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Conserved domains on  [gi|2075918467|gb|KAG8455845|]
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hypothetical protein GDO86_001878 [Hymenochirus boettgeri]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_BCR_vertebrate cd13367
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
 576-769 3.03e-127

Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. This hierarchy is composed of vertebrate BCRs. 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.


:

Pssm-ID: 270173  Cd Length: 194  Bit Score: 387.44  E-value: 3.03e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  576 FLSSINEEITPRRQSMTVRKGEHRQLLKDSFMVELIEGSRKLRHVFLFTDLLLCAKLKKQLGGKSQQYDCKWYIPLADLN 655
Cdd:cd13367      1 FLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCAKLKKQIGGKSQQYDCKWYIPLADLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  656 FQPIDESESCSNIPLIPDEELEAIKVKISQLKSDIQREKKANKGGKGLDRLRKKLSEQESVLLLLSPSMAFRIQNRNGKG 735
Cdd:cd13367     81 FQTVDESEAVPNIPLIPDEEIDALKVKISQIKSDIQREKRANKGGKVLERLRKKLSEQESLLLLMSPSMAFRVHNRNGKS 160

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2075918467  736 YTLLTWSDYERAEWGEHIREQQKKCFKSFSLSSL 769
Cdd:cd13367    161 YTFLISSDYERAEWRENIREQQKKCFKSFSLTSL 194
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 945-1145 4.09e-121

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


:

Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 371.18  E-value: 4.09e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDVSVIMSDMDVNAIAGTLKLY 1024
Cdd:cd04387      1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEMDVNAIAGTLKLY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1025 FRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTL 1104
Cdd:cd04387     81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2075918467 1105 LRPSEKDSKIPANptqpiSMADSWSLEVMSQVQVLLYFLQL 1145
Cdd:cd04387    161 LRPSEKESKIPTN-----TMTDSWSLEVMSQVQVLLYFLQL 196
C2_ABR cd08686
C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is ...
 805-926 4.15e-61

C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is similar to the breakpoint cluster region protein. It has homology to guanine nucleotide exchange proteins and GTPase-activating proteins (GAPs). ABR is expressed primarily in the brain, but also includes non-neuronal tissues such as the heart. It has been associated with human diseases such as Miller-Dieker syndrome in which mental retardation and malformations of the heart are present. ABR contains a RhoGEF domain and a PH-like domain upstream of its C2 domain and a RhoGAP domain downstream of this domain. A few members also contain a Bcr-Abl oncoprotein oligomerization domain at the very N-terminal end. Splice variants of ABR have been identified. ABR is found in a wide variety of organisms including chimpanzee, dog, mouse, rat, fruit fly, and mosquito. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 176068  Cd Length: 118  Bit Score: 203.89  E-value: 4.15e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  805 LNVIVHSATGYQQSSNLFCTLEVDSFGYFVNKAKTRVYRNTTEPNWNEEFEIELEGSQTLRILCYEKSYNrnrNVKEDGG 884
Cdd:cd08686      1 LNVIVHSAQGFKQSANLYCTLEVDSFGYFVKKAKTRVCRDTTEPNWNEEFEIELEGSQTLRILCYEKCYS---KVKLDGE 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2075918467  885 DTsERIVAKGQVQLESQLALGKDWQRSVVSMNGIEVKLSMKF 926
Cdd:cd08686     78 GT-DAIMGKGQIQLDPQSLQTKKWQEKVISMNGITVNLSIKF 118
Bcr-Abl_Oligo pfam09036
Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain ...
 3-75 1.68e-41

Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain consists of a short N-terminal helix (alpha-1), a flexible loop and a long C-terminal helix (alpha-2). Together these form an N-shaped structure, with the loop allowing the two helices to assume a parallel orientation. The monomeric domains associate into a dimer through the formation of an antiparallel coiled coil between the alpha-2 helices and domain swapping of two alpha-1 helices, where one alpha-1 helix swings back and packs against the alpha-2 helix from the second monomer. Two dimers then associate into a tetramer. The oligomerization domain is essential for the oncogenicity of the Bcr-Abl protein.


:

Pssm-ID: 430380  Cd Length: 73  Bit Score: 146.55  E-value: 1.68e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075918467    3 EPAGFAEAWRAQFPDAEPPRMELRTVRDMEQELERCRASVRRLERELNRERFRMIYLQTLLAKERRGYDRQRW 75
Cdd:pfam09036    1 EPAGFERHWRAEFPEGQVPKMELGSVEDIEQELERCKASLRRLQQELNEEKFKVIYLQTLLARERKSYDRQRW 73
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 394-581 1.13e-39

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


:

Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 145.13  E-value: 1.13e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  394 VLSAILASEETYLSHLEALL-----LPMKPLKAAAttsqpvltvQQIETIFFKVPELYEIHKEFYdaLFPRVQKWSHQQC 468
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVevflpPNSKPLSESE---------EEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQR 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  469 VGDLFQKLASQLGVYRAFVDNYEVAMETAEKCCQANAQFAEISENLKARntrepkDHSSKTSLEALLYKPVDRVTRNTLV 548
Cdd:pfam00621   70 IGDIFLKFAPGFKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEAN------PECRGLDLNSFLIKPVQRIPRYPLL 143

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2075918467  549 LHDLLKHTPAGHPDHPLLQDALRISQNFLSSIN 581
Cdd:pfam00621  144 LKELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
SF-CC1 super family cl36939
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 29-151 2.94e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


The actual alignment was detected with superfamily member TIGR01622:

Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 41.44  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467   29 RDMEQELERCRASVRRLERELNRERFRmiylqtllaKERRGYDRQRWGFEERPLHAGEQDPVGEERNMGIGRE---ERSP 105
Cdd:TIGR01622    3 RDRERERLRDSSSAGDRDRRRDKGRER---------SRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSRRPnrrYRPR 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2075918467  106 ENSHRGPGRREPPVGapDMSPGnvNKGPRRLLSLTEREAPEHRLDR 151
Cdd:TIGR01622   74 EKRRRRGDSYRRRRD--DRRSR--REKPRARDGTPEPLTEDERDRR 115
 
Name Accession Description Interval E-value
PH_BCR_vertebrate cd13367
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
 576-769 3.03e-127

Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. This hierarchy is composed of vertebrate BCRs. 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.


Pssm-ID: 270173  Cd Length: 194  Bit Score: 387.44  E-value: 3.03e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  576 FLSSINEEITPRRQSMTVRKGEHRQLLKDSFMVELIEGSRKLRHVFLFTDLLLCAKLKKQLGGKSQQYDCKWYIPLADLN 655
Cdd:cd13367      1 FLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCAKLKKQIGGKSQQYDCKWYIPLADLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  656 FQPIDESESCSNIPLIPDEELEAIKVKISQLKSDIQREKKANKGGKGLDRLRKKLSEQESVLLLLSPSMAFRIQNRNGKG 735
Cdd:cd13367     81 FQTVDESEAVPNIPLIPDEEIDALKVKISQIKSDIQREKRANKGGKVLERLRKKLSEQESLLLLMSPSMAFRVHNRNGKS 160

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2075918467  736 YTLLTWSDYERAEWGEHIREQQKKCFKSFSLSSL 769
Cdd:cd13367    161 YTFLISSDYERAEWRENIREQQKKCFKSFSLTSL 194
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 945-1145 4.09e-121

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 371.18  E-value: 4.09e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDVSVIMSDMDVNAIAGTLKLY 1024
Cdd:cd04387      1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEMDVNAIAGTLKLY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1025 FRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTL 1104
Cdd:cd04387     81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2075918467 1105 LRPSEKDSKIPANptqpiSMADSWSLEVMSQVQVLLYFLQL 1145
Cdd:cd04387    161 LRPSEKESKIPTN-----TMTDSWSLEVMSQVQVLLYFLQL 196
C2_ABR cd08686
C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is ...
 805-926 4.15e-61

