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Conserved domains on  [gi|33563250|ref|NP_034173|]
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desmin [Mus musculus]

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;
106-414 2.98e-132

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 384.66  E-value: 2.98e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   106 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEEMRELRRQVEVLTNQRARVDVERDNL 182
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   183 IDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 262
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   263 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 341
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33563250   342 DSLMRQMRELEDRFASEANGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESR 414
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 9-105 1.71e-20

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: 85.52  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250     9 QRVSSYRRTFGGapgfslgsplssPVFPRAGFGTKGSSSSMTSRVYQVSRTSGGAGGLGslRSSRLGTTRAPSYGAGELL 88
Cdd:pfam04732   1 YSSSSYRRMFGD------------SSSSRPSYSSSSGSRSVSSRSYSRSSSSSPSSSSR--RSSRSSSRSSYPSLAADSL 66

                          90
                  ....*....|....*..
gi 33563250    89 DFSLADAVNQEFLATRT 105
Cdd:pfam04732  67 DFSLADALNQEFKATRT 83
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
106-414 2.98e-132

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 384.66  E-value: 2.98e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   106 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEEMRELRRQVEVLTNQRARVDVERDNL 182
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   183 IDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 262
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   263 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 341
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33563250   342 DSLMRQMRELEDRFASEANGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESR 414
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 9-105 1.71e-20

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: 85.52  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250     9 QRVSSYRRTFGGapgfslgsplssPVFPRAGFGTKGSSSSMTSRVYQVSRTSGGAGGLGslRSSRLGTTRAPSYGAGELL 88
Cdd:pfam04732   1 YSSSSYRRMFGD------------SSSSRPSYSSSSGSRSVSSRSYSRSSSSSPSSSSR--RSSRSSSRSSYPSLAADSL 66

                          90
                  ....*....|....*..
gi 33563250    89 DFSLADAVNQEFLATRT 105
Cdd:pfam04732  67 DFSLADALNQEFKATRT 83
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-427 1.58e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 1.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    102 ATRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEEMR--ELRRQVEVLTNQRARVDVER 179
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    180 DNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADvdaatlaRIDLERRIESLNEEIAFLKK--------VHEEEIRELQA 251
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREaldelraeLTLLNEEAANL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    252 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYksKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 331
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    332 CEIDALKGTNDSLMRQMRELEDRFASeangYQDNIARLEEEIRHLKDEMArhlREYQDLLNVKMALDVEIATYRKLLEGE 411
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR 973

                          330
                   ....*....|....*.
gi 33563250    412 ESRINLPIQTFSALNF 427
Cdd:TIGR02168  974 LKRLENKIKELGPVNL 989
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-415 6.24e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 6.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 151 AELYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIES 230
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 231 LNEEIAFLKKVHEEEIRELQaqlqeqqvqvemdmskpDLTAALRDIRAQYETIAAKNISEAEEwykskVSDLTQAANKNN 310
Cdd:COG1196 321 LEEELAELEEELEELEEELE-----------------ELEEELEEAEEELEEAEAELAEAEEA-----LLEAEAELAEAE 378

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 311 DALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEdrfaSEANGYQDNIARLEEEIRHLKDEMARHLREYQDL 390
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE----EELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                       250       260
                ....*....|....*....|....*
gi 33563250 391 LNVKMALDVEIATYRKLLEGEESRI 415
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAAL 479
46 PHA02562
endonuclease subunit; Provisional
 161-386 3.04e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  161 LRRQVEVLTNQRARVDVERDNLIddlQRLKA--KLQEEiqLREEAENNLAAFRADVD-AATLARiDLERRIESLNEEIAf 237
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQ---QQIKTynKNIEE--QRKKNGENIARKQNKYDeLVEEAK-TIKAEIEELTDELL- 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  238 lkkvheeeirelqaqlqeqqvqvEMDMSKPDLTAALRDIRAQYETIAAK----------------------NISEAEEWY 295
Cdd:PHA02562 245 -----------------------NLVMDIEDPSAALNKLNTAAAKIKSKieqfqkvikmyekggvcptctqQISEGPDRI 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  296 ---KSKVSDLTQAANKNNDALRQAKQEMMEYRHQ---IQSYTCEIDALKGTNDSLMRQMRELE---DRFASEANGYQDNI 366
Cdd:PHA02562 302 tkiKDKLKELQHSLEKLDTAIDELEEIMDEFNEQskkLLELKNKISTNKQSLITLVDKAKKVKaaiEELQAEFVDNAEEL 381

