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Conserved domains on  [gi|196115327|ref|NP_001124492|]
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glial fibrillary acidic protein isoform 1 [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;
65-373 1.16e-125

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 366.17  E-value: 1.16e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   65 SERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAK---EPTKLADVYQAELRELRLRLDQLTANSARLEVERDNF 141
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  142 AQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEM 221
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  222 DVA-KPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTN 300
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 196115327  301 ESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENR 373
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 4-63 1.87e-07

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: 48.54  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327    4 RRITSARRSYA-SETVVRGLGPSRQLGTM------------PRFSLSRMTPPLPAR---------VDFSLAGALNAGFKE 61
Cdd:pfam04732   1 YSSSSYRRMFGdSSSSRPSYSSSSGSRSVssrsysrsssssPSSSSRRSSRSSSRSsypslaadsLDFSLADALNQEFKA 80


                  ..
gi 196115327   62 TR 63
Cdd:pfam04732  81 TR 82
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
65-373 1.16e-125

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 366.17  E-value: 1.16e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   65 SERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAK---EPTKLADVYQAELRELRLRLDQLTANSARLEVERDNF 141
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  142 AQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEM 221
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  222 DVA-KPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTN 300
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 196115327  301 ESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENR 373
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 82-372 3.55e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.42  E-value: 3.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  82 EKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLE 161
Cdd:COG1196  213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 162 AENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEMDVAKPDLTAALREIRTQYEA 241
Cdd:COG1196  293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 242 VATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQaltcdLESLRGTNESLERQMREQEERHARESASY 321
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEA 447

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 196115327 322 QEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEEN 372
Cdd:COG1196  448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 53-375 1.70e-11

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: 66.23  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327    53 GALNAGFKETRAS---ERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKladvyQAELRELRLRLDQLTA 129
Cdd:TIGR02168  659 GVITGGSAKTNSSileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-----RKELEELSRQISALRK 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   130 NSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIY---EEEVR 206
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelRAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   207 ELREQLAQQQVHVEMDVAKPDLTAALREIRTQyeavATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQL 286
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEE----QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   287 QALTCDLESLRGTNESLERQMRE--QEERHARES-ASYQEALARLEEEGQSLKEEMArhlQEYQDLLNVKLALDIEIATY 363
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSElrRELEELREKlAQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDD 966

                          330
                   ....*....|..
gi 196115327   364 RKLLEGEENRIT 375
Cdd:TIGR02168  967 EEEARRRLKRLE 978
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 4-63 1.87e-07

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: 48.54  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327    4 RRITSARRSYA-SETVVRGLGPSRQLGTM------------PRFSLSRMTPPLPAR---------VDFSLAGALNAGFKE 61
Cdd:pfam04732   1 YSSSSYRRMFGdSSSSRPSYSSSSGSRSVssrsysrsssssPSSSSRRSSRSSSRSsypslaadsLDFSLADALNQEFKA 80


                  ..
gi 196115327   62 TR 63
Cdd:pfam04732  81 TR 82
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
88-351 5.48e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  88 EQQNKALAAELNQLRAKEPTKLADVYQAE-LRELRLRLDQLTAN----SARLEVERDNFAQDLGTLRQKLQDETNLRLEA 162
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEdLVEAEDRIERLEERredlEELIAERRETIEEKRERAEELRERAAELEAEA 553

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 163 ENNLAA---YRQEADEATLARVDLERKVESLEEEIQFLRKI---------YEEEVRELREQLAQQQvhvEMDVAKPDLTA 230
Cdd:PRK02224 554 EEKREAaaeAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaiadAEDEIERLREKREALA---ELNDERRERLA 630

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 231 ALREIRTQYEAVATSNMQETEewyRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLrgtnESLERQMREQ 310
Cdd:PRK02224 631 EKRERKRELEAEFDEARIEEA---REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL----EELRERREAL 703

