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Conserved domains on  [gi|440355928|gb|AGC00771|]
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mutant desmin p.K241E [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 3.19e-123

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 361.55  E-value: 3.19e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKEVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 440355928  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 1.55e-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: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928    9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732   1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65

                          90
                  ....*....|....*...
gi 440355928   89 LDFSLADAVNQEFLTTRT 106
Cdd:pfam04732  66 LDFSLADALNQEFKATRT 83
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
107-415 3.19e-123

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 361.55  E-value: 3.19e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKEVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 440355928  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 1.55e-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: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928    9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732   1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65

                          90
                  ....*....|....*...
gi 440355928   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 2.45e-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: 56.60  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLK--GREPTRVAELYEEELRELRRQVEVLTNQRARVDVER 180
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   181 DNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADvdaatlaRIDLERRIESLNEEI--------AFLKEVHEEEIRELQA 252
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELkalrealdELRAELTLLNEEAANL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYksKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 332
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   333 CEIDALKGTNDSLMRQMRELEDRFASeasgYQDNIARLEEEIRHLKDEMArhlREYQDLLNVKMALDVEIATYRKLLEGE 412
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR 973


                   ....*....
gi 440355928   413 ESRINLPIQ 421
Cdd:TIGR02168  974 LKRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-416 1.18e-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: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKEVHE 244
Cdd:COG1196  254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 245 EEIRELQaqlqeqqvqvemdmskpDLTAALRDIRAQYETIAAKNISEAEEwykskVSDLTQAANKNNDALRQAKQEMMEY 324
Cdd:COG1196  334 ELEEELE-----------------ELEEELEEAEEELEEAEAELAEAEEA-----LLEAEAELAEAEEELEELAEELLEA 391

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 325 RHQIQSYTCEIDALKGTNDSLMRQMRELEdrfaSEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIAT 404
Cdd:COG1196  392 LRAAAELAAQLEELEEAEEALLERLERLE----EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467

                        250
                 ....*....|..
gi 440355928 405 YRKLLEGEESRI 416
Cdd:COG1196  468 LLEEAALLEAAL 479
PRK11281 PRK11281
mechanosensitive channel MscK;
276-411 9.26e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 9.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  276 DIRAQYETIAAKNISEAEEwyKSKVSDLTQA---------ANKNNDALRQAKQEMMEyrhQIQSYTCEIDALKGTNDSLM 346
Cdd:PRK11281   40 DVQAQLDALNKQKLLEAED--KLVQQDLEQTlalldkidrQKEETEQLKQQLAQAPA---KLRQAQAELEALKDDNDEET 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  347 RQ------MRELEDRFA-----------------SEASGYQ-----------DNIARLeEEIRHL----KDEMARHLREY 388
Cdd:PRK11281  115 REtlstlsLRQLESRLAqtldqlqnaqndlaeynSQLVSLQtqperaqaalyANSQRL-QQIRNLlkggKVGGKALRPSQ 193

                         170       180
                  ....*....|....*....|....
gi 440355928  389 QDLLNVKMA-LDVEIATYRKLLEG 411
Cdd:PRK11281  194 RVLLQAEQAlLNAQNDLQRKSLEG 217
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
107-415 3.19e-123

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 361.55  E-value: 3.19e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKEVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 440355928  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 1.55e-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: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928    9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732   1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65

                          90
                  ....*....|....*...
gi 440355928   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 2.45e-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: 56.60  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLK--GREPTRVAELYEEELRELRRQVEVLTNQRARVDVER 180
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   181 DNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADvdaatlaRIDLERRIESLNEEI--------AFLKEVHEEEIRELQA 252
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELkalrealdELRAELTLLNEEAANL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYksKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 332
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   333 CEIDALKGTNDSLMRQMRELEDRFASeasgYQDNIARLEEEIRHLKDEMArhlREYQDLLNVKMALDVEIATYRKLLEGE 412
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR 973