C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is similar to the breakpoint cluster region protein. It has homology to guanine nucleotide exchange proteins and GTPase-activating proteins (GAPs). ABR is expressed primarily in the brain, but also includes non-neuronal tissues such as the heart. It has been associated with human diseases such as Miller-Dieker syndrome in which mental retardation and malformations of the heart are present. ABR contains a RhoGEF domain and a PH-like domain upstream of its C2 domain and a RhoGAP domain downstream of this domain. A few members also contain a Bcr-Abl oncoprotein oligomerization domain at the very N-terminal end. Splice variants of ABR have been identified. ABR is found in a wide variety of organisms including chimpanzee, dog, mouse, rat, fruit fly, and mosquito. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176068  Cd Length: 118  Bit Score: 203.89  E-value: 4.15e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  805 LNVIVHSATGYQQSSNLFCTLEVDSFGYFVNKAKTRVYRNTTEPNWNEEFEIELEGSQTLRILCYEKSYNrnrNVKEDGG 884
Cdd:cd08686      1 LNVIVHSAQGFKQSANLYCTLEVDSFGYFVKKAKTRVCRDTTEPNWNEEFEIELEGSQTLRILCYEKCYS---KVKLDGE 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2075918467  885 DTsERIVAKGQVQLESQLALGKDWQRSVVSMNGIEVKLSMKF 926
Cdd:cd08686     78 GT-DAIMGKGQIQLDPQSLQTKKWQEKVISMNGITVNLSIKF 118
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 960-1122 3.97e-60

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 203.65  E-value: 3.97e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467   960 VPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDaNNKDVSVIMSDMDVNAIAGTLKLYFRELPAPLFTDELYP 1039
Cdd:smart00324    3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFD-SGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  1040 NFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTLLRPSEKDSKIPANPT 1119
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDIR 161


                    ...
gi 2075918467  1120 QPI 1122
Cdd:smart00324  162 HQN 164
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 961-1108 2.17e-58

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 197.38  E-value: 2.17e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  961 PYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDaNNKDVSVIMSDMDVNAIAGTLKLYFRELPAPLFTDELYPN 1040
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFD-RGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEE 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2075918467 1041 FAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTLLRPS 1108
Cdd:pfam00620   80 FIEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
Bcr-Abl_Oligo pfam09036
Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain ...
 3-75 1.68e-41

Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain consists of a short N-terminal helix (alpha-1), a flexible loop and a long C-terminal helix (alpha-2). Together these form an N-shaped structure, with the loop allowing the two helices to assume a parallel orientation. The monomeric domains associate into a dimer through the formation of an antiparallel coiled coil between the alpha-2 helices and domain swapping of two alpha-1 helices, where one alpha-1 helix swings back and packs against the alpha-2 helix from the second monomer. Two dimers then associate into a tetramer. The oligomerization domain is essential for the oncogenicity of the Bcr-Abl protein.


Pssm-ID: 430380  Cd Length: 73  Bit Score: 146.55  E-value: 1.68e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075918467    3 EPAGFAEAWRAQFPDAEPPRMELRTVRDMEQELERCRASVRRLERELNRERFRMIYLQTLLAKERRGYDRQRW 75
Cdd:pfam09036    1 EPAGFERHWRAEFPEGQVPKMELGSVEDIEQELERCKASLRRLQQELNEEKFKVIYLQTLLARERKSYDRQRW 73
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 394-581 1.13e-39

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 145.13  E-value: 1.13e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  394 VLSAILASEETYLSHLEALL-----LPMKPLKAAAttsqpvltvQQIETIFFKVPELYEIHKEFYdaLFPRVQKWSHQQC 468
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVevflpPNSKPLSESE---------EEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQR 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  469 VGDLFQKLASQLGVYRAFVDNYEVAMETAEKCCQANAQFAEISENLKARntrepkDHSSKTSLEALLYKPVDRVTRNTLV 548
Cdd:pfam00621   70 IGDIFLKFAPGFKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEAN------PECRGLDLNSFLIKPVQRIPRYPLL 143

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2075918467  549 LHDLLKHTPAGHPDHPLLQDALRISQNFLSSIN 581
Cdd:pfam00621  144 LKELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 391-581 4.99e-39

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 143.59  E-value: 4.99e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  391 RKWVLSAILASEETYLSHLEALLLP-MKPLKAaattSQPVLTVQQIETIFFKVPELYEIHKEFYDALFPRVQKW-SHQQC 468
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVfLKPLDK----ELLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdKSGPR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  469 VGDLFQKLASQLGVYRAFVDNYEVAMETAEKCCQANAQFAEISENLKARntrepkdhSSKTSLEALLYKPVDRVTRNTLV 548
Cdd:cd00160     77 IGDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESE--------CGRLKLESLLLKPVQRLTKYPLL 148

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2075918467  549 LHDLLKHTPAGHPDHPLLQDALRISQNFLSSIN 581
Cdd:cd00160    149 LKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 394-582 1.62e-37

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 138.97  E-value: 1.62e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467   394 VLSAILASEETYLSHLEALL-LPMKPLKAaattSQPVLTVQQIETIFFKVPELYEIHKEFYDALFPRVQKWSH-QQCVGD 471
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVeVFLKPLKK----ELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDsVERIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467   472 LFQKLASQLGVYRAFVDNYEVAMETAEKCCQANAQFAEISENLKARNTRepkdhssKTSLEALLYKPVDRVTRNTLVLHD 551
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCR-------RLTLESLLLKPVQRLTKYPLLLKE 149

                           170       180       190
                    ....*....|....*....|....*....|.
gi 2075918467   552 LLKHTPAGHPDHPLLQDALRISQNFLSSINE 582
Cdd:smart00325  150 LLKHTPEDHEDREDLKKALKAIKELANQVNE 180
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 804-876 2.86e-08

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 52.49  E-value: 2.86e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467   804 FLNVIVHSATGY-----QQSSNLFCTLEVDsfGYFVNKAKTRVYRNTTEPNWNEEFEIEL--EGSQTLRILCYEKSYNRN 876
Cdd:smart00239    1 TLTVKIISARNLppkdkGGKSDPYVKVSLD--GDPKEKKKTKVVKNTLNPVWNETFEFEVppPELAELEIEVYDKDRFGR 78
C2 pfam00168
C2 domain;
803-876 2.90e-06

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 46.93  E-value: 2.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  803 GFLNVIVHSATG-----YQQSSNLFCTLEVDSFgyfVNKAKTRVYRNTTEPNWNEEFEIEL--EGSQTLRILCYEKSYNR 875
Cdd:pfam00168    1 GRLTVTVIEAKNlppkdGNGTSDPYVKVYLLDG---KQKKKTKVVKNTLNPVWNETFTFSVpdPENAVLEIEVYDYDRFG 77


                   .
gi 2075918467  876 N 876
Cdd:pfam00168   78 R 78
PH_19 pfam19057
PH domain; This entry contains a PH domain found in RhoGEF proteins.
 599-667 4.98e-05

PH domain; This entry contains a PH domain found in RhoGEF proteins.


