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 546231404  945 SVEERGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREFCARRNTFELITVR 1024
Cdd:cd01263     1 SVEYRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCARPNTFLLETLR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 546231404 1025 PQREDDREtlvsqcrDTLCVTKNWLSADTKEERDLWMQKLNQVLVDIR 1072
Cdd:cd01263    81 PAEDDDRD-------DTNEKIRVLLSADTKEERIEWLSALNQTLADLR 121

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        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231404   142 VKTRMQKLAEQRRRWDNDDMTDDIPESSLFSPMPSEEKAASPPRPllSNASATPVGRRGRLANLAATICSWEDDVNHSFA 221
Cdd:pfam16018    1 VKSRMQKLAEQRRRWDNDDWSDDVPESSPVSPLKSEAEAASPPKP--ITSSETPVGRRGRLANLAATIGSWEDDLSHPSI 78

                   ....*...
gi 546231404   222 KQNSVQEQ 229
Cdd:pfam16018   79 PQNPAQEK 86

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 546231404  945 SVEERGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREFCARRNTFELITVR 1024
Cdd:cd01263     1 SVEYRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCARPNTFLLETLR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 546231404 1025 PQREDDREtlvsqcrDTLCVTKNWLSADTKEERDLWMQKLNQVLVDIR 1072
Cdd:cd01263    81 PAEDDDRD-------DTNEKIRVLLSADTKEERIEWLSALNQTLADLR 121

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        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231404   142 VKTRMQKLAEQRRRWDNDDMTDDIPESSLFSPMPSEEKAASPPRPllSNASATPVGRRGRLANLAATICSWEDDVNHSFA 221
Cdd:pfam16018    1 VKSRMQKLAEQRRRWDNDDWSDDVPESSPVSPLKSEAEAASPPKP--ITSSETPVGRRGRLANLAATIGSWEDDLSHPSI 78

                   ....*...
gi 546231404   222 KQNSVQEQ 229
Cdd:pfam16018   79 PQNPAQEK 86

PH domain; PH stands for pleckstrin homology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231404   949 RGFLTIFEDVSGFGaWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREfcARRNTFELITVRPQRe 1028
Cdd:pfam00169    4 EGWLLKKGGGKKKS-WKKRYFVLFDGSLLYYKDDKSGKSKEPKGSISLSGCEVVEVVASDSP--KRKFCFELRTGERTG- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 546231404  1029 ddRETLVsqcrdtlcvtknwLSADTKEERDLWMQKLNQVL 1068
Cdd:pfam00169   80 --KRTYL-------------LQAESEEERKDWIKAIQSAI 104

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 546231404  945 SVEERGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREFCARRNTFELITVR 1024
Cdd:cd01263     1 SVEYRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCARPNTFLLETLR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 546231404 1025 PQREDDREtlvsqcrDTLCVTKNWLSADTKEERDLWMQKLNQVLVDIR 1072
Cdd:cd01263    81 PAEDDDRD-------DTNEKIRVLLSADTKEERIEWLSALNQTLADLR 121

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        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231404   142 VKTRMQKLAEQRRRWDNDDMTDDIPESSLFSPMPSEEKAASPPRPllSNASATPVGRRGRLANLAATICSWEDDVNHSFA 221
Cdd:pfam16018    1 VKSRMQKLAEQRRRWDNDDWSDDVPESSPVSPLKSEAEAASPPKP--ITSSETPVGRRGRLANLAATIGSWEDDLSHPSI 78

                   ....*...
gi 546231404   222 KQNSVQEQ 229
Cdd:pfam16018   79 PQNPAQEK 86

PH domain; PH stands for pleckstrin homology.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231404   949 RGFLTIFEDVSGFGaWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREfcARRNTFELITVRPQRe 1028
Cdd:pfam00169    4 EGWLLKKGGGKKKS-WKKRYFVLFDGSLLYYKDDKSGKSKEPKGSISLSGCEVVEVVASDSP--KRKFCFELRTGERTG- 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 546231404  1029 ddRETLVsqcrdtlcvtknwLSADTKEERDLWMQKLNQVL 1068
Cdd:pfam00169   80 --KRTYL-------------LQAESEEERKDWIKAIQSAI 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 546231404  950 GFLTIFEDVSGFGaWHRRWCVLSGNCISYwTYPDDEKRKNPIGRINLANCTSrqIEPANREfcARRNTFELITvrpqreD 1029
Cdd:cd00821     3 GYLLKRGGGGLKS-WKKRWFVLFEGVLLY-YKSKKDSSYKPKGSIPLSGILE--VEEVSPK--ERPHCFELVT------P 70

