLK--GREPTRVAELYEEELRELRRQVEVLTNQRARVDVER 180
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 181 DNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADvdaatlaRIDLERRIESLNEEIAFLKK--------VHEEEIRELQA 252
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREaldelraeLTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYksKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 332
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 333 CEIDALKGTNDSLMRQMRELEDRFASeasgYQDNIARLEEEIRHLKDEMArhlREYQDLLNVKMALDVEIATYRKLLEGE 412
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR 973
|
....*....
gi 1843657965 413 ESRINLPIQ 421
Cdd:TIGR02168 974 LKRLENKIK 982
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-404 |
5.31e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 111 ELQELNDRFANyiekvrfLEQQNAALAAEVNRLKGReptRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRL 190
Cdd:COG4913 618 ELAELEEELAE-------AEERLEALEAELDALQER---REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 191 KAkLQEEIqlkEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEeirelqaqlqeqqvqvEMDMSKPDL 270
Cdd:COG4913 688 AA-LEEQL---EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA----------------AEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 271 TAALRDIRAQYetIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAkqeMMEYRHQIQSYTCEIDALKGTNDSLMRQMR 350
Cdd:COG4913 748 RALLEERFAAA--LGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLD 822
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1843657965 351 ELEDrfaseasgyqDNIARLEEEIRHLKDEmarhlREYQDLLNVKMALDVEIAT 404
Cdd:COG4913 823 RLEE----------DGLPEYEERFKELLNE-----NSIEFVADLLSKLRRAIRE 861
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
276-411 |
5.99e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 276 DIRAQYETIAAKNISEAEEwyKSKVSDLTQA---------ANKNNDALRQAKQEMMEyrhQIQSYTCEIDALKGTNDSLM 346
Cdd:PRK11281 40 DVQAQLDALNKQKLLEAED--KLVQQDLEQTlalldkidrQKEETEQLKQQLAQAPA---KLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 347 RQ------MRELEDRFA-----------------SEASGYQ-----------DNIARLeEEIRHL----KDEMARHLREY 388
Cdd:PRK11281 115 REtlstlsLRQLESRLAqtldqlqnaqndlaeynSQLVSLQtqperaqaalyANSQRL-QQIRNLlkggKVGGKALRPSQ 193
|
170 180
....*....|....*....|....
gi 1843657965 389 QDLLNVKMA-LDVEIATYRKLLEG 411
Cdd:PRK11281 194 RVLLQAEQAlLNAQNDLQRKSLEG 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
107-415 |
7.56e-126 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 368.09 E-value: 7.56e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1843657965 343 DSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESR 415
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Filament_head |
pfam04732 |
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ... |
9-106 |
1.48e-13 |
|
Intermediate filament head (DNA binding) region; This family represents the N-terminal head region of intermediate filaments. Intermediate filament heads bind DNA. Vimentin heads are able to alter nuclear architecture and chromatin distribution, and the liberation of heads by HIV-1 protease liberates may play an important role in HIV-1 associated cytopathogenesis and carcinogenesis. Phosphorylation of the head region can affect filament stability. The head has been shown to interaction with the rod domain of the same protein.
Pssm-ID: 461414 [Multi-domain] Cd Length: 83 Bit Score: 65.88 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732 1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65
|
90
....*....|....*...
gi 1843657965 89 LDFSLADAVNQEFLTTRT 106
Cdd:pfam04732 66 LDFSLADALNQEFKATRT 83
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-421 |
4.72e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLK--GREPTRVAELYEEELRELRRQVEVLTNQRARVDVER 180
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 181 DNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADvdaatlaRIDLERRIESLNEEIAFLKK--------VHEEEIRELQA 252
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREaldelraeLTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYksKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 332
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 333 CEIDALKGTNDSLMRQMRELEDRFASeasgYQDNIARLEEEIRHLKDEMArhlREYQDLLNVKMALDVEIATYRKLLEGE 412
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR 973
|
....*....
gi 1843657965 413 ESRINLPIQ 421
Cdd:TIGR02168 974 LKRLENKIK 982
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-404 |
5.31e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 111 ELQELNDRFANyiekvrfLEQQNAALAAEVNRLKGReptRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRL 190
Cdd:COG4913 618 ELAELEEELAE-------AEERLEALEAELDALQER---REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 191 KAkLQEEIqlkEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEeirelqaqlqeqqvqvEMDMSKPDL 270
Cdd:COG4913 688 AA-LEEQL---EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA----------------AEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 271 TAALRDIRAQYetIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAkqeMMEYRHQIQSYTCEIDALKGTNDSLMRQMR 350
Cdd:COG4913 748 RALLEERFAAA--LGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLD 822
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1843657965 351 ELEDrfaseasgyqDNIARLEEEIRHLKDEmarhlREYQDLLNVKMALDVEIAT 404
Cdd:COG4913 823 RLEE----------DGLPEYEERFKELLNE-----NSIEFVADLLSKLRRAIRE 861
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
165-416 |
1.30e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHE 244
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 245 EEIRELQaqlqeqqvqvemdmskpDLTAALRDIRAQYETIAAKNISEAEEwykskVSDLTQAANKNNDALRQAKQEMMEY 324
Cdd:COG1196 334 ELEEELE-----------------ELEEELEEAEEELEEAEAELAEAEEA-----LLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 325 RHQIQSYTCEIDALKGTNDSLMRQMRELEdrfaSEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIAT 404
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLE----EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250
....*....|..
