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Conserved domains on  [gi|237820624|ref|NP_001153656|]
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pleckstrin homology domain-containing family N member 1 isoform b [Homo sapiens]

Protein Classification

PH-like and PH_PLEKHN1 domain-containing protein( domain architecture ID 10351615)

PH-like and PH_PLEKHN1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_PLEKHN1 cd13323
Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain; Not ...
 228-348 1.88e-72

Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain; Not much is known about PLEKHN1. It is found in a wide range of animals including humans, green anole, frog, and zebrafish. It 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: 270132  Cd Length: 121  Bit Score: 227.36  E-value: 1.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624 228 HEPGGSAVCASRVKLQHLPAQEQWDRLLVLYPTSLAIFSEELDGLCFKGELPLRAVHINLEEKEKQIRSFLIEGPLINTI 307
Cdd:cd13323    1 RESLGSITCVSKVKLQHLPFQEQHDRLLVLYPSSLIILSEESDGLCFKGELPLNAIQVNFEENEKKIRSFLIEGRLINTI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 237820624 308 RVVCASYEDYGHWLLCLRAVTHREGAPPLPGAESFPGSQVM 348
Cdd:cd13323   81 RVSCLSYEDYQDWILCLKTAQVRNGDSSLPGSSSFYGSTQP 121
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 96-189 1.10e-17

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 cd01225:

Pssm-ID: 473070  Cd Length: 100  Bit Score: 78.51  E-value: 1.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624  96 VVHYAKVQLRFQHSQDVSDCYLELFPAHLYF--QAHGSEGLTFQGLLPLTELSVCPLEGSRE--HAFQITGPLPAPLLVL 171
Cdd:cd01225    1 VIHMSQVAVQNTGCQEKKERYFLLFPHVLLMlsASPRMSGFIYEGKLPLTGISVNRLEDTEGikNAFEISGPLIERIVVI 80

                         90
                 ....*....|....*...
gi 237820624 172 CPSRAELDRWLYHLEKQT 189
Cdd:cd01225   81 CNSQQDQQEWLEHLQQQT 98
PHA03378 super family cl33729
EBNA-3B; Provisional
 360-543 6.19e-03

EBNA-3B; Provisional


The actual alignment was detected with superfamily member PHA03378:

Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 6.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624 360 QTSW----DSGCLAPPSTRTShsLPESSVPSTVGCSSQHTPLHRLSLES---------SPDAPDHTSETSHSPLYAD--- 423
Cdd:PHA03378 594 QTPWpvphPSQTPEPPTTQSH--IPETSAPRQWPMPLRPIPMRPLRMQPitfnvlvfpTPHQPPQVEITPYKPTWTQigh 671

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624 424 -PYTPPATSHrrvTDVRGLEEFLSAMQS-ARGPTPSSP--LPSVPVSVPASDPRSCSSGPAGPYLLSKKGALQSRA---- 495
Cdd:PHA03378 672 iPYQPSPTGA---NTMLPIQWAPGTMQPpPRAPTPMRPpaAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRArppa 748

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 237820624 496 AQRHRGSAKDGGPQPPDAPQLVSSAREGSPEPWLPLTDGRSPRRSRDP 543
Cdd:PHA03378 749 AAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTP 796
 
Name Accession Description Interval E-value
PH_PLEKHN1 cd13323
Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain; Not ...
 228-348 1.88e-72

Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain; Not much is known about PLEKHN1. It is found in a wide range of animals including humans, green anole, frog, and zebrafish. It 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: 270132  Cd Length: 121  Bit Score: 227.36  E-value: 1.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624 228 HEPGGSAVCASRVKLQHLPAQEQWDRLLVLYPTSLAIFSEELDGLCFKGELPLRAVHINLEEKEKQIRSFLIEGPLINTI 307
Cdd:cd13323    1 RESLGSITCVSKVKLQHLPFQEQHDRLLVLYPSSLIILSEESDGLCFKGELPLNAIQVNFEENEKKIRSFLIEGRLINTI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 237820624 308 RVVCASYEDYGHWLLCLRAVTHREGAPPLPGAESFPGSQVM 348
Cdd:cd13323   81 RVSCLSYEDYQDWILCLKTAQVRNGDSSLPGSSSFYGSTQP 121
PH_Cool_Pix cd01225
Cloned out of library/PAK-interactive exchange factor pleckstrin homology (PH) domain; There ...
 96-189 1.10e-17

