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Conserved domains on  [gi|6531404|gb|AAF15400|]
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mutant desmin [Homo sapiens]

Protein Classification

intermediate filament family protein( domain architecture ID 12057329)

intermediate filament family protein similar to desmin, a muscle-specific type III intermediate filament essential for proper muscular structure and function

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
107-415 2.64e-124

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 364.24  E-value: 2.64e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6531404    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 1.75e-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: 65.49  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404      9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732   1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65
                          90
                  ....*....|....*...
gi 6531404     89 LDFSLADAVNQEFLTTRT 106
Cdd:pfam04732  66 LDFSLADALNQEFKATRT 83
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
107-415 2.64e-124

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 364.24  E-value: 2.64e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6531404    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 1.75e-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: 65.49  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404      9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732   1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65
                          90
                  ....*....|....*...
gi 6531404     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 5.87e-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: 55.45  E-value: 5.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLK--GREPTRVAELYEEELRELRRQVEVLTNQRARVDVER 180
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     181 DNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADvdaatlaRIDLERRIESLNEEIAFLKK--------VHEEEIRELQA 252
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREaldelraeLTLLNEEAANL 822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYksKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 332
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALALLRSELEELS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     333 CEIDALKGTNDSLMRQMRELEDRFASeasgYQDNIARLEEEIRHLKDEMArhlREYQDLLNVKMALDVEIATYRKLLEGE 412
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR 973

                   ....*....
gi 6531404     413 ESRINLPIQ 421
Cdd:TIGR02168  974 LKRLENKIK 982
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-404 6.96e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 6.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404   111 ELQELNDRFANyiekvrfLEQQNAALAAEVNRLKGReptRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRL 190
Cdd:COG4913  618 ELAELEEELAE-------AEERLEALEAELDALQER---REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404   191 KAkLQEEIqlkEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEeirelqaqlqeqqvqvEMDMSKPDL 270
Cdd:COG4913  688 AA-LEEQL---EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA----------------AEDLARLEL 747
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404   271 TAALRDIRAQYetIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAkqeMMEYRHQIQSYTCEIDALKGTNDSLMRQMR 350
Cdd:COG4913  748 RALLEERFAAA--LGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLD 822
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6531404   351 ELEDrfaseasgyqDNIARLEEEIRHLKDEmarhlREYQDLLNVKMALDVEIAT 404
Cdd:COG4913  823 RLEE----------DGLPEYEERFKELLNE-----NSIEFVADLLSKLRRAIRE 861
PRK11281 PRK11281
mechanosensitive channel MscK;
276-411 8.29e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 8.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    276 DIRAQYETIAAKNISEAEEwyKSKVSDLTQA---------ANKNNDALRQAKQEMMEyrhQIQSYTCEIDALKGTNDSLM 346
Cdd:PRK11281   40 DVQAQLDALNKQKLLEAED--KLVQQDLEQTlalldkidrQKEETEQLKQQLAQAPA---KLRQAQAELEALKDDNDEET 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    347 RQ------MRELEDRFA-----------------SEASGYQ-----------DNIARLeEEIRHL----KDEMARHLREY 388
Cdd:PRK11281  115 REtlstlsLRQLESRLAqtldqlqnaqndlaeynSQLVSLQtqperaqaalyANSQRL-QQIRNLlkggKVGGKALRPSQ 193
                         170       180
                  ....*....|....*....|....
gi 6531404    389 QDLLNVKMA-LDVEIATYRKLLEG 411
Cdd:PRK11281  194 RVLLQAEQAlLNAQNDLQRKSLEG 217
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
107-415 2.64e-124

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 364.24  E-value: 2.64e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6531404    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 1.75e-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: 65.49  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404      9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732   1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65
                          90
                  ....*....|....*...
gi 6531404     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 5.87e-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: 55.45  E-value: 5.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLK--GREPTRVAELYEEELRELRRQVEVLTNQRARVDVER 180
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     181 DNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADvdaatlaRIDLERRIESLNEEIAFLKK--------VHEEEIRELQA 252
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREaldelraeLTLLNEEAANL 822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYksKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 332
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALALLRSELEELS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     333 CEIDALKGTNDSLMRQMRELEDRFASeasgYQDNIARLEEEIRHLKDEMArhlREYQDLLNVKMALDVEIATYRKLLEGE 412
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR 973