                        250       260
                 ....*....|....*....|
gi 33563250  367 ARLEEEIRHLKDEMARHLRE 386
Cdd:PHA02562 382 AKLQDELDKIVKTKSELVKE 401
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 293-416 6.39e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.46  E-value: 6.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    293 EWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYtceIDALKGTNDSLMRQMRELEdRFASEANGY-QDNIARLEE 371
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSI---KPKLRDRKDALEEELRQLK-QLEDELEDCdPTELDRAKE 211

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 33563250    372 EIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRIN 416
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIA 256
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
106-414 2.98e-132

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 384.66  E-value: 2.98e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   106 NEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAELYEEEMRELRRQVEVLTNQRARVDVERDNL 182
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   183 IDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEM 262
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   263 DMS-KPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTN 341
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33563250   342 DSLMRQMRELEDRFASEANGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESR 414
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 9-105 1.71e-20

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: 85.52  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250     9 QRVSSYRRTFGGapgfslgsplssPVFPRAGFGTKGSSSSMTSRVYQVSRTSGGAGGLGslRSSRLGTTRAPSYGAGELL 88
Cdd:pfam04732   1 YSSSSYRRMFGD------------SSSSRPSYSSSSGSRSVSSRSYSRSSSSSPSSSSR--RSSRSSSRSSYPSLAADSL 66

                          90
                  ....*....|....*..
gi 33563250    89 DFSLADAVNQEFLATRT 105
Cdd:pfam04732  67 DFSLADALNQEFKATRT 83
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-427 1.58e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 1.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    102 ATRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEEMR--ELRRQVEVLTNQRARVDVER 179
Cdd:TIGR02168  670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    180 DNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADvdaatlaRIDLERRIESLNEEIAFLKK--------VHEEEIRELQA 251
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREaldelraeLTLLNEEAANL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    252 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYksKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYT 331
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE--LIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    332 CEIDALKGTNDSLMRQMRELEDRFASeangYQDNIARLEEEIRHLKDEMArhlREYQDLLNVKMALDVEIATYRKLLEGE 411
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQ----LELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRR 973

                          330
                   ....*....|....*.
gi 33563250    412 ESRINLPIQTFSALNF 427
Cdd:TIGR02168  974 LKRLENKIKELGPVNL 989
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 151-415 6.24e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.41  E-value: 6.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 151 AELYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIES 230
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 231 LNEEIAFLKKVHEEEIRELQaqlqeqqvqvemdmskpDLTAALRDIRAQYETIAAKNISEAEEwykskVSDLTQAANKNN 310
Cdd:COG1196 321 LEEELAELEEELEELEEELE-----------------ELEEELEEAEEELEEAEAELAEAEEA-----LLEAEAELAEAE 378

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 311 DALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEdrfaSEANGYQDNIARLEEEIRHLKDEMARHLREYQDL 390
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE----EELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                       250       260
                ....*....|....*....|....*
gi 33563250 391 LNVKMALDVEIATYRKLLEGEESRI 415
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAAL 479
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
110-403 5.42e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 5.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  110 ELQELNDRFANYIEKVRFLEQQNAALAAEVNRLkgrepTRVAELYEEE--MRELRRQVEVLTNQRARVDveRDNliDDLQ 187
Cdd:COG4913  618 ELAELEEELAEAEERLEALEAELDALQERREAL-----QRLAEYSWDEidVASAEREIAELEAELERLD--ASS--DDLA 688

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  188 RLKAKLqeeiqlrEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEeirelqaqlqeqqvqvEMDMSKP 267
Cdd:COG4913  689 ALEEQL-------EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA----------------AEDLARL 745

