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Conserved domains on  [gi|6912590|ref|NP_036528|]
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pleckstrin homology-like domain family A member 3 [Homo sapiens]

Protein Classification

PH domain-containing protein( domain architecture ID 10643714)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  22728242|17233582|15493994

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 ...
 9-88 4.42e-10

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: 52.94  E-value: 4.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912590       9 VLKEGVLEKRSGGLLQLWKRKRCVLTERGLQLFEAK--GTGGRPKE---LSFARIKAVECVESTGRHIYFTLVTEGGGEI 83
Cdd:smart00233   1 VIKEGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKSKkdKKSYKPKGsidLSGCTVREAPDPDSSKKPHCFEIKTSDRKTL 80


                   ....*
gi 6912590      84 DFRCP 88
Cdd:smart00233  81 LLQAE 85
 
Name Accession Description Interval E-value
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 9-88 4.42e-10

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: 52.94  E-value: 4.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912590       9 VLKEGVLEKRSGGLLQLWKRKRCVLTERGLQLFEAK--GTGGRPKE---LSFARIKAVECVESTGRHIYFTLVTEGGGEI 83
Cdd:smart00233   1 VIKEGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKSKkdKKSYKPKGsidLSGCTVREAPDPDSSKKPHCFEIKTSDRKTL 80


                   ....*
gi 6912590      84 DFRCP 88
Cdd:smart00233  81 LLQAE 85
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 9-88 4.11e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 45.25  E-value: 4.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912590      9 VLKEGVLEKRSGGLLQLWKRKRCVLTERGLQLFEAK--GTGGRPKE---LSFARIKAVECVESTGRHIYFTLVT---EGG 80
Cdd:pfam00169   1 VVKEGWLLKKGGGKKKSWKKRYFVLFDGSLLYYKDDksGKSKEPKGsisLSGCEVVEVVASDSPKRKFCFELRTgerTGK 80


                  ....*...
gi 6912590     81 GEIDFRCP 88
Cdd:pfam00169  81 RTYLLQAE 88
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 11-88 6.52e-07

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 44.46  E-value: 6.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912590   11 KEGVLEKRSGGLLQLWKRKRCVLTERGLQLFEAKGTGGRP--KELSFARIKAVECVESTGRHIYFTLVTEGGGEIDFRCP 88
Cdd:cd00821   1 KEGYLLKRGGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYKpkGSIPLSGILEVEEVSPKERPHCFELVTPDGRTYYLQAD 80
 
Name Accession Description Interval E-value
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 9-88 4.42e-10

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: 52.94  E-value: 4.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912590       9 VLKEGVLEKRSGGLLQLWKRKRCVLTERGLQLFEAK--GTGGRPKE---LSFARIKAVECVESTGRHIYFTLVTEGGGEI 83
Cdd:smart00233   1 VIKEGWLYKKSGGGKKSWKKRYFVLFNSTLLYYKSKkdKKSYKPKGsidLSGCTVREAPDPDSSKKPHCFEIKTSDRKTL 80


                   ....*
gi 6912590      84 DFRCP 88
Cdd:smart00233  81 LLQAE 85
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 9-88 4.11e-07

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 45.25  E-value: 4.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912590      9 VLKEGVLEKRSGGLLQLWKRKRCVLTERGLQLFEAK--GTGGRPKE---LSFARIKAVECVESTGRHIYFTLVT---EGG 80
Cdd:pfam00169   1 VVKEGWLLKKGGGKKKSWKKRYFVLFDGSLLYYKDDksGKSKEPKGsisLSGCEVVEVVASDSPKRKFCFELRTgerTGK 80


                  ....*...
gi 6912590     81 GEIDFRCP 88
Cdd:pfam00169  81 RTYLLQAE 88
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 11-88 6.52e-07

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 44.46  E-value: 6.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912590   11 KEGVLEKRSGGLLQLWKRKRCVLTERGLQLFEAKGTGGRP--KELSFARIKAVECVESTGRHIYFTLVTEGGGEIDFRCP 88
Cdd:cd00821   1 KEGYLLKRGGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYKpkGSIPLSGILEVEEVSPKERPHCFELVTPDGRTYYLQAD 80
 
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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