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Conserved domains on  [gi|5542142]
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Protein Classification

PH_Btk domain-containing protein (domain architecture ID 10100778)

PH_Btk domain-containing protein

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List of domain hits

Name Accession Description Interval E-value
PH_Btk cd01238
Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of ...
5-165 1.59e-65

Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of cytoplasmic protein tyrosine kinases that includes BMX, IL2-inducible T-cell kinase (Itk) and Tec. Btk plays a role in the maturation of B cells. Tec proteins general have an N-terminal PH domain, followed by a Tek homology (TH) domain, a SH3 domain, a SH2 domain and a kinase domain. The Btk PH domain binds phosphatidylinositol 3,4,5-trisphosphate and responds to signalling via phosphatidylinositol 3-kinase. The PH domain is also involved in membrane anchoring which is confirmed by the discovery of a mutation of a critical arginine residue in the BTK PH domain. This results in severe human immunodeficiency known as X-linked agammaglobulinemia (XLA) in humans and a related disorder is mice.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: 269944 [Multi-domain]  Cd Length: 140  Bit Score: 196.68  E-value: 1.59e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142    5 LESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYKYDFERgrRGSKKGSIDVEKITCVETVVPEknPPPERqiprrgee 84
Cdd:cd01238   1 LEGLLVKRSQGKKRFGPVNYKERWFVLTKSSLSYYEGDGEK--RGKEKGSIDLSKVRCVEEVKDE--AFFER-------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142   85 ssemeqisiierfPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGC 164
Cdd:cd01238  69 -------------KYPFQVVYDDYTLYVFAPSEEDRDEWIAALRKVCRNNSNLHDKYHPGFWTGGKWSCCGQTSKSAPGC 135

                .
gi 5542142  165 Q 165
Cdd:cd01238 136 Q 136
 
Name Accession Description Interval E-value
PH_Btk cd01238
Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of ...
5-165 1.59e-65

Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of cytoplasmic protein tyrosine kinases that includes BMX, IL2-inducible T-cell kinase (Itk) and Tec. Btk plays a role in the maturation of B cells. Tec proteins general have an N-terminal PH domain, followed by a Tek homology (TH) domain, a SH3 domain, a SH2 domain and a kinase domain. The Btk PH domain binds phosphatidylinositol 3,4,5-trisphosphate and responds to signalling via phosphatidylinositol 3-kinase. The PH domain is also involved in membrane anchoring which is confirmed by the discovery of a mutation of a critical arginine residue in the BTK PH domain. This results in severe human immunodeficiency known as X-linked agammaglobulinemia (XLA) in humans and a related disorder is mice.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: 269944 [Multi-domain]  Cd Length: 140  Bit Score: 196.68  E-value: 1.59e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142    5 LESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYKYDFERgrRGSKKGSIDVEKITCVETVVPEknPPPERqiprrgee 84
Cdd:cd01238   1 LEGLLVKRSQGKKRFGPVNYKERWFVLTKSSLSYYEGDGEK--RGKEKGSIDLSKVRCVEEVKDE--AFFER-------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142   85 ssemeqisiierfPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGC 164
Cdd:cd01238  69 -------------KYPFQVVYDDYTLYVFAPSEEDRDEWIAALRKVCRNNSNLHDKYHPGFWTGGKWSCCGQTSKSAPGC 135

                .
gi 5542142  165 Q 165
Cdd:cd01238 136 Q 136
BTK smart00107
Bruton's tyrosine kinase Cys-rich motif; Zinc-binding motif containing conserved cysteines and ...
134-169 1.32e-18

Bruton's tyrosine kinase Cys-rich motif; Zinc-binding motif containing conserved cysteines and a histidine. Always found C-terminal to PH domains (but not all PH domains are followed by BTK motifs). The crystal structure shows this motif packs against the PH domain. The PH+Btk module pair has been called the Tec homology (TH) region.