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  268 DLTAALRDIRAQYetIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAkqeMMEYRHQIQSYTCEIDALKGTNDSLMRQ 347
Cdd:COG4913  746 ELRALLEERFAAA--LGDAVERELRENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLAL 820

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 33563250  348 MRELEDrfaseangyqDNIARLEEEIRHLKDEmarhlREYQDLLNVKMALDVEIAT 403
Cdd:COG4913  821 LDRLEE----------DGLPEYEERFKELLNE-----NSIEFVADLLSKLRRAIRE 861
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-416 6.37e-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: 6.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    170 NQRARVDVERDNLIDDLQRLKAKLQEEIqlrEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIREL 249
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKI---AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    250 QAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEwYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQS 329
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE-LEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    330 YTCEIDALKGTNDSLMRQMRELEDRFASEangyQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLE 409
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEEL----SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897


                   ....*..
gi 33563250    410 GEESRIN 416
Cdd:TIGR02168  898 ELSEELR 904
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
103-392 3.84e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 51.45  E-value: 3.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 103 TRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKgreptrvaelyeEEMRELRRQVEVLTNQRARVDVERDNL 182
Cdd:COG1340   2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELA------------EKRDELNAQVKELREEAQELREKRDEL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 183 IDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARID---LERRIESLneEIAFLKKVH--EEEIRelqaqlqeqq 257
Cdd:COG1340  70 NEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidkLRKEIERL--EWRQQTEVLspEEEKE---------- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 258 vqvemdmskpdLTAALRDIRAQYETIaaknisEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDAL 337
Cdd:COG1340 138 -----------LVEKIKELEKELEKA------KKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIEL 200

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 33563250 338 KGTNDSLMRQMRELedrfASEANGYQDNIARLEEEIrhlkDEMARHLREYQDLLN 392
Cdd:COG1340 201 YKEADELRKEADEL----HKEIVEAQEKADELHEEI----IELQKELRELRKELK 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 152-417 3.37e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 3.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    152 ELYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIESL 231
Cdd:TIGR02168  228 ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    232 NEEIAFLKKVHEEEIRELQAQLQEQQVQVEmdmSKPDLTAALRDIRAQYETIAAKNISEAEEWY--KSKVSDLTQAANKN 309
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELESKLDELAE---ELAELEEKLEELKEELESLEAELEELEAELEelESRLEELEEQLETL 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    310 NDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFAS-EANGYQDNIARLEEEIRHLKDEMARHLREYQ 388
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALE 464

                          250       260
                   ....*....|....*....|....*....
gi 33563250    389 DLLNVKMALDVEIATYRKLLEGEESRINL 417
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQARLDS 493
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 112-415 3.76e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 49.73  E-value: 3.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    112 QELNDRFANYIEKVRFLEQQNAALAAEVnrlkgREPTRvaeLYEEEMRELRRQVEVLTNQRARVDVERD-------NLID 184
Cdd:pfam15921  306 EQARNQNSMYMRQLSDLESTVSQLRSEL-----REAKR---MYEDKIEELEKQLVLANSELTEARTERDqfsqesgNLDD 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    185 DLQRLKAKLQE-EIQLREEAENNLAAFraDVDAATLARID-LERRIESLNEEIAFLK---KVHEEEIRELQAQLQEQQVQ 259
Cdd:pfam15921  378 QLQKLLADLHKrEKELSLEKEQNKRLW--DRDTGNSITIDhLRRELDDRNMEVQRLEallKAMKSECQGQMERQMAAIQG 455

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    260 VEMDMSK-PDLTAALRD----IRAQYETIAAKNISeaEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEI 334
Cdd:pfam15921  456 KNESLEKvSSLTAQLEStkemLRKVVEELTAKKMT--LESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL 533

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    335 DALKGTNDSLMRQMRELEdRFASEANGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRklLEGEESR 414
Cdd:pfam15921  534 QHLKNEGDHLRNVQTECE-ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR--LELQEFK 610


                   .
gi 33563250    415 I 415
Cdd:pfam15921  611 I 611
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 122-352 6.71e-06

