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Conserved domains on  [gi|564398251|ref|XP_006256625|]
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centrosomal protein CEP57L1 isoform X2 [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 ...
 91-252 9.85e-60

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: 193.23  E-value: 9.85e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251   91 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKK----------------EKQL 154
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQelisqlaaaesrcsllEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  155 EYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLF 234
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*...
gi 564398251  235 QDRACELQTGLEISKILM 252
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 309-382 3.08e-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: 56.04  E-value: 3.08e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564398251  309 HSSGEPFSICDNLSELLRTMQDELDQMNMEHRELLRQIAQ---TGSHSDSEELEQELEHLARKMESKEDQISKLQKH 382
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 ...
 91-252 9.85e-60

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: 193.23  E-value: 9.85e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251   91 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKK----------------EKQL 154
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQelisqlaaaesrcsllEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  155 EYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLF 234
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*...
gi 564398251  235 QDRACELQTGLEISKILM 252
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 309-382 3.08e-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: 56.04  E-value: 3.08e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564398251  309 HSSGEPFSICDNLSELLRTMQDELDQMNMEHRELLRQIAQ---TGSHSDSEELEQELEHLARKMESKEDQISKLQKH 382
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-218 4.06e-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: 4.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQykkaLEEETNERNLAHEELTRQKKEKQLEYTKRM--VLNVERE 167
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLaeLARLEQD 303

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564398251 168 KNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIK 218
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-246 1.24e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251    96 LKTLQEKIRRLELERTQAEDNLNLLSREaaqyKKALEEETNERNLAHEELTRQKKEKQLEY--TKRMVLNVEREKNMILE 173
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELyaLANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564398251   174 QQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLFQDRACELQTGLE 246
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 90-206 3.46e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.18  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  90 QALVSALKTLQEKIRRLELERTQAEdnlnllsrEAAQYKKALEEETNErnlaHEELTRQKKEKQLEYTKRMVLNVEREKN 169
Cdd:cd16269  184 EAILQADQALTEKEKEIEAERAKAE--------AAEQERKLLEEQQRE----LEQKLEDQERSYEEHLRQLKEKMEEERE 251

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564398251 170 MILEQQAQLQREKEQDQMKLHAK--LEKLDVLEKECLRL 206
Cdd:cd16269  252 NLLKEQERALESKLKEQEALLEEgfKEQAELLQEEIRSL 290
PRK12704 PRK12704
phosphodiesterase; Provisional
 123-217 1.21e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251 123 EAAQYKKALEEETNERNlahEELtrQKKEKQLEYTKRmvlNVEREKNMILEQQAQLQREKEQdqmkLHAKLEKLDVLEKE 202
Cdd:PRK12704  65 EIHKLRNEFEKELRERR---NEL--QKLEKRLLQKEE---NLDRKLELLEKREEELEKKEKE----LEQKQQELEKKEEE 132

                         90
                 ....*....|....*
gi 564398251 203 CLRLTTTQQTAEEKI 217
Cdd:PRK12704 133 LEELIEEQLQELERI 147
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 91-252 9.85e-60

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: 193.23  E-value: 9.85e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251   91 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKK----------------EKQL 154
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQelisqlaaaesrcsllEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  155 EYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLF 234
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*...
gi 564398251  235 QDRACELQTGLEISKILM 252
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
 309-382 3.08e-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: 56.04  E-value: 3.08e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564398251  309 HSSGEPFSICDNLSELLRTMQDELDQMNMEHRELLRQIAQ---TGSHSDSEELEQELEHLARKMESKEDQISKLQKH 382
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-218 4.06e-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: 4.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQykkaLEEETNERNLAHEELTRQKKEKQLEYTKRM--VLNVERE 167
Cdd:COG1196  228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYELLaeLARLEQD 303

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564398251 168 KNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIK 218
Cdd:COG1196  304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 96-216 4.71e-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: 4.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  96 LKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKK-----EKQLEYTKRMVLNVEREKNM 170
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarlEQDIARLEERRRELEERLEE 320

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564398251 171 ILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEK 216
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-246 1.24e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251    96 LKTLQEKIRRLELERTQAEDNLNLLSREaaqyKKALEEETNERNLAHEELTRQKKEKQLEY--TKRMVLNVEREKNMILE 173
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELyaLANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564398251   174 QQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLFQDRACELQTGLE 246
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-217 4.99e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 4.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKE-----KQLEYTKRMVLNV 164
Cdd:COG1196  284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEleeaeEELEEAEAELAEA 363

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564398251 165 EREKNMILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKI 217
Cdd:COG1196  364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-218 7.17e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 7.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKEKQleytkRMVLNVEREKN 169
Cdd:COG1196  256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE-----ELEEELAELEE 330

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564398251 170 MILEQQAQLQR---EKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIK 218
Cdd:COG1196  331 ELEELEEELEEleeELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 90-218 1.21e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKE-----KQLEYTKRMVLNV 164
Cdd:COG1196  291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeaeAELAEAEEALLEA 370

