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Conserved domains on  [gi|1720416693|ref|XP_030110943|]
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pleckstrin homology domain-containing family A member 5 isoform X37 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
15-44 4.66e-12

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13248:

Pssm-ID: 450165  Cd Length: 104  Bit Score: 63.06  E-value: 4.66e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720416693  15 AAHPNMRTYYFCTDTGKEMELWMKAMLDAA 44
Cdd:cd13248    75 AEHANMRTYYFAADTAEEMEQWMNAMSLAA 104
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
408-537 8.45e-03

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.08  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416693  408 EAGIDAKLSRLCEQDKVVRALEEKLQQLHKEKYTLEQALLSASQEIEMNADNPAAIQTVVLQRDDLQNGLLSTCRELSRA 487
Cdd:COG1196    382 REELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDR 461
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720416693  488 TAELERAWREYDKLEYDVTVTRDQMQGQLDRLGEVQSESAGIQRAQIQKE 537
Cdd:COG1196    462 LKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALE 511
 
Name Accession Description Interval E-value
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
15-44 4.66e-12

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. 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: 270068  Cd Length: 104  Bit Score: 63.06  E-value: 4.66e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720416693  15 AAHPNMRTYYFCTDTGKEMELWMKAMLDAA 44
Cdd:cd13248    75 AEHANMRTYYFAADTAEEMEQWMNAMSLAA 104
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
408-537 8.45e-03

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.08  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416693  408 EAGIDAKLSRLCEQDKVVRALEEKLQQLHKEKYTLEQALLSASQEIEMNADNPAAIQTVVLQRDDLQNGLLSTCRELSRA 487
Cdd:COG1196    382 REELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDR 461
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720416693  488 TAELERAWREYDKLEYDVTVTRDQMQGQLDRLGEVQSESAGIQRAQIQKE 537
Cdd:COG1196    462 LKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALE 511
 
Name Accession Description Interval E-value
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
15-44 4.66e-12

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. 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: 270068  Cd Length: 104  Bit Score: 63.06  E-value: 4.66e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720416693  15 AAHPNMRTYYFCTDTGKEMELWMKAMLDAA 44
Cdd:cd13248    75 AEHANMRTYYFAADTAEEMEQWMNAMSLAA 104
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
17-40 2.72e-03

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: 37.91  E-value: 2.72e-03
                          10        20
                  ....*....|....*....|....
gi 1720416693  17 HPNMRTYYFCTDTGKEMELWMKAM 40
Cdd:cd00821    69 TPDGRTYYLQADSEEERQEWLKAL 92
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
408-537 8.45e-03

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 40.08  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416693  408 EAGIDAKLSRLCEQDKVVRALEEKLQQLHKEKYTLEQALLSASQEIEMNADNPAAIQTVVLQRDDLQNGLLSTCRELSRA 487
Cdd:COG1196    382 REELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDR 461
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720416693  488 TAELERAWREYDKLEYDVTVTRDQMQGQLDRLGEVQSESAGIQRAQIQKE 537
Cdd:COG1196    462 LKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALE 511
 
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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