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Conserved domains on  [gi|1958756963|ref|XP_038954547|]
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centrosomal protein CEP57L1 isoform X6 [Rattus norvegicus]

Protein Classification

Cep57_CLD domain-containing protein( domain architecture ID 12163496)

Cep57_CLD 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 ...
 91-268 4.67e-72

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: 221.73  E-value: 4.67e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  91 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQL 170
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963 171 EYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLF 250
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*...
gi 1958756963 251 QDRACELQTGLEISKILM 268
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 91-268 4.67e-72

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: 221.73  E-value: 4.67e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  91 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQL 170
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963 171 EYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLF 250
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*...
gi 1958756963 251 QDRACELQTGLEISKILM 268
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-232 8.76e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 8.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQykkaLEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQ 169
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958756963 170 LEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEK 232
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-262 4.52e-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: 4.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963   96 LKTLQEKIRRLELERTQAEDNLNLLSREaaqyKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQLEYTKR 175
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  176 MVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLtttqqtaEEKIKyleeklkEEEHQRRLFQDRAC 255
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL-------EAELE-------ELEAELEELESRLE 375


                   ....*..
gi 1958756963  256 ELQTGLE 262
Cdd:TIGR02168  376 ELEEQLE 382
PRK12704 PRK12704
phosphodiesterase; Provisional
 97-233 2.95e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  97 KTLQEKIRRLElerTQAEDNLNLLSREAAQYKK-----ALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQLE 171
Cdd:PRK12704   27 KIAEAKIKEAE---EEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958756963 172 ytkrmvlNVEREKNMILEQQAQLQREKEQdqmklhaklekLDVLEKECLRLTTTQQTAEEKI 233
Cdd:PRK12704  104 -------LLEKREEELEKKEKELEQKQQE-----------LEKKEEELEELIEEQLQELERI 147
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 91-268 4.67e-72

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: 221.73  E-value: 4.67e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  91 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQL 170
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQELISQLAAAESRCSLLEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963 171 EYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLF 250
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*...
gi 1958756963 251 QDRACELQTGLEISKILM 268
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-232 8.76e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 8.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQykkaLEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQ 169
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958756963 170 LEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEK 232
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-234 6.69e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 6.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHE---ELTRQKKDISIQLSSAQSRCILL 166
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEEL 335

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958756963 167 EKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIK 234
Cdd:COG1196   336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-234 2.71e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERnlahEELTRQKKDISIQLSSAQSRCILLEKQ 169
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL----EELEEELEEAEEELEEAEAELAEAEEA 366

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958756963 170 LEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIK 234
Cdd:COG1196   367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-233 3.12e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 3.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQY----------KKALEEETNERNLAHEELTRQKKDISIQLSSA 159
Cdd:COG1196   263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiarleerRRELEERLEELEEELAELEEELEELEEELEEL 342

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958756963 160 QSRCILLEKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKI 233
Cdd:COG1196   343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-262 4.52e-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: 4.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963   96 LKTLQEKIRRLELERTQAEDNLNLLSREaaqyKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQLEYTKR 175
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  176 MVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLtttqqtaEEKIKyleeklkEEEHQRRLFQDRAC 255
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL-------EAELE-------ELEAELEELESRLE 375


                   ....*..
gi 1958756963  256 ELQTGLE 262
Cdd:TIGR02168  376 ELEEQLE 382
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 90-268 1.98e-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: 46.59  E-value: 1.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963   90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKK---ALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILL 166
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEeleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  167 EKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAK-----LEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLK 241
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelQAELEELEEELEELQEELERLEEALEELREELE 471

                          170       180
                   ....*....|....*....|....*..
gi 1958756963  242 EEEHQRRLFQDRACELQTGLEISKILM 268
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLERLQ 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 95-262 3.46e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 3.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963   95 ALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDIS----------IQLSSAQSRCI 164
Cdd:TIGR02168  699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTeleaeieeleERLEEAEEELA 778

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  165 LLEKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEE 244
Cdd:TIGR02168  779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858

                          170
                   ....*....|....*...
gi 1958756963  245 HQRRLFQDRACELQTGLE 262
Cdd:TIGR02168  859 AEIEELEELIEELESELE 876
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 90-234 2.56e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQ---------LSSAQ 160
Cdd:COG3883    33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvLLGSE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963 161 S------RCILLEKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQdqmkLHAKLEKLDVLEKECLRLTTTQQTAEEKIK 234
Cdd:COG3883   113 SfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKAELEAAKAELEAQQAEQEALLAQLS 188
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
90-254 4.00e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 4.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963   90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNL--AHEELTRQKKDISiQLSSAQSRCILLE 167
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELE-RLDASSDDLAALE 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  168 KQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKEClrLTTTQQTAEEKIKYLEEKLKEEEHQR 247
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFAAALGDAVERELRE 769


                   ....*..
gi 1958756963  248 RLFQDRA 254
Cdd:COG4913    770 NLEERID 776
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 90-297 5.77e-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: 41.97  E-value: 5.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963   90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNlaheELTRQKKDISIQLSSAQSRCILLEKQ 169
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS----RLEQQKQILRERLANLERQLEELEAQ 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  170 LEYTKRMVLNVEREKNMILEQQAQLQREKEqdqmklhAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRL 249
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELE-------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958756963  250 FQDRACELQTGLEiskilMSTVSSSKLCNERKKLPKVRKLQEKVENSR 297
Cdd:TIGR02168  398 LNNEIERLEARLE-----RLEDRRERLQQEIEELLKKLEEAELKELQA 440
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 90-262 6.43e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQ-----SRCI 164
Cdd:COG4942    44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgrqPPLA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963 165 LL---------EKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKY 235
Cdd:COG4942   124 LLlspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203

