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Conserved domains on  [gi|84000448|ref|NP_034407|]
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glial fibrillary acidic protein isoform 2 [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 4.20e-124

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 362.32  E-value: 4.20e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    65 SERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAK---EPTKLADVYQAELRELRLRLDQLTANSARLEVERDNF 141
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448   142 AQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEM 221
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448   222 DVA-KPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTN 300
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84000448   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 3.00e-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: 47.77  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448     4 RRITSARRSYA-SETVVRGLGPSRQLGTM------------PRFSLSRMTPPLPAR---------VDFSLAGALNAGFKE 61
Cdd:pfam04732   1 YSSSSYRRMFGdSSSSRPSYSSSSGSRSVssrsysrsssssPSSSSRRSSRSSSRSsypslaadsLDFSLADALNQEFKA 80

                  ..
gi 84000448    62 TR 63
Cdd:pfam04732  81 TR 82
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
65-373 4.20e-124

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 362.32  E-value: 4.20e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    65 SERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAK---EPTKLADVYQAELRELRLRLDQLTANSARLEVERDNF 141
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448   142 AQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEM 221
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448   222 DVA-KPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTN 300
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84000448   301 ESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENR 373
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
82-372 4.21e-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: 4.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  82 EKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLE 161
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 162 AENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEMDVAKPDLTAALREIRTQYEA 241
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 242 VATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQaltcdLESLRGTNESLERQMREQEERHARESASY 321
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEA 447
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 84000448 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 2.97e-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: 65.46  E-value: 2.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448     53 GALNAGFKETRAS---ERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKladvyQAELRELRLRLDQLTA 129
Cdd:TIGR02168  659 GVITGGSAKTNSSileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-----RKELEELSRQISALRK 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    130 NSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIY---EEEVR 206
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    207 ELREQLAQQQVHVEMDVAKPDLTAALREIRTQyeavATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQL 286
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEE----QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    287 QALTCDLESLRGTNESLERQMRE--QEERHARES-ASYQEALARLEEEGQSLKEEMArhlQEYQDLLNVKLALDIEIATY 363
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSElrRELEELREKlAQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDD 966
                          330
                   ....*....|..
gi 84000448    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 3.00e-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: 47.77  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448     4 RRITSARRSYA-SETVVRGLGPSRQLGTM------------PRFSLSRMTPPLPAR---------VDFSLAGALNAGFKE 61
Cdd:pfam04732   1 YSSSSYRRMFGdSSSSRPSYSSSSGSRSVssrsysrsssssPSSSSRRSSRSSSRSsypslaadsLDFSLADALNQEFKA 80

                  ..
gi 84000448    62 TR 63
Cdd:pfam04732  81 TR 82
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
88-324 1.44e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448   88 EQQNKALAAELNQLRAKEPTKLADVYQAE-LRELRLRLDQLTAN----SARLEVERDNFAQDLGTLRQKLQDETNLRLEA 162
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEdLVEAEDRIERLEERredlEELIAERRETIEEKRERAEELRERAAELEAEA 553
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  163 ENNLAA---YRQEADEATLARVDLERKVESLEEEIQFLRKI---------YEEEVRELREQLAQQQvhvEMDVAKPDLTA 230
Cdd:PRK02224 554 EEKREAaaeAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaiadAEDEIERLREKREALA---ELNDERRERLA 630
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  231 ALREIRTQYEAVATSNMQETEewyRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLrgtnESLERQMREQ 310
Cdd:PRK02224 631 EKRERKRELEAEFDEARIEEA---REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL----EELRERREAL 703
                        250
                 ....*....|....