                   ....*....
gi 6531404     413 ESRINLPIQ 421
Cdd:TIGR02168  974 LKRLENKIK 982
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-404 6.96e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 6.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404   111 ELQELNDRFANyiekvrfLEQQNAALAAEVNRLKGReptRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRL 190
Cdd:COG4913  618 ELAELEEELAE-------AEERLEALEAELDALQER---REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404   191 KAkLQEEIqlkEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEeirelqaqlqeqqvqvEMDMSKPDL 270
Cdd:COG4913  688 AA-LEEQL---EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA----------------AEDLARLEL 747
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404   271 TAALRDIRAQYetIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAkqeMMEYRHQIQSYTCEIDALKGTNDSLMRQMR 350
Cdd:COG4913  748 RALLEERFAAA--LGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLD 822
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6531404   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 1.62e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHE 244
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  245 EEIRELQaqlqeqqvqvemdmskpDLTAALRDIRAQYETIAAKNISEAEEwykskVSDLTQAANKNNDALRQAKQEMMEY 324
Cdd:COG1196 334 ELEEELE-----------------ELEEELEEAEEELEEAEAELAEAEEA-----LLEAEAELAEAEEELEELAEELLEA 391
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  325 RHQIQSYTCEIDALKGTNDSLMRQMRELEdrfaSEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIAT 404
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLE----EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
                       250
                ....*....|..
gi 6531404  405 YRKLLEGEESRI 416
Cdd:COG1196 468 LLEEAALLEAAL 479
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
103-393 9.48e-05