Pssm-ID: 128417  Cd Length: 36  Bit Score: 73.95  E-value: 1.32e-18
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 5542142     134 NSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILEN 169
Cdd:smart00107   1 NNNLLQKYHPSFWVDGKWLCCQQSEKNAPGCTPYEA 36
PH pfam00169
PH domain; PH stands for pleckstrin homology.
3-130 1.18e-12

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 333896  Cd Length: 103  Bit Score: 60.63  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142      3 VILESIFLKRSQQKKKtsplNFKKRLFLLTVHKLSYYKYDfERGRRGSKKGSIDVEKITCVETVVPEKNPPperqiprrg 82
Cdd:pfam00169   1 VIKEGWLLKKGGGKKK----SWKKRYFVLFDGSLLYYKDS-SRGKSKEPKGSISLSGCTVVEVVAPDKPKR--------- 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 5542142     83 eessemeqisiierfPYPFQVVYDEG----PLYVFSPTEELRKRWIHQLKNV 130
Cdd:pfam00169  67 ---------------KFCFELRTGELdgkrTYLLQAESEEERKEWIKAIQSA 103
 
Name Accession Description Interval E-value
PH_Btk cd01238
Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of ...
5-165 1.59e-65

Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of cytoplasmic protein tyrosine kinases that includes BMX, IL2-inducible T-cell kinase (Itk) and Tec. Btk plays a role in the maturation of B cells. Tec proteins general have an N-terminal PH domain, followed by a Tek homology (TH) domain, a SH3 domain, a SH2 domain and a kinase domain. The Btk PH domain binds phosphatidylinositol 3,4,5-trisphosphate and responds to signalling via phosphatidylinositol 3-kinase. The PH domain is also involved in membrane anchoring which is confirmed by the discovery of a mutation of a critical arginine residue in the BTK PH domain. This results in severe human immunodeficiency known as X-linked agammaglobulinemia (XLA) in humans and a related disorder is mice.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: 269944 [Multi-domain]  Cd Length: 140  Bit Score: 196.68  E-value: 1.59e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142    5 LESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYKYDFERgrRGSKKGSIDVEKITCVETVVPEknPPPERqiprrgee 84
Cdd:cd01238   1 LEGLLVKRSQGKKRFGPVNYKERWFVLTKSSLSYYEGDGEK--RGKEKGSIDLSKVRCVEEVKDE--AFFER-------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142   85 ssemeqisiierfPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGC 164
Cdd:cd01238  69 -------------KYPFQVVYDDYTLYVFAPSEEDRDEWIAALRKVCRNNSNLHDKYHPGFWTGGKWSCCGQTSKSAPGC 135

                .
gi 5542142  165 Q 165
Cdd:cd01238 136 Q 136
BTK smart00107
Bruton's tyrosine kinase Cys-rich motif; Zinc-binding motif containing conserved cysteines and ...
134-169 1.32e-18

Bruton's tyrosine kinase Cys-rich motif; Zinc-binding motif containing conserved cysteines and a histidine. Always found C-terminal to PH domains (but not all PH domains are followed by BTK motifs). The crystal structure shows this motif packs against the PH domain. The PH+Btk module pair has been called the Tec homology (TH) region.


Pssm-ID: 128417  Cd Length: 36  Bit Score: 73.95  E-value: 1.32e-18
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 5542142     134 NSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILEN 169
Cdd:smart00107   1 NNNLLQKYHPSFWVDGKWLCCQQSEKNAPGCTPYEA 36
PH pfam00169
PH domain; PH stands for pleckstrin homology.
3-130 1.18e-12

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 333896  Cd Length: 103  Bit Score: 60.63  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142      3 VILESIFLKRSQQKKKtsplNFKKRLFLLTVHKLSYYKYDfERGRRGSKKGSIDVEKITCVETVVPEKNPPperqiprrg 82
Cdd:pfam00169   1 VIKEGWLLKKGGGKKK----SWKKRYFVLFDGSLLYYKDS-SRGKSKEPKGSISLSGCTVVEVVAPDKPKR--------- 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 5542142     83 eessemeqisiierfPYPFQVVYDEG----PLYVFSPTEELRKRWIHQLKNV 130
Cdd:pfam00169  67 ---------------KFCFELRTGELdgkrTYLLQAESEEERKEWIKAIQSA 103
BTK pfam00779
BTK motif; Zinc-binding motif containing conserved cysteines and a histidine. Always found ...
140-165 6.56e-12

BTK motif; Zinc-binding motif containing conserved cysteines and a histidine. Always found C-terminal to PH domains. The crystal structure shows this motif packs against the PH domain. The PH+Btk module pair has been called the Tec homology (TH) region.