gi 84000448  311 EERHARESASYQEA 324
Cdd:PRK02224 704 ENRVEALEALYDEA 717
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
65-373 4.20e-124

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 362.32  E-value: 4.20e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    65 SERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAK---EPTKLADVYQAELRELRLRLDQLTANSARLEVERDNF 141
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448   142 AQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEM 221
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448   222 DVA-KPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTN 300
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84000448   301 ESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENR 373
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
82-372 4.21e-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: 4.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  82 EKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLE 161
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 162 AENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEMDVAKPDLTAALREIRTQYEA 241
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 242 VATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQaltcdLESLRGTNESLERQMREQEERHARESASY 321
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER-----LEEELEELEEALAELEEEEEEEEEALEEA 447
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 84000448 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 2.97e-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: 65.46  E-value: 2.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448     53 GALNAGFKETRAS---ERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKladvyQAELRELRLRLDQLTA 129
Cdd:TIGR02168  659 GVITGGSAKTNSSileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-----RKELEELSRQISALRK 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    130 NSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIY---EEEVR 206
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelRAELT 813
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    207 ELREQLAQQQVHVEMDVAKPDLTAALREIRTQyeavATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQL 286
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEE----QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    287 QALTCDLESLRGTNESLERQMRE--QEERHARES-ASYQEALARLEEEGQSLKEEMArhlQEYQDLLNVKLALDIEIATY 363
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSElrRELEELREKlAQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDD 966
                          330
                   ....*....|..
gi 84000448    364 RKLLEGEENRIT 375
Cdd:TIGR02168  967 EEEARRRLKRLE 978
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
113-374 3.62e-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: 3.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 113 YQAELRELR-----LRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKV 187
Cdd:COG1196 218 LKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 188 ESLEEEIQFL---RKIYEEEVRELREQLAQQQVHVEmdvakpDLTAALREIRTQyEAVATSNMQETEEWYRSKFADLTDA 264
Cdd:COG1196 298 ARLEQDIARLeerRRELEERLEELEEELAELEEELE------ELEEELEELEEE-LEEAEEELEEAEAELAEAEEALLEA 370
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 265 ASRNAELLRQAKHEANDYRRQLQALTcDLESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQ 344
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                       250       260       270
                ....*....|....*....|....*....|
gi 84000448 345 EYQDLLNVKLALDIEIATYRKLLEGEENRI 374
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAAL 479
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
65-311 4.43e-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: 62.00  E-value: 4.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448     65 SERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAK--EPTKLADVYQAEL--------------RELRLRLDQLT 128
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELyalaneisrleqqkQILRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    129 ANSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKiyeeEVREL 208
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS----KVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    209 REQLAQQQVHVE-MDVAKPDLTAAL----REIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAEL---LRQAKHEAN 280
Cdd:TIGR02168  392 ELQIASLNNEIErLEARLERLEDRRerlqQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLeeaLEELREELE 471
                          250       260       270
                   ....*....|....*....|....*....|.
gi 84000448    281 DYRRQLQALTCDLESLRGTNESLERQMREQE 311
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLERLQENLE 502
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
60-335 1.86e-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: 1.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  60 KETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQA---------ELRELRLRLDQLTAN 130
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELlaelarleqDIARLEERRRELEER 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 131 SARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELRE 210
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 211 QLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALT 290
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 84000448 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 7.03e-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: 55.06  E-value: 7.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448     83 KVRFLEQQNKAlAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLEA 162
Cdd:TIGR02168  201 QLKSLERQAEK-AERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    163 ENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYeEEVRELREQLAQQQVHVEMDVAkpDLTAALREIRTQYEAV 242
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQL-EELEAQLEELESKLDELAEELA--ELEEKLEELKEELESL 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    243 ------ATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEAND---YRRQLQALTCDLESLRGTNESLERQMREQE-- 311
Cdd:TIGR02168  357 eaeleeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAElk 436
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84000448    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 8.09e-08

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: 54.00  E-value: 8.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 114 QAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEatlarvdLERKVESLEEE 193
Cdd:COG4942  26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------LEKEIAELRAE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 194 IQFLRKIYEEEVRELreQLAQQQVHVEMDVAKPDLTAALReiRTQYEAVATSNMQETEEWYRSKFADLTdaasRNAELLR 273
Cdd:COG4942  99 LEAQKEELAELLRAL--YRLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEELRADLAELA----ALRAELE 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84000448 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 3.00e-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: 47.77  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448     4 RRITSARRSYA-SETVVRGLGPSRQLGTM------------PRFSLSRMTPPLPAR---------VDFSLAGALNAGFKE 61
Cdd:pfam04732   1 YSSSSYRRMFGdSSSSRPSYSSSSGSRSVssrsysrsssssPSSSSRRSSRSSSRSsypslaadsLDFSLADALNQEFKA 80

                  ..