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.13  E-value: 9.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAelyeeelrelrrQVEVLTNQRARVDVERDN 182
Cdd:COG1340   1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNA------------QVKELREEAQELREKRDE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  183 LLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARID---LERRIESLneEIAFLKKVH--EEEIRelqaqlqeq 257
Cdd:COG1340  69 LNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERL--EWRQQTEVLspEEEKE--------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  258 qvqvemdmskpdLTAALRDIRAQYETIaaknisEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDA 337
Cdd:COG1340 138 ------------LVEKIKELEKELEKA------KKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6531404  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 1.63e-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: 44.28  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHE 244
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     245 EEIRELQAQLQEQQVQVEmdmSKPDLTAALRDIRAQYETIAAKNISEAEEWY--KSKVSDLTQAANKNNDALRQAKQEMM 322
Cdd:TIGR02168  320 ELEAQLEELESKLDELAE---ELAELEEKLEELKEELESLEAELEELEAELEelESRLEELEEQLETLRSKVAQLELQIA 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     323 EYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFAS-EASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVE 401
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
                          250
                   ....*....|....*..
gi 6531404     402 IATYRKLLEGEESRINL 418
Cdd:TIGR02168  477 LDAAERELAQLQARLDS 493
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
88-373 1.74e-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: 1.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404   88 LLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREptrvaelyeeelRELRRQVE 167
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE------------YELLAELA 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  168 VLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEI 247
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  248 RELQAQLQEQQvqvemdmskpDLTAALRDIRAQYETIAAKNISEAEEwykskVSDLTQAANKNNDALRQAKQEMMEYRHQ 327
Cdd:COG1196 379 EELEELAEELL----------EALRAAAELAAQLEELEEAEEALLER-----LERLEEELEELEEALAELEEEEEEEEEA 443
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 6531404  328 IQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEE 373
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
166-469 4.18e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 4.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     166 VEVLTNQRARVDVERDNLL--DDLQRLKAKLQEEIQL--KEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAflkk 241
Cdd:TIGR02169  193 IDEKRQQLERLRREREKAEryQALLKEKREYEGYELLkeKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE---- 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     242 vheeeirelqaqlqeqqvqvemdmskpdltAALRDIRAQYETIAAKNISEAEEwYKSKVSDLTQAANKNNDALRQAKQEM 321
Cdd:TIGR02169  269 ------------------------------EIEQLLEELNKKIKDLGEEEQLR-VKEKIGELEAEIASLERSIAEKEREL 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     322 MEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASeasgyqdniarLEEEIRHLKDEMARHLREYQDLLNVKMALDVE 401
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK-----------LTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6531404     402 IATYRKLLEGEESRINLPIQTYSALNFRETSPEQRGSEVHTKktvmIKTMETRDGEVVSEATQQQHEV 469
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA----IAGIEAKINELEEEKEDKALEI 450
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
165-393 3.02e-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: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404   165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLAR--IDLERRIESLNEEIAFLKKV 242
Cdd:COG4913  611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiAELEAELERLDASSDDLAAL 690
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404   243 HEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETiAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMM 322
Cdd:COG4913  691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE-LQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6531404   323 EYRHQIQSYTCEIDALkgtNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLK----DEMARHLREYQDLLN 393
Cdd:COG4913  770 NLEERIDALRARLNRA---EEELERAMRAFNREWPAETADLDADLESLPEYLALLDrleeDGLPEYEERFKELLN 841
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
162-383 3.18e-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: 39.75  E-value: 3.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  162 LRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDaatlariDLERRIESLNEEIAFLKK 241
Cdd:COG4942  32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAELRAELEAQKE 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  242 VHEEEIRelQAQLQEQQVQVEMDMSKPDLTAALRdiRAQYETIAAKNISEAEEWYKSKVSDLTQaankNNDALRQAKQEM 321
Cdd:COG4942 105 ELAELLR--ALYRLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAELAA----LRAELEAERAEL 176
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6531404  322 MEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMAR 383
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
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 6531404     108 EKVELQELNDRfanyIEKvrfLEQQNAALAAEVNRLKGR--EPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLD 185
Cdd:TIGR02169  672 EPAELQRLRER----LEG---LKRELSSLQSELRRIENRldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     186 DLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRI------------ESLNEEI-----------AFLKKV 242
Cdd:TIGR02169  745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsripeiqaelSKLEEEVsriearlreieQKLNRL 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     243 HEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAA--KNISEAEEWYKSKVSDLTQAANKNNDALRQAKQE 320
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404     321 MMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEAS---------GYQDNIARLEEEIRHLK-------DEMARH 384
Cdd:TIGR02169  905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsleDVQAELQRVEEEIRALEpvnmlaiQEYEEV 984
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 6531404     385 LREYQDLLNVKMALDVEIATYRKLLEG-EESRINLPIQTYSALN 427
Cdd:TIGR02169  985 LKRLDELKEKRAKLEEERKAILERIEEyEKKKREVFMEAFEAIN 1028
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
172-361 3.46e-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: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404   172 QRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARID-LERRIESLNEEIAflkkvheeeiREL 250
Cdd:COG4913  289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELE----------ERE 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404   251 QAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKniseaeewYKSKVSDLTQAANKNNDALRQAKQEmmeyRHQIQS 330
Cdd:COG4913  359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA--------LEEELEALEEALAEAEAALRDLRRE----LRELEA 426
                        170       180       190
                 ....*....|....*....|....*....|.
gi 6531404   331 ytcEIDALKGTNDSLMRQMRELEDRFASEAS 361
Cdd:COG4913  427 ---EIASLERRKSNIPARLLALRDALAEALG 454
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-241 3.65e-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: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404   111 ELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGReptrVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRL 190
Cdd:COG4913  296 ELEELRAELARLEAELERLEARLDALREELDELEAQ----IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6531404   191 K----------AKLQEEI-QLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKK 241
Cdd:COG4913  372 GlplpasaeefAALRAEAaALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
174-286 5.20e-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: 5.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  174 ARVDVERDNLLDDLQRLKAKLqeeIQLKEEAEnnlaAFRADVDAATLARID-LERRIESLNEEIAFLKKVHEEEIRELQA 252
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRL---EQLEIEKE----ALKKEQDEASFERLAeLRDELAELEEELEALKARWEAEKELIEE 472
                        90       100       110
                ....*....|....*....|....*....|....
gi 6531404  253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAA 286
Cdd:COG0542 473 IQELKEELEQRYGKIPELEKELAELEEELAELAP 506
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
179-387 8.18e-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: 8.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  179 ERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLkkvhEEEIRE--LQAQLQE 256
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAEleKEIAELR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404  257 QQVQVEMDMSKPDLTAALRDIRAQYETI--AAKNISEAE---EWYKSKV---SDLTQAANKNNDALRQAKQEMMEYRHQI 328
Cdd:COG4942  97 AELEAQKEELAELLRALYRLGRQPPLALllSPEDFLDAVrrlQYLKYLAparREQAEELRADLAELAALRAELEAERAEL 176
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6531404  329 QSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLRE 387
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
PRK11281 PRK11281
mechanosensitive channel MscK;
276-411 8.29e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 8.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    276 DIRAQYETIAAKNISEAEEwyKSKVSDLTQA---------ANKNNDALRQAKQEMMEyrhQIQSYTCEIDALKGTNDSLM 346
Cdd:PRK11281   40 DVQAQLDALNKQKLLEAED--KLVQQDLEQTlalldkidrQKEETEQLKQQLAQAPA---KLRQAQAELEALKDDNDEET 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6531404    347 RQ------MRELEDRFA-----------------SEASGYQ-----------DNIARLeEEIRHL----KDEMARHLREY 388
Cdd:PRK11281  115 REtlstlsLRQLESRLAqtldqlqnaqndlaeynSQLVSLQtqperaqaalyANSQRL-QQIRNLlkggKVGGKALRPSQ 193
                         170       180
                  ....*....|....*....|....
gi 6531404    389 QDLLNVKMA-LDVEIATYRKLLEG 411
Cdd:PRK11281  194 RVLLQAEQAlLNAQNDLQRKSLEG 217
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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