Cloned out of library/PAK-interactive exchange factor pleckstrin homology (PH) domain; There are two forms of Pix proteins: alpha Pix (also called Rho guanine nucleotide exchange factor (GEF) 6/90Cool-2) and beta Pix (GEF7/p85Cool-1). betaPix contains an N-terminal SH3 domain, a RhoGEF/DH domain, a PH domain, a GIT1 binding domain (GBD), and a C-terminal coiled-coil (CC) domain. alphaPix differs in that it contains a calponin homology (CH) domain, which interacts with beta-parvin, N-terminal to the SH3 domain. alphaPix is an exchange factor for Rac1 and Cdc42 and mediates Pak activation on cell adhesion to fibronectin. Mutations in alphaPix can cause X-linked mental retardation. alphaPix also interacts with Huntington's disease protein (htt), and enhances the aggregation of mutant htt (muthtt) by facilitating SDS-soluble muthtt-muthtt interactions. The DH-PH domain of a Pix was required for its binding to htt. In the majority of Rho GEF proteins, the DH-PH domain is responsible for the exchange activity. 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: 269932  Cd Length: 100  Bit Score: 78.51  E-value: 1.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624  96 VVHYAKVQLRFQHSQDVSDCYLELFPAHLYF--QAHGSEGLTFQGLLPLTELSVCPLEGSRE--HAFQITGPLPAPLLVL 171
Cdd:cd01225    1 VIHMSQVAVQNTGCQEKKERYFLLFPHVLLMlsASPRMSGFIYEGKLPLTGISVNRLEDTEGikNAFEISGPLIERIVVI 80

                         90
                 ....*....|....*...
gi 237820624 172 CPSRAELDRWLYHLEKQT 189
Cdd:cd01225   81 CNSQQDQQEWLEHLQQQT 98
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 114-190 2.76e-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: 46.00  E-value: 2.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624   114 DCYLELFPAHLYF--QAHGSEGLTFQGLLPLTELSVCPLEGS----REHAFQITGPLPAPLLVLCPSRAELDRWLYHLEK 187
Cdd:smart00233  20 KRYFVLFNSTLLYykSKKDKKSYKPKGSIDLSGCTVREAPDPdsskKPHCFEIKTSDRKTLLLQAESEEEREKWVEALRK 99


                   ...
gi 237820624   188 QTA 190
Cdd:smart00233 100 AIA 102
PHA03378 PHA03378
EBNA-3B; Provisional
 360-543 6.19e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 6.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624 360 QTSW----DSGCLAPPSTRTShsLPESSVPSTVGCSSQHTPLHRLSLES---------SPDAPDHTSETSHSPLYAD--- 423
Cdd:PHA03378 594 QTPWpvphPSQTPEPPTTQSH--IPETSAPRQWPMPLRPIPMRPLRMQPitfnvlvfpTPHQPPQVEITPYKPTWTQigh 671

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624 424 -PYTPPATSHrrvTDVRGLEEFLSAMQS-ARGPTPSSP--LPSVPVSVPASDPRSCSSGPAGPYLLSKKGALQSRA---- 495
Cdd:PHA03378 672 iPYQPSPTGA---NTMLPIQWAPGTMQPpPRAPTPMRPpaAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRArppa 748

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 237820624 496 AQRHRGSAKDGGPQPPDAPQLVSSAREGSPEPWLPLTDGRSPRRSRDP 543
Cdd:PHA03378 749 AAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTP 796
 