gi 84000448    62 TR 63
Cdd:pfam04732  81 TR 82
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
137-365 1.28e-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: 50.15  E-value: 1.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 137 ERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRK---IYEEEVRELREQLA 213
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAelaELEKEIAELRAELE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 214 QQQvhvemDVAKPDLTAALREIRTQYEAVATSNmqeteewyrSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDL 293
Cdd:COG4942 101 AQK-----EELAELLRALYRLGRQPPLALLLSP---------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84000448 294 ESLRGTNESLERQMREQEERHAR---ESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRK 365
Cdd:COG4942 167 AELEAERAELEALLAELEEERAAleaLKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
60-341 2.67e-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: 2.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448     60 KETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERD 139
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    140 nfaqdlgTLRQKLQDETNLRLEAENNLAAYRQEADEatlarvdLERKVESLEEEIqflrKIYEEEVRELREQLAQQQVHV 219
Cdd:TIGR02169  830 -------YLEKEIQELQEQRIDLKEQIKSIEKEIEN-------LNGKKEELEEEL----EELEAALRDLESRLGDLKKER 891
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    220 EmdvakpDLTAALREIRTQYEAVATSnMQETEEWYRSKFADLTDAASRNAELLRQAKHE---------ANDYRRQLQALT 290
Cdd:TIGR02169  892 D------ELEAQLRELERKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeelsLEDVQAELQRVE 964
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 84000448    291 CDLESLRGTNESLERQMREQEERHAresaSYQEALARLEEEGQSLKEEMAR 341
Cdd:TIGR02169  965 EEIRALEPVNMLAIQEYEEVLKRLD----ELKEKRAKLEEERKAILERIEE 1011
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
113-368 6.07e-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: 6.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    113 YQAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEE 192
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    193 EIQFLR---KIYEEEVRELREQLAQQQVHVEmDVAKPDLTAALREIRTQYEAVatsnmqeteEWYRSKFADLTDAASRNA 269
Cdd:TIGR02169  752 EIENVKselKELEARIEELEEDLHKLEEALN-DLEARLSHSRIPEIQAELSKL---------EEEVSRIEARLREIEQKL 821
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    270 ELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDL 349
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
                          250
                   ....*....|....*....
gi 84000448    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 1.64e-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: 47.36  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448     59 FKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQL--RAKEPTKLADVYQAELRELRLRLDQLTANSARLEV 136
Cdd:TIGR02168  801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLeeQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    137 ERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQ 216
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 84000448    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 1.80e-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: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448   51 LAGALNAGFKETRASE-RAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRA---KEPTKLADVYQAELRELRLRLDQ 126
Cdd:COG4913  277 LRAALRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAqirGNGGDRLEQLEREIERLERELEE 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  127 LTANSAR-------LEVERDNFAQDLGTLRQKLQDetnLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRK 199
Cdd:COG4913  357 RERRRARleallaaLGLPLPASAEEFAALRAEAAA---LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
                        170
                 ....*....|....*....
gi 84000448  200 ---IYEEEVRELREQLAQQ 215
Cdd:COG4913  434 rksNIPARLLALRDALAEA 452
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
67-305 3.22e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448   67 RAEMMELNDRFASY--IEKVRFLEQQNKALAAELNQLRAKeptkLADVYQA--ELRELRLRLDQLTANSARLEVERDNFA 142
Cdd:COG4913  637 EAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAE----LERLDASsdDLAALEEQLEELEAELEELEEELDELK 712
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  143 QDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVE-- 220
Cdd:COG4913  713 GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELEra 792
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  221 ---------MDVAKPDLT-AALREIRTQYEAVATSNMQEteewYRSKFADLTDAASRN--AELLRQAKHEANDYRRQLQA 288
Cdd:COG4913  793 mrafnrewpAETADLDADlESLPEYLALLDRLEEDGLPE----YEERFKELLNENSIEfvADLLSKLRRAIREIKERIDP 868
                        250
                 ....*....|....*..
gi 84000448  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 7.13e-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: 45.43  E-value: 7.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    159 RLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQflrkiYEEEVRELREQLAQQQVHVemdvakpdLTAALREIRTQ 238
Cdd:TIGR02168  174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAE-----KAERYKELKAELRELELAL--------LVLRLEELREE 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    239 YEAVatsnmQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHAR-- 316
Cdd:TIGR02168  241 LEEL-----QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANle 315
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 84000448    317 -ESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRI 374
Cdd:TIGR02168  316 rQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
68-243 9.71e-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: 9.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448   68 AEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERD-------- 139
Cdd:COG4913  255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDeleaqirg 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  140 NFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAqqqvhv 219
Cdd:COG4913  335 NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA------ 408
                        170       180
                 ....*....|....*....|....
