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Conserved domains on  [gi|242015490|ref|XP_002428386|]
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guanine nucleotide releasing protein X, putative [Pediculus humanus corporis]

Protein Classification

pleckstrin homology domain-containing family J member 1( domain architecture ID 10192634)

pleckstrin homology domain-containing family J member 1 (PLEKHJ1) may interact with IKBKG (inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma) and KRT33B (keratin 33B)

CATH:  2.30.29.30
Gene Ontology:  GO:0005515|GO:0042147
PubMed:  22728242|17233582|15766521
SCOP:  4002395

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_PLEKHJ1 cd13258
Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; ...
 1-133 3.17e-60

Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; PLEKHJ1 (also called GNRPX2/Guanine nucleotide-releasing protein x ). It contains a single PH domain. Very little information is known about PLEKHJ1. PLEKHJ1 has been shown to interact with IKBKG (inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma) and KRT33B (keratin 33B). 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: 270078  Cd Length: 123  Bit Score: 185.22  E-value: 3.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242015490   1 MKFNIKELADLSFGKATIEGRlhhkkinsSHSNSGENLTVMLVFKEKWFKLRANILFYFNLSETGqiNNNKPVGAYILEN 80
Cdd:cd13258    1 MRFNEKELAALSSQPAEKEGK--------IAERQMGGPKKSEVFKERWFKLKGNLLFYFRTNEFG--DCSEPIGAIVLEN 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242015490  81 TIVQFEMNSEAPFSFSLYFNDEVEKKHLFSGRSQDNIDKWIEALKEASYEYWR 133
Cdd:cd13258   71 CRVQMEEITEKPFAFSIVFNDEPEKKYIFSCRSEEQCEQWIEALRQASYEYLR 123
 
Name Accession Description Interval E-value
PH_PLEKHJ1 cd13258
Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; ...
 1-133 3.17e-60

Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; PLEKHJ1 (also called GNRPX2/Guanine nucleotide-releasing protein x ). It contains a single PH domain. Very little information is known about PLEKHJ1. PLEKHJ1 has been shown to interact with IKBKG (inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma) and KRT33B (keratin 33B). 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: 270078  Cd Length: 123  Bit Score: 185.22  E-value: 3.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242015490   1 MKFNIKELADLSFGKATIEGRlhhkkinsSHSNSGENLTVMLVFKEKWFKLRANILFYFNLSETGqiNNNKPVGAYILEN 80
Cdd:cd13258    1 MRFNEKELAALSSQPAEKEGK--------IAERQMGGPKKSEVFKERWFKLKGNLLFYFRTNEFG--DCSEPIGAIVLEN 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242015490  81 TIVQFEMNSEAPFSFSLYFNDEVEKKHLFSGRSQDNIDKWIEALKEASYEYWR 133
Cdd:cd13258   71 CRVQMEEITEKPFAFSIVFNDEPEKKYIFSCRSEEQCEQWIEALRQASYEYLR 123
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 17-129 5.36e-06

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: 44.08  E-value: 5.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242015490    17 TIEGRLHHKKINSSHSnsgenltvmlvFKEKWFKLRANILFYFNLSETGQINnnKPVGAYILENTIVQ---FEMNSEAPF 93
Cdd:smart00233   2 IKEGWLYKKSGGGKKS-----------WKKRYFVLFNSTLLYYKSKKDKKSY--KPKGSIDLSGCTVReapDPDSSKKPH 68

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 242015490    94 SFSLYFNDEveKKHLFSGRSQDNIDKWIEALKEASY 129
Cdd:smart00233  69 CFEIKTSDR--KTLLLQAESEEEREKWVEALRKAIA 102
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 44-129 9.57e-05

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 40.62  E-value: 9.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242015490   44 FKEKWFKLRANILFYFNLSETGQinNNKPVGAYILENTIVQ---FEMNSEAPFSFSLYFNDEVEKK-HLFSGRSQDNIDK 119
Cdd:pfam00169  18 WKKRYFVLFDGSLLYYKDDKSGK--SKEPKGSISLSGCEVVevvASDSPKRKFCFELRTGERTGKRtYLLQAESEEERKD 95