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: 48.91  E-value: 6.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    122 IEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLRE 201
Cdd:TIGR02169  253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    202 EAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLK-KVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDI---- 276
Cdd:TIGR02169  333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRaELEEVDKEFAETRDELKDYREKLEKLKREINELKRELdrlq 412

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33563250    277 -RAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELE 352
Cdd:TIGR02169  413 eELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 155-382 7.40e-06

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: 47.84  E-value: 7.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 155 EEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDaatlariDLERRIESLNEE 234
Cdd:COG4942  26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAELRAE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 235 IAFLKKVHEEEIRelQAQLQEQQVQVEMDMSKPDLTAALRdiRAQYETIAAKNISEAEEWYKSKVSDLTQaankNNDALR 314
Cdd:COG4942  99 LEAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAELAA----LRAELE 170

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33563250 315 QAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEANGYQDNIARLEEEIRHLKDEMAR 382
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
110-240 8.90e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 8.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  110 ELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYE---EEMRELRRQVEVLTNQRARVDVERDNLIDDL 186
Cdd:COG4913  289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggDRLEQLEREIERLERELEERERRRARLEALL 368

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33563250  187 QRLK----------AKLQEEI-QLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKK 240
Cdd:COG4913  369 AALGlplpasaeefAALRAEAaALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
110-360 1.98e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  110 ELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKgreptrvAELYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRL 189
Cdd:COG4913  256 PIRELAERYAAARERLAELEYLRAALRLWFAQRR-------LELLEAELEELRAELARLEAELERLEARLDALREELDEL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  190 KAklqeeiQLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLkkvheeeirelqaqlqeqqvqvemDMSKPDL 269
Cdd:COG4913  329 EA------QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL------------------------GLPLPAS 378

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  270 TAALRDIRAQYETIAAKniseaeewYKSKVSDLTQAANKNNDALRQAKQEmmeyRHQIQSytcEIDALKGTNDSLMRQMR 349
Cdd:COG4913  379 AEEFAALRAEAAALLEA--------LEEELEALEEALAEAEAALRDLRRE----LRELEA---EIASLERRKSNIPARLL 443

                        250
                 ....*....|.
gi 33563250  350 ELEDRFASEAN 360
Cdd:COG4913  444 ALRDALAEALG 454
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 150-468 3.00e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 3.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    150 VAElYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRL---KAKLQEEIQLREEAENNLAAFRADVDAATLARID-LE 225
Cdd:TIGR02169  165 VAE-FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLrreREKAERYQALLKEKREYEGYELLKEKEALERQKEaIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    226 RRIESLNEEIAFLkkvhEEEIrelqaqlqeqqvqvemdmskPDLTAALRDIRAQYETIAAKNISEAEEWY---KSKVSDL 302
Cdd:TIGR02169  244 RQLASLEEELEKL----TEEI--------------------SELEKRLEEIEQLLEELNKKIKDLGEEEQlrvKEKIGEL 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    303 TQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASeangyqdniarLEEEIRHLKDEMAR 382
Cdd:TIGR02169  300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK-----------LTEEYAELKEELED 368

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    383 HLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTFSALNFRETSPEQRGSEVHTKktvmIKTIETRDGEVVSEAT 462
Cdd:TIGR02169  369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA----IAGIEAKINELEEEKE 444


                   ....*.
gi 33563250    463 QQQHEV 468
Cdd:TIGR02169  445 DKALEI 450
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 107-426 3.56e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 3.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    107 EKVELQELNDRfanyIEKvrfLEQQNAALAAEVNRLKGR--EPTRVAELYEEEMRELRRQVEVLTNQRARVDVERDNLID 184
Cdd:TIGR02169  672 EPAELQRLRER----LEG---LKRELSSLQSELRRIENRldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    185 DLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRI------------ESLNEEI-----------AFLKKV 241
Cdd:TIGR02169  745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsripeiqaelSKLEEEVsriearlreieQKLNRL 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    242 HEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAA--KNISEAEEWYKSKVSDLTQAANKNNDALRQAKQE 319
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLRELERK 904

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    320 MMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASE---------ANGYQDNIARLEEEIRHLK-------DEMARH 383
Cdd:TIGR02169  905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeelsLEDVQAELQRVEEEIRALEpvnmlaiQEYEEV 984