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 196115327 311 EERHARESASYQEAlARLEEEGQSLKEEM-ARHLQEYQDLLN 351
Cdd:PRK02224 704 ENRVEALEALYDEA-EELESMYGDLRAELrQRNVETLERMLN 744
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
65-373 1.16e-125

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 366.17  E-value: 1.16e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   65 SERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAK---EPTKLADVYQAELRELRLRLDQLTANSARLEVERDNF 141
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  142 AQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEM 221
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  222 DVA-KPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTN 300
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 196115327  301 ESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENR 373
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 82-372 3.55e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.42  E-value: 3.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  82 EKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLE 161
Cdd:COG1196  213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 162 AENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEMDVAKPDLTAALREIRTQYEA 241
Cdd:COG1196  293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 242 VATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQaltcdLESLRGTNESLERQMREQEERHARESASY 321
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEA 447

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 196115327 322 QEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEEN 372
Cdd:COG1196  448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 53-375 1.70e-11

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: 66.23  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327    53 GALNAGFKETRAS---ERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKladvyQAELRELRLRLDQLTA 129
Cdd:TIGR02168  659 GVITGGSAKTNSSileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-----RKELEELSRQISALRK 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   130 NSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIY---EEEVR 206
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelRAELT 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   207 ELREQLAQQQVHVEMDVAKPDLTAALREIRTQyeavATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQL 286
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEE----QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   287 QALTCDLESLRGTNESLERQMRE--QEERHARES-ASYQEALARLEEEGQSLKEEMArhlQEYQDLLNVKLALDIEIATY 363
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSElrRELEELREKlAQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDD 966

                          330
                   ....*....|..
gi 196115327   364 RKLLEGEENRIT 375
Cdd:TIGR02168  967 EEEARRRLKRLE 978
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 65-311 2.76e-10

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: 62.38  E-value: 2.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327    65 SERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAK--EPTKLADVYQAEL--------------RELRLRLDQLT 128
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELyalaneisrleqqkQILRERLANLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   129 ANSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKiyeeEVREL 208
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS----KVAQL 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   209 REQLAQQQVHVE-MDVAKPDLTAAL----REIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAEL---LRQAKHEAN 280
Cdd:TIGR02168  392 ELQIASLNNEIErLEARLERLEDRRerlqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLeeaLEELREELE 471

                          250       260       270
                   ....*....|....*....|....*....|.
gi 196115327   281 DYRRQLQALTCDLESLRGTNESLERQMREQE 311
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLERLQENLE 502
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 113-374 2.98e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 2.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 113 YQAELRELR-----LRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKV 187
Cdd:COG1196  218 LKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 188 ESLEEEIQFL---RKIYEEEVRELREQLAQQQVHVEmdvakpDLTAALREIRTQyEAVATSNMQETEEWYRSKFADLTDA 264
Cdd:COG1196  298 ARLEQDIARLeerRRELEERLEELEEELAELEEELE------ELEEELEELEEE-LEEAEEELEEAEAELAEAEEALLEA 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 265 ASRNAELLRQAKHEANDYRRQLQALTcDLESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQ 344
Cdd:COG1196  371 EAELAEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                        250       260       270
                 ....*....|....*....|....*....|
gi 196115327 345 EYQDLLNVKLALDIEIATYRKLLEGEENRI 374
Cdd:COG1196  450 EEAELEEEEEALLELLAELLEEAALLEAAL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 60-335 1.64e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  60 KETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQA---------ELRELRLRLDQLTAN 130
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELlaelarleqDIARLEERRRELEER 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 131 SARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELRE 210
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 211 QLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALT 290
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 196115327 291 cDLESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQSL 335
Cdd:COG1196  478 -ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-372 4.67e-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: 4.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327    83 KVRFLEQQNKAlAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLEA 162
Cdd:TIGR02168  201 QLKSLERQAEK-AERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   163 ENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYeEEVRELREQLAQQQVHVEMDVAkpDLTAALREIRTQYEAV 242
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQL-EELEAQLEELESKLDELAEELA--ELEEKLEELKEELESL 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   243 ------ATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEAND---YRRQLQALTCDLESLRGTNESLERQMREQE-- 311
Cdd:TIGR02168  357 eaeleeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAElk 436

