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Conserved domains on  [gi|1622915247|ref|XP_014981215|]
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centriolar coiled-coil protein of 110 kDa isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CaM_bind pfam16025
Calcium-dependent calmodulin binding; This domain is found at the N-terminus of centriolar ...
 54-131 1.69e-22

Calcium-dependent calmodulin binding; This domain is found at the N-terminus of centriolar coiled-coil protein of 110 kDa (CCP110), where it binds calmodulin. Binding of calmodulin to this domain is calcium dependent.


:

Pssm-ID: 464981  Cd Length: 78  Bit Score: 92.01  E-value: 1.69e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622915247   54 QSESISLIRFHGVAILSPLLNVEKRREMQQEKQKALDVEARKQVNRKKTLLTRVQEILDNVQVRKAPNASDFDQWEME 131
Cdd:pfam16025    1 ESEFVSCIKINGVPILPPLMTDEKREEMQQYRQKAIAIEERLRKQRKAALLIRVQEILKNEQRRKLPTLEQTSTLDAE 78
Stathmin super family cl02980
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 663-729 9.70e-04

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


The actual alignment was detected with superfamily member pfam00836:

Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 40.41  E-value: 9.70e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  663 SKESEELLKSKMLAFEEMRKRLEeqhAQQLSLLIAEQEREQERLQKEIEEQE---KMLKEKKAMTAEASE 729
Cdd:pfam00836   40 KDSSLEEIQKKLEAAEERRKSLE---AQKLKQLAEKREKEEEALQKADEENNnfsKMAEEKLKQKMEAYK 106
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 664-833 3.28e-03

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 3.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  664 KESEELLKSKMLAFEEMRKRLEEQhAQQLSLLIAEQEREQERLQKEIEEQEKMLKE-KKAMTAEASELDinsavELEWRK 742
Cdd:COG4942    149 REQAEELRADLAELAALRAELEAE-RAELEALLAELEEERAALEALKAERQKLLARlEKELAELAAELA-----ELQQEA 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  743 ISDSSLLETmLSQADSLHTSNSNSSGFTNSALQYSFvsaneaPfylwgssTSGltklSVTRPFGRAKTrwSQVFSP--EI 820
Cdd:COG4942    223 EELEALIAR-LEAEAAAAAERTPAAGFAALKGKLPW------P-------VSG----RVVRRFGERDG--GGGRNKgiDI 282

                          170
                   ....*....|....
gi 1622915247  821 QAKFN-KITAVAKG 833
Cdd:COG4942    283 AAPPGaPVRAVADG 296
 
Name Accession Description Interval E-value
CaM_bind pfam16025
Calcium-dependent calmodulin binding; This domain is found at the N-terminus of centriolar ...
 54-131 1.69e-22

Calcium-dependent calmodulin binding; This domain is found at the N-terminus of centriolar coiled-coil protein of 110 kDa (CCP110), where it binds calmodulin. Binding of calmodulin to this domain is calcium dependent.


Pssm-ID: 464981  Cd Length: 78  Bit Score: 92.01  E-value: 1.69e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622915247   54 QSESISLIRFHGVAILSPLLNVEKRREMQQEKQKALDVEARKQVNRKKTLLTRVQEILDNVQVRKAPNASDFDQWEME 131
Cdd:pfam16025    1 ESEFVSCIKINGVPILPPLMTDEKREEMQQYRQKAIAIEERLRKQRKAALLIRVQEILKNEQRRKLPTLEQTSTLDAE 78
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 663-729 9.70e-04

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 40.41  E-value: 9.70e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  663 SKESEELLKSKMLAFEEMRKRLEeqhAQQLSLLIAEQEREQERLQKEIEEQE---KMLKEKKAMTAEASE 729
Cdd:pfam00836   40 KDSSLEEIQKKLEAAEERRKSLE---AQKLKQLAEKREKEEEALQKADEENNnfsKMAEEKLKQKMEAYK 106
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 678-727 3.08e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 3.08e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  678 EEMRKRLEEQHAQQLSL-LIAEQER----EQERL-----QKEIEEQEKMLKEKKAMTAEA 727
Cdd:PRK09510    78 EEQRKKKEQQQAEELQQkQAAEQERlkqlEKERLaaqeqKKQAEEAAKQAALKQKQAEEA 137
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 664-833 3.28e-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: 40.90  E-value: 3.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  664 KESEELLKSKMLAFEEMRKRLEEQhAQQLSLLIAEQEREQERLQKEIEEQEKMLKE-KKAMTAEASELDinsavELEWRK 742
Cdd:COG4942    149 REQAEELRADLAELAALRAELEAE-RAELEALLAELEEERAALEALKAERQKLLARlEKELAELAAELA-----ELQQEA 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  743 ISDSSLLETmLSQADSLHTSNSNSSGFTNSALQYSFvsaneaPfylwgssTSGltklSVTRPFGRAKTrwSQVFSP--EI 820
Cdd:COG4942    223 EELEALIAR-LEAEAAAAAERTPAAGFAALKGKLPW------P-------VSG----RVVRRFGERDG--GGGRNKgiDI 282