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564398251 165 EREKNMILEQ-----QAQLQ--REKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIK 218
Cdd:COG1196  371 EAELAEAEEEleelaEELLEalRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 94-202 2.67e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.53  E-value: 2.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  94 SALKTLQEKIRRLELERTQAEDNLNLLSRE-AAQYKKALEEETNERNlahEELTRQKKEKQLeytkrmvLNVEREKNMIL 172
Cdd:COG0542  411 EELDELERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELE---ALKARWEAEKEL-------IEEIQELKEEL 480

                         90       100       110
                 ....*....|....*....|....*....|
gi 564398251 173 EQQAQLQREKEQDQMKLHAKLEKLDVLEKE 202
Cdd:COG0542  481 EQRYGKIPELEKELAELEEELAELAPLLRE 510
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 90-206 3.46e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.18  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  90 QALVSALKTLQEKIRRLELERTQAEdnlnllsrEAAQYKKALEEETNErnlaHEELTRQKKEKQLEYTKRMVLNVEREKN 169
Cdd:cd16269  184 EAILQADQALTEKEKEIEAERAKAE--------AAEQERKLLEEQQRE----LEQKLEDQERSYEEHLRQLKEKMEEERE 251

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564398251 170 MILEQQAQLQREKEQDQMKLHAK--LEKLDVLEKECLRL 206
Cdd:cd16269  252 NLLKEQERALESKLKEQEALLEEgfKEQAELLQEEIRSL 290
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 99-246 4.16e-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: 43.12  E-value: 4.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251    99 LQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQkkEKQLEYTKRMVLNVEREKNMILEQQAQL 178
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDEL 808

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564398251   179 QREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIKYLEEKLKEEEHQRRLFQDRACELQTGLE 246
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 90-246 1.11e-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: 41.58  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251    90 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKEKQlEYTKRMVLNVEREKN 169
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELEE 362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251   170 MILEQQAQLQREKEQDQM------KLHAKLEKLDVLEKECLRLTTTQQTAEEKIKylEEKLKEEEHQRRLFQDRACELQT 243
Cdd:TIGR02168  363 LEAELEELESRLEELEEQletlrsKVAQLELQIASLNNEIERLEARLERLEDRRE--RLQQEIEELLKKLEEAELKELQA 440


                   ...
gi 564398251   244 GLE 246
Cdd:TIGR02168  441 ELE 443
PRK12704 PRK12704
phosphodiesterase; Provisional
 123-217 1.21e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251 123 EAAQYKKALEEETNERNlahEELtrQKKEKQLEYTKRmvlNVEREKNMILEQQAQLQREKEQdqmkLHAKLEKLDVLEKE 202
Cdd:PRK12704  65 EIHKLRNEFEKELRERR---NEL--QKLEKRLLQKEE---NLDRKLELLEKREEELEKKEKE----LEQKQQELEKKEEE 132

                         90
                 ....*....|....*
gi 564398251 203 CLRLTTTQQTAEEKI 217
Cdd:PRK12704 133 LEELIEEQLQELERI 147
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 102-397 2.64e-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: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251   102 KIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRqkKEKQLEYTKRMVLNVEREKNMILEQQAQLQRE 181
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--LSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251   182 ---KEQDQMKLHAKLEKLDVLEKEclrltttqqtAEEKIKYleeklkeeehQRRLFQDRACELQTGLEISKILmstvsSS 258
Cdd:TIGR02168  756 lteLEAEIEELEERLEEAEEELAE----------AEAEIEE----------LEAQIEQLKEELKALREALDEL-----RA 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251   259 KLCNERKKLPKKTNCLKREPPQHTDCRFRGPASERERppfrmtssaraephssgepfsicDNLSELLRTMQDELDQMNME 338
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI-----------------------EELSEDIESLAAEIEELEEL 867

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 564398251   339 HRELLRQIAqtgSHSDSEELEQELEHLARkmESKEDQISKLQKHQDRVRKLQEKVENSR 397
Cdd:TIGR02168  868 IEELESELE---ALLNERASLEEALALLR--SELEELSEELRELESKRSELRRELEELR 921
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-218 3.01e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  95 ALKTL---QEKIRRLELERTQAEDNLNLLSREAAQYKK--ALEEETNERNLAHEELTRQKKEKQLEYTKRMVLNVEREKN 169
Cdd:COG1196  177 AERKLeatEENLERLEDILGELERQLEPLERQAEKAERyrELKEELKELEAELLLLKLRELEAELEELEAELEELEAELE 256

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 564398251 170 MILEQQAQLQREKEQDQMKLHAKLEKLDVLEKECLRLTTTQQTAEEKIK 218
Cdd:COG1196  257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 86-184 5.65e-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: 38.98  E-value: 5.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564398251  86 SPNNQALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHEELTRQKKEKQlEYTKRMVLNVE 165
Cdd:COG4942  145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAE 223

                         90
                 ....*....|....*....
gi 564398251 166 REKNMILEQQAQLQREKEQ 184
Cdd:COG4942  224 ELEALIARLEAEAAAAAER 242
 
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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