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Conserved domains on  [gi|71011040|gb|AAZ17411|]
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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 1.79e-123

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 362.32  E-value: 1.79e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040   107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040   184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040   264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDARKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71011040   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 2.02e-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: 2.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040     9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732   1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65
                          90
                  ....*....|....*...
gi 71011040    89 LDFSLADAVNQEFLTTRT 106
Cdd:pfam04732  66 LDFSLADALNQEFKATRT 83
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
107-415 1.79e-123

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 362.32  E-value: 1.79e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040   107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040   184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040   264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDARKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71011040   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 2.02e-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: 2.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040     9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732   1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65
                          90
                  ....*....|....*...
gi 71011040    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 2.73e-07

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: 53.14  E-value: 2.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLK--GREPTRVAELYEEELRELRRQVEVLTNQRARVDVER 180
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    181 DNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADvdaatlaRIDLERRIESLNEEIAFLKK--------VHEEEIRELQA 252
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREaldelraeLTLLNEEAANL 822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYksKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 332
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALALLRSELEELS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    333 CEIDARKGTNDSLMRQMRELEDRFASeasgYQDNIARLEEEIRHLKDEMArhlREYQDLLNVKMALDVEIATYRKLLEGE 412
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR 973

                   ....*....
gi 71011040    413 ESRINLPIQ 421
Cdd:TIGR02168  974 LKRLENKIK 982
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-404 3.55e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 3.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040  111 ELQELNDRFANyiekvrfLEQQNAALAAEVNRLKGReptRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRL 190
Cdd:COG4913  618 ELAELEEELAE-------AEERLEALEAELDALQER---REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040  191 KAkLQEEIqlkEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEeirelqaqlqeqqvqvEMDMSKPDL 270
Cdd:COG4913  688 AA-LEEQL---EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA----------------AEDLARLEL 747
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040  271 TAALRDIRAQYetIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAkqeMMEYRHQIQSYTCEIDARKGTNDSLMRQMR 350
Cdd:COG4913  748 RALLEERFAAA--LGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLD 822
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71011040  351 ELEDrfaseasgyqDNIARLEEEIRHLKDEmarhlREYQDLLNVKMALDVEIAT 404
Cdd:COG4913  823 RLEE----------DGLPEYEERFKELLNE-----NSIEFVADLLSKLRRAIRE 861
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
107-415 1.79e-123

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 362.32  E-value: 1.79e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040   107 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNL 183
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040   184 LDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 263
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040   264 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDARKGTN 342
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71011040   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 2.02e-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: 2.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040     9 QRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGfgskgssssvtsRVYQVSRTSGGAGGLGslRASRLGTTRTPSSYgAGEL 88
Cdd:pfam04732   1 YSSSSYRRMFGDSSSSRPSYSSSSGSRSVSS------------RSYSRSSSSSPSSSSR--RSSRSSSRSSYPSL-AADS 65
                          90
                  ....*....|....*...
gi 71011040    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 2.73e-07

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: 53.14  E-value: 2.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLK--GREPTRVAELYEEELRELRRQVEVLTNQRARVDVER 180
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEeeLEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    181 DNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADvdaatlaRIDLERRIESLNEEIAFLKK--------VHEEEIRELQA 252
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREaldelraeLTLLNEEAANL 822
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYksKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 332
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALALLRSELEELS 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    333 CEIDARKGTNDSLMRQMRELEDRFASeasgYQDNIARLEEEIRHLKDEMArhlREYQDLLNVKMALDVEIATYRKLLEGE 412
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR 973

