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Conserved domains on  [gi|221330411|ref|NP_611384|]
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uncharacterized protein Dmel_CG18190 [Drosophila melanogaster]

Protein Classification

CH and EB1 domain-containing protein( domain architecture ID 13422870)

CH and EB1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BIM1 super family cl34944
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 19-124 9.31e-20

Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton];


The actual alignment was detected with superfamily member COG5217:

Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 86.59  E-value: 9.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330411  19 SRHDMLQWVNNMVHGHFKKIEELCSGAAYCQMMEMIFPNcINLKRVKMTAKLEHEYLHNLRLFQEAFNRLKLDKTVPIDR 98
Cdd:COG5217    8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIYVD-LPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86

                         90       100
                 ....*....|....*....|....*.
gi 221330411  99 LIKGRFQDNFEFLQWFKKFFDSQAPG 124
Cdd:COG5217   87 LVRCKLQDNLEFLQWLKDHWVRNLGH 112
EB1 pfam03271
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ...
 184-216 6.92e-06

EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related to the EB1 protein. The EB1 proteins contain an N-terminal CH domain pfam00307. The human EB1 protein was originally discovered as a protein interacting with the C-terminus of the APC protein. This interaction is often disrupted in colon cancer, due to deletions affecting the APC C-terminus. Several EB1 orthologues are also included in this family. The interaction between EB1 and APC has been shown to have a potent synergistic effect on microtubule polymerization. Neither of EB1 or APC alone has this effect. It is thought that EB1 targets APC to the + ends of microtubules, where APC promotes microtubule polymerization. This process is regulated by APC phosphorylation by Cdc2, which disrupts APC-EB1 binding. Human EB1 protein can functionally substitute for the yeast EB1 homolog Mal3. In addition, Mal3 can substitute for human EB1 in promoting microtubule polymerization with APC.


:

Pssm-ID: 460870  Cd Length: 41  Bit Score: 42.11  E-value: 6.92e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 221330411  184 YNKLRLVEDLVNDMINNNQLVELCKRIQAVLYK 216
Cdd:pfam03271   9 FNKLRDIEILCQEEEEDEEEDPLIKKIQDILYA 41
 
Name Accession Description Interval E-value
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 19-124 9.31e-20

Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton];


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 86.59  E-value: 9.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330411  19 SRHDMLQWVNNMVHGHFKKIEELCSGAAYCQMMEMIFPNcINLKRVKMTAKLEHEYLHNLRLFQEAFNRLKLDKTVPIDR 98
Cdd:COG5217    8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIYVD-LPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86

                         90       100
                 ....*....|....*....|....*.
gi 221330411  99 LIKGRFQDNFEFLQWFKKFFDSQAPG 124
Cdd:COG5217   87 LVRCKLQDNLEFLQWLKDHWVRNLGH 112
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 17-118 8.75e-10

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 54.60  E-value: 8.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330411   17 NMSRHDMLQWVNNMVHGHFKKI------EELCSGAAYCQMMEMIFPNCINLKRVKMTaklEHEYLHNLRLF-QEAFNRLK 89
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVrvtnftTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLAlDVAEKKLG 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 221330411   90 LDKTV--PIDrLIKGrfqDNFEFLQWFKKFF 118
Cdd:pfam00307  78 VPKVLiePED-LVEG---DNKSVLTYLASLF 104
EB1 pfam03271
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ...
 184-216 6.92e-06

EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related to the EB1 protein. The EB1 proteins contain an N-terminal CH domain pfam00307. The human EB1 protein was originally discovered as a protein interacting with the C-terminus of the APC protein. This interaction is often disrupted in colon cancer, due to deletions affecting the APC C-terminus. Several EB1 orthologues are also included in this family. The interaction between EB1 and APC has been shown to have a potent synergistic effect on microtubule polymerization. Neither of EB1 or APC alone has this effect. It is thought that EB1 targets APC to the + ends of microtubules, where APC promotes microtubule polymerization. This process is regulated by APC phosphorylation by Cdc2, which disrupts APC-EB1 binding. Human EB1 protein can functionally substitute for the yeast EB1 homolog Mal3. In addition, Mal3 can substitute for human EB1 in promoting microtubule polymerization with APC.


