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Conserved domains on  [gi|1199276954|ref|NP_001338765|]
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serine-protein kinase ATM isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TAN super family cl13144
Telomere-length maintenance and DNA damage repair; ATM is a large protein kinase, in humans, ...
8-110 2.21e-11

Telomere-length maintenance and DNA damage repair; ATM is a large protein kinase, in humans, critical for responding to DNA double-strand breaks (DSBs). Tel1, the orthologue from budding yeast, also regulates responses to DSBs. Tel1 is important for maintaining viability and for phosphorylation of the DNA damage signal transducer kinase Rad53 (an orthologue of mammalian CHK2). In addition to functioning in the response to DSBs, numerous findings indicate that Tel1/ATM regulates telomeres. The overall domain structure of Tel1/ATM is shared by proteins of the phosphatidylinositol 3-kinase (PI3K)-related kinase (PIKK) family, but this family carries a unique and functionally important TAN sequence motif, near its N-terminal, LxxxKxxE/DRxxxL. which is conserved specifically in the Tel1/ATM subclass of the PIKKs. The TAN motif is essential for both telomere length maintenance and Tel1 action in response to DNA damage. It is classified as an EC:2.7.11.1.


The actual alignment was detected with superfamily member pfam11640:

Pssm-ID: 431973  Cd Length: 150  Bit Score: 56.56  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276954   8 LLICCRQLEHDRATERKKEVEKFKRLIRDPetikhldRHSDSKQGKYLNWDAVFRFLQKYIQKETECLRIAKPNVSASTQ 87
Cdd:pfam11640   1 LLEILSLLSSSKIKERNDALEDLKHILSSN-------RNKSLSALNDKAWHSIFEALFRLIEAEKSAYLKAKKSSTTKSA 73
                          90       100
                  ....*....|....*....|...
gi 1199276954  88 AsrQKKMQEISSLVKYFIKCANR 110
Cdd:pfam11640  74 A--ARRLSSAASALRLVVEKAVS 94
 
Name Accession Description Interval E-value
TAN pfam11640
Telomere-length maintenance and DNA damage repair; ATM is a large protein kinase, in humans, ...
8-110 2.21e-11

Telomere-length maintenance and DNA damage repair; ATM is a large protein kinase, in humans, critical for responding to DNA double-strand breaks (DSBs). Tel1, the orthologue from budding yeast, also regulates responses to DSBs. Tel1 is important for maintaining viability and for phosphorylation of the DNA damage signal transducer kinase Rad53 (an orthologue of mammalian CHK2). In addition to functioning in the response to DSBs, numerous findings indicate that Tel1/ATM regulates telomeres. The overall domain structure of Tel1/ATM is shared by proteins of the phosphatidylinositol 3-kinase (PI3K)-related kinase (PIKK) family, but this family carries a unique and functionally important TAN sequence motif, near its N-terminal, LxxxKxxE/DRxxxL. which is conserved specifically in the Tel1/ATM subclass of the PIKKs. The TAN motif is essential for both telomere length maintenance and Tel1 action in response to DNA damage. It is classified as an EC:2.7.11.1.


Pssm-ID: 431973  Cd Length: 150  Bit Score: 56.56  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276954   8 LLICCRQLEHDRATERKKEVEKFKRLIRDPetikhldRHSDSKQGKYLNWDAVFRFLQKYIQKETECLRIAKPNVSASTQ 87
Cdd:pfam11640   1 LLEILSLLSSSKIKERNDALEDLKHILSSN-------RNKSLSALNDKAWHSIFEALFRLIEAEKSAYLKAKKSSTTKSA 73
                          90       100
                  ....*....|....*....|...
gi 1199276954  88 AsrQKKMQEISSLVKYFIKCANR 110
Cdd:pfam11640  74 A--ARRLSSAASALRLVVEKAVS 94
 
Name Accession Description Interval E-value
TAN pfam11640
Telomere-length maintenance and DNA damage repair; ATM is a large protein kinase, in humans, ...
8-110 2.21e-11

Telomere-length maintenance and DNA damage repair; ATM is a large protein kinase, in humans, critical for responding to DNA double-strand breaks (DSBs). Tel1, the orthologue from budding yeast, also regulates responses to DSBs. Tel1 is important for maintaining viability and for phosphorylation of the DNA damage signal transducer kinase Rad53 (an orthologue of mammalian CHK2). In addition to functioning in the response to DSBs, numerous findings indicate that Tel1/ATM regulates telomeres. The overall domain structure of Tel1/ATM is shared by proteins of the phosphatidylinositol 3-kinase (PI3K)-related kinase (PIKK) family, but this family carries a unique and functionally important TAN sequence motif, near its N-terminal, LxxxKxxE/DRxxxL. which is conserved specifically in the Tel1/ATM subclass of the PIKKs. The TAN motif is essential for both telomere length maintenance and Tel1 action in response to DNA damage. It is classified as an EC:2.7.11.1.


Pssm-ID: 431973  Cd Length: 150  Bit Score: 56.56  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199276954   8 LLICCRQLEHDRATERKKEVEKFKRLIRDPetikhldRHSDSKQGKYLNWDAVFRFLQKYIQKETECLRIAKPNVSASTQ 87
Cdd:pfam11640   1 LLEILSLLSSSKIKERNDALEDLKHILSSN-------RNKSLSALNDKAWHSIFEALFRLIEAEKSAYLKAKKSSTTKSA 73
                          90       100
                  ....*....|....*....|...
gi 1199276954  88 AsrQKKMQEISSLVKYFIKCANR 110
Cdd:pfam11640  74 A--ARRLSSAASALRLVVEKAVS 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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