gi 84000448  220 EMDVAKPDLTAALREIRTQYEAVA 243
Cdd:COG4913  409 EAEAALRDLRRELRELEAEIASLE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
161-391 3.58e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 161 EAENNLAAYRQEADEATLARVDLERKVESLEEE----IQFLRKIYEEEVRELREQLAQ-QQVHVEMDVAKPDLTAALREI 235
Cdd:COG1196 176 EAERKLEATEENLERLEDILGELERQLEPLERQaekaERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAEL 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 236 RTQYEAVATSNMQETEEwyRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHA 315
Cdd:COG1196 256 EELEAELAELEAELEEL--RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 84000448 316 RESASYQEA---LARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRITIPVQTFSNLQIRETSL 391
Cdd:COG1196 334 ELEEELEELeeeLEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
170-368 3.73e-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: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  170 RQEADEATLARVDLERKVESLEEEIQFLRkiyeEEVRELREQLAQQQVHVEmdvakpDLTAALREIRTQYEAVATSNMQE 249
Cdd:COG4913  273 ELEYLRAALRLWFAQRRLELLEAELEELR----AELARLEAELERLEARLD------ALREELDELEAQIRGNGGDRLEQ 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  250 teewyrskfadLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEALARLE 329
Cdd:COG4913  343 -----------LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 84000448  330 EEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLE 368
Cdd:COG4913  412 AALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
60-318 3.95e-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: 42.44  E-value: 3.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  60 KETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKeptklADVYQAELRELRLRLDQLtanSARLEVERD 139
Cdd:COG4942  33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE-----LAALEAELAELEKEIAEL---RAELEAQKE 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 140 NFAQDLGTL-RQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERkVESLEEEIqflrkiyeEEVRELREQLAQQQVh 218
Cdd:COG4942 105 ELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ-AEELRADL--------AELAALRAELEAERA- 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 219 vemdvakpDLTAALREIRTQYEAvatsnmqeteewyrskfadLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRG 298
Cdd:COG4942 175 --------ELEALLAELEEERAA-------------------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
                       250       260
                ....*....|....*....|
gi 84000448 299 TNESLERQMREQEERHARES 318
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAG 247
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
111-351 4.43e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  111 DVYQAELRELRLRLDQLTANSARLEVERDNfAQDLGTLRQKLQDETnlrlEAENNLAAYRQEADEATLARVDLER---KV 187
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLAEYS----WDEIDVASAEREIAELEAELERLDAssdDL 687
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  188 ESLEEEIQFLrkiyEEEVRELREQLAQQQvhVEMDVAKPDLTAALREIRtQYEAVATSNMQETEEWYRskfadlTDAASR 267
Cdd:COG4913  688 AALEEQLEEL----EAELEELEEELDELK--GEIGRLEKELEQAEEELD-ELQDRLEAAEDLARLELR------ALLEER 754
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  268 NAELLRQAKheANDYRRQLQAltcDLESLRGTNESLERQMREQEERHARES--------------ASYQEALARLEEEGq 333
Cdd:COG4913  755 FAAALGDAV--ERELRENLEE---RIDALRARLNRAEEELERAMRAFNREWpaetadldadleslPEYLALLDRLEEDG- 828
                        250
                 ....*....|....*...
