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Conserved domains on  [gi|1039791837|ref|XP_017168555|]
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pleckstrin homology domain-containing family O member 2 isoform X1 [Mus musculus]

Protein Classification

PH domain-containing protein( domain architecture ID 106840)

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

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 ...
83-104 3.85e-07

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 cd13317:

Pssm-ID: 473070  Cd Length: 102  Bit Score: 48.28  E-value: 3.85e-07
                          10        20
                  ....*....|....*....|..
gi 1039791837  83 KVSDIKFQAPSGEEKESWIKAL 104
Cdd:cd13317    81 KAPDLKFQAVSPEEKESWINAL 102
PHA03247 super family cl33720
large tegument protein UL36; Provisional
138-399 2.56e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 2.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  138 GQRRRPPTRIHLKEVASAASDGLSRLDldvPDSGPPVFAPLSDISEDQPQEPPRALMPPVKPSPGPETSAvedsketPAG 217
Cdd:PHA03247  2658 PGRVSRPRRARRLGRAAQASSPPQRPR---RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPG-------PAA 2727
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  218 ERALTPDSASSGANPESQEDAETPAKeDSDVKSLPNSTLSEKLKVSWENPSPEKPSAPESAQLSSSETPEATPRE---SK 294
Cdd:PHA03247  2728 ARQASPALPAAPAPPAVPAGPATPGG-PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPwdpAD 2806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  295 KPPAPPPKILSEKMKACMSGVDASGSSQSSEAPETTSPEPTQVSVNGMDDGPESALQAMGIPGPAPEDAAASPALPFSDL 374
Cdd:PHA03247  2807 PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRL 2886
                          250       260
                   ....*....|....*....|....*
gi 1039791837  375 PSQFHPRSSSLGDLLRESPQHPRLP 399
Cdd:PHA03247  2887 ARPAVSRSTESFALPPDQPERPPQP 2911
 
Name Accession Description Interval E-value
PH_PLEKHO1_PLEKHO2 cd13317
Pleckstrin homology domain-containing family O Pleckstrin homology domain; The PLEKHO family ...
83-104 3.85e-07

Pleckstrin homology domain-containing family O Pleckstrin homology domain; The PLEKHO family members are PLEKHO1 (also called CKIP-1/Casein kinase 2-interacting protein 1/CK2-interacting protein 1) and PLEKHO2 (PLEKHQ1/PH domain-containing family Q member 1). They both contain a single PH domain. PLEKHO1 acts as a scaffold protein that functions in plasma membrane recruitment, transcriptional activity modulation, and posttranscriptional modification regulation. As an adaptor protein it is involved in signaling pathways, apoptosis, differentiation, cytoskeleton, and bone formation. Not much is know about PLEKHO2. 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: 270127  Cd Length: 102  Bit Score: 48.28  E-value: 3.85e-07
                          10        20
                  ....*....|....*....|..
gi 1039791837  83 KVSDIKFQAPSGEEKESWIKAL 104
Cdd:cd13317    81 KAPDLKFQAVSPEEKESWINAL 102
PHA03247 PHA03247
large tegument protein UL36; Provisional
138-399 2.56e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 2.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  138 GQRRRPPTRIHLKEVASAASDGLSRLDldvPDSGPPVFAPLSDISEDQPQEPPRALMPPVKPSPGPETSAvedsketPAG 217
Cdd:PHA03247  2658 PGRVSRPRRARRLGRAAQASSPPQRPR---RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPG-------PAA 2727
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  218 ERALTPDSASSGANPESQEDAETPAKeDSDVKSLPNSTLSEKLKVSWENPSPEKPSAPESAQLSSSETPEATPRE---SK 294
Cdd:PHA03247  2728 ARQASPALPAAPAPPAVPAGPATPGG-PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPwdpAD 2806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  295 KPPAPPPKILSEKMKACMSGVDASGSSQSSEAPETTSPEPTQVSVNGMDDGPESALQAMGIPGPAPEDAAASPALPFSDL 374
Cdd:PHA03247  2807 PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRL 2886
                          250       260
                   ....*....|....*....|....*
gi 1039791837  375 PSQFHPRSSSLGDLLRESPQHPRLP 399
Cdd:PHA03247  2887 ARPAVSRSTESFALPPDQPERPPQP 2911
 
Name Accession Description Interval E-value
PH_PLEKHO1_PLEKHO2 cd13317
Pleckstrin homology domain-containing family O Pleckstrin homology domain; The PLEKHO family ...
83-104 3.85e-07

