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Conserved domains on  [gi|1907170022|ref|XP_036021635|]
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pleckstrin homology domain-containing family A member 5 isoform X38 [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 4.65e-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: 4.65e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907170022  15 AAHPNMRTYYFCTDTGKEMELWMKAMLDAA 44
Cdd:cd13248    75 AEHANMRTYYFAADTAEEMEQWMNAMSLAA 104
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
411-576 2.25e-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: 41.62  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170022  411 IDAKLSRLCEQDKVVRALEEKLQQLHKEKYTLEQALLSASQEIE-MNADNPAAIQTVVLQRDDLQNGLLSTCRELSRATA 489
Cdd:COG1196    332 IEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEeLFEALREELAELEAELAEIRNELEELKREIESLEE 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170022  490 ELERAWREYDKLEYDVTVTRDQMQGQLDRLGEVQSESAGIQRA-----QIQKELWR--------IQDVMEGLSKHKQQRG 556
Cdd:COG1196    412 RLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQleelrDRLKELERelaelqeeLQRLEKELSSLEARLD 491
                          170       180
                   ....*....|....*....|
gi 1907170022  557 SSETGLAGSKPFSSVKYKSE 576
Cdd:COG1196    492 RLEAEQRASQGVRAVLEALE 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 4.65e-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: 4.65e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907170022  15 AAHPNMRTYYFCTDTGKEMELWMKAMLDAA 44
Cdd:cd13248    75 AEHANMRTYYFAADTAEEMEQWMNAMSLAA 104
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
411-576 2.25e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.62  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170022  411 IDAKLSRLCEQDKVVRALEEKLQQLHKEKYTLEQALLSASQEIE-MNADNPAAIQTVVLQRDDLQNGLLSTCRELSRATA 489
Cdd:COG1196    332 IEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEeLFEALREELAELEAELAEIRNELEELKREIESLEE 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170022  490 ELERAWREYDKLEYDVTVTRDQMQGQLDRLGEVQSESAGIQRA-----QIQKELWR--------IQDVMEGLSKHKQQRG 556
Cdd:COG1196    412 RLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQleelrDRLKELERelaelqeeLQRLEKELSSLEARLD 491
                          170       180
                   ....*....|....*....|
gi 1907170022  557 SSETGLAGSKPFSSVKYKSE 576
Cdd:COG1196    492 RLEAEQRASQGVRAVLEALE 511
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
403-605 9.33e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 9.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170022  403 KYRPEEAGIDAKLSRLCEQDKVVRALEEKLQQLHKEKY-------TLEQALLSASQEIEMNADNPAAIQTvvlQRDDLQN 475
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYalaneisRLEQQKQILRERLANLERQLEELEA---QLEELES 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170022  476 GLLSTCRELSRATAELERAWREYDKLEYDVTVTRDQMQGQLDRLGEVQ-------SESAGI--QRAQIQKELWRIQDVME 546
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqletlrSKVAQLelQIASLNNEIERLEARLE 410
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907170022  547 GLsKHKQQRGSSETGLAGSKPFSSVKYKSEGpdyRLYKSEPELTTVAEVDESNGEEKSE 605
Cdd:TIGR02168  411 RL-EDRRERLQQEIEELLKKLEEAELKELQA---ELEELEEELEELQEELERLEEALEE 465
 
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 4.65e-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: 4.65e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907170022  15 AAHPNMRTYYFCTDTGKEMELWMKAMLDAA 44
Cdd:cd13248    75 AEHANMRTYYFAADTAEEMEQWMNAMSLAA 104
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
411-576 2.25e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.62  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170022  411 IDAKLSRLCEQDKVVRALEEKLQQLHKEKYTLEQALLSASQEIE-MNADNPAAIQTVVLQRDDLQNGLLSTCRELSRATA 489
Cdd:COG1196    332 IEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEeLFEALREELAELEAELAEIRNELEELKREIESLEE 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170022  490 ELERAWREYDKLEYDVTVTRDQMQGQLDRLGEVQSESAGIQRA-----QIQKELWR--------IQDVMEGLSKHKQQRG 556
Cdd:COG1196    412 RLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQleelrDRLKELERelaelqeeLQRLEKELSSLEARLD 491
                          170       180
                   ....*....|....*....|
gi 1907170022  557 SSETGLAGSKPFSSVKYKSE 576
Cdd:COG1196    492 RLEAEQRASQGVRAVLEALE 511
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 1907170022  17 HPNMRTYYFCTDTGKEMELWMKAM 40
Cdd:cd00821    69 TPDGRTYYLQADSEEERQEWLKAL 92
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
408-537 8.44e-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: 8.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170022  408 EAGIDAKLSRLCEQDKVVRALEEKLQQLHKEKYTLEQALLSASQEIEMNADNPAAIQTVVLQRDDLQNGLLSTCRELSRA 487
Cdd:COG1196    382 REELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDR 461
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907170022  488 TAELERAWREYDKLEYDVTVTRDQMQGQLDRLGEVQSESAGIQRAQIQKE 537
Cdd:COG1196    462 LKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALE 511
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
403-605 9.33e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 9.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170022  403 KYRPEEAGIDAKLSRLCEQDKVVRALEEKLQQLHKEKY-------TLEQALLSASQEIEMNADNPAAIQTvvlQRDDLQN 475
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYalaneisRLEQQKQILRERLANLERQLEELEA---QLEELES 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170022  476 GLLSTCRELSRATAELERAWREYDKLEYDVTVTRDQMQGQLDRLGEVQ-------SESAGI--QRAQIQKELWRIQDVME 546
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqletlrSKVAQLelQIASLNNEIERLEARLE 410
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907170022  547 GLsKHKQQRGSSETGLAGSKPFSSVKYKSEGpdyRLYKSEPELTTVAEVDESNGEEKSE 605
Cdd:TIGR02168  411 RL-EDRRERLQQEIEELLKKLEEAELKELQA---ELEELEEELEELQEELERLEEALEE 465
 
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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