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 196115327   312 ------ERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEEN 372
Cdd:TIGR02168  437 elqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 114-341 1.42e-07

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: 53.23  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 114 QAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEatlarvdLERKVESLEEE 193
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------LEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 194 IQFLRKIYEEEVRELreQLAQQQVHVEMDVAKPDLTAALReiRTQYEAVATSNMQETEEWYRSKFADLTdaasRNAELLR 273
Cdd:COG4942   99 LEAQKEELAELLRAL--YRLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAELA----ALRAELE 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 196115327 274 QAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMAR 341
Cdd:COG4942  171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 4-63 1.87e-07

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: 48.54  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327    4 RRITSARRSYA-SETVVRGLGPSRQLGTM------------PRFSLSRMTPPLPAR---------VDFSLAGALNAGFKE 61
Cdd:pfam04732   1 YSSSSYRRMFGdSSSSRPSYSSSSGSRSVssrsysrsssssPSSSSRRSSRSSSRSsypslaadsLDFSLADALNQEFKA 80


                  ..
gi 196115327   62 TR 63
Cdd:pfam04732  81 TR 82
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 60-341 9.53e-07

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: 51.22  E-value: 9.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327    60 KETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERD 139
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   140 nfaqdlgTLRQKLQDETNLRLEAENNLAAYRQEADEatlarvdLERKVESLEEEIqflrKIYEEEVRELREQLAQQQVHV 219
Cdd:TIGR02169  830 -------YLEKEIQELQEQRIDLKEQIKSIEKEIEN-------LNGKKEELEEEL----EELEAALRDLESRLGDLKKER 891

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   220 EmdvakpDLTAALREIRTQYEAVATSnMQETEEWYRSKFADLTDAASRNAELLRQAKHE---------ANDYRRQLQALT 290
Cdd:TIGR02169  892 D------ELEAQLRELERKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeelsLEDVQAELQRVE 964

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 196115327   291 CDLESLRGTNESLERQMREQEERHAresaSYQEALARLEEEGQSLKEEMAR 341
Cdd:TIGR02169  965 EEIRALEPVNMLAIQEYEEVLKRLD----ELKEKRAKLEEERKAILERIEE 1011
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 137-365 2.31e-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: 49.38  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 137 ERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRK---IYEEEVRELREQLA 213
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAelaELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 214 QQQvhvemDVAKPDLTAALREIRTQYEAVATSNmqeteewyrSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDL 293
Cdd:COG4942  101 AQK-----EELAELLRALYRLGRQPPLALLLSP---------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 196115327 294 ESLRGTNESLERQMREQEERHAR---ESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRK 365
Cdd:COG4942  167 AELEAERAELEALLAELEEERAAleaLKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 113-368 3.20e-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: 49.68  E-value: 3.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   113 YQAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEE 192
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   193 EIQFLR---KIYEEEVRELREQLAQQQVHVEmDVAKPDLTAALREIRTQYEAVatsnmqeteEWYRSKFADLTDAASRNA 269
Cdd:TIGR02169  752 EIENVKselKELEARIEELEEDLHKLEEALN-DLEARLSHSRIPEIQAELSKL---------EEEVSRIEARLREIEQKL 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   270 ELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDL 349
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901

                          250
                   ....*....|....*....
gi 196115327   350 LNVKLALDIEIATYRKLLE 368
Cdd:TIGR02169  902 ERKIEELEAQIEKKRKRLS 920
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-264 1.10e-05

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: 47.74  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327    59 FKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQL--RAKEPTKLADVYQAELRELRLRLDQLTANSARLEV 136
Cdd:TIGR02168  801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLeeQIEELSEDIESLAAEIEELEELIEELESELEALLN 880

