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Conserved domains on  [gi|226442929|ref|NP_033370|]
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pleckstrin homology-like domain family A member 1 [Mus musculus]

Protein Classification

PH domain-containing protein( domain architecture ID 10643714)

Pleckstrin homology (PH) domain-containing protein similar to Schizosaccharomyces pombe anillin-related medial ring protein mid1 and meiotically up-regulated gene 79 protein

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  15493994|22728242
SCOP:  3000134

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 154-261 2.48e-03

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


:

Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 37.14  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442929   154 LKEGVLEKRSDGLLQLWKKKCCILTEEGLLLIPPKQLQQQqqqqqpgqgtaepsqpsgptvASLEPPVKLKELHFSnmKT 233
Cdd:smart00233   2 IKEGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKS---------------------YKPKGSIDLSGCTVR--EA 58

                           90       100
                   ....*....|....*....|....*...
gi 226442929   234 VDCVERKGKYMyFTVVMTEGKEIDFRCP 261
Cdd:smart00233  59 PDPDSSKKPHC-FEIKTSDRKTLLLQAE 85
 
Name Accession Description Interval E-value
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 154-261 2.48e-03

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 37.14  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442929   154 LKEGVLEKRSDGLLQLWKKKCCILTEEGLLLIPPKQLQQQqqqqqpgqgtaepsqpsgptvASLEPPVKLKELHFSnmKT 233
Cdd:smart00233   2 IKEGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKS---------------------YKPKGSIDLSGCTVR--EA 58

                           90       100
                   ....*....|....*....|....*...
gi 226442929   234 VDCVERKGKYMyFTVVMTEGKEIDFRCP 261
Cdd:smart00233  59 PDPDSSKKPHC-FEIKTSDRKTLLLQAE 85
 
Name Accession Description Interval E-value
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 154-261 2.48e-03

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 37.14  E-value: 2.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226442929   154 LKEGVLEKRSDGLLQLWKKKCCILTEEGLLLIPPKQLQQQqqqqqpgqgtaepsqpsgptvASLEPPVKLKELHFSnmKT 233
Cdd:smart00233   2 IKEGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKS---------------------YKPKGSIDLSGCTVR--EA 58

                           90       100
                   ....*....|....*....|....*...
gi 226442929   234 VDCVERKGKYMyFTVVMTEGKEIDFRCP 261
Cdd:smart00233  59 PDPDSSKKPHC-FEIKTSDRKTLLLQAE 85
 
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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