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Conserved domains on  [gi|564398255|ref|XP_006256627|]
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centrosomal protein CEP57L1 isoform X3 [Rattus norvegicus]

Protein Classification

Cep57_CLD and Cep57_MT_bd domain-containing protein( domain architecture ID 12163498)

Cep57_CLD and Cep57_MT_bd domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
50-227 5.93e-69

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


:

Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 216.34  E-value: 5.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255   50 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQL 129
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  130 EYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLF 209
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160
                         170
                  ....*....|....*...
gi 564398255  210 QDRACELQTGLEISKILM 227
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
284-357 8.84e-10

Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, nucleates and bundles microtubules. The N-terminal part, family Cep57_CLD, pfam14073, is the centrosome localization domain Cep57.


:

Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 54.89  E-value: 8.84e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564398255  284 HSSGEPFSICDNLSELLRTMQDELDQMNMEHRELLRQIAQ---TGSHSDSEELEQELEHLARKMESKEDQISKLQKH 357
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
50-227 5.93e-69

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 216.34  E-value: 5.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255   50 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQL 129
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  130 EYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLF 209
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160
                         170
                  ....*....|....*...
gi 564398255  210 QDRACELQTGLEISKILM 227
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
284-357 8.84e-10

Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, nucleates and bundles microtubules. The N-terminal part, family Cep57_CLD, pfam14073, is the centrosome localization domain Cep57.


Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 54.89  E-value: 8.84e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564398255  284 HSSGEPFSICDNLSELLRTMQDELDQMNMEHRELLRQIAQ---TGSHSDSEELEQELEHLARKMESKEDQISKLQKH 357
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
49-191 5.40e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 5.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  49 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQykkaLEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQ 128
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564398255 129 LEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEK 191
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
55-221 2.40e-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: 46.97  E-value: 2.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255    55 LKTLQEKIRRLELERTQAEDNLNLLSREaaqyKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQLEYTKR 134
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255   135 MVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLtttqqtaEEKIKyleeklkEEEHQRRLFQDRAC 214
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL-------EAELE-------ELEAELEELESRLE 375

                   ....*..
gi 564398255   215 ELQTGLE 221
Cdd:TIGR02168  376 ELEEQLE 382
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
50-227 5.93e-69

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 216.34  E-value: 5.93e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255   50 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQL 129
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  130 EYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLF 209
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160
                         170
                  ....*....|....*...
gi 564398255  210 QDRACELQTGLEISKILM 227
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
284-357 8.84e-10

Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, nucleates and bundles microtubules. The N-terminal part, family Cep57_CLD, pfam14073, is the centrosome localization domain Cep57.


Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 54.89  E-value: 8.84e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564398255  284 HSSGEPFSICDNLSELLRTMQDELDQMNMEHRELLRQIAQ---TGSHSDSEELEQELEHLARKMESKEDQISKLQKH 357
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
49-191 5.40e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 5.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  49 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQykkaLEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQ 128
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564398255 129 LEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEK 191
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
49-193 3.75e-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: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  49 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHE---ELTRQKKDISIQLSSAQSRCILL 125
Cdd:COG1196  256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEEL 335
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564398255 126 EKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIK 193
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
49-193 1.44e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  49 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERnlahEELTRQKKDISIQLSSAQSRCILLEKQ 128
Cdd:COG1196  291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL----EELEEELEEAEEELEEAEAELAEAEEA 366
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564398255 129 LEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIK 193
Cdd:COG1196  367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
49-192 1.72e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  49 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQY----------KKALEEETNERNLAHEELTRQKKDISIQLSSA 118
Cdd:COG1196  263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiarleerRRELEERLEELEEELAELEEELEELEEELEEL 342
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564398255 119 QSRCILLEKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKI 192
Cdd:COG1196  343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
55-221 2.40e-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: 46.97  E-value: 2.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255    55 LKTLQEKIRRLELERTQAEDNLNLLSREaaqyKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQLEYTKR 134
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255   135 MVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLtttqqtaEEKIKyleeklkEEEHQRRLFQDRAC 214
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL-------EAELE-------ELEAELEELESRLE 375

                   ....*..
gi 564398255   215 ELQTGLE 221
Cdd:TIGR02168  376 ELEEQLE 382
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
49-227 8.47e-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: 45.05  E-value: 8.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255    49 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKK---ALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILL 125
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEeleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255   126 EKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAK-----LEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLK 200
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelQAELEELEEELEELQEELERLEEALEELREELE 471
                          170       180
                   ....*....|....*....|....*..
gi 564398255   201 EEEHQRRLFQDRACELQTGLEISKILM 227
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLERLQ 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
54-221 1.33e-04