Pssm-ID: 465965  Cd Length: 151  Bit Score: 44.75  E-value: 4.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  599 RQLLKDSFMVELIEGSR------KLRHVFLFTDLLLCAKLKKQLG------GKSQQYDCKWYIPLADLNFQPIDESESCS 666
Cdd:pfam19057   11 RYLIRQDDVVETVYNERgevlksKERRLFLLNDLLVCVTVNSKSGsdfgslPGGEKYKLKWSVPLSDVEVVESGQSPNTS 90


                   .
gi 2075918467  667 N 667
Cdd:pfam19057   91 N 91
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 29-151 2.94e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 41.44  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467   29 RDMEQELERCRASVRRLERELNRERFRmiylqtllaKERRGYDRQRWGFEERPLHAGEQDPVGEERNMGIGRE---ERSP 105
Cdd:TIGR01622    3 RDRERERLRDSSSAGDRDRRRDKGRER---------SRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSRRPnrrYRPR 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2075918467  106 ENSHRGPGRREPPVGapDMSPGnvNKGPRRLLSLTEREAPEHRLDR 151
Cdd:TIGR01622   74 EKRRRRGDSYRRRRD--DRRSR--REKPRARDGTPEPLTEDERDRR 115
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 416-583 3.13e-03

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 41.80  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  416 MKPLKAAATTSQPVlTVQQIETIFFKVPELYEIHKEFYDALfprvqkwSHQQC-------VGDLFQKLASQLGVYRAFVD 488
Cdd:COG5422    511 IKPLEESNIIPENA-RRNFIKHVFANINEIYAVNSKLLKAL-------TNRQClspivngIADIFLDYVPKFEPFIKYGA 582

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  489 NYEVAMETAEKCCQANAQFAEISENLkarntrEPKDHSSKTSLEALLYKPVDRVTRNTLVLHDLLKHTPAGHPDHPLLQD 568
Cdd:COG5422    583 SQPYAKYEFEREKSVNPNFARFDHEV------ERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPK 656

                          170
                   ....*....|....*
gi 2075918467  569 ALRISQNFLSSINEE 583
Cdd:COG5422    657 VIDMLREFLSRLNFE 671
 
Name Accession Description Interval E-value
PH_BCR_vertebrate cd13367
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
 576-769 3.03e-127

Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. This hierarchy is composed of vertebrate BCRs. 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.


Pssm-ID: 270173  Cd Length: 194  Bit Score: 387.44  E-value: 3.03e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  576 FLSSINEEITPRRQSMTVRKGEHRQLLKDSFMVELIEGSRKLRHVFLFTDLLLCAKLKKQLGGKSQQYDCKWYIPLADLN 655
Cdd:cd13367      1 FLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCAKLKKQIGGKSQQYDCKWYIPLADLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  656 FQPIDESESCSNIPLIPDEELEAIKVKISQLKSDIQREKKANKGGKGLDRLRKKLSEQESVLLLLSPSMAFRIQNRNGKG 735
Cdd:cd13367     81 FQTVDESEAVPNIPLIPDEEIDALKVKISQIKSDIQREKRANKGGKVLERLRKKLSEQESLLLLMSPSMAFRVHNRNGKS 160

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2075918467  736 YTLLTWSDYERAEWGEHIREQQKKCFKSFSLSSL 769
Cdd:cd13367    161 YTFLISSDYERAEWRENIREQQKKCFKSFSLTSL 194
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 945-1145 4.09e-121

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 371.18  E-value: 4.09e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDVSVIMSDMDVNAIAGTLKLY 1024
Cdd:cd04387      1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEMDVNAIAGTLKLY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1025 FRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTL 1104
Cdd:cd04387     81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2075918467 1105 LRPSEKDSKIPANptqpiSMADSWSLEVMSQVQVLLYFLQL 1145
Cdd:cd04387    161 LRPSEKESKIPTN-----TMTDSWSLEVMSQVQVLLYFLQL 196
PH_ABR cd13366
Active breakpoint cluster region-related protein pleckstrin homology (PH) domain; The ABR ...
 576-759 1.23e-85

Active breakpoint cluster region-related protein pleckstrin homology (PH) domain; The ABR protein contains multiple domains including a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. It is related to a slightly larger protein, BCR, which is structurally similar, but has an additional N-terminal kinase domain. ABR has GAP activity for both Rac and Cdc42. It promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. It is highly enriched in the brain and found to a lesser extent in heart, lung and muscle. 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.


Pssm-ID: 270172  Cd Length: 185  Bit Score: 275.34  E-value: 1.23e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  576 FLSSINEEITPRRQSMTVRKGEHRQLLKDSFMVELIEGSRKLRHVFLFTDLLLCAKLKKQLGGKSQQYDCKWYIPLADLN 655
Cdd:cd13366      1 FLSSINEDIDPRRTAVTTPKGETRQLVKDGFLVEVSEGSRKLRHVFLFTDLLLCAKLKKTAVGKHQQYDCKWYIPLADLV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  656 FQPIDESESCSNIPLIPDEELEAIKVKISQLKSDIQREKKANKG-GKGLDRLRKKLSEQESVLLLLSPSMAFRIQNRNGK 734
Cdd:cd13366     81 FPSPEESESLPQVHTLPDHEIEEMKMKISAIKSEIQKEKKNKKGqSRAIERLKKKMFENESWLLLNSPTIPFRIHNKNGK 160

                          170       180
                   ....*....|....*....|....*
gi 2075918467  735 GYTLLTWSDYERAEWGEHIREQQKK 759
Cdd:cd13366    161 SYLFLLSSDYERSEWREAIQKLQKK 185
PH_BCR-related cd01228
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
 599-759 1.45e-70

Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. ABR, a related smaller protein, is structurally similar to BCR, but lacks the N-terminal kinase domain and has GAP activity for both Rac and 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.


Pssm-ID: 269935  Cd Length: 166  Bit Score: 232.62  E-value: 1.45e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  599 RQLLKDSFMVELIEGSRKLRHVFLFTDLLLCAKLKKQLGGKSQQYDCKWYIPLADLNFQPIDESESCSNIPLIPDEELEA 678
Cdd:cd01228      1 RQLVKDGFLVELSEGSRKLRHLFLFTDVLLCAKLKSAGRGFQGQYECKWYIPLRDLSLHPKDESEASPIVPVTSDKELEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  679 IKVKISQLKS-----DIQREKKANKGGKGLDRLRKKLSEQESVLLLLSPSMAFRIQNRNGKGYTLLTWSDYERAEWGEHI 753
Cdd:cd01228     81 LKSKIAELKKqirddDAQRKKASSSGSKAIEKLRKKLAEQEAALLLASPSLPLRLYHRNGKTYTFLLSSDYERSEWKEAI 160


                   ....*.
gi 2075918467  754 REQQKK 759
Cdd:cd01228    161 LKLQKK 166
C2_ABR cd08686
C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is ...
 805-926 4.15e-61

C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is similar to the breakpoint cluster region protein. It has homology to guanine nucleotide exchange proteins and GTPase-activating proteins (GAPs). ABR is expressed primarily in the brain, but also includes non-neuronal tissues such as the heart. It has been associated with human diseases such as Miller-Dieker syndrome in which mental retardation and malformations of the heart are present. ABR contains a RhoGEF domain and a PH-like domain upstream of its C2 domain and a RhoGAP domain downstream of this domain. A few members also contain a Bcr-Abl oncoprotein oligomerization domain at the very N-terminal end. Splice variants of ABR have been identified. ABR is found in a wide variety of organisms including chimpanzee, dog, mouse, rat, fruit fly, and mosquito. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176068  Cd Length: 118  Bit Score: 203.89  E-value: 4.15e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  805 LNVIVHSATGYQQSSNLFCTLEVDSFGYFVNKAKTRVYRNTTEPNWNEEFEIELEGSQTLRILCYEKSYNrnrNVKEDGG 884
Cdd:cd08686      1 LNVIVHSAQGFKQSANLYCTLEVDSFGYFVKKAKTRVCRDTTEPNWNEEFEIELEGSQTLRILCYEKCYS---KVKLDGE 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2075918467  885 DTsERIVAKGQVQLESQLALGKDWQRSVVSMNGIEVKLSMKF 926
Cdd:cd08686     78 GT-DAIMGKGQIQLDPQSLQTKKWQEKVISMNGITVNLSIKF 118
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 960-1122 3.97e-60