Pssm-ID: 334250  Cd Length: 26  Bit Score: 56.75  E-value: 6.56e-12
                          10        20
                  ....*....|....*....|....*.
gi 5542142    140 KYHPCFWIDGQYLCCSQTAKNAMGCQ 165
Cdd:pfam00779   1 KYHPGAFVGGKWLCCKQTDKNAPGCS 26
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
3-132 7.44e-12

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  Cd Length: 102  Bit Score: 58.33  E-value: 7.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142       3 VILESIFLKRSQQKKKtsplNFKKRLFLLTVHKLSYYKyDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPerqiprrg 82
Cdd:smart00233   1 VIKEGWLYKKSGGGKK----SWKKRYFVLFNSTLLYYK-SKKDKKSYKPKGSIDLSGCTVREAPDPDSSKKP-------- 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 5542142      83 eessemeqisiierfpYPFQVVYDEGPLYVFS-PTEELRKRWIHQLKNVIR 132
Cdd:smart00233  68 ----------------HCFEIKTSDRKTLLLQaESEEEREKWVEALRKAIA 102
PH_GAP1m_mammal-like cd13370
GTPase activating protein 1 m pleckstrin homology (PH) domain; GAP1(m) (also called RASA2/RAS ...
11-149 6.70e-09

GTPase activating protein 1 m pleckstrin homology (PH) domain; GAP1(m) (also called RASA2/RAS p21 protein activator (GTPase activating protein) 2) is a member of the GAP1 family of GTPase-activating proteins, along with RASAL1, GAP1(IP4BP), and CAPRI. With the notable exception of GAP1(m), they all possess an arginine finger-dependent GAP activity on the Ras-related protein Rap1. GAP1(m) contains two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Its C2 domains, like those of GAP1IP4BP, do not contain the C2 motif that is known to be required for calcium-dependent phospholipid binding. GAP1(m) is regulated by the binding of its PH domains to phophoinositides, PIP3 (phosphatidylinositol 3,4,5-trisphosphate). It suppresses RAS, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. GAP1(m) binds inositol tetrakisphosphate (IP4). 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: 241521  Cd Length: 133  Bit Score: 51.48  E-value: 6.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142   11 KRSQQKKKTSPLNFKKRLFLLTVHKLSYYKydfERGRRGSKkgSIDVEKITCVEtvvpeknppperqiprRGEESSEMEQ 90
Cdd:cd13370  24 KRAQGRTRIGKKNFKKRWFCLTSRELTYHK---QKGKEAIF--TIPVKNILAVE----------------KLEESAFNKK 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5542142   91 isiierfpYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDG 149
Cdd:cd13370  83 --------NMFQVIHSEKPLYVQANNCVEANEWIEVLSRVSRCNQKRLSFYHPSAYLGG 133
PH_GAP1-like cd01244
RAS p21 protein activator (GTPase activating protein) family pleckstrin homology (PH) domain; ...
6-139 2.77e-08

RAS p21 protein activator (GTPase activating protein) family pleckstrin homology (PH) domain; RASAL1, GAP1(m), GAP1(IP4BP), and CAPRI are all members of the GAP1 family of GTPase-activating proteins. They contain N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. With the notable exception of GAP1(m), they all possess an arginine finger-dependent GAP activity on the Ras-related protein Rap1. They act as a suppressor of RAS enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. PH domains share little sequence conservation, but all have a common fold, which is electrostatically polarized. 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: 269950  Cd Length: 107  Bit Score: 49.21  E-value: 2.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142    6 ESIFLKRSQQ-KKKTSPLNFKKRLFLLTVHKLSYYKydfergRRGSKK-GSIDVEKITCVETVvpeknppperqiprrGE 83
Cdd:cd01244   2 EGYLIKRAQGrKKKFGRKNFKKRYFRLTNEALSYSK------SKGKQPlCSIPLEDILAVERV---------------EE 60
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5542142   84 ESSEMeqisiierfPYPFQVVYDEGPLYV--FSPTEElrKRWIHQLKNVIRYNSDLVQ 139
Cdd:cd01244  61 ESFKM---------KNMFQIVQPDRTLYLqaKNVVEL--NEWLSALRKVCLCNPNRLP 107
PH_GAP1_mammal-like cd13371
GAP1(IP4BP) pleckstrin homology (PH) domain; GAP1 (also called IP4BP, RASA3/Ras ...
3-141 7.45e-06

