PH-like domain of Exocyst complex component 1-like; Exocyst complex component 1-like proteins are short, higher eukaryotic proteins that show homology to the PH-domain of higher eukaryotic EXOC1 and yeast SEC3 which are part of the exocyst complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. Their function is unknown. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704848   2 SSLVKEDLEKKLFKPLSQNLYEFIEIEFSVQDRYYLCVSVTKKEEVKIVMVKHYRIGLDEKYEVTKKWSLNDLQMIDGKE 81
Cdd:cd14682     1 SSLVKEDMQKKLFRPLGQTLYEFIEIEEQSHGRHYLCASVAKDKEVQISMVKHYRVCLDEKYERTEIWSLKDLEMIDGKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1191704848  82 ADTDNPFFDLHFKKVYSLEAYSCASKYAFARTVNKLNH 119
Cdd:cd14682    81 ADTDNPCFDMHFEEVRSVEAYSCASKYAFARTLNKLND 118

PH-like domain of Exocyst complex component 1-like; Exocyst complex component 1-like proteins are short, higher eukaryotic proteins that show homology to the PH-domain of higher eukaryotic EXOC1 and yeast SEC3 which are part of the exocyst complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. Their function is unknown. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704848   2 SSLVKEDLEKKLFKPLSQNLYEFIEIEFSVQDRYYLCVSVTKKEEVKIVMVKHYRIGLDEKYEVTKKWSLNDLQMIDGKE 81
Cdd:cd14682     1 SSLVKEDMQKKLFRPLGQTLYEFIEIEEQSHGRHYLCASVAKDKEVQISMVKHYRVCLDEKYERTEIWSLKDLEMIDGKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1191704848  82 ADTDNPFFDLHFKKVYSLEAYSCASKYAFARTVNKLNH 119
Cdd:cd14682    81 ADTDNPCFDMHFEEVRSVEAYSCASKYAFARTLNKLND 118

PH-like domain of Exocyst complex component 1-like; Exocyst complex component 1-like proteins are short, higher eukaryotic proteins that show homology to the PH-domain of higher eukaryotic EXOC1 and yeast SEC3 which are part of the exocyst complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. Their function is unknown. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704848   2 SSLVKEDLEKKLFKPLSQNLYEFIEIEFSVQDRYYLCVSVTKKEEVKIVMVKHYRIGLDEKYEVTKKWSLNDLQMIDGKE 81
Cdd:cd14682     1 SSLVKEDMQKKLFRPLGQTLYEFIEIEEQSHGRHYLCASVAKDKEVQISMVKHYRVCLDEKYERTEIWSLKDLEMIDGKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1191704848  82 ADTDNPFFDLHFKKVYSLEAYSCASKYAFARTVNKLNH 119
Cdd:cd14682    81 ADTDNPCFDMHFEEVRSVEAYSCASKYAFARTLNKLND 118

Exocyst complex component SEC3 N-terminal PIP2 binding PH; This is the N-terminal domain of fungal and eukaryotic Sec3 proteins. Sec3 is a component of the exocyst complex that is involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.This N-terminal domain contains a cryptic pleckstrin homology (PH) fold, and all six positively charged lysine and arginine residues in the PH domain predicted to bind the PIP2 head group are conserved. The exocyst complex is essential for many exocytic events, by tethering vesicles at the plasma membrane for fusion. In fission yeast, polarised exocytosis for growth relies on the combined action of the exocyst at cell poles and myosin-driven transport along actin cables.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704848  36 YLCVSVTKKEEVKIVMVKHYRIGldeKYEVTKKWSLNDLQMIDGKEADTDnpfFDLHFKKVYSLEAYSCASKYAFARTVN 115
Cdd:pfam15277   7 YLCLSVTKSGRVFLHKVKENSNG---SFSIGKTWPLKELRLVEGINPDKG---FDLTFDKPYYWQANSPKEKNAFIRSLV 80

                  ....
gi 1191704848 116 KLNH 119
Cdd:pfam15277  81 KLYR 84

PH-like domain of Syntaxin binding protein 6; Syntaxin binding protein 6 (STXBP6, also called Amisyn) contains, beside the N-terminal PH-like domain, a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, with STXBP6 being a R-SNARE. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704848   5 VKEDLEKKLFKPLSQNLYEFIEIEFSV-----------QDRY--YLCVSVTKKEEVKIVMVKHYRIGLDEKYEVTKKWSL 71
Cdd:cd14681     2 AKSAISKEIFAPRDERMLGAVQVKRRTkkkipflatggQGEYltYICLSVTNKKPAQVFITKVKQFEGSTSFVRRSQWML 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1191704848  72 NDLQMIDGKEADTDNPFFDLHFKKVY-SLEAYSCASKYAFartVNKLNHA 120
Cdd:cd14681    82 EQLRQVNGIDPNKDSPEFDLVFDNGFdQWVASSASEKCTF---FQILHHT 128