Name Accession Description Interval E-value
PH_PLEKHN1 cd13323
Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain; Not ...
 228-348 1.88e-72

Pleckstrin homology domain containing family N member 1Pleckstrin homology-like domain; Not much is known about PLEKHN1. It is found in a wide range of animals including humans, green anole, frog, and zebrafish. It 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: 270132  Cd Length: 121  Bit Score: 227.36  E-value: 1.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624 228 HEPGGSAVCASRVKLQHLPAQEQWDRLLVLYPTSLAIFSEELDGLCFKGELPLRAVHINLEEKEKQIRSFLIEGPLINTI 307
Cdd:cd13323    1 RESLGSITCVSKVKLQHLPFQEQHDRLLVLYPSSLIILSEESDGLCFKGELPLNAIQVNFEENEKKIRSFLIEGRLINTI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 237820624 308 RVVCASYEDYGHWLLCLRAVTHREGAPPLPGAESFPGSQVM 348
Cdd:cd13323   81 RVSCLSYEDYQDWILCLKTAQVRNGDSSLPGSSSFYGSTQP 121
PH_Cool_Pix cd01225
Cloned out of library/PAK-interactive exchange factor pleckstrin homology (PH) domain; There ...
 96-189 1.10e-17

Cloned out of library/PAK-interactive exchange factor pleckstrin homology (PH) domain; There are two forms of Pix proteins: alpha Pix (also called Rho guanine nucleotide exchange factor (GEF) 6/90Cool-2) and beta Pix (GEF7/p85Cool-1). betaPix contains an N-terminal SH3 domain, a RhoGEF/DH domain, a PH domain, a GIT1 binding domain (GBD), and a C-terminal coiled-coil (CC) domain. alphaPix differs in that it contains a calponin homology (CH) domain, which interacts with beta-parvin, N-terminal to the SH3 domain. alphaPix is an exchange factor for Rac1 and Cdc42 and mediates Pak activation on cell adhesion to fibronectin. Mutations in alphaPix can cause X-linked mental retardation. alphaPix also interacts with Huntington's disease protein (htt), and enhances the aggregation of mutant htt (muthtt) by facilitating SDS-soluble muthtt-muthtt interactions. The DH-PH domain of a Pix was required for its binding to htt. In the majority of Rho GEF proteins, the DH-PH domain is responsible for the exchange activity. 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: 269932  Cd Length: 100  Bit Score: 78.51  E-value: 1.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624  96 VVHYAKVQLRFQHSQDVSDCYLELFPAHLYF--QAHGSEGLTFQGLLPLTELSVCPLEGSRE--HAFQITGPLPAPLLVL 171
Cdd:cd01225    1 VIHMSQVAVQNTGCQEKKERYFLLFPHVLLMlsASPRMSGFIYEGKLPLTGISVNRLEDTEGikNAFEISGPLIERIVVI 80

                         90
                 ....*....|....*...
gi 237820624 172 CPSRAELDRWLYHLEKQT 189
Cdd:cd01225   81 CNSQQDQQEWLEHLQQQT 98
PH_Cool_Pix cd01225
Cloned out of library/PAK-interactive exchange factor pleckstrin homology (PH) domain; There ...
 235-330 4.96e-11

