Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. 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 71994505 1029 DITYHGFLSMYQrTGEGLGSWTRYWCALENGEMKFWKQPEDEGTKGYTALMDLSTCCRSEGASVVEDICPFPNSFHIDVW 1108
Cdd:cd01263    1 SVEYRGFLTVFE-DVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCARPNTFLLETL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 71994505 1109 APKMDTSDPRGIERLRVMLAADTAQDLQTWLSLINSTSKQLC 1150
Cdd:cd01263   80 RPAEDDDRDDTNEKIRVLLSADTKEERIEWLSALNQTLADLR 121

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. 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 71994505 1029 DITYHGFLSMYQrTGEGLGSWTRYWCALENGEMKFWKQPEDEGTKGYTALMDLSTCCRSEGASVVEDICPFPNSFHIDVW 1108
Cdd:cd01263    1 SVEYRGFLTVFE-DVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCARPNTFLLETL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 71994505 1109 APKMDTSDPRGIERLRVMLAADTAQDLQTWLSLINSTSKQLC 1150
Cdd:cd01263   80 RPAEDDDRDDTNEKIRVLLSADTKEERIEWLSALNQTLADLR 121

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994505    1030 ITYHGFLsmYQRTGEGLGSWTRYWCALENGEMKFWKQPEDEGTKGYTALMDLSTCCRSEGASvvEDICPFPNSFHIdvwa 1109
Cdd:smart00233    1 VIKEGWL--YKKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVREAPD--PDSSKKPHCFEI---- 72

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 71994505    1110 pkmdtsdpRGIERLRVMLAADTAQDLQTWLSLINSTSK 1147
Cdd:smart00233   73 --------KTSDRKTLLLQAESEEEREKWVEALRKAIA 102

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. 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 71994505 1029 DITYHGFLSMYQrTGEGLGSWTRYWCALENGEMKFWKQPEDEGTKGYTALMDLSTCCRSEGASVVEDICPFPNSFHIDVW 1108
Cdd:cd01263    1 SVEYRGFLTVFE-DVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCARPNTFLLETL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 71994505 1109 APKMDTSDPRGIERLRVMLAADTAQDLQTWLSLINSTSKQLC 1150
Cdd:cd01263   80 RPAEDDDRDDTNEKIRVLLSADTKEERIEWLSALNQTLADLR 121

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994505    1030 ITYHGFLsmYQRTGEGLGSWTRYWCALENGEMKFWKQPEDEGTKGYTALMDLSTCCRSEGASvvEDICPFPNSFHIdvwa 1109
Cdd:smart00233    1 VIKEGWL--YKKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVREAPD--PDSSKKPHCFEI---- 72

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 71994505    1110 pkmdtsdpRGIERLRVMLAADTAQDLQTWLSLINSTSK 1147
Cdd:smart00233   73 --------KTSDRKTLLLQAESEEEREKWVEALRKAIA 102

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71994505 1032 YHGFLsmYQRTGEGLGSWTRYWCALENGEMKFWKqPEDEGTKGYTALMDLSTCCRSEGASVVEDicpfPNSFHIdvWAPK 1111
Cdd:cd00821    1 KEGYL--LKRGGGGLKSWKKRWFVLFEGVLLYYK-SKKDSSYKPKGSIPLSGILEVEEVSPKER----PHCFEL--VTPD 71

                         90       100       110
                 ....*....|....*....|....*....|.
gi 71994505 1112 MDTsdprgierlrVMLAADTAQDLQTWLSLI 1142
Cdd:cd00821   72 GRT----------YYLQADSEEERQEWLKAL 92

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. 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 71994505 1034 GFLSMyQRTGEGLGSWTRYWCALENGEMKFWKQPEDEGTKGYTAL---MDLSTCCRsegasVVEDICPFPnSFHIDVWap 1110
Cdd:cd13249    6 GYLSQ-QQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLtipINKETRIR-----AVEKDSKGR-ASSLSII-- 76

                         90       100       110
                 ....*....|....*....|....*....|
gi 71994505 1111 kmdtsDPRGIERLRVMLAADTAQDLQTWLS 1140
Cdd:cd13249   77 -----NPYSGEEVTHVLSADSREELQKWME 101