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 203.65  E-value: 3.97e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467   960 VPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDaNNKDVSVIMSDMDVNAIAGTLKLYFRELPAPLFTDELYP 1039
Cdd:smart00324    3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFD-SGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  1040 NFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTLLRPSEKDSKIPANPT 1119
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDIR 161


                    ...
gi 2075918467  1120 QPI 1122
Cdd:smart00324  162 HQN 164
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 961-1108 2.17e-58

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 197.38  E-value: 2.17e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  961 PYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDaNNKDVSVIMSDMDVNAIAGTLKLYFRELPAPLFTDELYPN 1040
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFD-RGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEE 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2075918467 1041 FAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTLLRPS 1108
Cdd:pfam00620   80 FIEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 961-1114 2.02e-51

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 178.26  E-value: 2.02e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  961 PYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDVsvIMSDMDVNAIAGTLKLYFRELPAPLFTDELYPN 1040
Cdd:cd00159      1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDID--DLEDYDVHDVASLLKLYLRELPEPLIPFELYDE 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075918467 1041 FAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTLLRPSEKDSKI 1114
Cdd:cd00159     79 FIELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDEL 152
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 945-1117 1.27e-50

RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 176.81  E-value: 1.27e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDVSVIMSDMDVNAIAGTLKLY 1024
Cdd:cd04403      1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLDLDDSKWEDIHVITGALKLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1025 FRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTL 1104
Cdd:cd04403     81 FRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTL 160

                          170
                   ....*....|...
gi 2075918467 1105 LRPSEKDSKIPAN 1117
Cdd:cd04403    161 LRPEQETGNIAVH 173
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 945-1105 7.80e-50

RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239863  Cd Length: 192  Bit Score: 174.90  E-value: 7.80e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDVSVIMSDM---DVNAIAGTL 1021
Cdd:cd04398      1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLISPEDyesDIHSVASLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1022 KLYFRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFG 1101
Cdd:cd04398     81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160


                   ....
gi 2075918467 1102 PTLL 1105
Cdd:cd04398    161 PTLM 164
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 945-1112 4.12e-47

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239837 [Multi-domain]  Cd Length: 194  Bit Score: 166.92  E-value: 4.12e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFD--ANNKDVSVIMSDmDVNAIAGTLK 1022
Cdd:cd04372      1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDrdGEKADISATVYP-DINVITGALK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1023 LYFRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGP 1102
Cdd:cd04372     80 LYFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGP 159

                          170
                   ....*....|
gi 2075918467 1103 TLLRPSEKDS 1112
Cdd:cd04372    160 TLMRPPEDSA 169
Bcr-Abl_Oligo pfam09036
Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain ...
 3-75 1.68e-41

Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain consists of a short N-terminal helix (alpha-1), a flexible loop and a long C-terminal helix (alpha-2). Together these form an N-shaped structure, with the loop allowing the two helices to assume a parallel orientation. The monomeric domains associate into a dimer through the formation of an antiparallel coiled coil between the alpha-2 helices and domain swapping of two alpha-1 helices, where one alpha-1 helix swings back and packs against the alpha-2 helix from the second monomer. Two dimers then associate into a tetramer. The oligomerization domain is essential for the oncogenicity of the Bcr-Abl protein.


Pssm-ID: 430380  Cd Length: 73  Bit Score: 146.55  E-value: 1.68e-41
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075918467    3 EPAGFAEAWRAQFPDAEPPRMELRTVRDMEQELERCRASVRRLERELNRERFRMIYLQTLLAKERRGYDRQRW 75
Cdd:pfam09036    1 EPAGFERHWRAEFPEGQVPKMELGSVEDIEQELERCKASLRRLQQELNEEKFKVIYLQTLLARERKSYDRQRW 73
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 944-1109 5.61e-41

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239860  Cd Length: 196  Bit Score: 149.47  E-value: 5.61e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  944 VFGVKI-SIVTKRERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFdaNNKDVSVIMSD---MDVNAIAG 1019
Cdd:cd04395      1 TFGVPLdDCPPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEEL--NRGGFDIDLQDprwRDVNVVSS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1020 TLKLYFRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATV 1099
Cdd:cd04395     79 LLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIV 158

                          170
                   ....*....|
gi 2075918467 1100 FGPTLLRPSE 1109
Cdd:cd04395    159 FGPTLVRTSD 168
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 394-581 1.13e-39

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 145.13  E-value: 1.13e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  394 VLSAILASEETYLSHLEALL-----LPMKPLKAAAttsqpvltvQQIETIFFKVPELYEIHKEFYdaLFPRVQKWSHQQC 468
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVevflpPNSKPLSESE---------EEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQR 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  469 VGDLFQKLASQLGVYRAFVDNYEVAMETAEKCCQANAQFAEISENLKARntrepkDHSSKTSLEALLYKPVDRVTRNTLV 548
Cdd:pfam00621   70 IGDIFLKFAPGFKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEAN------PECRGLDLNSFLIKPVQRIPRYPLL 143

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2075918467  549 LHDLLKHTPAGHPDHPLLQDALRISQNFLSSIN 581
Cdd:pfam00621  144 LKELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 945-1117 4.37e-39

RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239843  Cd Length: 203  Bit Score: 144.49  E-value: 4.37e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDaNNKDVsVIMSDMDVNAIAGTLKLY 1024
Cdd:cd04378      1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFE-NGKDL-VELSELSPHDISSVLKLF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1025 FRELPAPLFTDELYPNFaegIALS--------DPVAKESC---------MLNLLLSLPEPNLLTFLFLLDHLKRVSEKES 1087
Cdd:cd04378     79 LRQLPEPLILFRLYNDF---IALAkeiqrdteEDKAPNTPievnriirkLKDLLRQLPASNYNTLQHLIAHLYRVAEQFE 155

                          170       180       190
                   ....*....|....*....|....*....|
gi 2075918467 1088 QNKMSLHNLATVFGPTLLRPSEKDSKIPAN 1117
Cdd:cd04378    156 ENKMSPNNLGIVFGPTLIRPRPGDADVSLS 185
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 391-581 4.99e-39

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 143.59  E-value: 4.99e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  391 RKWVLSAILASEETYLSHLEALLLP-MKPLKAaattSQPVLTVQQIETIFFKVPELYEIHKEFYDALFPRVQKW-SHQQC 468
Cdd:cd00160      1 RQEVIKELLQTERNYVRDLKLLVEVfLKPLDK----ELLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWdKSGPR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  469 VGDLFQKLASQLGVYRAFVDNYEVAMETAEKCCQANAQFAEISENLKARntrepkdhSSKTSLEALLYKPVDRVTRNTLV 548
Cdd:cd00160     77 IGDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESE--------CGRLKLESLLLKPVQRLTKYPLL 148

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2075918467  549 LHDLLKHTPAGHPDHPLLQDALRISQNFLSSIN 581
Cdd:cd00160    149 LKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 945-1145 4.43e-38

RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239844  Cd Length: 207  Bit Score: 141.84  E-value: 4.43e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERSK--VPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDVSVIMSDM-DVNAIAGTL 1021
Cdd:cd04379      1 FGVPLSRLVEREGESrdVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEELYpDINVITGVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1022 KLYFRELPAPLFTDELYPNFAEGIAL---SDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLAT 1098
Cdd:cd04379     81 KDYLRELPEPLITPQLYEMVLEALAValpNDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2075918467 1099 VFGPTLLRPSEKDSKIPANPTQpiSMADSWSLEVMSQVQVLLYFLQL 1145
Cdd:cd04379    161 CFGPVLMFCSQEFSRYGISPTS--KMAAVSTVDFKQHIEVLHYLLQI 205
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 394-582 1.62e-37

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 138.97  E-value: 1.62e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467   394 VLSAILASEETYLSHLEALL-LPMKPLKAaattSQPVLTVQQIETIFFKVPELYEIHKEFYDALFPRVQKWSH-QQCVGD 471
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVeVFLKPLKK----ELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDsVERIGD 76