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 33563250    384 LREYQDLLNVKMALDVEIATYRKLLEG-EESRINLPIQTFSALN 426
Cdd:TIGR02169  985 LKRLDELKEKRAKLEEERKAILERIEEyEKKKREVFMEAFEAIN 1028
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 98-247 2.12e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 2.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  98 QEFLATRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAEL--YEEEMRELRRQVEVLTNQRARV 175
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALleAEAELAEAEEELEELAEELLEA 391

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33563250 176 DVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIR 247
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
162-392 2.86e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  162 RRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLAR--IDLERRIESLNEEIAFLK 239
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiAELEAELERLDASSDDLA 688

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  240 KVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETiAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQE 319
Cdd:COG4913  689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE-LQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33563250  320 MMEYRHQIQSYTCEIDALkgtNDSLMRQMRELEDRFASEANGYQDNIARLEEEIRHLK----DEMARHLREYQDLLN 392
Cdd:COG4913  768 RENLEERIDALRARLNRA---EEELERAMRAFNREWPAETADLDADLESLPEYLALLDrleeDGLPEYEERFKELLN 841
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
154-377 7.74e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 7.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  154 YEEEMRELRRQVEVLTNQRArvdverdnLIDDLQRLKAKLQEEIQLREeaennlaafRADVDAATLARIDLERRIESLNE 233
Cdd:COG4913  240 AHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRA---------ALRLWFAQRRLELLEAELEELRA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  234 EIAFLkkvhEEEIRELQAQLQeqqvqvemdmskpDLTAALRDIRAQYETIAAKNISEAE---EWYKSKVSDLTQAANKNN 310
Cdd:COG4913  303 ELARL----EAELERLEARLD-------------ALREELDELEAQIRGNGGDRLEQLEreiERLERELEERERRRARLE 365

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33563250  311 DALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEANGYQDNIARLEEEIRHLK 377
Cdd:COG4913  366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 159-385 1.95e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 40.81  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   159 RELRRQVEVLTNQRARVDVER-DNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDaatlariDLERRIESLNEEIAF 237
Cdd:pfam13166 267 AERKAALEAHFDDEFTEFQNRlQKLIEKVESAISSLLAQLPAVSDLASLLSAFELDVE-------DIESEAEVLNSQLDG 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   238 LKKVHEEEIRELQAQLQeqqvqveMDMSKPDLTAALRDIRAQYETIAAKNiseaeewykSKVSDLTQAANKNNDALRqak 317
Cdd:pfam13166 340 LRRALEAKRKDPFKSIE-------LDSVDAKIESINDLVASINELIAKHN---------EITDNFEEEKNKAKKKLR--- 400

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33563250   318 qemmeyRHQIQSYTCEIDALKGTNDSLMRQMRELEDrfasEANGYQDNIARLEEEIRHLKDEMARHLR 385
Cdd:pfam13166 401 ------LHLVEEFKSEIDEYKDKYAGLEKAINSLEK----EIKNLEAEIKKLREEIKELEAQLRDHKP 458
46 PHA02562
endonuclease subunit; Provisional
 161-386 3.04e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.00  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  161 LRRQVEVLTNQRARVDVERDNLIddlQRLKA--KLQEEiqLREEAENNLAAFRADVD-AATLARiDLERRIESLNEEIAf 237
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQ---QQIKTynKNIEE--QRKKNGENIARKQNKYDeLVEEAK-TIKAEIEELTDELL- 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  238 lkkvheeeirelqaqlqeqqvqvEMDMSKPDLTAALRDIRAQYETIAAK----------------------NISEAEEWY 295
Cdd:PHA02562 245 -----------------------NLVMDIEDPSAALNKLNTAAAKIKSKieqfqkvikmyekggvcptctqQISEGPDRI 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250  296 ---KSKVSDLTQAANKNNDALRQAKQEMMEYRHQ---IQSYTCEIDALKGTNDSLMRQMRELE---DRFASEANGYQDNI 366
Cdd:PHA02562 302 tkiKDKLKELQHSLEKLDTAIDELEEIMDEFNEQskkLLELKNKISTNKQSLITLVDKAKKVKaaiEELQAEFVDNAEEL 381