                          90
                  ....*....|
gi 242015490  120 WIEALKEASY 129
Cdd:pfam00169  96 WIKAIQSAIR 105
 
Name Accession Description Interval E-value
PH_PLEKHJ1 cd13258
Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; ...
 1-133 3.17e-60

Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; PLEKHJ1 (also called GNRPX2/Guanine nucleotide-releasing protein x ). It contains a single PH domain. Very little information is known about PLEKHJ1. PLEKHJ1 has been shown to interact with IKBKG (inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma) and KRT33B (keratin 33B). 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: 270078  Cd Length: 123  Bit Score: 185.22  E-value: 3.17e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242015490   1 MKFNIKELADLSFGKATIEGRlhhkkinsSHSNSGENLTVMLVFKEKWFKLRANILFYFNLSETGqiNNNKPVGAYILEN 80
Cdd:cd13258    1 MRFNEKELAALSSQPAEKEGK--------IAERQMGGPKKSEVFKERWFKLKGNLLFYFRTNEFG--DCSEPIGAIVLEN 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242015490  81 TIVQFEMNSEAPFSFSLYFNDEVEKKHLFSGRSQDNIDKWIEALKEASYEYWR 133
Cdd:cd13258   71 CRVQMEEITEKPFAFSIVFNDEPEKKYIFSCRSEEQCEQWIEALRQASYEYLR 123
PH_Ses cd13288
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ...
 44-133 2.08e-13

Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single 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: 270105 [Multi-domain]  Cd Length: 120  Bit Score: 64.57  E-value: 2.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242015490  44 FKEKWFKLRANILFYFNLSEtgqinNNKPVGAYILENTIVQFeMNSEAPFSFSLYFNDEVEKKHLFSGRSQDNIDKWIEA 123
Cdd:cd13288   24 YQKRWFVLKGNLLFYFEKKG-----DREPLGVIVLEGCTVEL-AEDAEPYAFAIRFDGPGARSYVLAAENQEDMESWMKA 97

                         90
                 ....*....|
gi 242015490 124 LKEASYEYWR 133
Cdd:cd13288   98 LSRASYDYLR 107
PH_INPP4A_INPP4B cd13272
Type I inositol 3,4-bisphosphate 4-phosphatase and Type II inositol 3,4-bisphosphate ...
 1-133 8.90e-11

Type I inositol 3,4-bisphosphate 4-phosphatase and Type II inositol 3,4-bisphosphate 4-phosphatase Pleckstrin homology (PH) domain; INPP4A (also called Inositol polyphosphate 4-phosphatase type I) and INPP4B (also called Inositol polyphosphate 4-phosphatase type II) both catalyze the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate and inositol 1,3,4-trisphosphate. They differ in that INPP4A additionally catalyzes the hydrolysis of the 4-position phosphate of inositol 3,4-bisphosphate, while INPP4B catalyzes the hydrolysis of the 4-position phosphate of inositol 1,4-bisphosphate. They both have a single PH domain followed by a C2 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: 270091  Cd Length: 144  Bit Score: 58.18  E-value: 8.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242015490   1 MKFNIKELADL------SFGKatiEGRLHHK-KINSSHSNSGENLtvmlvfkEKWFKLRANILFYFN----LSEtgqinn 69
Cdd:cd13272    1 MRFNKQELATLasqpstKFDK---EGLLIITeRQEGFFRRSEGSL-------ERWCRLRGNLLFYLKskdpWSE------ 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242015490  70 nkPVGAYILEN--TIVQFEMNSEAPFSFSLYFNDEVEKKhlFSGRSQDNIDKWIEALKEASYEYWR 133
Cdd:cd13272   65 --PAGVIVLEQcrPRIQNDERDSGGYPFDLVFEDGLCQR--LATRTEAERLSWVQAIELASYEVIR 126
PH_RasGRF1_2 cd13261
Ras-specific guanine nucleotide-releasing factors 1 and 2 Pleckstrin homology (PH) domain; ...
 16-129 3.66e-08