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467   472 LFQKLASQLGVYRAFVDNYEVAMETAEKCCQANAQFAEISENLKARNTRepkdhssKTSLEALLYKPVDRVTRNTLVLHD 551
Cdd:smart00325   77 VFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQKFLKEIESSPQCR-------RLTLESLLLKPVQRLTKYPLLLKE 149

                           170       180       190
                    ....*....|....*....|....*....|.
gi 2075918467   552 LLKHTPAGHPDHPLLQDALRISQNFLSSINE 582
Cdd:smart00325  150 LLKHTPEDHEDREDLKKALKAIKELANQVNE 180
PH_BCR_arthropod cd13368
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
 599-760 5.05e-37

Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the two genes in the BCR-ABL complex, which is associated with the Philadelphia chromosome, a product of a reciprocal translocation between chromosomes 22 and 9. BCR is a GTPase-activating protein (GAP) for RAC1 (primarily) and CDC42. The Dbl region of BCR has the most RhoGEF activity for Cdc42, and less activity towards Rac and Rho. Since BCR possesses both GAP and GEF activities, it may function to temporally regulate the activity of these GTPases. It also displays serine/threonine kinase activity. The BCR protein contains multiple domains including an N-terminal kinase domain, a RhoGEF domain, a PH domain, a C1 domain, a C2 domain, and a C-terminal RhoGAP domain. This hierarchy is composed of arthropod BCRs. 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.


Pssm-ID: 270174  Cd Length: 180  Bit Score: 137.66  E-value: 5.05e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  599 RQLLKDSFMVELIEGSRKLRHVFLFTDLLLCAKLKKqLGGKSQQYDCKWYIPLADLN-FQPIDESESCSNIPLIpdeelE 677
Cdd:cd13368     22 RRLVKNSFIVELADGHRKLRHLFLFNDVIACAKYKS-SGRTRITFELKWFIPLNDVTiLEEEAPAPKESSPPNI-----E 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  678 AIKVKISQLKSDIQREKKANkgGKGLDRLRKKLSEQESVLLLLSPSMAFRIQNRNGKGYTLLTWSDYERAEWGEHIREQQ 757
Cdd:cd13368     96 QLKSNACQVRDQLADRSRAS--TSGSDKIRKKLADLEAQLVLASPNLVFRIGNKNNKTYTFFLSSEFERTQWIEAILTLQ 173


                   ...
gi 2075918467  758 KKC 760
Cdd:cd13368    174 QTC 176
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 960-1147 1.97e-35

RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239847  Cd Length: 193  Bit Score: 133.57  E-value: 1.97e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  960 VPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFdANNKDVSvIMSDMDVNAIAGTLKLYFRELPAPLFTDELYP 1039
Cdd:cd04382     17 IPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKF-LRGKTVP-NLSKVDIHVICGCLKDFLRSLKEPLITFALWK 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1040 NFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKeSQNKMSLHNLATVFGPTLLrpsekdSKIPANPT 1119
Cdd:cd04382     95 EFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQS-PECKMDINNLARVFGPTIV------GYSVPNPD 167

                          170       180
                   ....*....|....*....|....*...
gi 2075918467 1120 QPISMADswsleVMSQVQVLLYFLQLDT 1147
Cdd:cd04382    168 PMTILQD-----TVRQPRVVERLLEIPS 190
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 963-1109 2.40e-34

RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239839  Cd Length: 203  Bit Score: 130.98  E-value: 2.40e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  963 IVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAF----DANNKDVSVIMSDMDVNAIAGTLKLYFRELPAPLFTDELY 1038
Cdd:cd04374     31 FVRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpkTSTPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTYELH 110

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2075918467 1039 PNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTLLRPSE 1109
Cdd:cd04374    111 NDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQE 181
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 944-1112 5.84e-34

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 129.55  E-value: 5.84e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  944 VFGVKISIVTKRERSKVPYIVRQCVEEIERRGLEEvGIYRVSGVATDIQALKNAFDANN-KDVSVIMSDMDVNAIAGTLK 1022
Cdd:cd04384      2 VFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSEQiPDLTKDVYIQDIHSVSSLCK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1023 LYFRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGP 1102
Cdd:cd04384     81 LYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWAP 160

                          170
                   ....*....|
gi 2075918467 1103 TLLRPSEKDS 1112
Cdd:cd04384    161 NLLRSKQIES 170
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 945-1106 1.57e-32

RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in class IX myosins. Class IX myosins contain a characteristic head domain, a neck domain, a tail domain which contains a C6H2-zinc binding motif and a RhoGAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239842  Cd Length: 186  Bit Score: 124.86  E-value: 1.57e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKrERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKdvSVIMSDMDVNAIAGTLKLY 1024
Cdd:cd04377      1 FGVSLSSLTS-EDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPD--SVNLEDYPIHVITSVLKQW 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1025 FRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTL 1104
Cdd:cd04377     78 LRELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCI 157


                   ..
gi 2075918467 1105 LR 1106
Cdd:cd04377    158 LR 159
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 944-1112 1.66e-32

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239851  Cd Length: 203  Bit Score: 125.65  E-value: 1.66e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  944 VFGVKISIVTKRERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDVSVIMSDMDVNAIAGTLKL 1023
Cdd:cd04386      4 VFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFYSDPHAVASALKS 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1024 YFRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPT 1103
Cdd:cd04386     84 YLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAPN 163


                   ....*....
gi 2075918467 1104 LLRPSEKDS 1112
Cdd:cd04386    164 LLWAKNEGS 172
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 944-1125 2.40e-32

RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239856  Cd Length: 216  Bit Score: 125.54  E-value: 2.40e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  944 VFGVKISIVTKRER-----SKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDVSVIMSDMDVNAIA 1018
Cdd:cd04391      1 LFGVPLSTLLERDQkkvpgSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKFYEGTFLWDQVKQHDAA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1019 GTLKLYFRELPAPLFTDELYPNFAEGIALSDPVAKeSCMLNLL-LSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLA 1097
Cdd:cd04391     81 SLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQ-LQALNLLvLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVA 159

                          170       180
                   ....*....|....*....|....*...
gi 2075918467 1098 TVFGPTLLRPSEKDSKIPANPTQPISMA 1125
Cdd:cd04391    160 MIMAPNLFPPRGKHSKDNESLQEEVNMA 187
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 945-1114 6.97e-32

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239874  Cd Length: 211  Bit Score: 124.15  E-value: 6.97e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDaNNKDVsVIMSDMDVNAIAGTLKLY 1024
Cdd:cd04409      1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFE-NGKDL-VELSELSPHDISNVLKLY 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1025 FRELPAPLFTDELYPNF-------------AEGIALSDPVAKESC---------MLNLLLSLPEPNLLTFLFLLDHLKRV 1082
Cdd:cd04409     79 LRQLPEPLILFRLYNEFiglakesqhvnetQEAKKNSDKKWPNMCtelnrillkSKDLLRQLPAPNYNTLQFLIVHLHRV 158

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2075918467 1083 SEKESQNKMSLHNLATVFGPTLLRPSEKDSKI 1114
Cdd:cd04409    159 SEQAEENKMSASNLGIIFGPTLIRPRPTDATV 190
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 945-1107 4.22e-30

RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239873  Cd Length: 200  Bit Score: 118.38  E-value: 4.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDaNNKDVsVIMSDMDVNAIAGTLKLY 1024
Cdd:cd04408      1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFE-NGRDL-VDLSGHSPHDITSVLKHF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1025 FRELPAPLFTDELYPNFaegIALS-----DPVAKESC----------MLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQN 1089
Cdd:cd04408     79 LKELPEPVLPFQLYDDF---IALAkelqrDSEKAAESpsiveniirsLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDN 155