                         170       180
                  ....*....|....*....|....*..
gi 1958756963 236 LEEKLKEEEHQRRLFQDRACELQTGLE 262
Cdd:COG4942   204 LEKELAELAAELAELQQEAEELEALIA 230
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-233 8.95e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 8.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  95 ALKTL---QEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQLE 171
Cdd:COG1196   177 AERKLeatEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELE 256

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958756963 172 YTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKI 233
Cdd:COG1196   257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
90-231 8.98e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 8.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAheELTRQKKDISIQLSSAQSRC------ 163
Cdd:COG3206   215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQ--QLRAQLAELEAELAELSARYtpnhpd 292

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958756963 164 -ILLEKQLE--------YTKRMVLNVEREKNMILEQQAQLQREKEQdqmkLHAKLEKLDVLEKECLRLTTTQQTAEE 231
Cdd:COG3206   293 vIALRAQIAalraqlqqEAQRILASLEAELEALQAREASLQAQLAQ----LEARLAELPELEAELRRLEREVEVARE 365
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 98-294 8.99e-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: 41.21  E-value: 8.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963   98 TLQEKIRRLELERTQAEDNLNLLSRE---AAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQLEYTK 174
Cdd:TIGR02169  291 RVKEKIGELEAEIASLERSIAEKEREledAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  175 RMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLFQDRA 254
Cdd:TIGR02169  371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1958756963  255 CELQTGLEISKILMSTVsSSKLCNERKKLPKVRKLQEKVE 294
Cdd:TIGR02169  451 KKQEWKLEQLAADLSKY-EQELYDLKEEYDRVEKELSKLQ 489
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
90-234 1.34e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLsreaaqykkaleeetnERNLAHEELTRQKKDISIQLSSAQSRCILLEKQ 169
Cdd:COG4717    91 AELQEELEELEEELEELEAELEELREELEKL----------------EKLLQLLPLYQELEALEAELAELPERLEELEER 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958756963 170 LEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKL----EKLDVLEKECLRLTTTQQTAEEKIK 234
Cdd:COG4717   155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELqdlaEELEELQQRLAELEEELEEAQEELE 223
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
86-231 1.41e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  86 SPNNQALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISI---QLSSAQSR 162
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQaqeELESLQEE 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958756963 163 CILLEKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEE 231
Cdd:COG4372   110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 94-258 1.56e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  94 SALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQLEYT 173
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963 174 KR---------MVLN----------------VEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKEclrLTTTQQT 228
Cdd:COG3883    96 YRsggsvsyldVLLGsesfsdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE---LEAAKAE 172

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958756963 229 AEEKIKYLEEKLKEEEHQRRLFQDRACELQ 258
Cdd:COG3883   173 LEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
PRK12704 PRK12704
phosphodiesterase; Provisional
 97-233 2.95e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  97 KTLQEKIRRLElerTQAEDNLNLLSREAAQYKK-----ALEEETNERNLAHEELTRQKKDISIQLSSAQSRCILLEKQLE 171
Cdd:PRK12704   27 KIAEAKIKEAE---EEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958756963 172 ytkrmvlNVEREKNMILEQQAQLQREKEQdqmklhaklekLDVLEKECLRLTTTQQTAEEKI 233
Cdd:PRK12704  104 -------LLEKREEELEKKEKELEQKQQE-----------LEKKEEELEELIEEQLQELERI 147
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-351 4.04e-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: 39.27  E-value: 4.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  102 KIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERnlahEELTRQKKDISIQLSSAQSRCILLEKQLEytkrmvlNVE 181
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEEL----EQLRKELEELSRQISALRKDLARLEAEVE-------QLE 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  182 REKNMILEQQAQLQREKEQdqmkLHAKLEKLDVLEKEclrltttqqtAEEKIKYLEEKLKEEEHQRRLFQDRACELQTGL 261
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEE----LEERLEEAEEELAE----------AEAEIEELEAQIEQLKEELKALREALDELRAEL 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  262 EISKILMSTVSSSKLCNERKKLPKVRKLQEKVENSRINESSGIHGNPKRSKnLKTSPRKCLSETSAFQKDRSFQPVKVHS 341
Cdd:TIGR02168  813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE-LEELIEELESELEALLNERASLEEALAL 891

                          250
                   ....*....|
gi 1958756963  342 LppRLRRDDV 351
Cdd:TIGR02168  892 L--RSELEEL 899
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 86-171 4.57e-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: 38.59  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  86 SPNNQALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSRCIL 165
Cdd:COG4942   145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224


                  ....*.
gi 1958756963 166 LEKQLE 171
Cdd:COG4942   225 LEALIA 230
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
90-235 7.94e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963  90 QALVSALKTLQEKIRRLELERTQAE-------DNLNLLsREAAQYKKALEEETNERNLAHEELTRQKKDISIQLSSAQSR 162
Cdd:COG4717   350 QELLREAEELEEELQLEELEQEIAAllaeagvEDEEEL-RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963 163 ciLLEKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQ-------DQM--KLHAKLEKLDVLEKECLRLTTTQQTAEEKI 233
Cdd:COG4717   429 --ELEEELEELEEELEELEEELEELREELAELEAELEQleedgelAELlqELEELKAELRELAEEWAALKLALELLEEAR 506


                  ..
gi 1958756963 234 KY 235
Cdd:COG4717   507 EE 508
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
90-218 9.63e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.97  E-value: 9.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958756963   90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNER--NLAHE--ELTRQKKDISIQLSSAQSRCIL 165
Cdd:COG4913    291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleQLEREieRLERELEERERRRARLEALLAA 370

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958756963  166 LEKQLEYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKL----DVLEKE 218
Cdd:COG4913    371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLrrelRELEAE 427
 
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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