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   137 ERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQ 216
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 196115327   217 VHVEMDVAKpdLTAALREIRTQYEAVATSNM------QETEEWYR---SKFADLTDA 264
Cdd:TIGR02168  961 NKIEDDEEE--ARRRLKRLENKIKELGPVNLaaieeyEELKERYDfltAQKEDLTEA 1015
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
51-215 1.45e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   51 LAGALNAGFKETRASE-RAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRA---KEPTKLADVYQAELRELRLRLDQ 126
Cdd:COG4913   277 LRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAqirGNGGDRLEQLEREIERLERELEE 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  127 LTANSAR-------LEVERDNFAQDLGTLRQKLQDetnLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRK 199
Cdd:COG4913   357 RERRRARleallaaLGLPLPASAEEFAALRAEAAA---LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433

                         170
                  ....*....|....*....
gi 196115327  200 ---IYEEEVRELREQLAQQ 215
Cdd:COG4913   434 rksNIPARLLALRDALAEA 452
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
67-305 2.53e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   67 RAEMMELNDRFASY--IEKVRFLEQQNKALAAELNQLRAKeptkLADVYQA--ELRELRLRLDQLTANSARLEVERDNFA 142
Cdd:COG4913   637 EAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAE----LERLDASsdDLAALEEQLEELEAELEELEEELDELK 712

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  143 QDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVE-- 220
Cdd:COG4913   713 GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELEra 792

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  221 ---------MDVAKPDLT-AALREIRTQYEAVATSNMQEteewYRSKFADLTDAASRN--AELLRQAKHEANDYRRQLQA 288
Cdd:COG4913   793 mrafnrewpAETADLDADlESLPEYLALLDRLEEDGLPE----YEERFKELLNENSIEfvADLLSKLRRAIREIKERIDP 868

                         250
                  ....*....|....*..
gi 196115327  289 LtcdleslrgtNESLER 305
Cdd:COG4913   869 L----------NDSLKR 875
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-374 5.28e-05

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: 45.82  E-value: 5.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   159 RLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQflrkiYEEEVRELREQLAQQQVHVemdvakpdLTAALREIRTQ 238
Cdd:TIGR02168  174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAE-----KAERYKELKAELRELELAL--------LVLRLEELREE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   239 YEAVatsnmQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHAR-- 316
Cdd:TIGR02168  241 LEEL-----QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANle 315

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 196115327   317 -ESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRI 374
Cdd:TIGR02168  316 rQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
68-243 8.39e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 8.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   68 AEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERD-------- 139
Cdd:COG4913   255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDeleaqirg 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  140 NFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAqqqvhv 219
Cdd:COG4913   335 NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA------ 408

                         170       180
                  ....*....|....*....|....
gi 196115327  220 EMDVAKPDLTAALREIRTQYEAVA 243
Cdd:COG4913   409 EAEAALRDLRRELRELEAEIASLE 432
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 58-353 3.09e-04

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: 43.18  E-value: 3.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327    58 GFKETRASERAEMMELNDRFASYIEKVR----FLEQQNKALAAELNQLRAkEPTKLADVYQAELRELRLRLDQLTANSAR 133
Cdd:pfam15921  282 GLTEKASSARSQANSIQSQLEIIQEQARnqnsMYMRQLSDLESTVSQLRS-ELREAKRMYEDKIEELEKQLVLANSELTE 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   134 LEVERDNFAQDLGTLRQKLQD--------ETNLRLEAENNLAAYrqEADEATLARVD-LERKVESLEEEIQFLRKIYEEE 204
Cdd:pfam15921  361 ARTERDQFSQESGNLDDQLQKlladlhkrEKELSLEKEQNKRLW--DRDTGNSITIDhLRRELDDRNMEVQRLEALLKAM 438

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   205 VRELREQLAQQQVHV----EMDVAKPDLTAALREIRTQYEAVA--------------------TSNMQETEEWYRSKFAD 260
Cdd:pfam15921  439 KSECQGQMERQMAAIqgknESLEKVSSLTAQLESTKEMLRKVVeeltakkmtlessertvsdlTASLQEKERAIEATNAE 518

