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Conserved domains on  [gi|66393075|ref|NP_571448|]
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glial fibrillary acidic protein [Danio rerio]

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;
80-388 6.60e-133

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 385.04  E-value: 6.60e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    80 NEKVEMMGLNDRFASYIEKVRFLEQQNKMLVAELNQLRGK---EPSRLGDIYQEELRELRRQVDGLNAGKARLEIERDNL 156
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   157 ASDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDEINFLKKVHEEEMRELHEQLMAQQVHVDL 236
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   237 DVS-KPDLTAALKEIRAQFEAMANSNMQETEEWYRSKFADLTDAANRNGEALRQAKQEANDYRRQIQGLTCDLESLRGSN 315
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66393075   316 ESLERQLKEMEERFAIETAGYQDTVARLEDEIQMLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEESR 388
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 5-79 7.48e-14

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: 66.65  E-value: 7.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075     5 RSFSSYRKRFGT-----PGGSPSVGVTSRHSTGRLSLHSSPRHLTSSPLTLSTSRLS---LGGERLDFSADSLLKAQYRE 76
Cdd:pfam04732   1 YSSSSYRRMFGDssssrPSYSSSSGSRSVSSRSYSRSSSSSPSSSSRRSSRSSSRSSypsLAADSLDFSLADALNQEFKA 80


                  ...
gi 66393075    77 TRT 79
Cdd:pfam04732  81 TRT 83
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
80-388 6.60e-133

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 385.04  E-value: 6.60e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    80 NEKVEMMGLNDRFASYIEKVRFLEQQNKMLVAELNQLRGK---EPSRLGDIYQEELRELRRQVDGLNAGKARLEIERDNL 156
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   157 ASDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDEINFLKKVHEEEMRELHEQLMAQQVHVDL 236
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   237 DVS-KPDLTAALKEIRAQFEAMANSNMQETEEWYRSKFADLTDAANRNGEALRQAKQEANDYRRQIQGLTCDLESLRGSN 315
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66393075   316 ESLERQLKEMEERFAIETAGYQDTVARLEDEIQMLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEESR 388
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 5-79 7.48e-14

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: 66.65  E-value: 7.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075     5 RSFSSYRKRFGT-----PGGSPSVGVTSRHSTGRLSLHSSPRHLTSSPLTLSTSRLS---LGGERLDFSADSLLKAQYRE 76
Cdd:pfam04732   1 YSSSSYRRMFGDssssrPSYSSSSGSRSVSSRSYSRSSSSSPSSSSRRSSRSSSRSSypsLAADSLDFSLADALNQEFKA 80


                  ...
gi 66393075    77 TRT 79
Cdd:pfam04732  81 TRT 83
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 97-370 2.74e-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: 62.77  E-value: 2.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075     97 EKVRFLEQQNKMLVAELNQLRGKEPSRLGDIYQ--EELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRLQDETALR 174
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    175 QEAENNLNTFRQDVDEAALNRVQLERKIEALQDEINFLKKVHEEEMRELHE-----------QLMAQQVHVDLDVSKPDL 243
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrerLESLERRIAATERRLEDL 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    244 TAALKEIRAQFEAMANS--NMQETEEWYRSKFADLTDAANRNGEALRQAK-------QEANDYRRQIQGLTCDLESLRGS 314
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRseleelsEELRELESKRSELRRELEELREK 923

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66393075    315 NESLERQLKEMEERFA--IE--TAGYQDT-------VARLEDEIQMLKEEMARHLQEYQDLLNVKLA 370
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDnlQErlSEEYSLTleeaealENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 129-356 6.79e-10

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: 60.55  E-value: 6.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 129 QEELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDE 208
Cdd:COG4942  26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 209 InflkkvhEEEMRELheQLMAQQVHVDLDVSKPDLTAALKEIRAqFEAMANSNMQETEEwYRSKFADLTDAAnrngEALR 288
Cdd:COG4942 106 L-------AELLRAL--YRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEE-LRADLAELAALR----AELE 170

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66393075 289 QAKQEANDYRRQIQGLTCDLESLRGSNESLERQLKEMEERFAIETAGYQDTVARLEDEIQMLKEEMAR 356
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
PLN02939 PLN02939
transferase, transferring glycosyl groups
 4-363 4.17e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.97  E-value: 4.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    4 QRSFSSYRKRFGTPGGSPSVGVTSRHSTGRLSLHSSPRHL---TSSPLTLSTSRLSLGGERLDFSADSLLKAQYRETRTN 80
Cdd:PLN02939  39 RRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTslrTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTN 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   81 EKVEMMGLNDRFASYIEKVRFLEQqNKMLvaeLNQLRGKEPSRLGDIYQEElRELRRQVDGLNAGKARLEiERDNLASDL 160
Cdd:PLN02939 119 SKDGEQLSDFQLEDLVGMIQNAEK-NILL---LNQARLQALEDLEKILTEK-EALQGKINILEMRLSETD-ARIKLAAQE 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  161 GTLKQRLQDE-TALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDEINFLKkvheEEMRELHEqlmAQQVHVDLDVS 239
Cdd:PLN02939 193 KIHVEILEEQlEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLK----AELIEVAE---TEERVFKLEKE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  240 KPDLTAALKEIRAQF----EAMANSNMQETEEWYR--SKFADLTDAANRNGEALRQAKQEANDYRRQIQGLTCDLESLRG 313
Cdd:PLN02939 266 RSLLDASLRELESKFivaqEDVSKLSPLQYDCWWEkvENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANV 345