                          170
                   ....*....|....*...
gi 2075918467 1090 KMSLHNLATVFGPTLLRP 1107
Cdd:cd04408    156 KMSPNNLGIVFGPTLLRP 173
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 957-1112 5.68e-30

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239850  Cd Length: 184  Bit Score: 117.41  E-value: 5.68e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  957 RSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDVSVIMSDMDVNAIAGTLKLYFRELPAPLFTDE 1036
Cdd:cd04385     12 DNDIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSE 91

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2075918467 1037 LYPNFAEgiALSDPVAKESCML--NLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTLLRPSEKDS 1112
Cdd:cd04385     92 LHAEWIE--AAELENKDERIARykELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTDEHSV 167
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 945-1122 4.87e-29

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239869 [Multi-domain]  Cd Length: 195  Bit Score: 115.13  E-value: 4.87e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKIS-IVTK-RERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFdanNKDVSVIMSDM-DVNAIAGTL 1021
Cdd:cd04404      6 FGVSLQfLKEKnPEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKY---NMGEPVDFDQYeDVHLPAVIL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1022 KLYFRELPAPLFTDELYPNFAEGIALSDPVAKESCmLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFG 1101
Cdd:cd04404     83 KTFLRELPEPLLTFDLYDDIVGFLNVDKEERVERV-KQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFG 161

                          170       180
                   ....*....|....*....|.
gi 2075918467 1102 PTLLRPseKDSKIPANPTQPI 1122
Cdd:cd04404    162 PNLLWA--KDASMSLSAINPI 180
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 960-1111 6.63e-29

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 114.44  E-value: 6.63e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  960 VPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDVSVIMSDMDVNAIAGTLKLYFRELPAPLFTDELYP 1039
Cdd:cd04383     18 IPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADDQNDHDINSVAGVLKLYFRGLENPLFPKERFE 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2075918467 1040 NFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTLLR-PSEKD 1111
Cdd:cd04383     98 DLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLMPvPEGQD 170
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 945-1107 1.53e-28

RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239838  Cd Length: 185  Bit Score: 113.32  E-value: 1.53e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERsKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDannKDVSVIMSDMD--VNAIAGTLK 1022
Cdd:cd04373      1 FGVPLANVVTSEK-PIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFD---QDHNLDLVSKDftVNAVAGALK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1023 LYFRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGP 1102
Cdd:cd04373     77 SFFSELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWP 156


                   ....*
gi 2075918467 1103 TLLRP 1107
Cdd:cd04373    157 TLMRP 161
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 945-1104 1.60e-28

RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 113.30  E-value: 1.60e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERS----KVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFdanNKDVSVIMSDMDVNAIAGT 1020
Cdd:cd04381      1 FGASLSLAVERSRChdgiDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAY---NRRESPNLEEYEPPTVASL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1021 LKLYFRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVF 1100
Cdd:cd04381     78 LKQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVL 157


                   ....
gi 2075918467 1101 GPTL 1104
Cdd:cd04381    158 SPTV 161
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 943-1111 3.68e-28

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 112.92  E-value: 3.68e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  943 GVFGVKISIVTKRERS----KVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKdvSVIMSDMDVNAIA 1018
Cdd:cd04390      1 GVFGQRLEDTVAYERKfgprLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGER--PSFDSDTDVHTVA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1019 GTLKLYFRELPAPLFTDELYPNF--AEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNL 1096
Cdd:cd04390     79 SLLKLYLRELPEPVIPWAQYEDFlsCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNL 158

                          170
                   ....*....|....*
gi 2075918467 1097 ATVFGPTLLRPSEKD 1111
Cdd:cd04390    159 ATVFGPNILRPKVED 173
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 944-1109 1.06e-27

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 111.30  E-value: 1.06e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  944 VFGVKISIVT-----KRERSKVPYIVRQCVEEIE-RRGLEEVGIYRVSGVATDIQALKNAFDaNNKDVSVIMSDM--DVN 1015
Cdd:cd04400      1 IFGSPLEEAVelsshKYNGRDLPSVVYRCIEYLDkNRAIYEEGIFRLSGSASVIKQLKERFN-TEYDVDLFSSSLypDVH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1016 AIAGTLKLYFRELPAPLFTDELYPNFaEGIA--LSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSL 1093
Cdd:cd04400     80 TVAGLLKLYLRELPTLILGGELHNDF-KRLVeeNHDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNL 158

                          170
                   ....*....|....*.
gi 2075918467 1094 HNLATVFGPTLLRPSE 1109
Cdd:cd04400    159 RNVCIVFSPTLNIPAG 174
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 945-1111 2.23e-26

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 107.38  E-value: 2.23e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKrERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKdvSVIMSDMDVNAIAGTLKLY 1024
Cdd:cd04407      1 FGVRVGSLTS-NKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPE--NVKLENYPIHAITGLLKQW 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1025 FRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTL 1104
Cdd:cd04407     78 LRELPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCL 157


                   ....*...
gi 2075918467 1105 LR-PSEKD 1111
Cdd:cd04407    158 LRcPDSSD 165
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 959-1116 6.80e-24

RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239841  Cd Length: 206  Bit Score: 100.98  E-value: 6.80e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  959 KVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDaNNKDVsVIMSDMDVNAIAGTLKLYFRELPAPLFTDELY 1038
Cdd:cd04376      8 QVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFD-RGIDV-VLDENHSVHDVAALLKEFFRDMPDPLLPRELY 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1039 PNFAeGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVS-----------EKESQNKMSLHNLATVFGPTLLR- 1106
Cdd:cd04376     86 TAFI-GTALLEPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAehaadsidedgQEVSGNKMTSLNLATIFGPNLLHk 164

                          170
                   ....*....|..
gi 2075918467 1107 --PSEKDSKIPA 1116
Cdd:cd04376    165 qkSGEREFVQAS 176
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 945-1123 7.19e-23

RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239871  Cd Length: 186  Bit Score: 97.38  E-value: 7.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERSkVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDVSviMSDMDVNAIAGTLKLY 1024
Cdd:cd04406      1 FGVELSRLTSEDRS-VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVN--LDDYNIHVIASVFKQW 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1025 FRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTL 1104
Cdd:cd04406     78 LRDLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCI 157

                          170
                   ....*....|....*....
gi 2075918467 1105 LRPSekDSKIPANPTQPIS 1123
Cdd:cd04406    158 LRCP--DTTDPLQSVQDIS 174
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 944-1102 2.30e-22

RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by up several orders of magnitude.


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 95.99  E-value: 2.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  944 VFGVKISIVTKR--ERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDaNNKDVSVIMSDmDVNAIAGTL 1021
Cdd:cd04393      2 VFGVPLQELQQAgqPENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLD-SGEEVDLSKEA-DVCSAASLL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1022 KLYFRELPAPLFTDELYPNF--------AEGIALSDpvakescMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSL 1093
Cdd:cd04393     80 RLFLQELPEGLIPASLQIRLmqlyqdynGEDEFGRK-------LRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTA 152


                   ....*....
gi 2075918467 1094 HNLATVFGP 1102
Cdd:cd04393    153 ENLAAVFGP 161
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 944-1120 2.70e-21

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239840  Cd Length: 220  Bit Score: 93.64  E-value: 2.70e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  944 VFGVKISIVTKRERSKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNKDvsVIMSDMDVNAIAGTLKL 1023
Cdd:cd04375      4 VFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDN--VNYDGQQAYDVADMLKQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1024 YFRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPT 1103
Cdd:cd04375     82 YFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAPS 161

                          170
                   ....*....|....*....
gi 2075918467 1104 L--LRPSEKDSKIPANPTQ 1120
Cdd:cd04375    162 LfhLNTSRRENSSPARRMQ 180
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 945-1114 1.48e-18