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   261 LTDAASRNAELLRQAKHEAN--DYRRQLQAlTCDLESLRGTN-----ESLERQMREQEE---RHARESASYQEALARLEE 330
Cdd:pfam15921  519 ITKLRSRVDLKLQELQHLKNegDHLRNVQT-ECEALKLQMAEkdkviEILRQQIENMTQlvgQHGRTAGAMQVEKAQLEK 597

                          330       340
                   ....*....|....*....|...
gi 196115327   331 EGQSLKEEmarhLQEYQDLLNVK 353
Cdd:pfam15921  598 EINDRRLE----LQEFKILKDKK 616
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
170-368 3.23e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  170 RQEADEATLARVDLERKVESLEEEIQFLRkiyeEEVRELREQLAQQQVHVEmdvakpDLTAALREIRTQYEAVATSNMQE 249
Cdd:COG4913   273 ELEYLRAALRLWFAQRRLELLEAELEELR----AELARLEAELERLEARLD------ALREELDELEAQIRGNGGDRLEQ 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  250 teewyrskfadLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEALARLE 329
Cdd:COG4913   343 -----------LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 196115327  330 EEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLE 368
Cdd:COG4913   412 AALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-351 3.58e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  111 DVYQAELRELRLRLDQLTANSARLEVERDNfAQDLGTLRQKLQDETnlrlEAENNLAAYRQEADEATLARVDLER---KV 187
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLAEYS----WDEIDVASAEREIAELEAELERLDAssdDL 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  188 ESLEEEIQFLrkiyEEEVRELREQLAQQQvhVEMDVAKPDLTAALREIRtQYEAVATSNMQETEEWYRskfadlTDAASR 267
Cdd:COG4913   688 AALEEQLEEL----EAELEELEEELDELK--GEIGRLEKELEQAEEELD-ELQDRLEAAEDLARLELR------ALLEER 754

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  268 NAELLRQAKheANDYRRQLQAltcDLESLRGTNESLERQMREQEERHARES--------------ASYQEALARLEEEGq 333
Cdd:COG4913   755 FAAALGDAV--ERELRENLEE---RIDALRARLNRAEEELERAMRAFNREWpaetadldadleslPEYLALLDRLEEDG- 828

                         250
                  ....*....|....*...
gi 196115327  334 slkeeMARHLQEYQDLLN 351
Cdd:COG4913   829 -----LPEYEERFKELLN 841
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
88-351 5.48e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  88 EQQNKALAAELNQLRAKEPTKLADVYQAE-LRELRLRLDQLTAN----SARLEVERDNFAQDLGTLRQKLQDETNLRLEA 162
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEdLVEAEDRIERLEERredlEELIAERRETIEEKRERAEELRERAAELEAEA 553

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 163 ENNLAA---YRQEADEATLARVDLERKVESLEEEIQFLRKI---------YEEEVRELREQLAQQQvhvEMDVAKPDLTA 230
Cdd:PRK02224 554 EEKREAaaeAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaiadAEDEIERLREKREALA---ELNDERRERLA 630

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 231 ALREIRTQYEAVATSNMQETEewyRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLrgtnESLERQMREQ 310
Cdd:PRK02224 631 EKRERKRELEAEFDEARIEEA---REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL----EELRERREAL 703

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 196115327 311 EERHARESASYQEAlARLEEEGQSLKEEM-ARHLQEYQDLLN 351
Cdd:PRK02224 704 ENRVEALEALYDEA-EELESMYGDLRAELrQRNVETLERMLN 744
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 161-374 7.40e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 7.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 161 EAENNLAAYRQEADEATLARVDLERKVESLEEE----IQFLRKIYEEEVRELREQLAQ-QQVHVEMDVAKPDLTAALREI 235
Cdd:COG1196  176 EAERKLEATEENLERLEDILGELERQLEPLERQaekaERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAEL 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 236 RTQYEAVATSNMQETEEwyRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHA 315
Cdd:COG1196  256 EELEAELAELEAELEEL--RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 196115327 316 RESASYQEA---LARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRI 374
Cdd:COG1196  334 ELEEELEELeeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 60-318 7.64e-04