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66393075  314 SNES------LERQLKEMEERFAIETAG-------YQDTVARLEDEIQMLKEEMA-RHLQEYQD 363
Cdd:PLN02939 346 SKFSsykvelLQQKLKLLEERLQASDHEihsyiqlYQESIKEFQDTLSKLKEESKkRSLEHPAD 409
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
80-388 6.60e-133

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 385.04  E-value: 6.60e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    80 NEKVEMMGLNDRFASYIEKVRFLEQQNKMLVAELNQLRGK---EPSRLGDIYQEELRELRRQVDGLNAGKARLEIERDNL 156
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   157 ASDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDEINFLKKVHEEEMRELHEQLMAQQVHVDL 236
Cdd:pfam00038  81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   237 DVS-KPDLTAALKEIRAQFEAMANSNMQETEEWYRSKFADLTDAANRNGEALRQAKQEANDYRRQIQGLTCDLESLRGSN 315
Cdd:pfam00038 161 DAArKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66393075   316 ESLERQLKEMEERFAIETAGYQDTVARLEDEIQMLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEESR 388
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Filament_head pfam04732
Intermediate filament head (DNA binding) region; This family represents the N-terminal head ...
 5-79 7.48e-14

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: 66.65  E-value: 7.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075     5 RSFSSYRKRFGT-----PGGSPSVGVTSRHSTGRLSLHSSPRHLTSSPLTLSTSRLS---LGGERLDFSADSLLKAQYRE 76
Cdd:pfam04732   1 YSSSSYRRMFGDssssrPSYSSSSGSRSVSSRSYSRSSSSSPSSSSRRSSRSSSRSSypsLAADSLDFSLADALNQEFKA 80


                  ...
gi 66393075    77 TRT 79
Cdd:pfam04732  81 TRT 83
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 97-370 2.74e-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: 62.77  E-value: 2.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075     97 EKVRFLEQQNKMLVAELNQLRGKEPSRLGDIYQ--EELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRLQDETALR 174
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    175 QEAENNLNTFRQDVDEAALNRVQLERKIEALQDEINFLKKVHEEEMRELHE-----------QLMAQQVHVDLDVSKPDL 243
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrerLESLERRIAATERRLEDL 843

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    244 TAALKEIRAQFEAMANS--NMQETEEWYRSKFADLTDAANRNGEALRQAK-------QEANDYRRQIQGLTCDLESLRGS 314
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRseleelsEELRELESKRSELRRELEELREK 923

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66393075    315 NESLERQLKEMEERFA--IE--TAGYQDT-------VARLEDEIQMLKEEMARHLQEYQDLLNVKLA 370
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDnlQErlSEEYSLTleeaealENKIEDDEEEARRRLKRLENKIKELGPVNLA 990
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 129-356 6.79e-10

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: 60.55  E-value: 6.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 129 QEELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDE 208
Cdd:COG4942  26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 209 InflkkvhEEEMRELheQLMAQQVHVDLDVSKPDLTAALKEIRAqFEAMANSNMQETEEwYRSKFADLTDAAnrngEALR 288
Cdd:COG4942 106 L-------AELLRAL--YRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEE-LRADLAELAALR----AELE 170

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66393075 289 QAKQEANDYRRQIQGLTCDLESLRGSNESLERQLKEMEERFAIETAGYQDTVARLEDEIQMLKEEMAR 356
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 131-389 1.83e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 1.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    131 ELRELRRQVDG-------LNAGKARLEIERDNLASDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIE 203
Cdd:TIGR02168  678 EIEELEEKIEEleekiaeLEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    204 ALQDEINFLKKVHEEEMRELHEqlmAQQVHVDLDVSKPDLTAALKEIRAQFEAMansNMQETEEwyRSKFADLTDAANRN 283
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELKALREALDEL---RAELTLL--NEEAANLRERLESL 829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    284 GEALRQAKQEANDYRRQIQGLTCDLESLRGSNESLERQLKEMEERFAIET---AGYQDTVARLEDEIQMLKEEMARHLQE 360
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnerASLEEALALLRSELEELSEELRELESK 909

                          250       260
                   ....*....|....*....|....*....
gi 66393075    361 YQDLLNVKLALDIEIATYRKLLEGEESRI 389
Cdd:TIGR02168  910 RSELRRELEELREKLAQLELRLEGLEVRI 938
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 128-388 1.05e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 1.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 128 YQEELRELRRQV-----DGLNAGKARLEIERDNLASDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKI 202
Cdd:COG1196 218 LKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 203 EALQDEINFLK---KVHEEEMRELHEQL-MAQQVHVDLDVSKPDLTAALKEIRAQFEAMANSNMQETEEWYR--SKFADL 276
Cdd:COG1196 298 ARLEQDIARLEerrRELEERLEELEEELaELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEaeAELAEA 377