                   ....*....
gi 71011040    413 ESRINLPIQ 421
Cdd:TIGR02168  974 LKRLENKIK 982
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-404 3.55e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 3.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040  111 ELQELNDRFANyiekvrfLEQQNAALAAEVNRLKGReptRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRL 190
Cdd:COG4913  618 ELAELEEELAE-------AEERLEALEAELDALQER---REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL 687
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040  191 KAkLQEEIqlkEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEeirelqaqlqeqqvqvEMDMSKPDL 270
Cdd:COG4913  688 AA-LEEQL---EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA----------------AEDLARLEL 747
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040  271 TAALRDIRAQYetIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAkqeMMEYRHQIQSYTCEIDARKGTNDSLMRQMR 350
Cdd:COG4913  748 RALLEERFAAA--LGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLD 822
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 71011040  351 ELEDrfaseasgyqDNIARLEEEIRHLKDEmarhlREYQDLLNVKMALDVEIAT 404
Cdd:COG4913  823 RLEE----------DGLPEYEERFKELLNE-----NSIEFVADLLSKLRRAIRE 861
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
165-414 1.35e-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: 1.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHE 244
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 245 EEIRELQAQLQEQQVQVEMDMSkpdLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEY 324
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEE---AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 325 RHQIQSytCEIDARKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIAT 404
Cdd:COG1196 411 ALLERL--ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
                       250
                ....*....|
gi 71011040 405 YRKLLEGEES 414
Cdd:COG1196 489 AAARLLLLLE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
88-373 3.44e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 3.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040  88 LLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREptrvaelyeeelRELRRQVE 167
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE------------YELLAELA 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 168 VLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEI 247
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 248 RELQAQLQEQQvqvemdmskpDLTAALRDIRAQYETIAAKNISEAEEwykskVSDLTQAANKNNDALRQAKQEMMEYRHQ 327
Cdd:COG1196 379 EELEELAEELL----------EALRAAAELAAQLEELEEAEEALLER-----LERLEEELEELEEALAELEEEEEEEEEA 443
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 71011040 328 IQSYTCEIDARKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEE 373
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
166-469 3.55e-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: 3.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    166 VEVLTNQRARVDVERDNLL--DDLQRLKAKLQEEIQL--KEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAflkk 241
Cdd:TIGR02169  193 IDEKRQQLERLRREREKAEryQALLKEKREYEGYELLkeKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE---- 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    242 vheeeirelqaqlqeqqvqvemdmskpdltAALRDIRAQYETIAAKNISEAEEwYKSKVSDLTQAANKNNDALRQAKQEM 321
Cdd:TIGR02169  269 ------------------------------EIEQLLEELNKKIKDLGEEEQLR-VKEKIGELEAEIASLERSIAEKEREL 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    322 MEYRHQIQSYTCEIDARKGTNDSLMRQMRELEDRFASeasgyqdniarLEEEIRHLKDEMARHLREYQDLLNVKMALDVE 401
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK-----------LTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71011040    402 IATYRKLLEGEESRINLPIQTYSALNFRETSPEQRGSEVHTKktvmIKTIETRDGEVVSEATQQQHEV 469
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA----IAGIEAKINELEEEKEDKALEI 450
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
103-393 5.38e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.82  E-value: 5.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 103 TTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAelyeeelrelrrQVEVLTNQRARVDVERDN 182
Cdd:COG1340   1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNA------------QVKELREEAQELREKRDE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 183 LLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARID---LERRIESLneEIAFLKKVH--EEEIRelqaqlqeq 257
Cdd:COG1340  69 LNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERL--EWRQQTEVLspEEEKE--------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 258 qvqvemdmskpdLTAALRDIRAQYETIaaknisEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDA 337
Cdd:COG1340 138 ------------LVEKIKELEKELEKA------KKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71011040 338 RKGTNDSLMRQMRELedrfASEASGYQDNIARLEEEIrhlkDEMARHLREYQDLLN 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 1.39e-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: 41.20  E-value: 1.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHE 244
Cdd:TIGR02168  240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    245 EEIRELQAQLQEQQVQVEmdmSKPDLTAALRDIRAQYETIAAKNISEAEEWY--KSKVSDLTQAANKNNDALRQAKQEMM 322
Cdd:TIGR02168  320 ELEAQLEELESKLDELAE---ELAELEEKLEELKEELESLEAELEELEAELEelESRLEELEEQLETLRSKVAQLELQIA 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    323 EYRHQIQSYTCEIDARKGTNDSLMRQMRELEDRFAS-EASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVE 401
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
                          250
                   ....*....|....*..
gi 71011040    402 IATYRKLLEGEESRINL 418
Cdd:TIGR02168  477 LDAAERELAQLQARLDS 493
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