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: 41.29  E-value: 7.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  60 KETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKeptklADVYQAELRELRLRLDQLtanSARLEVERD 139
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE-----LAALEAELAELEKEIAEL---RAELEAQKE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 140 NFAQDLGTL-RQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERkVESLEEEIqflrkiyeEEVRELREQLAQQQVh 218
Cdd:COG4942  105 ELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ-AEELRADL--------AELAALRAELEAERA- 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 219 vemdvakpDLTAALREIRTQYEAvatsnmqeteewyrskfadLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRG 298
Cdd:COG4942  175 --------ELEALLAELEEERAA-------------------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227

                        250       260
                 ....*....|....*....|
gi 196115327 299 TNESLERQMREQEERHARES 318
Cdd:COG4942  228 LIARLEAEAAAAAERTPAAG 247
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
166-375 1.48e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  166 LAAYRQEADEATLARVDLERKVESLEEEIQflrkiyeeEVRELREQLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATS 245
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELD--------ALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAS 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  246 NMQeteewyrskfadltdaasrnaelLRQAKheandyrRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEAL 325
Cdd:COG4913   684 SDD-----------------------LAALE-------EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 196115327  326 ARLEEEGQSLKEEMARHLQEYQDLLN-------VKLALDIEIATYRKLLEGEENRIT 375
Cdd:COG4913   734 DRLEAAEDLARLELRALLEERFAAALgdavereLRENLEERIDALRARLNRAEEELE 790
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
94-214 1.70e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.61  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  94 LAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDnfaqdlgTLRQKL--QDETNLRLEAEnnLAAYRQ 171
Cdd:COG2433  385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-------ELEAELeeKDERIERLERE--LSEARS 455

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 196115327 172 EADEatlaRVDLERKVESLEEEIQFLRKIYEEE---VRELREQLAQ 214
Cdd:COG2433  456 EERR----EIRKDREISRLDREIERLERELEEErerIEELKRKLER 497
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 131-252 2.23e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 131 SARLEVERDNFAQDLGTLRQKLQdetnlRLEAEnnLAAYRQEADEATLARVD-LERKVESLEEEIQFLRKIYEEEVRELR 209
Cdd:COG0542  399 AARVRMEIDSKPEELDELERRLE-----QLEIE--KEALKKEQDEASFERLAeLRDELAELEEELEALKARWEAEKELIE 471

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 196115327 210 EQLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATSNMQE-TEE 252
Cdd:COG0542  472 EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEvTEE 515
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
108-330 2.33e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.39  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 108 KLADVYQAELRELRLrlDQLTANSARLEVERDNFAQDLGTLRQKLQDetnlrLEAENNLAAYRQEADEATLARVDLERKV 187
Cdd:COG3206  156 ALAEAYLEQNLELRR--EEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQL 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 188 ESLEEEIQFLRKIYEEeVRELREQLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATS------NMQETeewyRSKFADL 261
Cdd:COG3206  229 AEARAELAEAEARLAA-LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpDVIAL----RAQIAAL 303

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 196115327 262 TDA-ASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESL---ERQMREQEERHARESASYQEALARLEE 330
Cdd:COG3206  304 RAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEE 376
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
113-331 2.34e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  113 YQAELRELRLRLDQLT-----ANSARLEVERDNFAQDLGTLRQKLQDETNLRLeAENNLAAYRQEADEATLARVDLERKV 187
Cdd:COG4913   240 AHEALEDAREQIELLEpirelAERYAAARERLAELEYLRAALRLWFAQRRLEL-LEAELEELRAELARLEAELERLEARL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  188 ESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEMDVAKpdltaaLREIRTQYEAVATSnMQETEEWYRSKFADLTDAASR 267
Cdd:COG4913   319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEE------RERRRARLEALLAA-LGLPLPASAEEFAALRAEAAA 391