Cloned out of library/PAK-interactive exchange factor pleckstrin homology (PH) domain; There are two forms of Pix proteins: alpha Pix (also called Rho guanine nucleotide exchange factor (GEF) 6/90Cool-2) and beta Pix (GEF7/p85Cool-1). betaPix contains an N-terminal SH3 domain, a RhoGEF/DH domain, a PH domain, a GIT1 binding domain (GBD), and a C-terminal coiled-coil (CC) domain. alphaPix differs in that it contains a calponin homology (CH) domain, which interacts with beta-parvin, N-terminal to the SH3 domain. alphaPix is an exchange factor for Rac1 and Cdc42 and mediates Pak activation on cell adhesion to fibronectin. Mutations in alphaPix can cause X-linked mental retardation. alphaPix also interacts with Huntington's disease protein (htt), and enhances the aggregation of mutant htt (muthtt) by facilitating SDS-soluble muthtt-muthtt interactions. The DH-PH domain of a Pix was required for its binding to htt. In the majority of Rho GEF proteins, the DH-PH domain is responsible for the exchange activity. 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: 269932  Cd Length: 100  Bit Score: 59.63  E-value: 4.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624 235 VCASRVKLQHLPAQEQWDRLLVLYPTSLAIFS--EELDGLCFKGELPLRAVHIN-LEEKEKQIRSFLIEGPLINTIRVVC 311
Cdd:cd01225    2 IHMSQVAVQNTGCQEKKERYFLLFPHVLLMLSasPRMSGFIYEGKLPLTGISVNrLEDTEGIKNAFEISGPLIERIVVIC 81

                         90
                 ....*....|....*....
gi 237820624 312 ASYEDYGHWLLCLRAVTHR 330
Cdd:cd01225   82 NSQQDQQEWLEHLQQQTKA 100
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 114-190 2.76e-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: 46.00  E-value: 2.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624   114 DCYLELFPAHLYF--QAHGSEGLTFQGLLPLTELSVCPLEGS----REHAFQITGPLPAPLLVLCPSRAELDRWLYHLEK 187
Cdd:smart00233  20 KRYFVLFNSTLLYykSKKDKKSYKPKGSIDLSGCTVREAPDPdsskKPHCFEIKTSDRKTLLLQAESEEEREKWVEALRK 99


                   ...
gi 237820624   188 QTA 190
Cdd:smart00233 100 AIA 102
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 115-185 1.97e-05

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: 43.30  E-value: 1.97e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237820624 115 CYLELFPAHL-YFQAHGSEGLTFQGLLPLTELSVC--PLEGSREHAFQITGPLPAPLLVLCPSRAELDRWLYHL 185
Cdd:cd00821   19 RWFVLFEGVLlYYKSKKDSSYKPKGSIPLSGILEVeeVSPKERPHCFELVTPDGRTYYLQADSEEERQEWLKAL 92
PHA03378 PHA03378
EBNA-3B; Provisional
 360-543 6.19e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 6.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624 360 QTSW----DSGCLAPPSTRTShsLPESSVPSTVGCSSQHTPLHRLSLES---------SPDAPDHTSETSHSPLYAD--- 423
Cdd:PHA03378 594 QTPWpvphPSQTPEPPTTQSH--IPETSAPRQWPMPLRPIPMRPLRMQPitfnvlvfpTPHQPPQVEITPYKPTWTQigh 671

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624 424 -PYTPPATSHrrvTDVRGLEEFLSAMQS-ARGPTPSSP--LPSVPVSVPASDPRSCSSGPAGPYLLSKKGALQSRA---- 495
Cdd:PHA03378 672 iPYQPSPTGA---NTMLPIQWAPGTMQPpPRAPTPMRPpaAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRArppa 748

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 237820624 496 AQRHRGSAKDGGPQPPDAPQLVSSAREGSPEPWLPLTDGRSPRRSRDP 543
Cdd:PHA03378 749 AAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTP 796
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 370-534 7.09e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.38  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624  370 PPSTRTSHSLPESSVPSTVGCSSQHTPLHRLSLESSPDAPDHTSETS-HSPLYADPYTPPATSHRRvtdvrgleeflsAM 448
Cdd:PHA03307  284 PASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSsSSESSRGAAVSPGPSPSR------------SP 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237820624  449 QSARGPTPSSPLPSVPVSVPASDPRSCSSGPAGPYLLSKKGALQSRAAQRHRGSAKDGGPQPPDAPQLVSSAREGSPEPW 528
Cdd:PHA03307  352 SPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYP 431


                  ....*.
gi 237820624  529 LPLTDG 534
Cdd:PHA03307  432 LLTPSG 437
 
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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