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Conserved domains on  [gi|1919270868|ref|NP_001375281|]
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ensconsin isoform 21 [Homo sapiens]

Protein Classification

MAP7 domain-containing protein( domain architecture ID 12064852)

MAP7 domain-containing protein such as MAP7D1 (microtubule-associated protein 7 domain containing 1) identified as a novel substrate of doublecortin-like kinase 1 (DCLK1)

Gene Ontology:  GO:0005737

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 240-389 2.90e-21

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


:

Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 90.10  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270868 240 KTSAGTTDPEEATRLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQ 319
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1919270868 320 RQAEERALREREEAERAQRQK---EEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATD 389
Cdd:pfam05672  81 AEEEAEEREQREQEEQERLQKqkeEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIMKRTRKSDQAE 153
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 240-389 2.90e-21

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 90.10  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270868 240 KTSAGTTDPEEATRLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQ 319
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1919270868 320 RQAEERALREREEAERAQRQK---EEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATD 389
Cdd:pfam05672  81 AEEEAEEREQREQEEQERLQKqkeEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIMKRTRKSDQAE 153
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 240-389 2.90e-21

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 90.10  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919270868 240 KTSAGTTDPEEATRLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQ 319
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1919270868 320 RQAEERALREREEAERAQRQK---EEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATD 389
Cdd:pfam05672  81 AEEEAEEREQREQEEQERLQKqkeEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIMKRTRKSDQAE 153
 
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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