Ras-specific guanine nucleotide-releasing factors 1 and 2 Pleckstrin homology (PH) domain; RasGRF1 (also called GRF1; CDC25Mm/Ras-specific nucleotide exchange factor CDC25; GNRP/Guanine nucleotide-releasing protein) and RasGRF2 (also called GRF2; Ras guanine nucleotide exchange factor 2) are a family of guanine nucleotide exchange factors (GEFs). They both promote the exchange of Ras-bound GDP by GTP, thereby regulating the RAS signaling pathway. RasGRF1 and RasGRF2 form homooligomers and heterooligomers. GRF1 has 3 isoforms and GRF2 has 2 isoforms. The longest isoforms of RasGRF1 and RasGRF2 contain the following domains: a Rho-GEF domain sandwiched between 2 PH domains, IQ domains, a REM (Ras exchanger motif) domain, and a Ras-GEF domainwhich gives them the capacity to activate both Ras and Rac GTPases in response to signals from a variety of neurotransmitter receptors. Their IQ domains allow them to act as calcium sensors to mediate the actions of NMDA-type and calcium-permeable AMPA-type glutamate receptors. GRF1 also mediates the action of dopamine receptors that signal through cAMP. GRF1 and GRF2 play strikingly different roles in regulating MAP kinase family members, neuronal synaptic plasticity, specific forms of learning and memory, and behavioral responses to psychoactive drugs. 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: 270081  Cd Length: 136  Bit Score: 50.89  E-value: 3.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242015490  16 ATIEGRLHHKkinSSHSNSgenltvmlvFKEKWFKLRANILFYFNlSETgqinNNKPVGAYILE----------NTIVQF 85
Cdd:cd13261    5 GTKRGYLSKK---TSDSGK---------WHERWFALYQNLLFYFE-NES----SSRPSGLYLLEgcycerlptpKGALKG 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 242015490  86 EMNSEAPFSFSLYFNDEVEKKHLFSGRSQDNIDKWIEALKEASY 129
Cdd:cd13261   68 KDHLEKQHYFTISFRHENQRQYELRAETESDCDEWVEAIKQASF 111
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 17-129 5.36e-06

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: 44.08  E-value: 5.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242015490    17 TIEGRLHHKKINSSHSnsgenltvmlvFKEKWFKLRANILFYFNLSETGQINnnKPVGAYILENTIVQ---FEMNSEAPF 93
Cdd:smart00233   2 IKEGWLYKKSGGGKKS-----------WKKRYFVLFNSTLLYYKSKKDKKSY--KPKGSIDLSGCTVReapDPDSSKKPH 68

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 242015490    94 SFSLYFNDEveKKHLFSGRSQDNIDKWIEALKEASY 129
Cdd:smart00233  69 CFEIKTSDR--KTLLLQAESEEEREKWVEALRKAIA 102
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 44-129 9.57e-05

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 40.62  E-value: 9.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242015490   44 FKEKWFKLRANILFYFNLSETGQinNNKPVGAYILENTIVQ---FEMNSEAPFSFSLYFNDEVEKK-HLFSGRSQDNIDK 119
Cdd:pfam00169  18 WKKRYFVLFDGSLLYYKDDKSGK--SKEPKGSISLSGCEVVevvASDSPKRKFCFELRTGERTGKRtYLLQAESEEERKD 95

                          90
                  ....*....|
gi 242015490  120 WIEALKEASY 129
Cdd:pfam00169  96 WIKAIQSAIR 105
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 44-124 6.61e-04

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: 6.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242015490  44 FKEKWFKLRANILFYFnlsETGQINNNKPVGAYILENTI-VQFEMNSEAPFSFSLYFNDevEKKHLFSGRSQDNIDKWIE 122
Cdd:cd00821   16 WKKRWFVLFEGVLLYY---KSKKDSSYKPKGSIPLSGILeVEEVSPKERPHCFELVTPD--GRTYYLQADSEEERQEWLK 90


                 ..
gi 242015490 123 AL 124
Cdd:cd00821   91 AL 92
 
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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