                   ....*....
gi 440355928   413 ESRINLPIQ 421
Cdd:TIGR02168  974 LKRLENKIK 982
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-416 1.18e-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: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKEVHE 244
Cdd:COG1196  254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 245 EEIRELQaqlqeqqvqvemdmskpDLTAALRDIRAQYETIAAKNISEAEEwykskVSDLTQAANKNNDALRQAKQEMMEY 324
Cdd:COG1196  334 ELEEELE-----------------ELEEELEEAEEELEEAEAELAEAEEA-----LLEAEAELAEAEEELEELAEELLEA 391

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 325 RHQIQSYTCEIDALKGTNDSLMRQMRELEdrfaSEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIAT 404
Cdd:COG1196  392 LRAAAELAAQLEELEEAEEALLERLERLE----EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467

                        250
                 ....*....|..
gi 440355928 405 YRKLLEGEESRI 416
Cdd:COG1196  468 LLEEAALLEAAL 479
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
103-393 7.93e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.52  E-value: 7.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAelyeeelrelrrQVEVLTNQRARVDVERDN 182
Cdd:COG1340    1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNA------------QVKELREEAQELREKRDE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 183 LLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARID---LERRIESLneEIAFLKEVH--EEEIRelqaqlqeq 257
Cdd:COG1340   69 LNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERL--EWRQQTEVLspEEEKE--------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 258 qvqvemdmskpdLTAALRDIRAQYETIaaknisEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDA 337
Cdd:COG1340  138 ------------LVEKIKELEKELEKA------KKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE 199

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 440355928 338 LKGTNDSLMRQMRELedrfASEASGYQDNIARLEEEIrhlkDEMARHLREYQDLLN 393
Cdd:COG1340  200 LYKEADELRKEADEL----HKEIVEAQEKADELHEEI----IELQKELRELRKELK 247
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 88-373 1.23e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  88 LLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREptrvaelyeeelRELRRQVE 167
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE------------YELLAELA 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 168 VLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKEVHEEEI 247
Cdd:COG1196  299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 248 RELQAQLQEQQvqvemdmskpDLTAALRDIRAQYETIAAKNISEAEEwykskVSDLTQAANKNNDALRQAKQEMMEYRHQ 327
Cdd:COG1196  379 EELEELAEELL----------EALRAAAELAAQLEELEEAEEALLER-----LERLEEELEELEEALAELEEEEEEEEEA 443

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 440355928 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 1.34e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   166 VEVLTNQRARVDVERDNLL--DDLQRLKAKLQEEIQL--KEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAflke 241
Cdd:TIGR02169  193 IDEKRQQLERLRREREKAEryQALLKEKREYEGYELLkeKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE---- 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   242 vheeeirelqaqlqeqqvqvemdmskpdltAALRDIRAQYETIAAKNISEAEEwYKSKVSDLTQAANKNNDALRQAKQEM 321
Cdd:TIGR02169  269 ------------------------------EIEQLLEELNKKIKDLGEEEQLR-VKEKIGELEAEIASLERSIAEKEREL 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   322 MEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASeasgyqdniarLEEEIRHLKDEMARHLREYQDLLNVKMALDVE 401
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK-----------LTEEYAELKEELEDLRAELEEVDKEFAETRDE 386

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440355928   402 IATYRKLLEGEESRINLPIQTYSALNFRETSPEQRGSEVHTKktvmIKTIETRDGEVVSEATQQQHEV 469
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA----IAGIEAKINELEEEKEDKALEI 450
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-418 2.61e-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: 43.51  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEiafLKEVHE 244
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER---LANLER 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   245 EEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWY--KSKVSDLTQAANKNNDALRQAKQEMM 322
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEelESRLEELEEQLETLRSKVAQLELQIA 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   323 EYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFAS-EASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVE 401
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476