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239854  Cd Length: 187  Bit Score: 84.75  E-value: 1.48e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERS-----KVPYIVRQCVEEIERRGLEEV-GIYRVSGVATDIQALKNAFDANNKDVSVIMsdmDVNAIA 1018
Cdd:cd04389      1 FGSSLEEIMDRQKEkypelKLPWILTFLSEKVLALGGFQTeGIFRVPGDIDEVNELKLRVDQWDYPLSGLE---DPHVPA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1019 GTLKLYFRELPAPLFTDELYpnfAEGIALSDPVAKescMLNLLLSLPEPNLLTFLFLLDHLKRVSEKE--SQNKMSLHNL 1096
Cdd:cd04389     78 SLLKLWLRELEEPLIPDALY---QQCISASEDPDK---AVEIVQKLPIINRLVLCYLINFLQVFAQPEnvAHTKMDVSNL 151

                          170
                   ....*....|....*...
gi 2075918467 1097 ATVFGPTLLRPSEKDSKI 1114
Cdd:cd04389    152 AMVFAPNILRCTSDDPRV 169
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 980-1117 3.61e-18

RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 84.06  E-value: 3.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  980 GIYRVSGVATDIQALKNAFD-ANNKDVSVIMSDmdvnaIAGTLKLYFRELPAPLFTDELYPNFAEGIALSDPVAKESCML 1058
Cdd:cd04394     39 GLFRKSGSVVRQKELKAKLEgGEACLSSALPCD-----VAGLLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATL 113

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2075918467 1059 NLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTLLRPSEKDSKIPAN 1117
Cdd:cd04394    114 LLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAPNLFQSEEGGEKMSSS 172
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 945-1112 7.45e-16

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239862  Cd Length: 213  Bit Score: 77.79  E-value: 7.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRE-----------RSKVPYIVRQCVEEIERRGLEEVGIYRVSGvatDIQALKNAFDA--NNKDVSVIMSD 1011
Cdd:cd04397      1 FGVPLEILVEKFgadstlgvgpgKLRIPALIDDIISAMRQMDMSVEGVFRKNG---NIRRLKELTEEidKNPTEVPDLSK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1012 MDVNAIAGTLKLYFRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVS-----EKE 1086
Cdd:cd04397     78 ENPVQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSsfshiDEE 157

                          170       180
                   ....*....|....*....|....*.
gi 2075918467 1087 SQNKMSLHNLATVFGPTLLRPSEKDS 1112
Cdd:cd04397    158 TGSKMDIHNLATVITPNILYSKTDNP 183
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 966-1107 1.52e-15

RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239857  Cd Length: 208  Bit Score: 76.73  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  966 QCVEEIE--RRGLEEVGIYRVSGVATDIQALKNAFDaNNKDVSVIMSDMDVNAIAGTLKLYFRELPAPLFTDELYP---- 1039
Cdd:cd04392     12 QIYQLIEylEKNLRVEGLFRKPGNSARQQELRDLLN-SGTDLDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPahlq 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2075918467 1040 -----NFAEGiALSDPVAKESCMLN----LLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTLLRP 1107
Cdd:cd04392     91 iadlcQFDEK-GNKTSAPDKERLLEalqlLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICP 166
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 945-1115 4.01e-15

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239867  Cd Length: 192  Bit Score: 75.03  E-value: 4.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRErsKVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFdanNKDVSVIMSDMDVNAIAGTLKLY 1024
Cdd:cd04402      2 FGQPLSNICEDD--NLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKL---NSGVEVDLKAEPVLLLASVLKDF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1025 FRELPAPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPEPNLLtflfLLDHLKRV----SEKESQNKMSLHNLATVF 1100
Cdd:cd04402     77 LRNIPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVL----LLKHLICVlhniSQNSETNKMDAFNLAVCI 152

                          170       180
                   ....*....|....*....|..
gi 2075918467 1101 GPTLLRPS-------EKDSKIP 1115
Cdd:cd04402    153 APSLLWPPasselqnEDLKKVT 174
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 961-1132 2.53e-13

RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239853  Cd Length: 200  Bit Score: 69.90  E-value: 2.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  961 PYIVRQCVEEIERRGLEEVGIYR--VSGVATDiqaLKNAFDANNKdvSVIMSDMDVNAIAGTLKLYFRELPAPLFTDELY 1038
Cdd:cd04388     16 PPLLIKLVEAIEKKGLESSTLYRtqSSSSLTE---LRQILDCDAA--SVDLEQFDVAALADALKRYLLDLPNPVIPAPVY 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1039 PNFAEgiALSDPVAKESCMLNLLLSLPEPNL-----LTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTLLRPSEKDSK 1113
Cdd:cd04388     91 SEMIS--RAQEVQSSDEYAQLLRKLIRSPNLphqywLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQPASSD 168

                          170       180
                   ....*....|....*....|.
gi 2075918467 1114 IPANPTQPIS--MADSWSLEV 1132
Cdd:cd04388    169 SPEFHIRIIEvlITSEWNERQ 189
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 936-1105 9.32e-13

RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239861  Cd Length: 225  Bit Score: 68.98  E-value: 9.32e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  936 LPSRKQTGVFGVKISIVTKRERS----KVPYIVRQCVEEIERRGLEEVGIYRVSGVATDIQALKNAFDANNK-DVSVIMS 1010
Cdd:cd04396      4 VSLEESLKYASVAISIVDEDGEQyvygYIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDyGKSFDWD 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1011 DMDVNAIAGTLKLYFRELPAPLFTDELYPNFAEGIALSDPVAKESCMLN-----------------LLLSLPEPNLLTFL 1073
Cdd:cd04396     84 GYTVHDAASVLRRYLNNLPEPLVPLDLYEEFRNPLRKRPRILQYMKGRIneplntdidqaikeyrdLITRLPNLNRQLLL 163

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2075918467 1074 FLLDHLKRVSEKESQNKMSLHNLATVFGPTLL 1105
Cdd:cd04396    164 YLLDLLAVFARNSDKNLMTASNLAAIFQPGIL 195
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 966-1110 7.65e-09

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239845  Cd Length: 220  Bit Score: 57.35  E-value: 7.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  966 QCVEEIERRGLEEVGIYRVSGVATD----IQALKNAFDANNKDVSVImsdmDVNAIAGTLKLYFRELPAPLFTDELYPNF 1041
Cdd:cd04380     56 RLVDYLYTRGLAQEGLFEEPGLPSEpgelLAEIRDALDTGSPFNSPG----SAESVAEALLLFLESLPDPIIPYSLYERL 131

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2075918467 1042 AEGIALSDpvakESCMLNLLLSLPEPNLLTFLFLLDHLKRVSEKESQNKMSLHNLATVFGPTLLRPSEK 1110
Cdd:cd04380    132 LEAVANNE----EDKRQVIRISLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPR 196
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 945-1107 8.08e-09

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239864  Cd Length: 212  Bit Score: 56.96  E-value: 8.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  945 FGVKISIVTKRERSKVPYIVrQCV------------EEIERRGleeVGIYRVSgvATDIQALKNAFDANNKDVS--VIMS 1010
Cdd:cd04399      1 FGVDLETRCRLDKKVVPLIV-SAIlsyldqlypdliNDEVRRN---VWTDPVS--LKETHQLRNLLNKPKKPDKevIILK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467 1011 DMDVNAIAGTLKLYFRELPAPLFTDE-------LYPNFAEGIALSDPvAKESCMLNLLLSLPEPNLLTFLFLLDHLKRVS 1083
Cdd:cd04399     75 KFEPSTVASVLKLYLLELPDSLIPHDiydlirsLYSAYPPSQEDSDT-ARIQGLQSTLSQLPKSHIATLDAIITHFYRLI 153

                          170       180
                   ....*....|....*....|....*...
gi 2075918467 1084 E----KESQNKMSLHnLATVFGPTLLRP 1107
Cdd:cd04399    154 EitkmGESEEEYADK-LATSLSREILRP 180
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 804-876 2.86e-08

