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Conserved domains on  [gi|1183596669|ref|NP_001337595|]
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centrosomal protein CEP57L1 isoform 8 [Homo sapiens]

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 ...
 54-215 9.00e-57

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: 178.59  E-value: 9.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669  54 ALILALKTLQEKIHRLELERTQAEDNLNILSREAAQYKKALENETNERNLAHQELIKQKK----------------EKQL 117
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQelisqlaaaesrcsllEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669 118 EYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLYAKLEKLDVLEKECFRLTTTQKTAEDKIKHLEEKLKEEEHQRKLF 197
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*...
gi 1183596669 198 QDKASELQTGLEISKIIM 215
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 ...
 54-215 9.00e-57

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: 178.59  E-value: 9.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669  54 ALILALKTLQEKIHRLELERTQAEDNLNILSREAAQYKKALENETNERNLAHQELIKQKK----------------EKQL 117
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQelisqlaaaesrcsllEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669 118 EYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLYAKLEKLDVLEKECFRLTTTQKTAEDKIKHLEEKLKEEEHQRKLF 197
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*...
gi 1183596669 198 QDKASELQTGLEISKIIM 215
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 55-209 5.37e-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: 43.89  E-value: 5.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669   55 LILALKTLQEKIHRLELERTQAEDNLNILSREaaqyKKALENETNERNLAHQELIKQKKEKQLEY--TKRMVLNVEREKN 132
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELyaLANEISRLEQQKQ 305

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1183596669  133 MILEQQAQLQREKEQDQMKLYAKLEKLDVLEKECFRLTTTQKTAEDKIKHLEEKLKEEEHQRKLFQDKASELQTGLE 209
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-209 2.10e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669  55 LILALKTLQEKIHRLELERTQAEDNLNILSREAAQyKKALENETNERNLAHQELIKQKKEKQLEYTKRM--VLNVEREKN 132
Cdd:COG1196   227 AELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYELLaeLARLEQDIA 305

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1183596669 133 MILEQQAQLQREKEQDQMKLYAKLEKLDVLEKECFRLTTTQKTAEDKIKHLEEKLKEEEHQRKLFQDKASELQTGLE 209
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 52-169 5.25e-03

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: 37.17  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669  52 SQALILALKTLQEKIHRLELERTQAEdnlnilsrEAAQYKKALEnetnERNLAHQELIKQKKEKQLEYTKRMVLNVEREK 131
Cdd:cd16269   183 AEAILQADQALTEKEKEIEAERAKAE--------AAEQERKLLE----EQQRELEQKLEDQERSYEEHLRQLKEKMEEER 250

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1183596669 132 NMILEQQAQLQREKEQDQMKLYAK--LEKLDVLEKECFRL 169
Cdd:cd16269   251 ENLLKEQERALESKLKEQEALLEEgfKEQAELLQEEIRSL 290
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
 54-215 9.00e-57

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: 178.59  E-value: 9.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669  54 ALILALKTLQEKIHRLELERTQAEDNLNILSREAAQYKKALENETNERNLAHQELIKQKK----------------EKQL 117
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQelisqlaaaesrcsllEKQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669 118 EYTKRMVLNVEREKNMILEQQAQLQREKEQDQMKLYAKLEKLDVLEKECFRLTTTQKTAEDKIKHLEEKLKEEEHQRKLF 197
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                         170
                  ....*....|....*...
gi 1183596669 198 QDKASELQTGLEISKIIM 215
Cdd:pfam14073 161 QEKAAQLQTGLETNRILL 178
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 55-209 5.37e-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: 43.89  E-value: 5.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669   55 LILALKTLQEKIHRLELERTQAEDNLNILSREaaqyKKALENETNERNLAHQELIKQKKEKQLEY--TKRMVLNVEREKN 132
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAE----LQELEEKLEELRLEVSELEEEIEELQKELyaLANEISRLEQQKQ 305

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1183596669  133 MILEQQAQLQREKEQDQMKLYAKLEKLDVLEKECFRLTTTQKTAEDKIKHLEEKLKEEEHQRKLFQDKASELQTGLE 209
Cdd:TIGR02168  306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-209 2.10e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669  55 LILALKTLQEKIHRLELERTQAEDNLNILSREAAQyKKALENETNERNLAHQELIKQKKEKQLEYTKRM--VLNVEREKN 132
Cdd:COG1196   227 AELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYELLaeLARLEQDIA 305

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1183596669 133 MILEQQAQLQREKEQDQMKLYAKLEKLDVLEKECFRLTTTQKTAEDKIKHLEEKLKEEEHQRKLFQDKASELQTGLE 209
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 53-205 2.34e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669  53 QALILALKTLQEKIHRLELERTQAEDNLNILSREAAQYKKALENETNERNLAHQELI-----KQKKEKQLEYTKRMVLNV 127
Cdd:COG1196   284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEeleeeLEEAEEELEEAEAELAEA 363

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1183596669 128 EREKNMILEQQAQLQREKEQDQMKLYAKLEKLDVLEKECFRLTTTQKTAEDKIKHLEEKLKEEEHQRKLFQDKASELQ 205
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 53-209 3.47e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669  53 QALILALKTLQEKIHRLELERTQAEDNLNILSREAAQYKKALENETNERNLAHQELIKQKKEKQLEytKRMVLNVEREKN 132
Cdd:COG1196   277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL--EEELEEAEEELE 354

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1183596669 133 MILEQQAQLQREKEQDQMKLYAKLEKLDVLEKECFRLTTTQKTAEDKIKHLEEKLKEEEHQRKLFQDKASELQTGLE 209
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 52-169 5.25e-03

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: 37.17  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183596669  52 SQALILALKTLQEKIHRLELERTQAEdnlnilsrEAAQYKKALEnetnERNLAHQELIKQKKEKQLEYTKRMVLNVEREK 131
Cdd:cd16269   183 AEAILQADQALTEKEKEIEAERAKAE--------AAEQERKLLE----EQQRELEQKLEDQERSYEEHLRQLKEKMEEER 250

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1183596669 132 NMILEQQAQLQREKEQDQMKLYAK--LEKLDVLEKECFRL 169
Cdd:cd16269   251 ENLLKEQERALESKLKEQEALLEEgfKEQAELLQEEIRSL 290
 
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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