Pleckstrin homology domain-containing family O Pleckstrin homology domain; The PLEKHO family members are PLEKHO1 (also called CKIP-1/Casein kinase 2-interacting protein 1/CK2-interacting protein 1) and PLEKHO2 (PLEKHQ1/PH domain-containing family Q member 1). They both contain a single PH domain. PLEKHO1 acts as a scaffold protein that functions in plasma membrane recruitment, transcriptional activity modulation, and posttranscriptional modification regulation. As an adaptor protein it is involved in signaling pathways, apoptosis, differentiation, cytoskeleton, and bone formation. Not much is know about PLEKHO2. 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: 270127  Cd Length: 102  Bit Score: 48.28  E-value: 3.85e-07
                          10        20
                  ....*....|....*....|..
gi 1039791837  83 KVSDIKFQAPSGEEKESWIKAL 104
Cdd:cd13317    81 KAPDLKFQAVSPEEKESWINAL 102
PHA03247 PHA03247
large tegument protein UL36; Provisional
138-399 2.56e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 2.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  138 GQRRRPPTRIHLKEVASAASDGLSRLDldvPDSGPPVFAPLSDISEDQPQEPPRALMPPVKPSPGPETSAvedsketPAG 217
Cdd:PHA03247  2658 PGRVSRPRRARRLGRAAQASSPPQRPR---RRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPG-------PAA 2727
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  218 ERALTPDSASSGANPESQEDAETPAKeDSDVKSLPNSTLSEKLKVSWENPSPEKPSAPESAQLSSSETPEATPRE---SK 294
Cdd:PHA03247  2728 ARQASPALPAAPAPPAVPAGPATPGG-PARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPwdpAD 2806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  295 KPPAPPPKILSEKMKACMSGVDASGSSQSSEAPETTSPEPTQVSVNGMDDGPESALQAMGIPGPAPEDAAASPALPFSDL 374
Cdd:PHA03247  2807 PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRL 2886
                          250       260
                   ....*....|....*....|....*
gi 1039791837  375 PSQFHPRSSSLGDLLRESPQHPRLP 399
Cdd:PHA03247  2887 ARPAVSRSTESFALPPDQPERPPQP 2911
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
135-367 3.33e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  135 VRGGQRRRPPTriHLKEVASAASDGLSRLDLDVPDSGPPVFAPLSDISEDQPQEPPRALMPPVKPSPG-PETSAVEDSKE 213
Cdd:PHA03307   145 GPPPAASPPAA--GASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSsPISASASSPAP 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  214 TPAGERALTPD-SASSGANPESQEDAETPAKEDSDVKSLPNSTLS-EKLKVSWENPSPEKPSAPESAQlSSSETPEATPR 291
Cdd:PHA03307   223 APGRSAADDAGaSSSDSSSSESSGCGWGPENECPLPRPAPITLPTrIWEASGWNGPSSRPGPASSSSS-PRERSPSPSPS 301
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039791837  292 ESKKPpapppkilsekmkACMSGVDASGSSQSSEAPETTSPEPTQVSVNGMDDGPESALQAMGIPGPAPEDAAASP 367
Cdd:PHA03307   302 SPGSG-------------PAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSS 364
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
166-289 2.38e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 40.29  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837 166 DVPDSGPPVFAPLSDISEDQPQEPPRA----------------LMPPVKPSPGPETSAVEDSKETPAGERALTPDSASSG 229
Cdd:PLN03209  337 DGPKPVPTKPVTPEAPSPPIEEEPPQPkavvprplspytayedLKPPTSPIPTPPSSSPASSKSVDAVAKPAEPDVVPSP 416
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837 230 ANPESQEDAETPAKEDSDVKSLPNSTLSEKLKvsweNPSPEKPSAPESAQLSSSETPEAT 289
Cdd:PLN03209  417 GSASNVPEVEPAQVEAKKTRPLSPYARYEDLK----PPTSPSPTAPTGVSPSVSSTSSVP 472
PHA03247 PHA03247
large tegument protein UL36; Provisional
137-377 5.30e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 5.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  137 GGQRRRPPTRIHLKEVASAASDGLSRLDLDVPDSGPPVFAplsdISEDQPQEPPRalmPPVKPSPGPETSAVEDSKETPA 216
Cdd:PHA03247  2860 GDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFA----LPPDQPERPPQ---PQAPPPPQPQPQPPPPPQPQPP 2932
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  217 GERALTPDS-ASSGANPESQEDAETPAKEDSDVKSLPNSTLSEKLKVSWENPSPEKPsAPESAQLSSSETPEATPRESKK 295
Cdd:PHA03247  2933 PPPPPRPQPpLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAP-ASSTPPLTGHSLSRVSSWASSL 3011
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039791837  296 PPAPPPKILSEKMKACMSGVDASGSSQSSEAPETTSPEPTQVSVNGMDDGPESALQAMGIPGPAPEDAAASPALPFSDLP 375
Cdd:PHA03247  3012 ALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGPPP 3091

                   ..
gi 1039791837  376 SQ 377
Cdd:PHA03247  3092 LS 3093
 
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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