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 1907132344 200 SLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDRNRSKVAQQPLSLVGCDVLPDPSPDHLYSFRILHNGEELAKLEAKSS 279
Cdd:cd13307     1 GVPTCGYLNVLVNQQWRSRWCCVKDGQLHFYQDRNKTKSPQQSLPLHGCEVVPGPDPKHPYSFRILRNGEEVAALEASSS 80

                          90       100
                  ....*....|....*....|.
gi 1907132344 280 EEMGHWLGLLLSESGSKTDPE 300
Cdd:cd13307    81 EDMGRWLGVLLAETGSATDPE 101

DNA double-strand break repair ATPase Rad50;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 496 KEKLRVTSAEIKLGKNRTEAEVKRYTEEKERLERSKEEIRGHLAQLRREKRELKETLLRCTDKGV-LAKLEQTLKKIDEE 574
Cdd:PRK03918  181 LEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKeLESLEGSKRKLEEK 260

                          90       100
                  ....*....|....*....|....*.
gi 1907132344 575 CRMEESRRVDLELSIMEVKDNLKKAE 600
Cdd:PRK03918  261 IRELEERIEELKKEIEELEEKVKELK 286

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 1907132344 200 SLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDRNRSKVAQQPLSLVGCDVLPDPSPDHLYSFRILHNGEELAKLEAKSS 279
Cdd:cd13307     1 GVPTCGYLNVLVNQQWRSRWCCVKDGQLHFYQDRNKTKSPQQSLPLHGCEVVPGPDPKHPYSFRILRNGEEVAALEASSS 80

                          90       100
                  ....*....|....*....|.
gi 1907132344 280 EEMGHWLGLLLSESGSKTDPE 300
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 1907132344  212 NSQWKSRWCFVRDSHLHFYQDR--NRSKVAQQPLSLVGCDVLPDPSPDHL---YSFRILHNGEELAKLEAKSSEEMGHWL 286
Cdd:smart00233  15 KKSWKKRYFVLFNSTLLYYKSKkdKKSYKPKGSIDLSGCTVREAPDPDSSkkpHCFEIKTSDRKTLLLQAESEEEREKWV 94

PH domain; PH stands for pleckstrin homology.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 213 SQWKSRWCFVRDSHLHFYQDR--NRSKVAQQPLSLVGC---DVLPDPSPDHLYSFRILH---NGEELAKLEAKSSEEMGH 284
Cdd:pfam00169  16 KSWKKRYFVLFDGSLLYYKDDksGKSKEPKGSISLSGCevvEVVASDSPKRKFCFELRTgerTGKRTYLLQAESEEERKD 95

                  ..
gi 1907132344 285 WL 286
Cdd:pfam00169  96 WI 97

DNA double-strand break repair ATPase Rad50;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 496 KEKLRVTSAEIKLGKNRTEAEVKRYTEEKERLERSKEEIRGHLAQLRREKRELKETLLRCTDKGV-LAKLEQTLKKIDEE 574
Cdd:PRK03918  181 LEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKeLESLEGSKRKLEEK 260

                          90       100
                  ....*....|....*....|....*.
gi 1907132344 575 CRMEESRRVDLELSIMEVKDNLKKAE 600
Cdd:PRK03918  261 IRELEERIEELKKEIEELEEKVKELK 286

capsid maturational protease; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 317 SAAKTSLLLMQRKFSEpntyIDGLPSRDcqddlyddvEVSELIAVVEPAEEAAPAVDANSGSEPDRVYldltpvksflhS 396
Cdd:PHA03369  322 TVIEQYLIEGRKLFST----INGLKAHN---------EILKTASLTAPSRVLAAAAKVAVIAAPQTHT-----------G 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 397 SSEAQAQASLPAVPHQDDVAETLTVDPKPGTTPEEPHTESPGDP--EVQQRQPEVQESSEPIEPTPRITmvklqaeqqri 474
Cdd:PHA03369  378 PADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPGLVSPYNPqsPGTSYGPEPVGPVPPQPTNPYVM----------- 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 475 sfpancPDTMASAPIAASPPVKEKLRVTSAEIKLGKNRTE--AEVKRYTEEKERLERSKEEirghLAQLRREKRELKETL 552
Cdd:PHA03369  447 ------PISMANMVYPGHPQEHGHERKRKRGGELKEELIEtlKLVKKLKEEQESLAKELEA----TAHKSEIKKIAESEF 516