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: 44.28  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255    54 ALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDIS----------IQLSSAQSRCI 123
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTeleaeieeleERLEEAEEELA 778
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255   124 LLEKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEE 203
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
                          170
                   ....*....|....*...
gi 564398255   204 HQRRLFQDRACELQTGLE 221
Cdd:TIGR02168  859 AEIEELEELIEELESELE 876
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
49-193 1.31e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  49 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQ---------LSSAQ 119
Cdd:COG3883   33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvLLGSE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255 120 S------RCILLEKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQdqmkLHAKLEKLDVLEKECLRLTTTQQTAEEKIK 193
Cdd:COG3883  113 SfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEAAKAELEAQQAEQEALLAQLS 188
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
49-213 1.35e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255   49 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNL--AHEELTRQKKDISiQLSSAQSRCILLE 126
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELE-RLDASSDDLAALE 691
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  127 KQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKEClrLTTTQQTAEEKIKYLEEKLKEEEHQR 206
Cdd:COG4913   692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFAAALGDAVERELRE 769

                  ....*..
gi 564398255  207 RLFQDRA 213
Cdd:COG4913   770 NLEERID 776
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
49-221 1.35e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  49 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQ-----SRCI 123
Cdd:COG4942   44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgrqPPLA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255 124 LL---------EKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKY 194
Cdd:COG4942  124 LLlspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203
                        170       180
                 ....*....|....*....|....*..
gi 564398255 195 LEEKLKEEEHQRRLFQDRACELQTGLE 221
Cdd:COG4942  204 LEKELAELAAELAELQQEAEELEALIA 230
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
49-190 1.63e-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: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  49 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAheELTRQKKDISIQLSSAQSRC------ 122
Cdd:COG3206  215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSARYtpnhpd 292
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564398255 123 -ILLEKQLE--------YTKRMVLNVEREKNMILEQQAQLQREKEQdqmkLHAKLEKLDVLEKECLRLTTTQQTAEE 190
Cdd:COG3206  293 vIALRAQIAalraqlqqEAQRILASLEAELEALQAREASLQAQLAQ----LEARLAELPELEAELRRLEREVEVARE 365
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
49-224 2.13e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255    49 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNlaheELTRQKKDISIQLSSAQSRCILLEKQ 128
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS----RLEQQKQILRERLANLERQLEELEAQ 324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255   129 LEYTKRMVLNVEREKNMILEQQAQLQREKEqdqmklhAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRL 208
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELE-------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
                          170
                   ....*....|....*.
gi 564398255   209 FQDRACELQTGLEISK 224
Cdd:TIGR02168  398 LNNEIERLEARLERLE 413
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
55-192 3.26e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  55 LKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQLEYTKR 134
Cdd:COG1196  181 LEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564398255 135 MVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKI 192
Cdd:COG1196  261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
49-193 6.62e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 6.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  49 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEeetnernlaHEELTRQKKDISIQLSSAQSRCILLEKQ 128
Cdd:COG4717   84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---------LLPLYQELEALEAELAELPERLEELEER 154
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564398255 129 LEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKL----EKLDVLEKECLRLTTTQQTAEEKIK 193
Cdd:COG4717  155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELqdlaEELEELQQRLAELEEELEEAQEELE 223
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
57-252 6.91e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 6.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255    57 TLQEKIRRLELERTQAEDNLNLLSRE---AAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQLEYTK 133
Cdd:TIGR02169  291 RVKEKIGELEAEIASLERSIAEKEREledAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255   134 RMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLFQDRA 213
Cdd:TIGR02169  371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 564398255   214 CELQTGLEISKILMSTVSSS--KLCNERKKLPKKTNCLKRE 252
Cdd:TIGR02169  451 KKQEWKLEQLAADLSKYEQElyDLKEEYDRVEKELSKLQRE 491
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
53-217 7.78e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  53 SALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQLEYT 132
Cdd:COG3883   16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255 133 KR---------MVLN----------------VEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKEclrLTTTQQT 187
Cdd:COG3883   96 YRsggsvsyldVLLGsesfsdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE---LEAAKAE 172
                        170       180       190
                 ....*....|....*....|....*....|
gi 564398255 188 AEEKIKYLEEKLKEEEHQRRLFQDRACELQ 217
Cdd:COG3883  173 LEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
45-130 9.22e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 9.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398255  45 SPNNQALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCIL 124
Cdd:COG4942  145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224

                 ....*.
gi 564398255 125 LEKQLE 130
Cdd:COG4942  225 LEALIA 230
 
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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