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 277 TDAANRNGEALRQAKQEANDYRRQIQGLTCDLESLRGSNESLERQLKEMEER---FAIETAGYQDTVARLEDEIQMLKEE 353
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAlaeLEEEEEEEEEALEEAAEEEAELEEE 457

                       250       260       270
                ....*....|....*....|....*....|....*
gi 66393075 354 MARHLQEYQDLLNVKLALDIEIATYRKLLEGEESR 388
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-370 2.37e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 2.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075     73 QYRETRTNEK-VEMMGLNDRFASYIEKVRFLEQQNKMLVAELNQLRGKEpsrlgDIYQEELRELRRQVDGLNAGKARLEI 151
Cdd:TIGR02168  214 RYKELKAELReLELALLVLRLEELREELEELQEELKEAEEELEELTAEL-----QELEEKLEELRLEVSELEEEIEELQK 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    152 ERDNLASDLGTL-------KQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDEINFLKKVHEE---EMR 221
Cdd:TIGR02168  289 ELYALANEISRLeqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaELE 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    222 ELHEQLMAQQVHVDldvskpDLTAALKEIRAQFEAMANsnmqeTEEWYRSKFADLTDAANR---NGEALRQAKQEAN--D 296
Cdd:TIGR02168  369 ELESRLEELEEQLE------TLRSKVAQLELQIASLNN-----EIERLEARLERLEDRRERlqqEIEELLKKLEEAElkE 437

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66393075    297 YRRQIQGLTCDLESLRGSNESLERQLKEMEERFAIETAGYQDT---VARLEDEIQMLKEEMARHLQEYQDLLNVKLA 370
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKN 514
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 123-389 2.63e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 2.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 123 RLGDIyqeeLRELRRQVDGLN--AGKAR-----------LEIE-----RDNLASDLGTLKQRLQDETALRQEAENNLNTF 184
Cdd:COG1196 190 RLEDI----LGELERQLEPLErqAEKAEryrelkeelkeLEAEllllkLRELEAELEELEAELEELEAELEELEAELAEL 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 185 RQDVDEAALNRVQLERKIEALQDEINFL-KKVHEEEMRELHEQLMAQQVHVDLDvskpDLTAALKEIRAQFEAMAnsnmQ 263
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELlAELARLEQDIARLEERRRELEERLE----ELEEELAELEEELEELE----E 337

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 264 ETEEWyrskFADLTDAANRNGEALRQAKQEANDYRRqiqgltcdLESLRGSNESLERQLKEMEERFAIETAGYQDTVARL 343
Cdd:COG1196 338 ELEEL----EEELEEAEEELEEAEAELAEAEEALLE--------AEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 66393075 344 EDEIQMLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEESRI 389
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 70-356 3.56e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 3.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  70 LKAQYRETRTNEKV-EMMGLNDRFASYIEKVRFLEQQNKMLVAELNQLRGK---------EPSRLGDIYQEELRELRRQV 139
Cdd:COG1196 218 LKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAEleelrleleELELELEEAQAEEYELLAEL 297

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 140 DGLNAGKARLEIERDNLASDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDEINFLKKVHEEE 219
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 220 MRELHEQLMAQQvhvdldvsKPDLTAALKEIRAQFEAMANSNMQETEEWYRSKFADLTDAANRNGEALRQAKQEANDYRR 299
Cdd:COG1196 378 EEELEELAEELL--------EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 66393075 300 QIQGLTCDLESLRGSNESLERQLKEMEERFAIETAGYQDTVARLEDEIQMLKEEMAR 356
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 146-380 4.70e-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: 51.69  E-value: 4.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 146 KARLEIERDNLASDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDEINFLkkvhEEEMRELHE 225
Cdd:COG4942  22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----EKEIAELRA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 226 QLMAQQVHVDldvskpDLTAALKEIRAQFEAMANSNMQETEEWYRSK--FADLTDAANRNGEALRQAKQEANDYRRQIQG 303
Cdd:COG4942  98 ELEAQKEELA------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEA 171

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66393075 304 LTCDLESLRGSNESLERQLKEMEERfaietagYQDTVARLEDEIQMLKEEMARHLQEYQDLLNVKLALDIEIATYRK 380
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAE-------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
147-366 6.17e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 6.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  147 ARLEIERDNLASDLGTLKQRLQDETALRQEAENNLNTFR--QDVDEAALNRVQLERKIEALQDEINFLKKVH------EE 218
Cdd:COG4913  613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSddlaalEE 692

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  219 EMRELHEQL-MAQQVHVDLDVSKPDLTAALKEIRAQFEAmANSNMQETEEwyRSKFADLTDAANRNGEAL--RQAKQEAN 295
Cdd:COG4913  693 QLEELEAELeELEEELDELKGEIGRLEKELEQAEEELDE-LQDRLEAAED--LARLELRALLEERFAAALgdAVERELRE 769