                          250
                   ....*....|....*..
gi 440355928   402 IATYRKLLEGEESRINL 418
Cdd:TIGR02168  477 LDAAERELAQLQARLDS 493
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
165-393 1.65e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLAR--IDLERRIESLNEEIAFLKEV 242
Cdd:COG4913   611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiAELEAELERLDASSDDLAAL 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  243 HEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETiAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMM 322
Cdd:COG4913   691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE-LQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 440355928  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 2.40e-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: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 162 LRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDaatlariDLERRIESLNEEIAFLKE 241
Cdd:COG4942   32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAELRAELEAQKE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 242 VHEEEIRelQAQLQEQQVQVEMDMSKPDLTAALRdiRAQYETIAAKNISEAEEWYKSKVSDLTQaankNNDALRQAKQEM 321
Cdd:COG4942  105 ELAELLR--ALYRLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAELAA----LRAELEAERAEL 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440355928 322 MEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMAR 383
Cdd:COG4942  177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 174-286 3.65e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.06  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 174 ARVDVERDNLLDDLQRLKAKLqeeIQLKEEAEnnlaAFRADVDAATLARID-LERRIESLNEEIAFLKEVHEEEIRELQA 252
Cdd:COG0542  400 ARVRMEIDSKPEELDELERRL---EQLEIEKE----ALKKEQDEASFERLAeLRDELAELEEELEALKARWEAEKELIEE 472

                         90       100       110
                 ....*....|....*....|....*....|....
gi 440355928 253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAA 286
Cdd:COG0542  473 IQELKEELEQRYGKIPELEKELAELEEELAELAP 506
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
172-361 3.97e-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: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  172 QRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARID-LERRIESLNEEIAflkevheeeiREL 250
Cdd:COG4913   289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELE----------ERE 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  251 QAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKniseaeewYKSKVSDLTQAANKNNDALRQAKQEmmeyRHQIQS 330
Cdd:COG4913   359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA--------LEEELEALEEALAEAEAALRDLRRE----LRELEA 426

                         170       180       190
                  ....*....|....*....|....*....|.
gi 440355928  331 ytcEIDALKGTNDSLMRQMRELEDRFASEAS 361
Cdd:COG4913   427 ---EIASLERRKSNIPARLLALRDALAEALG 454
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 212-417 4.04e-03

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: 39.65  E-value: 4.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   212 RADVDAATLARidlERRIESLNEEIAFLK----EVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAK 287
Cdd:TIGR02168  665 SAKTNSSILER---RREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   288 NISEAEEW---------YKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFAS 358
Cdd:TIGR02168  742 VEQLEERIaqlskelteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928   359 EASGYQDN------------------------IARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEES 414
Cdd:TIGR02168  822 LRERLESLerriaaterrledleeqieelsedIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901


                   ...
gi 440355928   415 RIN 417
Cdd:TIGR02168  902 ELR 904
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-286 5.01e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  111 ELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL------- 183
Cdd:COG4913   256 PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaqirgn 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  184 -LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKEVHEEEIRELQAQLQeqqvqve 262
Cdd:COG4913   336 gGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA------- 408

                         170       180
                  ....*....|....*....|....
gi 440355928  263 mdmskpDLTAALRDIRAQYETIAA 286
Cdd:COG4913   409 ------EAEAALRDLRRELRELEA 426
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 179-387 8.47e-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: 38.21  E-value: 8.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 179 ERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLK------EVHEEEIRELQA 252
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaelaelEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928 253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 332
Cdd:COG4942  101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 440355928 333 CEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLRE 387
Cdd:COG4942  181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
PRK11281 PRK11281
mechanosensitive channel MscK;
276-411 9.26e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 38.74  E-value: 9.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  276 DIRAQYETIAAKNISEAEEwyKSKVSDLTQA---------ANKNNDALRQAKQEMMEyrhQIQSYTCEIDALKGTNDSLM 346
Cdd:PRK11281   40 DVQAQLDALNKQKLLEAED--KLVQQDLEQTlalldkidrQKEETEQLKQQLAQAPA---KLRQAQAELEALKDDNDEET 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440355928  347 RQ------MRELEDRFA-----------------SEASGYQ-----------DNIARLeEEIRHL----KDEMARHLREY 388
Cdd:PRK11281  115 REtlstlsLRQLESRLAqtldqlqnaqndlaeynSQLVSLQtqperaqaalyANSQRL-QQIRNLlkggKVGGKALRPSQ 193

                         170       180
                  ....*....|....*....|....
gi 440355928  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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