Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 2; There are 3 members of the AFAP family of adaptor proteins: AFAP1, AFAP1L1, and AFAP1L2/XB130. AFAP1 is a cSrc binding partner and actin cross-linking protein. AFAP1L1 is thought to play a similar role to AFAP1 in terms of being an actin cross-linking protein, but it preferentially binds to cortactin and not cSrc, thereby playing a role in invadosome formation. AFAP1L2 is a cSrc binding protein, but does not bind to actin filaments. AFAP1L2 acts as an intermediary between the RET/PTC kinase and PI-3kinase pathway in the thyroid. The AFAPs share a similar structure of a SH3 binding motif, 3 SH2 binding motifs, 2 PH domains, a coiled-coil region corresponding to the AFAP1 leucine zipper, and an actin binding domain. This cd is the second PH domain of AFAP. 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 1907132330 418 SLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDRNRSKVAQQPLSLVGCDVLPDPSPDHLYSFRILHNGEELAKLEAKSS 497
Cdd:cd13307     1 GVPTCGYLNVLVNQQWRSRWCCVKDGQLHFYQDRNKTKSPQQSLPLHGCEVVPGPDPKHPYSFRILRNGEEVAALEASSS 80

                          90       100
                  ....*....|....*....|.
gi 1907132330 498 EEMGHWLGLLLSESGSKTDPE 518
Cdd:cd13307    81 EDMGRWLGVLLAETGSATDPE 101

capsid maturational protease; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132330 535 SAAKTSLLLMQRKFSEpntyIDGLPSRDcqddlyddvEVSELIAVVEPAEEAAPAVDANSGSEPDRVYldltpvksflhS 614
Cdd:PHA03369  322 TVIEQYLIEGRKLFST----INGLKAHN---------EILKTASLTAPSRVLAAAAKVAVIAAPQTHT-----------G 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132330 615 SSEAQAQASLPAVPHQDDVAETLTVDPKPGTTPEEPHTESPGDP--EVQQRQPEVQESSEPIEPTPRITmvklqaeqqri 692
Cdd:PHA03369  378 PADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPGLVSPYNPqsPGTSYGPEPVGPVPPQPTNPYVM----------- 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132330 693 sfpancPDTMASAPIAASPPVKEKLRVTSAEIKLGKNRTE--AEVKRYTEEKERLERSKEEirghLAQLRREKRELKETL 770
Cdd:PHA03369  447 ------PISMANMVYPGHPQEHGHERKRKRGGELKEELIEtlKLVKKLKEEQESLAKELEA----TAHKSEIKKIAESEF 516

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132330 771 LRCTDKGVLAKLEQTLKKIDEECRMEESRRVDLE--LSIMEVKDNLKKAEAGPVTLGTTVDT---------THLDNMSP- 838
Cdd:PHA03369  517 KNAGAKTAAANIEPNCSADAAAPATKRARPETKTelEAVVRFPYQIRNMESPAFVHSFTSTTlaaaagqgsDTAEALAGa 596

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1907132330 839 -RPQPKAATPNPPPDSTPVNSASVLKNRPLSV 869
Cdd:PHA03369  597 iETLLTQASAQPAGLSLPAPAVPVNASTPAST 628

Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 2; There are 3 members of the AFAP family of adaptor proteins: AFAP1, AFAP1L1, and AFAP1L2/XB130. AFAP1 is a cSrc binding partner and actin cross-linking protein. AFAP1L1 is thought to play a similar role to AFAP1 in terms of being an actin cross-linking protein, but it preferentially binds to cortactin and not cSrc, thereby playing a role in invadosome formation. AFAP1L2 is a cSrc binding protein, but does not bind to actin filaments. AFAP1L2 acts as an intermediary between the RET/PTC kinase and PI-3kinase pathway in the thyroid. The AFAPs share a similar structure of a SH3 binding motif, 3 SH2 binding motifs, 2 PH domains, a coiled-coil region corresponding to the AFAP1 leucine zipper, and an actin binding domain. This cd is the second PH domain of AFAP. 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 1907132330 418 SLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDRNRSKVAQQPLSLVGCDVLPDPSPDHLYSFRILHNGEELAKLEAKSS 497
Cdd:cd13307     1 GVPTCGYLNVLVNQQWRSRWCCVKDGQLHFYQDRNKTKSPQQSLPLHGCEVVPGPDPKHPYSFRILRNGEEVAALEASSS 80