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66393075  296 DYRRQIQGLTcdlESLRGSNESLERQLKEMEERFAIETAGYQDTVARLEDEIQMLK----EEMARHLQEYQDLLN 366
Cdd:COG4913  770 NLEERIDALR---ARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDrleeDGLPEYEERFKELLN 841
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 107-356 1.29e-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: 50.84  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    107 KMLVAELNQLRGKEPSRLGDIYQEELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRLQDETA-LRQEAENNLNTFR 185
Cdd:TIGR02169  214 QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkIKDLGEEEQLRVK 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    186 QDVDEAALNRVQLERKIEALQDEI----NFLKKVHEE------EMRELHEQLMAQQVHVD-LDVSKPDLTAALKEIRAQF 254
Cdd:TIGR02169  294 EKIGELEAEIASLERSIAEKERELedaeERLAKLEAEidkllaEIEELEREIEEERKRRDkLTEEYAELKEELEDLRAEL 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    255 EAMANSNMQETEEW--YRSKFADLT--------------DAANRNGEALRQAKQEANDYRRQIQGLTCDLESLRGSNESL 318
Cdd:TIGR02169  374 EEVDKEFAETRDELkdYREKLEKLKreinelkreldrlqEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 66393075    319 ERQLKEMEERFAIETAGYQD---TVARLEDEIQMLKEEMAR 356
Cdd:TIGR02169  454 EWKLEQLAADLSKYEQELYDlkeEYDRVEKELSKLQRELAE 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 123-388 1.67e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 1.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    123 RLGDIyqeeLRELRRQVDGLNAgKARLEIERDNLASDLGTLKQRLQdeTALRQEAENNLNTFRQDVDEAALNRVQLERKI 202
Cdd:TIGR02168  190 RLEDI----LNELERQLKSLER-QAEKAERYKELKAELRELELALL--VLRLEELREELEELQEELKEAEEELEELTAEL 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    203 EALQDEINFLKKVHEEEMRELHEqlmAQQVHVDLDVSKPDLTAALKEIRAQFEAMANSNMQETEEWYR--SKFADLTDAA 280
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEE---LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEleSKLDELAEEL 339

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    281 NRNGEALRQAKQEANDYRRQIQGLTCDLESLRGSNESLERQLKEMEERFAIETAGYQD---TVARLEDEIQMLKEEMARH 357
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERL 419

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 66393075    358 LQEYQDLL-----NVKLALDIEIATYRKLLEGEESR 388
Cdd:TIGR02168  420 QQEIEELLkkleeAELKELQAELEELEEELEELQEE 455
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 128-383 3.06e-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: 3.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    128 YQEELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRLQDETALRQEAENNLN-------TFRQDVDEAALNRVQLER 200
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqeeeKLKERLEELEEDLSSLEQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    201 KIEALQDEINFLKKVHEEEMRELHE-QLMAQQVHVDLDVSKpdltaaLKEIRAQfeamansnMQETEEwYRSKFADLTDA 279
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKlEEALNDLEARLSHSR------IPEIQAE--------LSKLEE-EVSRIEARLRE 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    280 ANRNGEALRQAKQEANDYRRQIQGLTCDLESLRGSNESLERQLKEMEERFAIETAGYQDTVARLEDEIQMLKEEMARHLQ 359
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896

                          250       260
                   ....*....|....*....|....
gi 66393075    360 EYQDLLNVKLALDIEIATYRKLLE 383
Cdd:TIGR02169  897 QLRELERKIEELEAQIEKKRKRLS 920
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
88-330 3.24e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   88 LNDRFASYIEKVRFLEQQNKMLVAELNQLRGkepsrlgDIYQEELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRL 167
Cdd:COG4913  260 LAERYAAARERLAELEYLRAALRLWFAQRRL-------ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  168 QDetalrqeaennlntfrQDVDEAAlnrvQLERKIEALQDEInflkkvheEEMRELHEQLMAQQVHVDLDVskPDLTAAL 247
Cdd:COG4913  333 RG----------------NGGDRLE----QLEREIERLEREL--------EERERRRARLEALLAALGLPL--PASAEEF 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  248 KEIRAQFEAMAnsnmqeteewyrskfADLTDAANRNGEALRQAKQEANDYRRQIQGLTCDLESLRGSNESLERQLKEMEE 327
Cdd:COG4913  383 AALRAEAAALL---------------EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447


                 ...
gi 66393075  328 RFA 330
Cdd:COG4913  448 ALA 450
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 97-386 4.74e-06

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: 49.18  E-value: 4.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   97 EKVRFLEQQNKMLVAELNQLRGKEPSrlgdiYQEELRELRRQVDGLNAGKARLEIERDNlasdlgTLKQRLQDETALRQE 176
Cdd:COG3096  836 AELAALRQRRSELERELAQHRAQEQQ-----LRQQLDQLKEQLQLLNKLLPQANLLADE------TLADRLEELREELDA 904