gi 84000448  334 slkeeMARHLQEYQDLLN 351
Cdd:COG4913  829 -----LPEYEERFKELLN 841
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
58-353 9.47e-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: 41.64  E-value: 9.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448     58 GFKETRASERAEMMELNDRFASYIEKVR----FLEQQNKALAAELNQLRAkEPTKLADVYQAELRELRLRLDQLTANSAR 133
Cdd:pfam15921  282 GLTEKASSARSQANSIQSQLEIIQEQARnqnsMYMRQLSDLESTVSQLRS-ELREAKRMYEDKIEELEKQLVLANSELTE 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    134 LEVERDNFAQDLGTLRQKLQD--------ETNLRLEAENNLAAYrqEADEATLARVD-LERKVESLEEEIQFLRKIYEEE 204
Cdd:pfam15921  361 ARTERDQFSQESGNLDDQLQKlladlhkrEKELSLEKEQNKRLW--DRDTGNSITIDhLRRELDDRNMEVQRLEALLKAM 438
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    205 VRELREQLAQQQVHV----EMDVAKPDLTAALREIRTQYEAVA--------------------TSNMQETEEWYRSKFAD 260
Cdd:pfam15921  439 KSECQGQMERQMAAIqgknESLEKVSSLTAQLESTKEMLRKVVeeltakkmtlessertvsdlTASLQEKERAIEATNAE 518
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    261 LTDAASRNAELLRQAKHEAN--DYRRQLQAlTCDLESLRGTN-----ESLERQMREQEE---RHARESASYQEALARLEE 330
Cdd:pfam15921  519 ITKLRSRVDLKLQELQHLKNegDHLRNVQT-ECEALKLQMAEkdkviEILRQQIENMTQlvgQHGRTAGAMQVEKAQLEK 597
                          330       340
                   ....*....|....*....|...
gi 84000448    331 EGQSLKEEmarhLQEYQDLLNVK 353
Cdd:pfam15921  598 EINDRRLE----LQEFKILKDKK 616
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
88-324 1.44e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448   88 EQQNKALAAELNQLRAKEPTKLADVYQAE-LRELRLRLDQLTAN----SARLEVERDNFAQDLGTLRQKLQDETNLRLEA 162
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEdLVEAEDRIERLEERredlEELIAERRETIEEKRERAEELRERAAELEAEA 553
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  163 ENNLAA---YRQEADEATLARVDLERKVESLEEEIQFLRKI---------YEEEVRELREQLAQQQvhvEMDVAKPDLTA 230
Cdd:PRK02224 554 EEKREAaaeAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaiadAEDEIERLREKREALA---ELNDERRERLA 630
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  231 ALREIRTQYEAVATSNMQETEewyRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLrgtnESLERQMREQ 310
Cdd:PRK02224 631 EKRERKRELEAEFDEARIEEA---REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL----EELRERREAL 703
                        250
                 ....*....|....
gi 84000448  311 EERHARESASYQEA 324
Cdd:PRK02224 704 ENRVEALEALYDEA 717
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
108-330 1.62e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 1.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 108 KLADVYQAELreLRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDetnlrLEAENNLAAYRQEADEATLARVDLERKV 187
Cdd:COG3206 156 ALAEAYLEQN--LELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQL 228
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 188 ESLEEEIQFLRKIYEEeVRELREQLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATS------NMQETeewyRSKFADL 261
Cdd:COG3206 229 AEARAELAEAEARLAA-LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpDVIAL----RAQIAAL 303
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 84000448 262 TDA-ASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESL---ERQMREQEERHARESASYQEALARLEE 330
Cdd:COG3206 304 RAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEE 376
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
166-375 1.90e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  166 LAAYRQEADEATLARVDLERKVESLEEEIQflrkiyeeEVRELREQLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATS 245
Cdd:COG4913  612 LAALEAELAELEEELAEAEERLEALEAELD--------ALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAS 683
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  246 NMQeteewyrskfadltdaasrnaelLRQAKheandyrRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEAL 325
Cdd:COG4913  684 SDD-----------------------LAALE-------EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 84000448  326 ARLEEEGQSLKEEMARHLQEYQDLLN-------VKLALDIEIATYRKLLEGEENRIT 375
Cdd:COG4913  734 DRLEAAEDLARLELRALLEERFAAALgdavereLRENLEERIDALRARLNRAEEELE 790
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
131-252 2.43e-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: 2.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 131 SARLEVERDNFAQDLGTLRQKLQdetnlRLEAEnnLAAYRQEADEATLARVD-LERKVESLEEEIQFLRKIYEEEVRELR 209
Cdd:COG0542 399 AARVRMEIDSKPEELDELERRLE-----QLEIE--KEALKKEQDEASFERLAeLRDELAELEEELEALKARWEAEKELIE 471
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 84000448 210 EQLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATSNMQE-TEE 252
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEvTEE 515
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
113-331 2.71e-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: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  113 YQAELRELRLRLDQLT-----ANSARLEVERDNFAQDLGTLRQKLQDETNLRLeAENNLAAYRQEADEATLARVDLERKV 187
Cdd:COG4913  240 AHEALEDAREQIELLEpirelAERYAAARERLAELEYLRAALRLWFAQRRLEL-LEAELEELRAELARLEAELERLEARL 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  188 ESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEMDVAKpdltaaLREIRTQYEAVATSnMQETEEWYRSKFADLTDAASR 267