gi 1843657965 405 YRKLLEGEESRI 416
Cdd:COG1196 468 LLEEAALLEAAL 479
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
103-393 |
4.82e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAelyeeelrelrrQVEVLTNQRARVDVERDN 182
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNA------------QVKELREEAQELREKRDE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 183 LLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARID---LERRIESLneEIAFLKKVH--EEEIRelqaqlqeq 257
Cdd:COG1340 69 LNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERL--EWRQQTEVLspEEEKE--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 258 qvqvemdmskpdLTAALRDIRAQYETIaaknisEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDA 337
Cdd:COG1340 138 ------------LVEKIKELEKELEKA------KKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1843657965 338 LKGTNDSLMRQMRELedrfASEASGYQDNIARLEEEIrhlkDEMARHLREYQDLLN 393
Cdd:COG1340 200 LYKEADELRKEADEL----HKEIVEAQEKADELHEEI----IELQKELRELRKELK 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-418 |
1.45e-04 |
|
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: 44.66 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHE 244
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 245 EEIRELQAQLQEQQVQVEmdmSKPDLTAALRDIRAQYETIAAKNISEAEEWY--KSKVSDLTQAANKNNDALRQAKQEMM 322
Cdd:TIGR02168 320 ELEAQLEELESKLDELAE---ELAELEEKLEELKEELESLEAELEELEAELEelESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 323 EYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFAS-EASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVE 401
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250
....*....|....*..
gi 1843657965 402 IATYRKLLEGEESRINL 418
Cdd:TIGR02168 477 LDAAERELAQLQARLDS 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
88-373 |
1.65e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 88 LLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREptrvaelyeeelRELRRQVE 167
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE------------YELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 168 VLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEI 247
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 248 RELQAQLQEQQvqvemdmskpDLTAALRDIRAQYETIAAKNISEAEEwykskVSDLTQAANKNNDALRQAKQEMMEYRHQ 327
Cdd:COG1196 379 EELEELAEELL----------EALRAAAELAAQLEELEEAEEALLER-----LERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1843657965 328 IQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEE 373
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
166-463 |
4.76e-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: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 166 VEVLTNQRARVDVERDNLL--DDLQRLKAKLQEEIQL--KEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAflkk 241
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAEryQALLKEKREYEGYELLkeKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE---- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 242 vheeeirelqaqlqeqqvqvemdmskpdltAALRDIRAQYETIAAKNISEAEEwYKSKVSDLTQAANKNNDALRQAKQEM 321
Cdd:TIGR02169 269 ------------------------------EIEQLLEELNKKIKDLGEEEQLR-VKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 322 MEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASeasgyqdniarLEEEIRHLKDEMARHLREYQDLLNVKMALDVE 401
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK-----------LTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1843657965 402 IATYRKLLEGEESRINLPIQTYSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVLEVGA 463
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
162-383 |
2.54e-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: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 162 LRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDaatlariDLERRIESLNEEIAFLKK 241
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 242 VHEEEIRelQAQLQEQQVQVEMDMSKPDLTAALRdiRAQYETIAAKNISEAEEWYKSKVSDLTQaankNNDALRQAKQEM 321
Cdd:COG4942 105 ELAELLR--ALYRLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAELAA----LRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1843657965 322 MEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMAR 383
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
165-393 |
2.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLAR--IDLERRIESLNEEIAFLKKV 242
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 243 HEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETiAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMM 322
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE-LQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1843657965 323 EYRHQIQSYTCEIDALkgtNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLK----DEMARHLREYQDLLN 393
Cdd:COG4913 770 NLEERIDALRARLNRA---EEELERAMRAFNREWPAETADLDADLESLPEYLALLDrleeDGLPEYEERFKELLN 841
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
172-361 |
3.29e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 172 QRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARID-LERRIESLNEEIAflkkvheeeiREL 250
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELE----------ERE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 251 QAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKniseaeewYKSKVSDLTQAANKNNDALRQAKQEmmeyRHQIQS 330
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA--------LEEELEALEEALAEAEAALRDLRRE----LRELEA 426
|
170 180 190
....*....|....*....|....*....|.