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 553 LRCTDKGVLAKLEQTLKKIDEECRMEESRRVDLE--LSIMEVKDNLKKAEAGPVTLGTTVDT---------THLDNMSP- 620
Cdd:PHA03369  517 KNAGAKTAAANIEPNCSADAAAPATKRARPETKTelEAVVRFPYQIRNMESPAFVHSFTSTTlaaaagqgsDTAEALAGa 596

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1907132344 621 -RPQPKAATPNPPPDSTPVNSASVLKNRPLSV 651
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 1907132344 200 SLETSSYLNVLVNSQWKSRWCFVRDSHLHFYQDRNRSKVAQQPLSLVGCDVLPDPSPDHLYSFRILHNGEELAKLEAKSS 279
Cdd:cd13307     1 GVPTCGYLNVLVNQQWRSRWCCVKDGQLHFYQDRNKTKSPQQSLPLHGCEVVPGPDPKHPYSFRILRNGEEVAALEASSS 80

                          90       100
                  ....*....|....*....|.
gi 1907132344 280 EEMGHWLGLLLSESGSKTDPE 300
Cdd:cd13307    81 EDMGRWLGVLLAETGSATDPE 101

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 1907132344 212 NSQWKSRWCFVRDSHLHFYQDRN-RSKVAQQPLSLVG-CDVLPDPSPDHLYSFRILHNGEELAKLEAKSSEEMGHWLGLL 289
Cdd:cd00821    13 LKSWKKRWFVLFEGVLLYYKSKKdSSYKPKGSIPLSGiLEVEEVSPKERPHCFELVTPDGRTYYLQADSEEERQEWLKAL 92

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 1907132344    9 FLWRKKW--LGQWAKQLCVIRDTRLLCYKSSK---DHSPQLDVNLRGSSVVH-KEKQVRKKGHKLKITPMNADVIVLGLQ 82
Cdd:smart00233   6 WLYKKSGggKKSWKKRYFVLFNSTLLYYKSKKdkkSYKPKGSIDLSGCTVREaPDPDSSKKPHCFEIKTSDRKTLLLQAE 85

                           90
                   ....*....|....*.
gi 1907132344   83 SKDQAEQWLRVIQEVS 98
Cdd:smart00233  86 SEEEREKWVEALRKAI 101

PH domain; PH stands for pleckstrin homology.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344   1 MRDARICAFLWRKKWlgqwakqlCVIRDTRLLCYKSS---KDHSPQLDVNLRGSSVVHKEKQV---RKKGHKLKITPM-N 73
Cdd:pfam00169   8 LKKGGGKKKSWKKRY--------FVLFDGSLLYYKDDksgKSKEPKGSISLSGCEVVEVVASDspkRKFCFELRTGERtG 79

                          90       100
                  ....*....|....*....|....*
gi 1907132344  74 ADVIVLGLQSKDQAEQWLRVIQEVS 98
Cdd:pfam00169  80 KRTYLLQAESEEERKDWIKAIQSAI 104

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 1907132344   1 MRDARICAFLWRK----KWLGQWAKQLCVIRDTRLLCYKSSKDHSPQLDVNLRGSSVVHKEKQVRKKGHKLKITPMNADV 76
Cdd:cd13308     6 PRDVIHSGTLTKKggsqKTLQNWQLRYVIIHQGCVYYYKNDQSAKPKGVFSLNGYNRRAAEERTSKLKFVFKIIHLSPDH 85

                          90       100
                  ....*....|....*....|....*
gi 1907132344  77 IVLGLQSKDQAEQ--WLRVIQEVSG 99
Cdd:cd13308    86 RTWYFAAKSEDEMseWMEYIRREID 110

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 1907132344 215 WKSRWCFVRDSHLHFYQDRNRSK-VAQQPLSLVGCDVLPDPSpdhlysfriLHNGEELAKLEAKSSEEM-GHWL 286
Cdd:cd01237    20 YKRYWFVFKDTHLSYYKSKEESNgAPIQQINLKGCEVTPDVN---------VSQQKFCIKLLVPSPEGMsEVWL 84

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 1907132344 213 SQWKSRWCFVRDSHLHFYQDRNRSK-VAQQPLS-LVGCDVLPDPSPDH---LYS-FRILHngeelakLEAKSSEEMGHWL 286
Cdd:cd13298    20 KNWKKRWVVLRPCQLSYYKDEKEYKlRRVINLSeLLAVAPLKDKKRKNvfgIYTpSKNLH-------FRATSEKDANEWV 92

                          90
                  ....*....|....
gi 1907132344 287 GLLLSESGSKTDPE 300
Cdd:cd13298    93 EALREEFRLDDEEE 106

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 496 KEKLRVTSAEIKLGK-NRTEAEVKRYTEEKERLERSKEEIRGHLAQLRREKRELKETLLRCTDK-----GVLAKLEQTLK 569
Cdd:COG1196   219 KEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeaqAEEYELLAELA 298