                          90       100
                  ....*....|....*....|.
gi 1907132330 498 EEMGHWLGLLLSESGSKTDPE 518
Cdd:cd13307    81 EDMGRWLGVLLAETGSATDPE 101

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 1907132330  227 FLWRKKW--LGQWAKQLCVIRDTRLLCYKSSK---DHSPQLDVNLRGSSVVH-KEKQVRKKGHKLKITPMNADVIVLGLQ 300
Cdd:smart00233   6 WLYKKSGggKKSWKKRYFVLFNSTLLYYKSKKdkkSYKPKGSIDLSGCTVREaPDPDSSKKPHCFEIKTSDRKTLLLQAE 85

                           90
                   ....*....|....*.
gi 1907132330  301 SKDQAEQWLRVIQEVS 316
Cdd:smart00233  86 SEEEREKWVEALRKAI 101

PH domain; PH stands for pleckstrin homology.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132330 217 ELMRDARICAFLWRKKWlgqwakqlCVIRDTRLLCYKSS---KDHSPQLDVNLRGSSVVHKEKQV---RKKGHKLKITPM 290
Cdd:pfam00169   6 WLLKKGGGKKKSWKKRY--------FVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDspkRKFCFELRTGER 77

                          90       100
                  ....*....|....*....|....*..
gi 1907132330 291 -NADVIVLGLQSKDQAEQWLRVIQEVS 316
Cdd:pfam00169  78 tGKRTYLLQAESEEERKDWIKAIQSAI 104

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132330 714 KEKLRVTSAEIKLGK-NRTEAEVKRYTEEKERLERSKEEIRGHLAQLRREKRELKETLLRCTDK-----GVLAKLEQTLK 787
Cdd:COG1196   219 KEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeaqAEEYELLAELA 298

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907132330 788 KIDEECRMEESRRVDLELSIMEVKDNLKKAEA 819
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELAELEE 330

Cortexillin I, coiled coil; Members of this family are predominantly found in the actin-bundling protein Cortexillin I from Dictyostelium discoideum. They adopt a structure consisting of an 18-heptad-repeat alpha-helical coiled-coil, and are a prerequisite for the assembly of Cortexillin I.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132330 740 EEKERLERSKEEIRGHLA--------------QLRREKRELKETLLRCTDKG---------VLAKLEQTLKKIDEE--CR 794
Cdd:pfam09304   2 EEKERLEASKNSLANKLAglenslesektsreQLIKQKDELESLLASLEQENaerekrlreLEAKLDEALKNLELEklAR 81

                          90       100
                  ....*....|....*....|....*.
gi 1907132330 795 ME-ESR-------RVDLELSIMEVKD 812
Cdd:pfam09304  82 MElESRlsktekdKAILELKLAEALD 107

Actin filament associated protein family Pleckstrin homology (PH) domain, repeat 2; There are 3 members of the AFAP family of adaptor proteins: AFAP1, AFAP1L1, and AFAP1L2/XB130. AFAP1 is a cSrc binding partner and actin cross-linking protein. AFAP1L1 is thought to play a similar role to AFAP1 in terms of being an actin cross-linking protein, but it preferentially binds to cortactin and not cSrc, thereby playing a role in invadosome formation. AFAP1L2 is a cSrc binding protein, but does not bind to actin filaments. AFAP1L2 acts as an intermediary between the RET/PTC kinase and PI-3kinase pathway in the thyroid. The AFAPs share a similar structure of a SH3 binding motif, 3 SH2 binding motifs, 2 PH domains, a coiled-coil region corresponding to the AFAP1 leucine zipper, and an actin binding domain. This cd is the second PH domain of AFAP. 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 1907132330 418 SLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDRNRSKVAQQPLSLVGCDVLPDPSPDHLYSFRILHNGEELAKLEAKSS 497
Cdd:cd13307     1 GVPTCGYLNVLVNQQWRSRWCCVKDGQLHFYQDRNKTKSPQQSLPLHGCEVVPGPDPKHPYSFRILRNGEEVAALEASSS 80