gi 1843657965 331 ytcEIDALKGTNDSLMRQMRELEDRFASEAS 361
Cdd:COG4913 427 ---EIASLERRKSNIPARLLALRDALAEALG 454
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-241 |
3.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 111 ELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGReptrVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRL 190
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQ----IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1843657965 191 K----------AKLQEEI-QLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKK 241
Cdd:COG4913 372 GlplpasaeefAALRAEAaALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
108-427 |
3.37e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 108 EKVELQELNDRfanyIEKvrfLEQQNAALAAEVNRLKGR--EPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLD 185
Cdd:TIGR02169 672 EPAELQRLRER----LEG---LKRELSSLQSELRRIENRldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 186 DLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRI------------ESLNEEI-----------AFLKKV 242
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsripeiqaelSKLEEEVsriearlreieQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 243 HEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAA--KNISEAEEWYKSKVSDLTQAANKNNDALRQAKQE 320
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 321 MMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEAS---------GYQDNIARLEEEIRHLK-------DEMARH 384
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsleDVQAELQRVEEEIRALEpvnmlaiQEYEEV 984
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1843657965 385 LREYQDLLNVKMALDVEIATYRKLLEG-EESRINLPIQTYSALN 427
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAILERIEEyEKKKREVFMEAFEAIN 1028
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
174-286 |
5.43e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.29 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 174 ARVDVERDNLLDDLQRLKAKLqeeIQLKEEAEnnlaAFRADVDAATLARID-LERRIESLNEEIAFLKKVHEEEIRELQA 252
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRL---EQLEIEKE----ALKKEQDEASFERLAeLRDELAELEEELEALKARWEAEKELIEE 472
|
90 100 110
....*....|....*....|....*....|....
gi 1843657965 253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAA 286
Cdd:COG0542 473 IQELKEELEQRYGKIPELEKELAELEEELAELAP 506
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
276-411 |
5.99e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 276 DIRAQYETIAAKNISEAEEwyKSKVSDLTQA---------ANKNNDALRQAKQEMMEyrhQIQSYTCEIDALKGTNDSLM 346
Cdd:PRK11281 40 DVQAQLDALNKQKLLEAED--KLVQQDLEQTlalldkidrQKEETEQLKQQLAQAPA---KLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 347 RQ------MRELEDRFA-----------------SEASGYQ-----------DNIARLeEEIRHL----KDEMARHLREY 388
Cdd:PRK11281 115 REtlstlsLRQLESRLAqtldqlqnaqndlaeynSQLVSLQtqperaqaalyANSQRL-QQIRNLlkggKVGGKALRPSQ 193
|
170 180
....*....|....*....|....
gi 1843657965 389 QDLLNVKMA-LDVEIATYRKLLEG 411
Cdd:PRK11281 194 RVLLQAEQAlLNAQNDLQRKSLEG 217
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-387 |
6.82e-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: 38.59 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 179 ERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLkkvhEEEIRELQAQLQE-- 256
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIAElr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 257 QQVQVEMDMSKPDLTAALRDIRAQYETI--AAKNISEAE---EWYKSKV---SDLTQAANKNNDALRQAKQEMMEYRHQI 328
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALllSPEDFLDAVrrlQYLKYLAparREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1843657965 329 QSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLRE 387
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-416 |
8.68e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 38.56 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 161 ELRRQVEVLTNQRARVDVERD-------NLLDDLQRLKAKLQE-EIQLKEEAENNLAAFraDVDAATLARID-LERRIES 231
Cdd:pfam15921 346 ELEKQLVLANSELTEARTERDqfsqesgNLDDQLQKLLADLHKrEKELSLEKEQNKRLW--DRDTGNSITIDhLRRELDD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 232 LNEEIAFLK---KVHEEEIRELQAQLQEQQVQVEMDMSK-PDLTAALRD----IRAQYETIAAKNIS-EAEEwykSKVSD 302
Cdd:pfam15921 424 RNMEVQRLEallKAMKSECQGQMERQMAAIQGKNESLEKvSSLTAQLEStkemLRKVVEELTAKKMTlESSE---RTVSD 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1843657965 303 LTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEdRFASEASGYQDNIARLEEEIRHLKDEMA 382
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECE-ALKLQMAEKDKVIEILRQQIENMTQLVG 579
|
250 260 270
....*....|....*....|....*....|....
gi 1843657965 383 RHLREYQDLLNVKMALDVEIATYRklLEGEESRI 416
Cdd:pfam15921 580 QHGRTAGAMQVEKAQLEKEINDRR--LELQEFKI 611
|
|
| |