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907132344 570 KIDEECRMEESRRVDLELSIMEVKDNLKKAEA 601
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELAELEE 330

capsid maturational protease; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 317 SAAKTSLLLMQRKFSEpntyIDGLPSRDcqddlyddvEVSELIAVVEPAEEAAPAVDANSGSEPDRVYldltpvksflhS 396
Cdd:PHA03369  322 TVIEQYLIEGRKLFST----INGLKAHN---------EILKTASLTAPSRVLAAAAKVAVIAAPQTHT-----------G 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 397 SSEAQAQASLPAVPHQDDVAETLTVDPKPGTTPEEPHTESPGDP--EVQQRQPEVQESSEPIEPTPRITmvklqaeqqri 474
Cdd:PHA03369  378 PADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPGLVSPYNPqsPGTSYGPEPVGPVPPQPTNPYVM----------- 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 475 sfpancPDTMASAPIAASPPVKEKLRVTSAEIKLGKNRTE--AEVKRYTEEKERLERSKEEirghLAQLRREKRELKETL 552
Cdd:PHA03369  447 ------PISMANMVYPGHPQEHGHERKRKRGGELKEELIEtlKLVKKLKEEQESLAKELEA----TAHKSEIKKIAESEF 516

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 553 LRCTDKGVLAKLEQTLKKIDEECRMEESRRVDLE--LSIMEVKDNLKKAEAGPVTLGTTVDT---------THLDNMSP- 620
Cdd:PHA03369  517 KNAGAKTAAANIEPNCSADAAAPATKRARPETKTelEAVVRFPYQIRNMESPAFVHSFTSTTlaaaagqgsDTAEALAGa 596

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1907132344 621 -RPQPKAATPNPPPDSTPVNSASVLKNRPLSV 651
Cdd:PHA03369  597 iETLLTQASAQPAGLSLPAPAVPVNASTPAST 628

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 1907132344 522 EEKERLERSKEEIRGHLA--------------QLRREKRELKETLLRCTDKG---------VLAKLEQTLKKIDEE--CR 576
Cdd:pfam09304   2 EEKERLEASKNSLANKLAglenslesektsreQLIKQKDELESLLASLEQENaerekrlreLEAKLDEALKNLELEklAR 81

                          90       100
                  ....*....|....*....|....*.
gi 1907132344 577 ME-ESR-------RVDLELSIMEVKD 594
Cdd:pfam09304  82 MElESRlsktekdKAILELKLAEALD 107

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344 465 VKLQAEQQRISFPANCPDTMASAPIAASPPVKEKLRVTSAEIKlGKNRTEAEVKRyTEEKERLERSKEEIRGHLAQLRRE 544
Cdd:pfam11600   7 VQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEK-ERAKEEARRKK-EEEKELKEKERREKKEKDEKEKAE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907132344 545 KRELKETLLRCTDKGVLAKLEQTLKKIDEECRMEESRRVDLE 586
Cdd:pfam11600  85 KLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAE 126

ribonuclease E; Reviewed

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344  350 YDDVEVSELIAVVEPAEEAAPAVDANSGSEPDRVYLDLTPVKsflhsssEAQAQASlpAVPHQDDVAETLTVDPKPGTTP 429
Cdd:PRK10811   909 VVVVETTHPEVIAAPVTEQPQVITESDVAVAQEVAEHAEPVV-------EPQDETA--DIEEAAETAEVVVAEPEVVAQP 979

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132344  430 EEPHTESPgdpevqqRQPEVQESSEPIEPTPritmvKLQAEQQRISFPANCPDTMASAP-IAASPPV 495
Cdd:PRK10811   980 AAPVVAEV-------AAEVETVTAVEPEVAP-----AQVPEATVEHNHATAPMTRAPAPeYVPEAPR 1034

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132344  10 LWRKKWlgqwakqlCVIRDTRLLCYKSSKDHSPQLDVNLRGSSV--VHKEKQVRKKgHKLKITPMNADVIVLGLQSKDQA 87
Cdd:cd13248    23 NWRKRW--------FVLKDNCLYYYKDPEEEKALGSILLPSYTIspAPPSDEISRK-FAFKAEHANMRTYYFAADTAEEM 93

                          90
                  ....*....|.
gi 1907132344  88 EQWLRVIQEVS 98
Cdd:cd13248    94 EQWMNAMSLAA 104