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  177 AENNLNTFRQDVDEAAlnrvQLERKIEALQDEinflkKVHEEEMRELHEQLMAQQVHVDLDVSkpdltaALKEIRAQFEA 256
Cdd:COG3096  905 AQEAQAFIQQHGKALA----QLEPLVAVLQSD-----PEQFEQLQADYLQAKEQQRRLKQQIF------ALSEVVQRRPH 969

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  257 MANSNM-------QETEEWYRSKFADLTDAANRNGEALRQAKQEANDYRRQIQgltcdleSLRGSNESLERQLKEMEERF 329
Cdd:COG3096  970 FSYEDAvgllgenSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-------SLKSSRDAKQQTLQELEQEL 1042

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 66393075  330 -AIETAGYQDTVARLEDEIQMLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEE 386
Cdd:COG3096 1043 eELGVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-389 6.96e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 6.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    174 RQEAENNLNTFRQDVDEAALNRVQLERKIEALQdeinfLKKVHEEEMRELHEQLMaqqvHVDLDVSKPDLTAALKEIRAQ 253
Cdd:TIGR02168  174 RKETERKLERTRENLDRLEDILNELERQLKSLE-----RQAEKAERYKELKAELR----ELELALLVLRLEELREELEEL 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    254 feamansnmQETEEWYRSKFADLTDAANRNGEALRQAKQEANDYRRQIQGLTCDLESLRGSNESLERQLKEMEERFA--- 330
Cdd:TIGR02168  245 ---------QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAnle 315

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 66393075    331 IETAGYQDTVARLEDEIQMLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEESRI 389
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
130-383 2.55e-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: 2.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  130 EELRELRRQVDGLNAGKARLEIERDNLASdLGTLKQRLQDETALRQEAEnnlntfRQDVDEAALNRVQLERKIEALQDEI 209
Cdd:COG4913  225 EAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLELLEAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  210 NFLkkvhEEEMRELHEQLMAQQVHVDldvskpDLTAALKEIRAQfeaMANSNMQETEEwyrskfadLTDAANRNGEALRQ 289
Cdd:COG4913  298 EEL----RAELARLEAELERLEARLD------ALREELDELEAQ---IRGNGGDRLEQ--------LEREIERLERELEE 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  290 AKQEANDYRRQIQGLTCDLESLRGSNESLERQLKEMEERFAIETAGYQDTVARLEDEIQMLKEEMARHLQEYQDLLNVKL 369
Cdd:COG4913  357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436

                        250
                 ....*....|....
gi 66393075  370 ALDIEIATYRKLLE 383
Cdd:COG4913  437 NIPARLLALRDALA 450
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 105-389 4.52e-05

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: 45.88  E-value: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    105 QNKMLVAELNQLRG------KEPSRLGDIYQEELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRLQD--------E 170
Cdd:pfam15921  311 QNSMYMRQLSDLEStvsqlrSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlhkrE 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    171 TALRQEAENN-------------LNTFRQDVD---------EAALNRV------QLERKIEALQDEINFLKKVH------ 216
Cdd:pfam15921  391 KELSLEKEQNkrlwdrdtgnsitIDHLRRELDdrnmevqrlEALLKAMksecqgQMERQMAAIQGKNESLEKVSsltaql 470

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    217 ---EEEMRELHEQLMAQQVHVD-LDVSKPDLTAALKEIRAQFEAmANSNMQETEEWYRSKFADLTDAANRnGEALRQAKQ 292
Cdd:pfam15921  471 estKEMLRKVVEELTAKKMTLEsSERTVSDLTASLQEKERAIEA-TNAEITKLRSRVDLKLQELQHLKNE-GDHLRNVQT 548

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    293 EANDYRRQIQGLTCDLESLRGSNESLeRQLKEMEERFAietAGYQDTVARLEDEIQMLKEEmarhLQEYQDLLNVKLALD 372
Cdd:pfam15921  549 ECEALKLQMAEKDKVIEILRQQIENM-TQLVGQHGRTA---GAMQVEKAQLEKEINDRRLE----LQEFKILKDKKDAKI 620

                          330
                   ....*....|....*..
gi 66393075    373 IEIATYRKLLEGEESRI 389
Cdd:pfam15921  621 RELEARVSDLELEKVKL 637
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 80-348 3.22e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075     80 NEKVEMMGlNDRFASYIEKVRFLEQQNKMLVA--ELNQLRGKEPSRLGDIYQEELRELRRQVDGLNAGKARLEIERDNLA 157
Cdd:TIGR02169  278 NKKIKDLG-EEEQLRVKEKIGELEAEIASLERsiAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    158 SDLGTLKQRLQDetaLRQEAENNLNTFRQDVDEAAlnrvQLERKIEALQDEINFLKKVHE---EEMRELHEQLMaqqvhv 234
Cdd:TIGR02169  357 EEYAELKEELED---LRAELEEVDKEFAETRDELK----DYREKLEKLKREINELKRELDrlqEELQRLSEELA------ 423