170-407 2.22e-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: 2.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 170 TNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKvHEEEIRE 249
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRA 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 250 LQAQLQEQQVQVemdmskpdLTAALRDIRAQYETI--AAKNISEAEEWYKSkVSDLTQAANKNNDALRQAKQEMMEYRHQ 327
Cdd:COG4942  98 ELEAQKEELAEL--------LRALYRLGRQPPLALllSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 328 IQsytceidARKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRK 407
Cdd:COG4942 169 LE-------AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
165-393 3.71e-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: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040  165 QVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLAR--IDLERRIESLNEEIAFLKKV 242
Cdd:COG4913  611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiAELEAELERLDASSDDLAAL 690
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040  243 HEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETiAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMM 322
Cdd:COG4913  691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE-LQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71011040  323 EYRHQIQSYTceiDARKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLK----DEMARHLREYQDLLN 393
Cdd:COG4913  770 NLEERIDALR---ARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDrleeDGLPEYEERFKELLN 841
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-241 4.22e-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: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040  111 ELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGReptrVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRL 190
Cdd:COG4913  296 ELEELRAELARLEAELERLEARLDALREELDELEAQ----IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL 371
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71011040  191 K----------AKLQEEI-QLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKK 241
Cdd:COG4913  372 GlplpasaeefAALRAEAaALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
162-387 4.92e-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: 38.98  E-value: 4.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 162 LRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDaatlariDLERRIESLNEEIAFLKK 241
Cdd:COG4942  32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAELRAELEAQKE 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 242 VHEEEIRelQAQLQEQQVQVEMDMSKPDLTAALRDIRAqYETIAAKNISEAEEWykskvsdltqaaNKNNDALRQAKQEM 321
Cdd:COG4942 105 ELAELLR--ALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEEL------------RADLAELAALRAEL 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71011040 322 MEYRHQIQSYTCEIDARKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLRE 387
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
174-286 5.33e-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: 5.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040 174 ARVDVERDNLLDDLQRLKAKLqeeIQLKEEAEnnlaAFRADVDAATLARID-LERRIESLNEEIAFLKKVHEEEIRELQA 252
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRL---EQLEIEKE----ALKKEQDEASFERLAeLRDELAELEEELEALKARWEAEKELIEE 472
                        90       100       110
                ....*....|....*....|....*....|....
gi 71011040 253 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAA 286
Cdd:COG0542 473 IQELKEELEQRYGKIPELEKELAELEEELAELAP 506
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
184-410 6.75e-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: 39.28  E-value: 6.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    184 LDDLQRLKAKLQEEIqlkEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 263
Cdd:TIGR02169  683 LEGLKRELSSLQSEL---RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    264 ----DMSKPDLTAALRDIRAQYETIAAK-----------NISEAEEWYK---SKVSDLTQAANKNNDALRQAKQEMMEYR 325
Cdd:TIGR02169  760 lkelEARIEELEEDLHKLEEALNDLEARlshsripeiqaELSKLEEEVSrieARLREIEQKLNRLTLEKEYLEKEIQELQ 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    326 HQIQSYTCEIDARKGTNDSLMRQMRELEdrfaSEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATY 405
Cdd:TIGR02169  840 EQRIDLKEQIKSIEKEIENLNGKKEELE----EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915

                   ....*
gi 71011040    406 RKLLE 410
Cdd:TIGR02169  916 RKRLS 920
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
108-427 8.73e-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: 38.90  E-value: 8.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    108 EKVELQELNDRfanyIEKvrfLEQQNAALAAEVNRLKGR--EPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLD 185
Cdd:TIGR02169  672 EPAELQRLRER----LEG---LKRELSSLQSELRRIENRldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    186 DLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRI------------ESLNEEI-----------AFLKKV 242
Cdd:TIGR02169  745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsripeiqaelSKLEEEVsriearlreieQKLNRL 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    243 HEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAA--KNISEAEEWYKSKVSDLTQAANKNNDALRQAKQE 320
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71011040    321 MMEYRHQIQSYTCEIDARKGTNDSLMRQMRELEDRFASEAS---------GYQDNIARLEEEIRHLK-------DEMARH 384
Cdd:TIGR02169  905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsleDVQAELQRVEEEIRALEpvnmlaiQEYEEV 984
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 71011040    385 LREYQDLLNVKMALDVEIATYRKLLEG-EESRINLPIQTYSALN 427
Cdd:TIGR02169  985 LKRLDELKEKRAKLEEERKAILERIEEyEKKKREVFMEAFEAIN 1028
 
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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