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 1318663214 279 DAFAGFLNEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEIEAKVEPALVVPIDKETRIQAVEKDSK-KMHCFSVLSTAAG 357
Cdd:cd13249     2 EMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKgRASSLSIINPYSG 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1318663214 358 RAVSHIFAADSLADFQEWMGAFRQHFFDLS 387
Cdd:cd13249    82 EEVTHVLSADSREELQKWMEALWQHFYDMS 111

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 1318663214 279 DAFAGFLNEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEIEAKVEPALVVPIDKETRIQAVEKDSK-KMHCFSVLSTAAG 357
Cdd:cd13249     2 EMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKgRASSLSIINPYSG 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1318663214 358 RAVSHIFAADSLADFQEWMGAFRQHFFDLS 387
Cdd:cd13249    82 EEVTHVLSADSREELQKWMEALWQHFYDMS 111

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1318663214   12 QQDCSIREKIDLEIRMREGIWKLLSLSTKKDQVL-HAVKNLMVCSARIQAYTAELQK 67
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSNDRKVLsEAQSMLRESNQKLDLLKEELEK 57

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 1318663214 279 DAFAGFLNEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEIEAKVEPALVVPIDKETRIQAVEKDSK-KMHCFSVLSTAAG 357
Cdd:cd13249     2 EMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKgRASSLSIINPYSG 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1318663214 358 RAVSHIFAADSLADFQEWMGAFRQHFFDLS 387
Cdd:cd13249    82 EEVTHVLSADSREELQKWMEALWQHFYDMS 111

Rho effector or protein kinase C-related kinase homology region 1 homologues; Alpha-helical domain found in vertebrate PRK1 and yeast PKC1 protein kinases C. The HR1 in rhophilin bind RhoGTP; those in PRK1 bind RhoA and RhoB. Also called RBD - Rho-binding domain

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1318663214   12 QQDCSIREKIDLEIRMREGIWKLLSLSTKKDQVL-HAVKNLMVCSARIQAYTAELQK 67
Cdd:smart00742   1 LRLEDLRRKIEKELKVKEGAENMRKLTSNDRKVLsEAQSMLRESNQKLDLLKEELEK 57

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 1318663214 282 AGFLnEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEieAKVEPALVVPIDKETRIQAVEKDSKKmHCFSvLSTAAGRavS 361
Cdd:cd00821     2 EGYL-LKRGGGGLKSWKKRWFVLFEGVLLYYKSKKD--SSYKPKGSIPLSGILEVEEVSPKERP-HCFE-LVTPDGR--T 74

                          90
                  ....*....|....*...
gi 1318663214 362 HIFAADSLADFQEWMGAF 379
Cdd:cd00821    75 YYLQADSEEERQEWLKAL 92

RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 (also called RasGap1 or p120) is a member of the RasGAP family of GTPase-activating proteins. RASA1 contains N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Splice variants lack the N-terminal domains. It is a cytosolic vertebrate protein that acts as a suppressor of RAS via its C-terminal GAP domain function, 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. Additionally, it is involved in mitogenic signal transmission towards downstream interacting partners through its N-terminal SH2-SH3-SH2 domains. RASA1 interacts with a number of proteins including: G3BP1, SOCS3, ANXA6, Huntingtin, KHDRBS1, Src, EPHB3, EPH receptor B2, Insulin-like growth factor 1 receptor, PTK2B, DOK1, PDGFRB, HCK, Caveolin 2, DNAJA3, HRAS, GNB2L1 and NCK1. 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 1318663214 280 AFAGFLNEQqtGKGLVGWRRLYCALRGGKLR-CFYgpeEIEAKVEPALVvpID-KETRIQAVEkDS--KKMHCFSVLSTA 355
Cdd:cd13260     4 DKKGYLLKK--GGKNKKWKNLYFVLEGKEQHlYFF---DNEKRTKPKGL--IDlSYCSLYPVH-DSlfGRPNCFQIVVRA 75

                          90       100
                  ....*....|....*....|....*.
gi 1318663214 356 AGRAVSHIFAADSLADFQEWMGAFRQ 381
Cdd:cd13260    76 LNESTITYLCADTAELAQEWMRALRA 101

Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from insects, spiders, mollusks, and nematodes. 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 1318663214 291 GKGLVGWRRLYCALRGGKLRCFYGPEEIEAkvepALVVPIDKETRIQAVEKDSKKmHCFSVLSTAagraVSHIFAADSLA 370
Cdd:cd13326    12 GKGGGKWAKRWFVLKGSNLYGFRSQESTKA----DCVIFLPGFTVSPAPEVKSRK-YAFKVYHTG----TVFYFAAESQE 82

                  ....*....
gi 1318663214 371 DFQEWMGAF 379
Cdd:cd13326    83 DMKKWLDLL 91

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663214 296 GWRRLYCALRGGKLrcFY-GPEEIEAKVEPALVVpIDKETRIQaVEKDSKKMHCFS-VLSTAAGRavSHIFAADSLADFQ 373
Cdd:cd13258    35 VFKERWFKLKGNLL--FYfRTNEFGDCSEPIGAI-VLENCRVQ-MEEITEKPFAFSiVFNDEPEK--KYIFSCRSEEQCE 108

                  ....*....
gi 1318663214 374 EWMGAFRQH 382
Cdd:cd13258   109 QWIEALRQA 117