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    235 dldvskpDLTAALKEIRAQFEAMAnsnmqeteewyrskfADLTDAANRNGEA---LRQAKQEANDYRRQIQGLTCDLESL 311
Cdd:TIGR02169  424 -------DLNAAIAGIEAKINELE---------------EEKEDKALEIKKQewkLEQLAADLSKYEQELYDLKEEYDRV 481

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 66393075    312 RGSNESLERQLKEME-ERFAIETA--GYQDTVARLEDEIQ 348
Cdd:TIGR02169  482 EKELSKLQRELAEAEaQARASEERvrGGRAVEEVLKASIQ 521
PLN02939 PLN02939
transferase, transferring glycosyl groups
 4-363 4.17e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 42.97  E-value: 4.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    4 QRSFSSYRKRFGTPGGSPSVGVTSRHSTGRLSLHSSPRHL---TSSPLTLSTSRLSLGGERLDFSADSLLKAQYRETRTN 80
Cdd:PLN02939  39 RRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTslrTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTN 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   81 EKVEMMGLNDRFASYIEKVRFLEQqNKMLvaeLNQLRGKEPSRLGDIYQEElRELRRQVDGLNAGKARLEiERDNLASDL 160
Cdd:PLN02939 119 SKDGEQLSDFQLEDLVGMIQNAEK-NILL---LNQARLQALEDLEKILTEK-EALQGKINILEMRLSETD-ARIKLAAQE 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  161 GTLKQRLQDE-TALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDEINFLKkvheEEMRELHEqlmAQQVHVDLDVS 239
Cdd:PLN02939 193 KIHVEILEEQlEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLK----AELIEVAE---TEERVFKLEKE 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  240 KPDLTAALKEIRAQF----EAMANSNMQETEEWYR--SKFADLTDAANRNGEALRQAKQEANDYRRQIQGLTCDLESLRG 313
Cdd:PLN02939 266 RSLLDASLRELESKFivaqEDVSKLSPLQYDCWWEkvENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANV 345

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66393075  314 SNES------LERQLKEMEERFAIETAG-------YQDTVARLEDEIQMLKEEMA-RHLQEYQD 363
Cdd:PLN02939 346 SKFSsykvelLQQKLKLLEERLQASDHEihsyiqlYQESIKEFQDTLSKLKEESKkRSLEHPAD 409
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 148-400 6.11e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 6.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 148 RLEIERDNLAsdlgtlkqRLQDetaLRQEAENNLNTFRQDVdEAALNRVQLERKIEALQDEINFLK-KVHEEEMRELHEQ 226
Cdd:COG1196 180 KLEATEENLE--------RLED---ILGELERQLEPLERQA-EKAERYRELKEELKELEAELLLLKlRELEAELEELEAE 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 227 LMAQQVHVDldvskpDLTAALKEIRAQFEAMansnmqeteewyRSKFADLTDAANRNGEALRQAKQEANDYRRQIQGLTC 306
Cdd:COG1196 248 LEELEAELE------ELEAELAELEAELEEL------------RLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 307 DLESLRGSNESLERQLKEMEER---FAIETAGYQDTVARLEDEIQMLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLE 383
Cdd:COG1196 310 RRRELEERLEELEEELAELEEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389

                       250
                ....*....|....*..
gi 66393075 384 GEESRITVPVQNFTNLQ 400
Cdd:COG1196 390 EALRAAAELAAQLEELE 406
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 129-391 6.34e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   129 QEELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDE 208
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   209 INFLKKVHEEE-MRELHEQLMAQQvhVDLDVSKPDLTAALKEIraqfeamanSNMQETEEWYRSKFADLTDAANRNGEAL 287
Cdd:TIGR04523 297 ISDLNNQKEQDwNKELKSELKNQE--KKLEEIQNQISQNNKII---------SQLNEQISQLKKELTNSESENSEKQREL 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   288 RQAKQEANDYRRQIQGLTCDLESLRGSNESLERQLKEMEE---RFAIETAGYQDTVARLEDEIQMLKEEMARHLQEYQDL 364
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKlnqQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445

                         250       260
                  ....*....|....*....|....*..
gi 66393075   365 LNVKLALDIEIATYRKLLEGEESRITV 391
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKV 472
46 PHA02562
endonuclease subunit; Provisional
 67-360 8.19e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 8.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   67 DSLLKAQYRETRTNEKVEMMglndrfasyieKVRFLEQQNKM---LVAELNQLRGKEPSRLGDIYQEEL---RELRRQVD 140
Cdd:PHA02562 169 DKLNKDKIRELNQQIQTLDM-----------KIDHIQQQIKTynkNIEEQRKKNGENIARKQNKYDELVeeaKTIKAEIE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  141 GLNAGKARLEIERDNLASDLgtlkqrlqdetalrqeaeNNLNTFrqdvdeaalnRVQLERKIEALQDEINFLKKVHEeem 220
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAAL------------------NKLNTA----------AAKIKSKIEQFQKVIKMYEKGGV--- 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  221 relheqlmaqqvhvdldvsKPDLTAALKEIRAQFEAMANSNMQeteewYRSKFADLTDAAnrngEALRQAKQEANDYRRQ 300
Cdd:PHA02562 287 -------------------CPTCTQQISEGPDRITKIKDKLKE-----LQHSLEKLDTAI----DELEEIMDEFNEQSKK 338