                          170
                   ....*....|....
gi 1622915247  821 QAKFN-KITAVAKG 833
Cdd:COG4942    283 AAPPGaPVRAVADG 296
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 634-734 6.72e-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: 39.87  E-value: 6.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  634 TEQERQHLPEKRypKGSVFINKNKILGTSSKESEELLKSKMLAFEEMRKRLEEQHAQQLSLLIAEQEREQERLQKeieEQ 713
Cdd:cd16269    194 TEKEKEIEAERA--KAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLK---EQ 268

                           90       100
                   ....*....|....*....|.
gi 1622915247  714 EKMLKEKKAMTAEASELDINS 734
Cdd:cd16269    269 EALLEEGFKEQAELLQEEIRS 289
 
Name Accession Description Interval E-value
CaM_bind pfam16025
Calcium-dependent calmodulin binding; This domain is found at the N-terminus of centriolar ...
 54-131 1.69e-22

Calcium-dependent calmodulin binding; This domain is found at the N-terminus of centriolar coiled-coil protein of 110 kDa (CCP110), where it binds calmodulin. Binding of calmodulin to this domain is calcium dependent.


Pssm-ID: 464981  Cd Length: 78  Bit Score: 92.01  E-value: 1.69e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622915247   54 QSESISLIRFHGVAILSPLLNVEKRREMQQEKQKALDVEARKQVNRKKTLLTRVQEILDNVQVRKAPNASDFDQWEME 131
Cdd:pfam16025    1 ESEFVSCIKINGVPILPPLMTDEKREEMQQYRQKAIAIEERLRKQRKAALLIRVQEILKNEQRRKLPTLEQTSTLDAE 78
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 663-729 9.70e-04

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 40.41  E-value: 9.70e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  663 SKESEELLKSKMLAFEEMRKRLEeqhAQQLSLLIAEQEREQERLQKEIEEQE---KMLKEKKAMTAEASE 729
Cdd:pfam00836   40 KDSSLEEIQKKLEAAEERRKSLE---AQKLKQLAEKREKEEEALQKADEENNnfsKMAEEKLKQKMEAYK 106
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 678-727 3.08e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 3.08e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  678 EEMRKRLEEQHAQQLSL-LIAEQER----EQERL-----QKEIEEQEKMLKEKKAMTAEA 727
Cdd:PRK09510    78 EEQRKKKEQQQAEELQQkQAAEQERlkqlEKERLaaqeqKKQAEEAAKQAALKQKQAEEA 137
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 664-833 3.28e-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: 40.90  E-value: 3.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  664 KESEELLKSKMLAFEEMRKRLEEQhAQQLSLLIAEQEREQERLQKEIEEQEKMLKE-KKAMTAEASELDinsavELEWRK 742
Cdd:COG4942    149 REQAEELRADLAELAALRAELEAE-RAELEALLAELEEERAALEALKAERQKLLARlEKELAELAAELA-----ELQQEA 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  743 ISDSSLLETmLSQADSLHTSNSNSSGFTNSALQYSFvsaneaPfylwgssTSGltklSVTRPFGRAKTrwSQVFSP--EI 820
Cdd:COG4942    223 EELEALIAR-LEAEAAAAAERTPAAGFAALKGKLPW------P-------VSG----RVVRRFGERDG--GGGRNKgiDI 282

                          170
                   ....*....|....
gi 1622915247  821 QAKFN-KITAVAKG 833
Cdd:COG4942    283 AAPPGaPVRAVADG 296
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 655-733 5.68e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.96  E-value: 5.68e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622915247  655 KNKILGTSSKESEELLKSKMLAFEEMRKRLEEQHAQQLSLLIAEQEREQERLQKeieEQEKMLKEKKAMTAEASELDIN 733
Cdd:pfam02841  219 EQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQ---EQEELLKEGFKTEAESLQKEIQ 294
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 634-734 6.72e-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: 39.87  E-value: 6.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  634 TEQERQHLPEKRypKGSVFINKNKILGTSSKESEELLKSKMLAFEEMRKRLEEQHAQQLSLLIAEQEREQERLQKeieEQ 713
Cdd:cd16269    194 TEKEKEIEAERA--KAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLK---EQ 268

                           90       100
                   ....*....|....*....|.
gi 1622915247  714 EKMLKEKKAMTAEASELDINS 734
Cdd:cd16269    269 EALLEEGFKEQAELLQEEIRS 289
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 668-795 7.35e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 7.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915247  668 ELLKSKMLAFEEMRKRLEEQhAQQLSLLIAEQEREQERLQKEIEEQEKML----KEKKAMTAEASELDINSAVELEWRKI 743
Cdd:COG3883    136 EELKADKAELEAKKAELEAK-LAELEALKAELEAAKAELEAQQAEQEALLaqlsAEEAAAEAQLAELEAELAAAEAAAAA 214

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622915247  744 SDSSLLETMLSQADSLHTSNSNSSGFTNSALQYSFVSANEAPFYLWGSSTSG 795
Cdd:COG3883    215 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAG 266
 
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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