GAP1(IP4BP) pleckstrin homology (PH) domain; GAP1 (also called IP4BP, RASA3/Ras GTPase-activating protein 3, and RAS p21 protein activator (GTPase activating protein) 3/GAPIII/MGC46517/MGC47588)) is a member of the GAP1 family of GTPase-activating proteins, along with RASAL1, GAP1(m), and CAPRI. With the notable exception of GAP1(m), they all possess an arginine finger-dependent GAP activity on the Ras-related protein Rap1. GAP1(IP4BP) contains two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Its C2 domains, like those of GAP1M, do not contain the C2 motif that is known to be required for calcium-dependent phospholipid binding. GAP1(IP4BP) is regulated by the binding of its PH domains to phophoinositides, PIP3 (phosphatidylinositol 3,4,5-trisphosphate) and PIP2 (phosphatidylinositol 4,5-bisphosphate). It suppresses RAS, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. GAP1(IP4BP) binds tyrosine-protein kinase, HCK. Members here include humans, chickens, frogs, and fish. 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: 241522  Cd Length: 125  Bit Score: 43.10  E-value: 7.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142    3 VILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYKYDFERGRrgskkGSIDVEKITCVEtvvpeknppperqipRRG 82
Cdd:cd13371  16 LLKEGFMIKRAQGRKRFGMKNFKKRWFRLTNHEFTYHKSKGDHPL-----CSIPIENILAVE---------------RLE 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5542142   83 EESSEMEQIsiierfpypFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKY 141
Cdd:cd13371  76 EESFKMKNM---------FQVIQPERALYIQANNCVEAKDWIDILTKVSQCNKKRLTVY 125
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
5-127 3.10e-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  Cd Length: 92  Bit Score: 40.60  E-value: 3.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142    5 LESIFLKRSQQKKKtsplNFKKRLFLLTVHKLSYYKYDFERGRRgsKKGSIDVEKITCVETVVPEKNppperqiprrgee 84
Cdd:cd00821   1 KEGYLLKRGGGGLK----SWKKRWFVLFEGVLLYYKSKKDSSYK--PKGSIPLSGILEVEEVSPKER------------- 61
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 5542142   85 ssemeqisiierfPYPFQVVYDEGPLYVFS-PTEELRKRWIHQL 127
Cdd:cd00821  62 -------------PHCFELVTPDGRTYYLQaDSEEERQEWLKAL 92
PH3_MyoX-like cd13297
Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a ...
1-131 1.12e-03

Myosin X-like Pleckstrin homology (PH) domain, repeat 3; MyoX, a MyTH-FERM myosin, is a molecular motor that has crucial functions in the transport and/or tethering of integrins in the actin-based extensions known as filopodia, microtubule binding, and in netrin-mediated axon guidance. It functions as a dimer. MyoX walks on bundles of actin, rather than single filaments, unlike the other unconventional myosins. MyoX is present in organisms ranging from humans to choanoflagellates, but not in Drosophila and Caenorhabditis elegans.MyoX consists of a N-terminal motor/head region, a neck made of 3 IQ motifs, and a tail consisting of a coiled-coil domain, a PEST region, 3 PH domains, a myosin tail homology 4 (MyTH4), and a FERM domain at its very C-terminus. The first PH domain in the MyoX tail is a split-PH domain, interupted by the second PH domain such that PH 1a and PH 1b flanks PH 2. The third PH domain (PH 3) follows the PH 1b domain. This cd contains the third MyoX PH repeat. PLEKHH3/Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) member 3 is also part of this CD and like MyoX contains a FERM domain, a MyTH4 domain, and a single PH domain. Not much is known about the function of PLEKHH3. 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: 270109  Cd Length: 126  Bit Score: 37.03  E-value: 1.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142    1 AAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYKydfERGRRGSKKGSIDVEKItCveTVVpeknPPPERQIPR 80
Cdd:cd13297  11 QDVIERGWLYKEGGKGGARGNLTKKKRWFVLTGNSLDYYK---SSEKNSLKLGTLVLNSL-C--SVV----PPDEKMAKE 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 5542142   81 RGEessemeqisiierfpYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVI 131
Cdd:cd13297  81 TGY---------------WTFTVHGRKHSFRLYTKLQEEAMRWVNAIQDVI 116
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
3-136 1.93e-03

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. 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: 270110  Cd Length: 106  Bit Score: 36.06  E-value: 1.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542142    3 VILESIFLKRSQQKKktsplNFKKRLFLLTVHKLSYYKydfergrrgskkgsidvekitcvetvvPEKNPPPERQIPRrg 82
Cdd:cd13298   6 VLKSGYLLKRSRKTK-----NWKKRWVVLRPCQLSYYK---------------------------DEKEYKLRRVINL-- 51
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5542142   83 eesSEMEQISIIE--RFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSD 136
Cdd:cd13298  52 ---SELLAVAPLKdkKRKNVFGIYTPSKNLHFRATSEKDANEWVEALREEFRLDDE 104
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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