                          90       100
                  ....*....|....*....|.
gi 1907132330 498 EEMGHWLGLLLSESGSKTDPE 518
Cdd:cd13307    81 EDMGRWLGVLLAETGSATDPE 101

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 1907132330  430 NSQWKSRWCFVRDSHLHFYQDR--NRSKVAQQPLSLVGCDVLPDPSPDHL---YSFRILHNGEELAKLEAKSSEEMGHWL 504
Cdd:smart00233  15 KKSWKKRYFVLFNSTLLYYKSKkdKKSYKPKGSIDLSGCTVREAPDPDSSkkpHCFEIKTSDRKTLLLQAESEEEREKWV 94

PH domain; PH stands for pleckstrin homology.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132330 431 SQWKSRWCFVRDSHLHFYQDR--NRSKVAQQPLSLVGC---DVLPDPSPDHLYSFRILH---NGEELAKLEAKSSEEMGH 502
Cdd:pfam00169  16 KSWKKRYFVLFDGSLLYYKDDksGKSKEPKGSISLSGCevvEVVASDSPKRKFCFELRTgerTGKRTYLLQAESEEERKD 95

                  ..
gi 1907132330 503 WL 504
Cdd:pfam00169  96 WI 97

SH3 domain-binding protein 2 Pleckstrin homology (PH) domain; SH3BP2 (the gene that encodes the adaptor protein 3BP2), HD, ITU, IT10C3, and ADD1 are located near the Huntington's Disease Gene on Human Chromosome 4pl6.3. SH3BP2 lies in a region that is often missing in individuals with Wolf-Hirschhorn syndrome (WHS). Gain of function mutations in SH3BP2 causes enhanced B-cell antigen receptor (BCR)-mediated activation of nuclear factor of activated T cells (NFAT), resulting in a rare, genetic disorder called cherubism. This results in an increase in the signaling complex formation with Syk, phospholipase C-gamma2 (PLC-gamma2), and Vav1. It was recently discovered that Tankyrase regulates 3BP2 stability through ADP-ribosylation and ubiquitylation by the E3-ubiquitin ligase. Cherubism mutations uncouple 3BP2 from Tankyrase-mediated protein destruction, which results in its stabilization and subsequent hyperactivation of the Src, Syk, and Vav signaling pathways. SH3BP2 is also a potential negative regulator of the abl oncogene. 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 1907132330 214 ASIELMRDARICAFLWRK----KWLGQWAKQLCVIRDTRLLCYKSSKDHSPQLDVNLRGSSVVHKEKQVRKKGHKLKITP 289
Cdd:cd13308     1 QLLTLPRDVIHSGTLTKKggsqKTLQNWQLRYVIIHQGCVYYYKNDQSAKPKGVFSLNGYNRRAAEERTSKLKFVFKIIH 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907132330 290 MNADVIVLGLQSKDQAEQ--WLRVIQEVSG 317
Cdd:cd13308    81 LSPDHRTWYFAAKSEDEMseWMEYIRREID 110

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. 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 1907132330 416 ERSLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDRNRSKVAQ-----QPLSLVG--CDVLPDpspdhlY-----SFRI- 482
Cdd:cd10571     6 ERKHEWESGGKKASNRSWKNVYTVLRGQELSFYKDQKAAKSGItyaaePPLNLYNavCEVASD------YtkkkhVFRLk 79

                          90       100
                  ....*....|....*....|..
gi 1907132330 483 LHNGEELAkLEAKSSEEMGHWL 504
Cdd:cd10571    80 LSDGAEFL-FQAKDEEEMNQWV 100

