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 24586311 1106 SVEYKGFLTMFEDISGFGAWHRRWCYLNGSVINYWKYPDDEKRKTPMGSIDLNSCTSQKVTTAPRDICARLNTMLLECER 1185
Cdd:cd01263    1 SVEYRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCARPNTFLLETLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 24586311 1186 PALETDqesliivPNGRTTTVRHLLSADTKEEREEWCAYLNKALTLLR 1233
Cdd:cd01263   81 PAEDDD-------RDDTNEKIRVLLSADTKEERIEWLSALNQTLADLR 121

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586311   549 TDEDSKRARKSHSDRLYPALSDLDSSGDNCCAAETASATDDSHQQDEEETESCMDESDDQSQTEDSSAGMCNGSLGREIM 628
Cdd:NF033609  722 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 801

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586311   629 SAVQRNEVEMQQQQTGKKTVRYADQDMYYDDSSLNSSQVSAGIDDYLDEALVEDYGSTQDDQSDSGDEQNASRLSLGSKG 708
Cdd:NF033609  802 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNG 881

                  ....*
gi 24586311   709 TTASN 713
Cdd:NF033609  882 TNASN 886

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 24586311 1106 SVEYKGFLTMFEDISGFGAWHRRWCYLNGSVINYWKYPDDEKRKTPMGSIDLNSCTSQKVTTAPRDICARLNTMLLECER 1185
Cdd:cd01263    1 SVEYRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCARPNTFLLETLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 24586311 1186 PALETDqesliivPNGRTTTVRHLLSADTKEEREEWCAYLNKALTLLR 1233
Cdd:cd01263   81 PAEDDD-------RDDTNEKIRVLLSADTKEERIEWLSALNQTLADLR 121

PH domain; PH stands for pleckstrin homology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586311   1107 VEYKGFLtMFEDISGFGAWHRRWCYLNGSVINYWKYPDDEKRKTPMGSIDLNSCTSQKVTTAPRdicarlntmlleCERP 1186
Cdd:pfam00169    1 VVKEGWL-LKKGGGKKKSWKKRYFVLFDGSLLYYKDDKSGKSKEPKGSISLSGCEVVEVVASDS------------PKRK 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 24586311   1187 aletdqESLIIVPNGRTTTVRHLLSADTKEEREEWCAYLNKAL 1229
Cdd:pfam00169   68 ------FCFELRTGERTGKRTYLLQAESEEERKDWIKAIQSAI 104

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586311   549 TDEDSKRARKSHSDRLYPALSDLDSSGDNCCAAETASATDDSHQQDEEETESCMDESDDQSQTEDSSAGMCNGSLGREIM 628
Cdd:NF033609  722 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 801

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586311   629 SAVQRNEVEMQQQQTGKKTVRYADQDMYYDDSSLNSSQVSAGIDDYLDEALVEDYGSTQDDQSDSGDEQNASRLSLGSKG 708
Cdd:NF033609  802 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNG 881

                  ....*
gi 24586311   709 TTASN 713
Cdd:NF033609  882 TNASN 886

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 24586311 1106 SVEYKGFLTMFEDISGFGAWHRRWCYLNGSVINYWKYPDDEKRKTPMGSIDLNSCTSQKVTTAPRDICARLNTMLLECER 1185
Cdd:cd01263    1 SVEYRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCARPNTFLLETLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 24586311 1186 PALETDqesliivPNGRTTTVRHLLSADTKEEREEWCAYLNKALTLLR 1233
Cdd:cd01263   81 PAEDDD-------RDDTNEKIRVLLSADTKEERIEWLSALNQTLADLR 121

PH domain; PH stands for pleckstrin homology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586311   1107 VEYKGFLtMFEDISGFGAWHRRWCYLNGSVINYWKYPDDEKRKTPMGSIDLNSCTSQKVTTAPRdicarlntmlleCERP 1186
Cdd:pfam00169    1 VVKEGWL-LKKGGGKKKSWKKRYFVLFDGSLLYYKDDKSGKSKEPKGSISLSGCEVVEVVASDS------------PKRK 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 24586311   1187 aletdqESLIIVPNGRTTTVRHLLSADTKEEREEWCAYLNKAL 1229
Cdd:pfam00169   68 ------FCFELRTGERTGKRTYLLQAESEEERKDWIKAIQSAI 104

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 24586311 1109 YKGFLTMFEDISGFGaWHRRWCYLNGSVINYWKYPDDeKRKTPMGSIDLNSCtsqkvttaprdicarlntmlLECERPAL 1188
Cdd:cd00821    1 KEGYLLKRGGGGLKS-WKKRWFVLFEGVLLYYKSKKD-SSYKPKGSIPLSGI--------------------LEVEEVSP 58

                         90       100       110
                 ....*....|....*....|....*....|....
gi 24586311 1189 ETDQESL-IIVPNGRTttvrHLLSADTKEEREEW 1221
Cdd:cd00821   59 KERPHCFeLVTPDGRT----YYLQADSEEERQEW 88

Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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 24586311 1125 WHRRWCYLNGSVINYWKYPDDEKrktPMGSIDLNSCTSQKVTTAPRDIcarlNTMLLEcerpaletdqesliIVPNGRTT 1204
Cdd:cd13263   19 WQQRWFVLRGDQLYYYKDEDDTK---PQGTIPLPGNKVKEVPFNPEEP----GKFLFE--------------IIPGGGGD 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 24586311 1205 TVR-----HLLSADTKEEREEWCAYLNKAL 1229
Cdd:cd13263   78 RMTsnhdsYLLMANSQAEMEEWVKVIRRVI 107

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. 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 24586311 1125 WHRRWCYLNGSVINYWKYPDDEKRKTPMGSIDLNSCTSQKvttAPRDICARLNtmllecerpALETDqesliivpngrTT 1204
Cdd:cd13276   15 WRRRWFVLKQGKLFWFKEPDVTPYSKPRGVIDLSKCLTVK---SAEDATNKEN---------AFELS-----------TP 71

                         90       100
                 ....*....|....*....|....*
gi 24586311 1205 TVRHLLSADTKEEREEWCAYLNKAL 1229
Cdd:cd13276   72 EETFYFIADNEKEKEEWIGAIGRAI 96

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 1; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but 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 24586311 1111 GFLTMFEDISGFgaWHRRWCYLNGSVINYwkYPDDEKRKTPMGSIDLNSCTS----QKVTTAPRDICarlntmllecerp 1186
Cdd:cd13215   25 GYLSKRSKRTLR--YTRYWFVLKGDTLSW--YNSSTDLYFPAGTIDLRYATSielsKSNGEATTSFK------------- 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 24586311 1187 aletdqesliIVPNGRTttvrHLLSADTKEEREEWCAYLNKA 1228
Cdd:cd13215   88 ----------IVTNSRT----YKFKADSETSADEWVKALKKQ 115

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586311   549 TDEDSKRARKSHSDRLYPALSDLDSSGDNCCAAETASATDDSHQQDEEETESCMDESDDQSQTEDSSAGMCNGSLGREIM 628
Cdd:NF033609  722 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 801

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586311   629 SAVQRNEVEMQQQQTGKKTVRYADQDMYYDDSSLNSSQVSAGIDDYLDEALVEDYGSTQDDQSDSGDEQNASRLSLGSKG 708
Cdd:NF033609  802 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNG 881

                  ....*
gi 24586311   709 TTASN 713
Cdd:NF033609  882 TNASN 886

Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian anillin this domain is repeated. This domain overlaps with the region responsible for nuclear localization of anillin.

                           10        20        30
                   ....*....|....*....|....*....|...
gi 24586311    195 SSRQPKQRLGKLAALADTINQWEDDTSHHEVHR 227
Cdd:pfam16018   48 SSETPVGRRGRLANLAATIGSWEDDLSHPSIPQ 80

ArfGAP with dual PH domains Pleckstrin homology (PH) domain, repeat 2; ADAP (also called centaurin alpha) is a phophatidlyinositide binding protein consisting of an N-terminal ArfGAP domain and two PH domains. In response to growth factor activation, PI3K phosphorylates phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 3,4,5-trisphosphate. Centaurin alpha 1 is recruited to the plasma membrane following growth factor stimulation by specific binding of its PH domain to phosphatidylinositol 3,4,5-trisphosphate. Centaurin alpha 2 is constitutively bound to the plasma membrane since it binds phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate with equal affinity. This cd contains the second PH domain 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586311 1124 AWHRRWCYLNGSVINYWKYPDDekrKTPMGSIDLNSCTS-QKVTT-APRDICARlntmllecerpaletDQESLIIVPNG 1201
Cdd:cd01251   18 GFRKRWFTLDDRRLMYFKDPLD---AFPKGEIFIGSKEEgYSVREgLPPGIKGH---------------WGFGFTLVTPD 79

                         90       100
                 ....*....|....*....|....*...
gi 24586311 1202 RTTtvrhLLSADTKEEREEWCAYLNKAL 1229
Cdd:cd01251   80 RTF----LLSAETEEERREWITAIQKVL 103

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 24586311 1110 KGFLTMFEDISGFGAWHRRWCYLNGSVIN-YWKYPDDEKRKTPMGSIDLNSCTsqkvttaprdicaRLNTMLLECERPAl 1188
Cdd:cd13249    5 SGYLSQQQSVEGLQSWTRLYCVLKGGNLLcYYSPEEIEAKVEPLLTIPINKET-------------RIRAVEKDSKGRA- 70

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 24586311 1189 etdqESLIIVPNGRTTTVRHLLSADTKEEREEWCAYL 1225
Cdd:cd13249   71 ----SSLSIINPYSGEEVTHVLSADSREELQKWMEAL 103