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 546231404 1030 DRETLVsqcrdtlcvtknwLSADTKEERDLWMQKL 1064
Cdd:cd00821    71 DGRTYY-------------LQADSEEERQEWLKAL 92

ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP (also called centaurin beta) functions both as a Rab35 effector and as an Arf6-GTPase-activating protein (GAP) by which it controls actin remodeling and membrane trafficking. ACAP contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain, a phospholipid-binding domain, a PH domain, a GAP domain, and four ankyrin repeats. The AZAPs constitute a family of Arf GAPs that are characterized by an NH2-terminal pleckstrin homology (PH) domain and a central Arf GAP domain followed by two or more ankyrin repeats. On the basis of sequence and domain organization, the AZAP family is further subdivided into four subfamilies: 1) the ACAPs contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain (a phospholipid-binding domain that is thought to sense membrane curvature), a single PH domain followed by the GAP domain, and four ankyrin repeats; 2) the ASAPs also contain an NH2-terminal BAR domain, the tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 domain; 3) the AGAPs contain an NH2-terminal GTPase-like domain (GLD), a split PH domain, and the GAP domain followed by four ankyrin repeats; and 4) the ARAPs contain both an Arf GAP domain and a Rho GAP domain, as well as an NH2-terminal sterile-a motif (SAM), a proline-rich region, a GTPase-binding domain, and five PH domains. PMID 18003747 and 19055940 Centaurin can bind to phosphatidlyinositol (3,4,5)P3. 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 546231404  959 SGFGAWHRRWCVLSGNCISYwtYPDDEKRKNPIGRINLANCTSRQIEPANREFCarrntFELITvrPQReddreTLVsqc 1038
Cdd:cd13250    11 NAFKTWKRRWFSLQNGQLYY--QKRDKKDEPTVMVEDLRLCTVKPTEDSDRRFC-----FEVIS--PTK-----SYM--- 73

                          90       100
                  ....*....|....*....|....*..
gi 546231404 1039 rdtlcvtknwLSADTKEERDLWMQKLN 1065
Cdd:cd13250    74 ----------LQAESEEDRQAWIQAIQ 90

Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single 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 546231404  943 NSSVEERGFLtiFEDVSGFGAWHRRWCVLSGNCISYWTYPDDekrKNPIGRINLANCTsrqIEPANrefCARRNTFELIT 1022
Cdd:cd13288     5 NSPVDKEGYL--WKKGERNTSYQKRWFVLKGNLLFYFEKKGD---REPLGVIVLEGCT---VELAE---DAEPYAFAIRF 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 546231404 1023 vrpQREDDReTLVsqcrdtlcvtknwLSADTKEERDLWMQKL 1064
Cdd:cd13288    74 ---DGPGAR-SYV-------------LAAENQEDMESWMKAL 98

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 546231404  950 GFLTIFEDVSGFGAWHRRWCVLSGNCIS-YWTYPDDEKRKNPIGRINLANCTsrQIEPANREFCARRNTFELITVRPqre 1028
Cdd:cd13249     6 GYLSQQQSVEGLQSWTRLYCVLKGGNLLcYYSPEEIEAKVEPLLTIPINKET--RIRAVEKDSKGRASSLSIINPYS--- 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 546231404 1029 DDRETLVsqcrdtlcvtknwLSADTKEERDLWMQKLNQVLVD 1070
Cdd:cd13249    81 GEEVTHV-------------LSADSREELQKWMEALWQHFYD 109

