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Conserved domains on  [gi|15241860|ref|NP_201056|]
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end binding protein 1B [Arabidopsis thaliana]

Protein Classification

RP/EB family microtubule-associated protein( domain architecture ID 1000504)

RP/EB family microtubule-associated protein may play important roles in microtubule dynamic regulation, cytokinesis, mitotic spindle positioning, and episome segregation

Gene Ontology:  GO:0008017|GO:0051301
PubMed:  10188731

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 ...
 8-225 1.33e-36

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: 133.20  E-value: 1.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241860   8 MDSAYFVGRNEILSWINDRLHLNLSRIEEAASGAVQCQMLDMTFpGVVPMHKVNFEAKNEYEMIQNYKVMQEVFTKLKIT 87
Cdd:COG5217   1 CDKALVESREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGID 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241860  88 KPLEVNRLVKGRPLDNLEFLQWLKRFCDSINGGIMNE------NYNPVERRSRGGREKSVKGSSKISKSLQTNNMHHPPV 161
Cdd:COG5217  80 KAVLVLVLVRCKLQDNLEFLQWLKDHWVRNLGHISYDrnarrlGRTPKSTRELIEWIRSLGIPISAIRELSKGVASCKSL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15241860 162 ATSNKPAGPKQAKSHGIGGG--SNSSAEVQ---ALSKEVEDLKVSVDLLEKERDFYFSKLRDIEILCQT 225
Cdd:COG5217 160 STIHSSFPQNFVKNTAGTHDylRAMQACQEfigSLNIKLYFPVDTLVKLEMERAFYFNKLRSIEILVET 228
 
Name Accession Description Interval E-value
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 8-225 1.33e-36

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


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 133.20  E-value: 1.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241860   8 MDSAYFVGRNEILSWINDRLHLNLSRIEEAASGAVQCQMLDMTFpGVVPMHKVNFEAKNEYEMIQNYKVMQEVFTKLKIT 87
Cdd:COG5217   1 CDKALVESREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGID 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241860  88 KPLEVNRLVKGRPLDNLEFLQWLKRFCDSINGGIMNE------NYNPVERRSRGGREKSVKGSSKISKSLQTNNMHHPPV 161
Cdd:COG5217  80 KAVLVLVLVRCKLQDNLEFLQWLKDHWVRNLGHISYDrnarrlGRTPKSTRELIEWIRSLGIPISAIRELSKGVASCKSL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15241860 162 ATSNKPAGPKQAKSHGIGGG--SNSSAEVQ---ALSKEVEDLKVSVDLLEKERDFYFSKLRDIEILCQT 225
Cdd:COG5217 160 STIHSSFPQNFVKNTAGTHDylRAMQACQEfigSLNIKLYFPVDTLVKLEMERAFYFNKLRSIEILVET 228
EB1 pfam03271
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ...
 205-243 9.40e-17

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: 72.16  E-value: 9.40e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 15241860   205 LEKERDFYFSKLRDIEILCQTPELD--DLPIVVAVKKILYA 243
Cdd:pfam03271   1 LEKERDFYFNKLRDIEILCQEEEEDeeEDPLIKKIQDILYA 41
 
Name Accession Description Interval E-value
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 8-225 1.33e-36

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


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 133.20  E-value: 1.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241860   8 MDSAYFVGRNEILSWINDRLHLNLSRIEEAASGAVQCQMLDMTFpGVVPMHKVNFEAKNEYEMIQNYKVMQEVFTKLKIT 87
Cdd:COG5217   1 CDKALVESREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGID 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241860  88 KPLEVNRLVKGRPLDNLEFLQWLKRFCDSINGGIMNE------NYNPVERRSRGGREKSVKGSSKISKSLQTNNMHHPPV 161
Cdd:COG5217  80 KAVLVLVLVRCKLQDNLEFLQWLKDHWVRNLGHISYDrnarrlGRTPKSTRELIEWIRSLGIPISAIRELSKGVASCKSL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15241860 162 ATSNKPAGPKQAKSHGIGGG--SNSSAEVQ---ALSKEVEDLKVSVDLLEKERDFYFSKLRDIEILCQT 225
Cdd:COG5217 160 STIHSSFPQNFVKNTAGTHDylRAMQACQEfigSLNIKLYFPVDTLVKLEMERAFYFNKLRSIEILVET 228
EB1 pfam03271
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ...
 205-243 9.40e-17

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: 72.16  E-value: 9.40e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 15241860   205 LEKERDFYFSKLRDIEILCQTPELD--DLPIVVAVKKILYA 243
Cdd:pfam03271   1 LEKERDFYFNKLRDIEILCQEEEEDeeEDPLIKKIQDILYA 41
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 16-107 4.53e-06

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: 44.59  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241860    16 RNEILSWINDRLHLNLSRIEEA------ASGAVQCQMLDMTFPGVVPMHKVNfeaKNEYEMIQNYK-VMQEVFTKLKITK 88
Cdd:pfam00307   4 EKELLRWINSHLAEYGPGVRVTnfttdlRDGLALCALLNKLAPGLVDKKKLN---KSEFDKLENINlALDVAEKKLGVPK 80

                          90       100
                  ....*....|....*....|
gi 15241860    89 PL-EVNRLVKGRPLDNLEFL 107
Cdd:pfam00307  81 VLiEPEDLVEGDNKSVLTYL 100
 
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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