Fermitin family pleckstrin homology (PH) domain; Fermitin functions as a mediator of integrin inside-out signalling. The recruitment of Fermitin proteins and Talin to the membrane mediates the terminal event of integrin signalling, via interaction with integrin beta subunits. Fermatin has FERM domain interrupted with a pleckstrin homology (PH) domain. Fermitin family homologs (Fermt1, 2, and 3, also known as Kindlins) are each encoded by a different gene. In mammalian studies, Fermt1 is generally expressed in epithelial cells, Fermt2 is expressed inmuscle tissues, and Fermt3 is expressed in hematopoietic lineages. Specifically Fermt2 is expressed in smooth and striated muscle tissues in mice and in the somites (a trunk muscle precursor) and neural crest in Xenopus embryos. As such it has been proposed that Fermt2 plays a role in cardiomyocyte and neural crest differentiation. Expression of mammalian Fermt3 is associated with hematopoietic lineages: the anterior ventral blood islands, vitelline veins, and early myeloid cells. In Xenopus embryos this expression, also include the notochord and cement gland. 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907132330 433 WKSRWCFVRDSHLHFYQDRNRSK-VAQQPLSLVGCDVLPDPSpdhlysfriLHNGEELAKLEAKSSEEM-GHWL 504
Cdd:cd01237    20 YKRYWFVFKDTHLSYYKSKEESNgAPIQQINLKGCEVTPDVN---------VSQQKFCIKLLVPSPEGMsEVWL 84

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907132330 432 QWKSRWCFVRDSHLHFYQDRNrSKVAQQPLSLVGCDVLPDPSPDHL---YSFRILHNGEELAKLEAKSSEEMGHWL 504
Cdd:cd13248    23 NWRKRWFVLKDNCLYYYKDPE-EEKALGSILLPSYTISPAPPSDEIsrkFAFKAEHANMRTYYFAADTAEEMEQWM 97

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132330 714 KEKLRVTSAEIKLGKNRTEAEVKRYTEEKERLERSKEEI---RGHLAQLRREKRELKETllrctdkgvLAKLEQTLKKID 790
Cdd:COG2433   384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVerlEAEVEELEAELEEKDER---------IERLERELSEAR 454

                          90       100
                  ....*....|....*....|....*..
gi 1907132330 791 EECRMEEsrRVDLELSIMEVK-DNLKK 816
Cdd:COG2433   455 SEERREI--RKDREISRLDREiERLER 479

Cortexillin I, coiled coil; Members of this family are predominantly found in the actin-bundling protein Cortexillin I from Dictyostelium discoideum. They adopt a structure consisting of an 18-heptad-repeat alpha-helical coiled-coil, and are a prerequisite for the assembly of Cortexillin I.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132330 740 EEKERLERSKEEIRGHLA--------------QLRREKRELKETLLRCTDKG---------VLAKLEQTLKKIDEE--CR 794
Cdd:pfam09304   2 EEKERLEASKNSLANKLAglenslesektsreQLIKQKDELESLLASLEQENaerekrlreLEAKLDEALKNLELEklAR 81

                          90       100
                  ....*....|....*....|....*.
gi 1907132330 795 ME-ESR-------RVDLELSIMEVKD 812
Cdd:pfam09304  82 MElESRlsktekdKAILELKLAEALD 107

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132330 715 EKLRVTSAEIKLGKNRtEAEVKRYTEEKERLERSKEEIRGHLAQLRREKRELKETLLRCTDKGVLAKLEQTLKKID---E 791
Cdd:COG4717    71 KELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPerlE 149

                          90       100
                  ....*....|....*....|....*...
gi 1907132330 792 ECRMEESRRVDLELSIMEVKDNLKKAEA 819
Cdd:COG4717   150 ELEERLEELRELEEELEELEAELAELQE 177

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH 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 1907132330 229 WRKKWLgqwakqlcVIRDTRLLCYKSSKDHSPQLDVNLRGSSVVHKEKqVRKKGHKLKI-TPMNadviVLGLQSKDQAE- 306
Cdd:cd13298    22 WKKRWV--------VLRPCQLSYYKDEKEYKLRRVINLSELLAVAPLK-DKKRKNVFGIyTPSK----NLHFRATSEKDa 88

                          90
                  ....*....|....*.
gi 1907132330 307 -QWLRVIQEVSGLPSE 321
Cdd:cd13298    89 nEWVEALREEFRLDDE 104