Bud emergence protein 3 (Bem3) Pleckstrin homology (PH) domain; Bud emergence in Saccharomyces cerevisiae involves cell cycle-regulated reorganizations of cortical cytoskeletal elements and requires the action of the Rho-type GTPase Cdc42. Bem3 contains a RhoGAP domain and a PH domain. Though Bem3 and Bem2 both contain a RhoGAP, but only Bem3 is able to stimulate the hydrolysis of GTP on Cdc42. Bem3 is thought to be the GAP for Cdc42. 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 546231404  959 SGFGAWHRRWCVLSGNCISYWtypddEKRKNP-IGRINLANCTSRQIEPANREFCARRNTFeLITvrpqrEDDRETLVSQ 1037
Cdd:cd13277    18 GSTGGWKLRYGVLDGNILELY-----ESRGGQlLESIKLRNAQIERQPNLPDDKYGTRHGF-LIN-----EHKKSGLSST 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 546231404 1038 CRDTLCvtknwlsADTKEERDLWMQKLNQVL 1068
Cdd:cd13277    87 TKYYLC-------AETDKERDEWVSALSEYI 110

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 546231404  925 PFLSSLEGHIylkIKCqvnssveerGFLTIFEDVSGFgaWHRRWCVLSGNCISYwtYPDDEKRKNPIGRINLANCTSRQI 1004
Cdd:cd13215    12 AYLPKRSGAV---IKS---------GYLSKRSKRTLR--YTRYWFVLKGDTLSW--YNSSTDLYFPAGTIDLRYATSIEL 75

                          90
                  ....*....|....*...
gi 546231404 1005 EPANREfcaRRNTFELIT 1022
Cdd:cd13215    76 SKSNGE---ATTSFKIVT 90

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
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 546231404  964 WHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSrqIEPANREFcARRNTFELIT 1022
Cdd:cd13276    15 WRRRWFVLKQGKLFWFKEPDVTPYSKPRGVIDLSKCLT--VKSAEDAT-NKENAFELST 70

Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; DAPP1 (also known as PHISH/3' phosphoinositide-interacting SH2 domain-containing protein or Bam32) plays a role in B-cell activation and has potential roles in T-cell and mast cell function. DAPP1 promotes B cell receptor (BCR) induced activation of Rho GTPases Rac1 and Cdc42, which feed into mitogen-activated protein kinases (MAPK) activation pathways and affect cytoskeletal rearrangement. DAPP1can also regulate BCR-induced activation of extracellular signal-regulated kinase (ERK), and c-jun NH2-terminal kinase (JNK). DAPP1 contains an N-terminal SH2 domain and a C-terminal pleckstrin homology (PH) domain with a single tyrosine phosphorylation site located centrally. DAPP1 binds strongly to both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The PH domain is essential for plasma membrane recruitment of PI3K upon cell activation. 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.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231404  964 WHRRWCVLSGNCISYWTYPDDEKrknPIGRINLANCTSRQIEPAnrefCARRNTFELitVRPQREddretlvsqcrdtlc 1043
Cdd:cd10573    19 WKTRWFVLRRNELKYFKTRGDTK---PIRVLDLRECSSVQRDYS----QGKVNCFCL--VFPERT--------------- 74

                          90       100
                  ....*....|....*....|..
gi 546231404 1044 vtkNWLSADTKEERDLWMQKLN 1065
Cdd:cd10573    75 ---FYMYANTEEEADEWVKLLK 93

ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 1; ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the first PH domain in ARAP. 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 546231404  964 WHRRWCVLSGNCISYWtypDDEKRKNPIGRINLAnCTSRQIEPANrefcarrNTFELITVrpQReddreTLVsqcrdtlc 1043
Cdd:cd13253    18 FQKRWVVFDGLSLRYF---DSEKDAYSKRIIPLS-AISTVRAVGD-------NKFELVTT--NR-----TFV-------- 71

                          90       100
                  ....*....|....*....|....*
gi 546231404 1044 vtknwLSADTKEERDLWMQKLNQVL 1068
Cdd:cd13253    72 -----FRAESDDERNLWCSTLQAAI 91