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66393075  301 IQGLTCDLESLRGSNESLERQLKEME---ERFAIETAGYQDTVARLEDEIQMLKEEMARHLQE 360
Cdd:PHA02562 339 LLELKNKISTNKQSLITLVDKAKKVKaaiEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 100-209 8.60e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.70  E-value: 8.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    100 RFLEQQNKMLVAELNQLRGKEPSRLgDIYQEELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRLQDETALRQEAEN 179
Cdd:pfam01576  334 KALEEETRSHEAQLQEMRQKHTQAL-EELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEG 412

                           90       100       110
                   ....*....|....*....|....*....|
gi 66393075    180 NLNTFRQDVDEAALNRVQLERKIEALQDEI 209
Cdd:pfam01576  413 QLQELQARLSESERQRAELAEKLSKLQSEL 442
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
129-334 1.43e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 129 QEELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRLQDETALRQeaennlntfrqdvdeaalnRVQLERKIEALQDE 208
Cdd:COG4717  87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-------------------LEALEAELAELPER 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 209 INFLKKvHEEEMRELHEQLMAQQVHVDldvskpDLTAALKEIRAQFEAMANSNMQETEEwyrsKFADLTDAANRNGEALR 288
Cdd:COG4717 148 LEELEE-RLEELRELEEELEELEAELA------ELQEELEELLEQLSLATEEELQDLAE----ELEELQQRLAELEEELE 216

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 66393075 289 QAKQEANDYRRQIQGLTCDLESlrgsnESLERQLKEMEERFAIETA 334
Cdd:COG4717 217 EAQEELEELEEELEQLENELEA-----AALEERLKEARLLLLIAAA 257
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
131-320 1.82e-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: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  131 ELRELRRQVDGLNAGKARLEIERDNLASDLGTLKQRLQDETALRQEAENNLNT----------------FRQDVDEAALN 194
Cdd:COG4913  686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlarlelralleerFAAALGDAVER 765

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  195 RV--QLERKIEALQDEINFLKKVHEEEMRELHEQLMAQQVHVDLDVskpdltAALKEIRAQFEAMANSNMQEteewYRSK 272
Cdd:COG4913  766 ELreNLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADL------ESLPEYLALLDRLEEDGLPE----YEER 835

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 66393075  273 FAD-LTDAANRNGEALRQA-KQEANDYRRQIQGLtcdleslrgsNESLER 320
Cdd:COG4913  836 FKElLNENSIEFVADLLSKlRRAIREIKERIDPL----------NDSLKR 875
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
60-370 2.14e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075   60 ERLDFSADSLLKAQYRETRTNEKVEmmGLNDRFASYIEKVRFLEQQNKMLVAELNQLRGKEPSRLGDI--YQEELRELRR 137
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAE--SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIeeLEEEIEELRE 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  138 QVDGLNAGKARLEIERDNLASDLGTLKQRLQDETALRQEAENNLNTFRQ------------------DVDEAALNRVQ-- 197
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegspHVETIEEDRERve 478

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  198 -LERKIEALQDEINFLKKVHE--EEMRELHEQLMaqqvhvDLDVSKPDLTAALKEIRAQFEAmansnMQETEEWYRSKFA 274
Cdd:PRK02224 479 eLEAELEDLEEEVEEVEERLEraEDLVEAEDRIE------RLEERREDLEELIAERRETIEE-----KRERAEELRERAA 547

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  275 DLTDAANRNGEALRQAKQEANDYRRQIQGLTCDLESLRGSNESLERqlkemeerfaIETAgyQDTVARLEDEIQMLKEEM 354
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER----------IRTL--LAAIADAEDEIERLREKR 615

                        330
                 ....*....|....*.
gi 66393075  355 ArHLQEYQDLLNVKLA 370
Cdd:PRK02224 616 E-ALAELNDERRERLA 630
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 72-408 2.54e-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: 40.44  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075     72 AQYRETRTNEKVEMMGLNDRFASYIEKVRFLEQQNKMLVAELNQLRGKEPSRLGDIYQEELRELRRQVDGLNAGKARLEi 151
Cdd:TIGR02169  733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE- 811

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    152 erdnlaSDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDEInflkkvheeemRELHEQLMAQQ 231
Cdd:TIGR02169  812 ------ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK-----------EELEEELEELE 874

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    232 VHV-DLDVSKPDLTAALKEIRAQFEAMANsnmqeteewyrskfadltdaanrngeALRQAKQEANDYRRQIQGLTCDLES 310
Cdd:TIGR02169  875 AALrDLESRLGDLKKERDELEAQLRELER--------------------------KIEELEAQIEKKRKRLSELKAKLEA 928