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 196115327  268 NAELLRQAKHEANDYRRQLQAltcDLESLRGTNESLERQMREQEERHARESASYQEALARLEEE 331
Cdd:COG4913   392 LLEALEEELEALEEALAEAEA---ALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 61-376 4.57e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  61 ETRASERAEMMELNDRFASYIEKVRFLEQQNKALAA---ELNQLRAKEPTKLADVyQAELRELRLRLDQLTANSARLEVE 137
Cdd:COG1196  393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEalaELEEEEEEEEEALEEA-AEEEAELEEEEEALLELLAELLEE 471

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 138 RDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLAR-VDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQ 216
Cdd:COG1196  472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALlLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 217 VHVEMDVAK-------------------------PDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAEL 271
Cdd:COG1196  552 VVEDDEVAAaaieylkaakagratflpldkirarAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 272 LRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDLLN 351
Cdd:COG1196  632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711

                        330       340
                 ....*....|....*....|....*
gi 196115327 352 VKLALDIEIATYRKLLEGEENRITI 376
Cdd:COG1196  712 AEEERLEEELEEEALEEQLEAEREE 736
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 57-220 5.88e-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: 5.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327    57 AGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRA--KEPTKLADVYQAELRELRLRLDQLTANSARL 134
Cdd:TIGR02169  339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDelKDYREKLEKLKREINELKRELDRLQEELQRL 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   135 EVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQ 214
Cdd:TIGR02169  419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498


                   ....*.
gi 196115327   215 QQVHVE 220
Cdd:TIGR02169  499 ARASEE 504
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 85-208 7.45e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 38.78  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327   85 RFLEQQNKA--LAAELNQLRAKEPTKLADV--YQAELRELRLRLDQLTANS----ARLEVERDNFAQDLGTLRQK----- 151
Cdd:COG3096   526 QRLRQQQNAerLLEEFCQRIGQQLDAAEELeeLLAELEAQLEELEEQAAEAveqrSELRQQLEQLRARIKELAARapawl 605

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 196115327  152 --------LQDETNLRLEAENNLAAYRQEAdeatlarVDLERKVESLEEEIQFLRKIYEEEVREL 208
Cdd:COG3096   606 aaqdalerLREQSGEALADSQEVTAAMQQL-------LEREREATVERDELAARKQALESQIERL 663
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
183-374 8.75e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 8.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 183 LERKVESLEEEIQFLrkiyEEEVRELREQLAQQQvhvemdvakpdltAALREIRTQYEAVATSNMQETeewYRSKFADLT 262
Cdd:COG3206  166 LELRREEARKALEFL----EEQLPELRKELEEAE-------------AALEEFRQKNGLVDLSEEAKL---LLQQLSELE 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 263 DAASRNAELLRQAKHEANDYRRQLQALTCD---------LESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQ 333
Cdd:COG3206  226 SQLAEARAELAEAEARLAALRAQLGSGPDAlpellqspvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA 305

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 196115327 334 SLKEEMARHLQEYQdllNVKLALDIEIATYRKLLEGEENRI 374
Cdd:COG3206  306 QLQQEAQRILASLE---AELEALQAREASLQAQLAQLEARL 343
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
61-345 9.75e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 37.58  E-value: 9.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327  61 ETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQ--AELRELRLRLDQLTANSARLEVER 138
Cdd:COG1340    1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKElrEEAQELREKRDELNEKVKELKEER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 139 DNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIyeeevRELREQLAQQQVH 218
Cdd:COG1340   81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKI-----KELEKELEKAKKA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 196115327 219 VEMDVAKPDLTAALREIRTQYEAvatsnmqeteewYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRG 298
Cdd:COG1340  156 LEKNEKLKELRAELKELRKEAEE------------IHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQE 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 196115327 299 TNESLERQMREQEErharESASYQEALARLEEEGQSLKEEMARHLQE 345
Cdd:COG1340  224 KADELHEEIIELQK----ELRELRKELKKLRKKQRALKREKEKEELE 266
 
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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