                        250       260
                 ....*....|....*....|
gi 33563250  367 ARLEEEIRHLKDEMARHLRE 386
Cdd:PHA02562 382 AKLQDELDKIVKTKSELVKE 401
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 151-236 4.12e-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: 39.36  E-value: 4.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 151 AELYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIES 230
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231


                ....*.
gi 33563250 231 LNEEIA 236
Cdd:COG4942 232 LEAEAA 237
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 178-386 5.22e-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: 38.98  E-value: 5.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 178 ERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLkkvhEEEIRE--LQAQLQE 255
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAEleKEIAELR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 256 QQVQVEMDMSKPDLTAALRDIRAQYETI--AAKNISEAE---EWYKSKV---SDLTQAANKNNDALRQAKQEMMEYRHQI 327
Cdd:COG4942  97 AELEAQKEELAELLRALYRLGRQPPLALllSPEDFLDAVrrlQYLKYLAparREQAEELRADLAELAALRAELEAERAEL 176

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 33563250 328 QSYTCEIDALKGTNDSLMRQMRELEDRFASEANGYQDNIARLEEEIRHLKDEMARHLRE 386
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
PRK11281 PRK11281
mechanosensitive channel MscK;
275-410 5.81e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.12  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   275 DIRAQYETIAAKNISEAEEwyKSKVSDLTQA---------ANKNNDALRQAKQEMMEyrhQIQSYTCEIDALKGTNDSLM 345
Cdd:PRK11281   40 DVQAQLDALNKQKLLEAED--KLVQQDLEQTlalldkidrQKEETEQLKQQLAQAPA---KLRQAQAELEALKDDNDEET 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250   346 RQ------MRELEDRFA-------------SEAN----GYQ-----------DNIARLeEEIRHL----KDEMARHLREY 387
Cdd:PRK11281  115 REtlstlsLRQLESRLAqtldqlqnaqndlAEYNsqlvSLQtqperaqaalyANSQRL-QQIRNLlkggKVGGKALRPSQ 193

                         170       180
                  ....*....|....*....|....
gi 33563250   388 QDLLNVKMA-LDVEIATYRKLLEG 410
Cdd:PRK11281  194 RVLLQAEQAlLNAQNDLQRKSLEG 217
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 293-416 6.39e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.46  E-value: 6.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    293 EWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYtceIDALKGTNDSLMRQMRELEdRFASEANGY-QDNIARLEE 371
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSI---KPKLRDRKDALEEELRQLK-QLEDELEDCdPTELDRAKE 211

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 33563250    372 EIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRIN 416
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIA 256
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 110-246 7.09e-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: 38.88  E-value: 7.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    110 ELQELNDRFANYIEKVRFLEQQNAALAAEVNRL---KGREPTRVAEL------YEEEMRELRRQVEVLTNQRARVDV--- 177
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLeeqIEELSEDIESLaaeieeLEELIEELESELEALLNERASLEEala 890

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250    178 ----ERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAA--TLARI---------------------------DL 224
Cdd:TIGR02168  891 llrsELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLevRIDNLqerlseeysltleeaealenkieddeeEA 970

                          170       180
                   ....*....|....*....|..
gi 33563250    225 ERRIESLNEEIAFLKKVHEEEI 246
Cdd:TIGR02168  971 RRRLKRLENKIKELGPVNLAAI 992
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 173-285 9.46e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.52  E-value: 9.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33563250 173 ARVDVERDNLIDDLQRLKAKLqeeIQLREEAEnnlaAFRADVDAATLARID-LERRIESLNEEIAFLKKVHEEEIRELQA 251
Cdd:COG0542 400 ARVRMEIDSKPEELDELERRL---EQLEIEKE----ALKKEQDEASFERLAeLRDELAELEEELEALKARWEAEKELIEE 472

                        90       100       110
                ....*....|....*....|....*....|....
gi 33563250 252 QLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAA 285
Cdd:COG0542 473 IQELKEELEQRYGKIPELEKELAELEEELAELAP 506
 
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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