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    311 LRGSNESLERQLKEMEERFAiETAGYQDTVA---RLEDEIQMLKEEMARHLQEYQDllnVKLALDiEIATYRKLLEGEES 387
Cdd:TIGR02169  929 LEEELSEIEDPKGEDEEIPE-EELSLEDVQAelqRVEEEIRALEPVNMLAIQEYEE---VLKRLD-ELKEKRAKLEEERK 1003

                          330       340
                   ....*....|....*....|.
gi 66393075    388 RITVPVQNFTNLQfRDTSMDT 408
Cdd:TIGR02169 1004 AILERIEEYEKKK-REVFMEA 1023
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 158-360 4.81e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 4.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 158 SDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAalnrvqlERKIEALQDEInflkKVHEEEMRELHEQLMAQQVHVDld 237
Cdd:COG3883  16 PQIQAKQKELSELQAELEAAQAELDALQAELEEL-------NEEYNELQAEL----EALQAEIDKLQAEIAEAEAEIE-- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 238 vskpDLTAALKE-IRAQFEAMANSNMqeTEEWYRSK-FAD----------LTDAANRNGEALRQAKQEANDYRRQIQGLT 305
Cdd:COG3883  83 ----ERREELGErARALYRSGGSVSY--LDVLLGSEsFSDfldrlsalskIADADADLLEELKADKAELEAKKAELEAKL 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66393075 306 CDLESLRgsnESLERQLKEMEErfaiETAGYQDTVARLEDEIQMLKEEMARHLQE 360
Cdd:COG3883 157 AELEALK---AELEAAKAELEA----QQAEQEALLAQLSAEEAAAEAQLAELEAE 204
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
76-353 5.72e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.74  E-value: 5.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075  76 ETRTNEKVEMMGLNDRFASYIEKVRFLEQQNKMLVAELNQLRGKEPSRLGDIYQ--EELRELRRQVDGLNAGKARLEIER 153
Cdd:COG1340   1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKElrEEAQELREKRDELNEKVKELKEER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 154 DNLASDLGTLKQRLqdeTALRQEAeNNLNTFRQDVDEaalnrvqLERKIEALQDEI--NFLKKVHE----EEMRELHEQL 227
Cdd:COG1340  81 DELNEKLNELREEL---DELRKEL-AELNKAGGSIDK-------LRKEIERLEWRQqtEVLSPEEEkelvEKIKELEKEL 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 228 MAQQVHVDLDVSKPDLTAALKEIRAQFEAmansnmqeteewYRSKFADLTDAANRNGEALRQAKQEANDYRRQIQGLTCD 307
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEAEE------------IHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKE 217

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 66393075 308 LESLRGSNESLERQLKEMEERfaietagyqdtVARLEDEIQMLKEE 353
Cdd:COG1340 218 IVEAQEKADELHEEIIELQKE-----------LRELRKELKKLRKK 252
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 130-232 8.23e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.52  E-value: 8.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 130 EELRELRRQVDGLNAGKARLEIERDNLASD-LGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLER---KIEAL 205
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQrygKIPEL 490

                        90       100
                ....*....|....*....|....*..
gi 66393075 206 QDEINFLKKVHEEEMRELHEQLMAQQV 232
Cdd:COG0542 491 EKELAELEEELAELAPLLREEVTEEDI 517
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 140-360 8.74e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 38.67  E-value: 8.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    140 DGLNAGKARLEIER----------DNLASDLGTLKQRLQDETALRQEAENNLNTFRQDVDEAALNRVQLERKIEALQDEI 209
Cdd:pfam12128  576 GELNLYGVKLDLKRidvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDL 655

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    210 NFLKKVHEEEMRELHEQLMA---------QQVHVDLDVSKPDLTAALKEIRAQF---EAMANSNMQETEEWYRSKFADLT 277
Cdd:pfam12128  656 RRLFDEKQSEKDKKNKALAErkdsanerlNSLEAQLKQLDKKHQAWLEEQKEQKreaRTEKQAYWQVVEGALDAQLALLK 735

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075    278 DA-ANRNGEALRQAKQEANDYRRQIQGLTCD---LESLRGSNESLERQLKE--------------MEERFAIETAGYQDT 339
Cdd:pfam12128  736 AAiAARRSGAKAELKALETWYKRDLASLGVDpdvIAKLKREIRTLERKIERiavrrqevlryfdwYQETWLQRRPRLATQ 815

                          250       260
                   ....*....|....*....|.
gi 66393075    340 VARLEDEIQMLKEEMARHLQE 360
Cdd:pfam12128  816 LSNIERAISELQQQLARLIAD 836
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
128-225 8.90e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.30  E-value: 8.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66393075 128 YQEELRELRRQVdglnagkARLEIERDNLASDLGTLKQRLQdetalrqEAENNLNTFRQDVDEaalnRVQLERKIEALQD 207
Cdd:COG2433 411 EEEEIRRLEEQV-------ERLEAEVEELEAELEEKDERIE-------RLERELSEARSEERR----EIRKDREISRLDR 472

                        90
                ....*....|....*...
gi 66393075 208 EINFLKKVHEEEMRELHE 225
Cdd:COG2433 473 EIERLERELEEERERIEE 490
 
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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