Pssm-ID: 460870  Cd Length: 41  Bit Score: 42.11  E-value: 6.92e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 221330411  184 YNKLRLVEDLVNDMINNNQLVELCKRIQAVLYK 216
Cdd:pfam03271   9 FNKLRDIEILCQEEEEDEEEDPLIKKIQDILYA 41
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 20-94 7.62e-04

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 38.09  E-value: 7.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330411  20 RHDMLQWVNNMVHGHFKK-----IEELCSGAAYCQMMEMIFPNCInlKRVKMTAKLEHEYLHNLRLFQEAFNRLKLDKTV 94
Cdd:cd00014    1 EEELLKWINEVLGEELPVsitdlFESLRDGVLLCKLINKLSPGSI--PKINKKPKSPFKKRENINLFLNACKKLGLPELD 78
 
Name Accession Description Interval E-value
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 19-124 9.31e-20

Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton];


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 86.59  E-value: 9.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330411  19 SRHDMLQWVNNMVHGHFKKIEELCSGAAYCQMMEMIFPNcINLKRVKMTAKLEHEYLHNLRLFQEAFNRLKLDKTVPIDR 98
Cdd:COG5217    8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIYVD-LPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86

                         90       100
                 ....*....|....*....|....*.
gi 221330411  99 LIKGRFQDNFEFLQWFKKFFDSQAPG 124
Cdd:COG5217   87 LVRCKLQDNLEFLQWLKDHWVRNLGH 112
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 17-118 8.75e-10

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 54.60  E-value: 8.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330411   17 NMSRHDMLQWVNNMVHGHFKKI------EELCSGAAYCQMMEMIFPNCINLKRVKMTaklEHEYLHNLRLF-QEAFNRLK 89
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVrvtnftTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLAlDVAEKKLG 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 221330411   90 LDKTV--PIDrLIKGrfqDNFEFLQWFKKFF 118
Cdd:pfam00307  78 VPKVLiePED-LVEG---DNKSVLTYLASLF 104
EB1 pfam03271
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ...
 184-216 6.92e-06

EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related to the EB1 protein. The EB1 proteins contain an N-terminal CH domain pfam00307. The human EB1 protein was originally discovered as a protein interacting with the C-terminus of the APC protein. This interaction is often disrupted in colon cancer, due to deletions affecting the APC C-terminus. Several EB1 orthologues are also included in this family. The interaction between EB1 and APC has been shown to have a potent synergistic effect on microtubule polymerization. Neither of EB1 or APC alone has this effect. It is thought that EB1 targets APC to the + ends of microtubules, where APC promotes microtubule polymerization. This process is regulated by APC phosphorylation by Cdc2, which disrupts APC-EB1 binding. Human EB1 protein can functionally substitute for the yeast EB1 homolog Mal3. In addition, Mal3 can substitute for human EB1 in promoting microtubule polymerization with APC.


Pssm-ID: 460870  Cd Length: 41  Bit Score: 42.11  E-value: 6.92e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 221330411  184 YNKLRLVEDLVNDMINNNQLVELCKRIQAVLYK 216
Cdd:pfam03271   9 FNKLRDIEILCQEEEEDEEEDPLIKKIQDILYA 41
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 20-94 7.62e-04

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 38.09  E-value: 7.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221330411  20 RHDMLQWVNNMVHGHFKK-----IEELCSGAAYCQMMEMIFPNCInlKRVKMTAKLEHEYLHNLRLFQEAFNRLKLDKTV 94
Cdd:cd00014    1 EEELLKWINEVLGEELPVsitdlFESLRDGVLLCKLINKLSPGSI--PKINKKPKSPFKKRENINLFLNACKKLGLPELD 78
 
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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