Cdd:COG4913  319 DALREELDELEAQIRGNGGDRLEQLEREIERLERELEE------RERRRARLEALLAA-LGLPLPASAEEFAALRAEAAA 391
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84000448  268 NAELLRQAKHEANDYRRQLQAltcDLESLRGTNESLERQMREQEERHARESASYQEALARLEEE 331
Cdd:COG4913  392 LLEALEEELEALEEALAEAEA---ALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
94-214 3.06e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 3.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  94 LAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDnfaqdlgTLRQKL--QDETNLRLEAEnnLAAYRQ 171
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-------ELEAELeeKDERIERLERE--LSEARS 455
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 84000448 172 EADEatlaRVDLERKVESLEEEIQFLRKIYEEE---VRELREQLAQ 214
Cdd:COG2433 456 EERR----EIRKDREISRLDREIERLERELEEErerIEELKRKLER 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
61-376 4.93e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 4.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448  61 ETRASERAEMMELNDRFASYIEKVRFLEQQNKALAA---ELNQLRAKEPTKLADVyQAELRELRLRLDQLTANSARLEVE 137
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEalaELEEEEEEEEEALEEA-AEEEAELEEEEEALLELLAELLEE 471
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 138 RDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLAR-VDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQ 216
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALlLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 217 VHVEMDVAK-------------------------PDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAEL 271
Cdd:COG1196 552 VVEDDEVAAaaieylkaakagratflpldkirarAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 272 LRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDLLN 351
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
                       330       340
                ....*....|....*....|....*
gi 84000448 352 VKLALDIEIATYRKLLEGEENRITI 376
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREE 736
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
183-374 6.08e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 6.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 183 LERKVESLEEEIQFLrkiyEEEVRELREQLAQQQvhvemdvakpdltAALREIRTQYEAVATSNMQETeewYRSKFADLT 262
Cdd:COG3206 166 LELRREEARKALEFL----EEQLPELRKELEEAE-------------AALEEFRQKNGLVDLSEEAKL---LLQQLSELE 225
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 263 DAASRNAELLRQAKHEANDYRRQLQALTCD---------LESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQ 333
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDAlpellqspvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA 305
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 84000448 334 SLKEEMARHLQEYQdllNVKLALDIEIATYRKLLEGEENRI 374
Cdd:COG3206 306 QLQQEAQRILASLE---AELEALQAREASLQAQLAQLEARL 343
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
144-341 6.76e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 6.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 144 DLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRK---IYEEEVRELREQLAQQQVHVE 220
Cdd:COG3883  17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeiaEAEAEIEERREELGERARALY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448 221 MDVAKPDLTAALREIRTQYEAVATSNMQETeewYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRgtn 300
Cdd:COG3883  97 RSGGSVSYLDVLLGSESFSDFLDRLSALSK---IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK--- 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 84000448 301 ESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMAR 341
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
85-208 7.06e-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: 7.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448   85 RFLEQQNKA--LAAELNQLRAKEPTKLADV--YQAELRELRLRLDQLTANS----ARLEVERDNFAQDLGTLRQK----- 151
Cdd:COG3096  526 QRLRQQQNAerLLEEFCQRIGQQLDAAEELeeLLAELEAQLEELEEQAAEAveqrSELRQQLEQLRARIKELAARapawl 605
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 84000448  152 --------LQDETNLRLEAENNLAAYRQEAdeatlarVDLERKVESLEEEIQFLRKIYEEEVREL 208
Cdd:COG3096  606 aaqdalerLREQSGEALADSQEVTAAMQQL-------LEREREATVERDELAARKQALESQIERL 663
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
57-220 9.26e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.51  E-value: 9.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448     57 AGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRA--KEPTKLADVYQAELRELRLRLDQLTANSARL 134
Cdd:TIGR02169  339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDelKDYREKLEKLKREINELKRELDRLQEELQRL 418
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84000448    135 EVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQ 214
Cdd:TIGR02169  419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498

                   ....*.
gi 84000448    215 QQVHVE 220
Cdd:TIGR02169  499 ARASEE 504
 
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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