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 52.49  E-value: 2.86e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467   804 FLNVIVHSATGY-----QQSSNLFCTLEVDsfGYFVNKAKTRVYRNTTEPNWNEEFEIEL--EGSQTLRILCYEKSYNRN 876
Cdd:smart00239    1 TLTVKIISARNLppkdkGGKSDPYVKVSLD--GDPKEKKKTKVVKNTLNPVWNETFEFEVppPELAELEIEVYDKDRFGR 78
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 805-871 1.05e-07

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 50.91  E-value: 1.05e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075918467  805 LNVIVHSATG-----YQQSSNLFCTLEVDSFgyfvNKAKTRVYRNTTEPNWNEEFEIELE--GSQTLRILCYEK 871
Cdd:cd00030      1 LRVTVIEARNlpakdLNGKSDPYVKVSLGGK----QKFKTKVVKNTLNPVWNETFEFPVLdpESDTLTVEVWDK 70
C2 pfam00168
C2 domain;
803-876 2.90e-06

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 46.93  E-value: 2.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  803 GFLNVIVHSATG-----YQQSSNLFCTLEVDSFgyfVNKAKTRVYRNTTEPNWNEEFEIEL--EGSQTLRILCYEKSYNR 875
Cdd:pfam00168    1 GRLTVTVIEAKNlppkdGNGTSDPYVKVYLLDG---KQKKKTKVVKNTLNPVWNETFTFSVpdPENAVLEIEVYDYDRFG 77


                   .
gi 2075918467  876 N 876
Cdd:pfam00168   78 R 78
PH_19 pfam19057
PH domain; This entry contains a PH domain found in RhoGEF proteins.
 599-667 4.98e-05

PH domain; This entry contains a PH domain found in RhoGEF proteins.


Pssm-ID: 465965  Cd Length: 151  Bit Score: 44.75  E-value: 4.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  599 RQLLKDSFMVELIEGSR------KLRHVFLFTDLLLCAKLKKQLG------GKSQQYDCKWYIPLADLNFQPIDESESCS 666
Cdd:pfam19057   11 RYLIRQDDVVETVYNERgevlksKERRLFLLNDLLVCVTVNSKSGsdfgslPGGEKYKLKWSVPLSDVEVVESGQSPNTS 90


                   .
gi 2075918467  667 N 667
Cdd:pfam19057   91 N 91
PH_puratrophin-1 cd13242
Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell ...
 597-639 1.09e-04

Puratrophin-1 pleckstrin homology (PH) domain; Puratrophin-1 (also called Purkinje cell atrophy-associated protein 1 or PLEKHG4/Pleckstrin homology domain-containing family G member 4) contains a spectrin repeat, a RhoGEF (DH) domain, and a PH domain. It is thought to function in intracellular signaling and cytoskeleton dynamics at the Golgi. Puratrophin-1 is expressed in kidney, Leydig cells in the testis, epithelial cells in the prostate gland and Langerhans islet in the pancreas. A single nucleotide substitution in the puratrophin-1 gene were once thought to result in autosomal dominant cerebellar ataxia (ADCA), but now it has been demonstrated that this ataxia is a result of defects in the BEAN gene. Puratrophin contains a domain architecture similar to that of Dbl family members Dbs and Trio. Dbs is a guanine nucleotide exchange factor (GEF), which contains spectrin repeats, a RhoGEF (DH) domain and a PH domain. The Dbs PH domain participates in binding to both the Cdc42 and RhoA GTPases. Trio plays an essential role in regulating the actin cytoskeleton during axonal guidance and branching. Trio is a multidomain signaling protein that contains two RhoGEF(DH)-PH domains in tandem. 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.


Pssm-ID: 270062  Cd Length: 136  Bit Score: 43.43  E-value: 1.09e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2075918467  597 EHRQLLK-DSFMVelIEGSRK-LRHVFLFTDLLLCAKLKKQLGGK 639
Cdd:cd13242     25 EQGQLLRqDEFLV--WQGRKKcLRHVFLFEDLILFSKPKKTPGGK 67
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 817-871 1.57e-04

C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176060 [Multi-domain]  Cd Length: 126  Bit Score: 42.74  E-value: 1.57e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2075918467  817 QSSNLFCTLEVDsfgYFVNKAKTRVYRNTTEPNWNEEFEIELEG-SQTLRILCYEK 871
Cdd:cd08678     16 GSSNPYCVLEMD---EPPQKYQSSTQKNTSNPFWDEHFLFELSPnSKELLFEVYDN 68
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 29-151 2.94e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 41.44  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467   29 RDMEQELERCRASVRRLERELNRERFRmiylqtllaKERRGYDRQRWGFEERPLHAGEQDPVGEERNMGIGRE---ERSP 105
Cdd:TIGR01622    3 RDRERERLRDSSSAGDRDRRRDKGRER---------SRDRSRDRERSRSRRRDRHRDRDYYRGRERRSRSRRPnrrYRPR 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2075918467  106 ENSHRGPGRREPPVGapDMSPGnvNKGPRRLLSLTEREAPEHRLDR 151
Cdd:TIGR01622   74 EKRRRRGDSYRRRRD--DRRSR--REKPRARDGTPEPLTEDERDRR 115
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 416-583 3.13e-03

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 41.80  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  416 MKPLKAAATTSQPVlTVQQIETIFFKVPELYEIHKEFYDALfprvqkwSHQQC-------VGDLFQKLASQLGVYRAFVD 488
Cdd:COG5422    511 IKPLEESNIIPENA-RRNFIKHVFANINEIYAVNSKLLKAL-------TNRQClspivngIADIFLDYVPKFEPFIKYGA 582

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2075918467  489 NYEVAMETAEKCCQANAQFAEISENLkarntrEPKDHSSKTSLEALLYKPVDRVTRNTLVLHDLLKHTPAGHPDHPLLQD 568
Cdd:COG5422    583 SQPYAKYEFEREKSVNPNFARFDHEV------ERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPK 656

                          170
                   ....*....|....*
gi 2075918467  569 ALRISQNFLSSINEE 583
Cdd:COG5422    657 VIDMLREFLSRLNFE 671
PH_ephexin cd01221
Ephexin Pleckstrin homology (PH) domain; Ephexin-1 (also called NGEF/ neuronal guanine ...
 593-666 5.40e-03

Ephexin Pleckstrin homology (PH) domain; Ephexin-1 (also called NGEF/ neuronal guanine nucleotide exchange factor) plays a role in the homeostatic modulation of presynaptic neurotransmitter release. Specific functions are still unknown for Ephexin-2 (also called RhoGEF19) and Ephexin-3 (also called Rho guanine nucleotide exchange factor 5/RhoGEF5, Transforming immortalized mammary oncogene/p60 TIM, and NGEF/neuronalGEF). Ephexin-4 (also called RhoGEF16) acts downstream of EphA2 to promote ligand-independent breast cancer cell migration and invasion toward epidermal growth factor through activation of RhoG. This in turn results in the activation of RhoG which recruits ELMO2 and Dock4 to form a complex with EphA2 at the tips of cortactin-rich protrusions in migrating breast cancer cells. Ephexin-5 is the specific GEF for RhoA activation and the regulation of vascular smooth muscle contractility. It interacts with EPHA4 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. The members of the Ephexin family contains a RhoGEF (DH) followed by a PH domain and an SH3 domain. The ephexin PH domain is believed to act with the DH domain in mediating protein-protein interactions. 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.


Pssm-ID: 269929  Cd Length: 131  Bit Score: 38.39  E-value: 5.40e-03
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gi 2075918467  593 VRKGEHRQLLKDSfmVELIEGSRKLR---HVFLFTDLLLCAKLKkqlggKSQQYDCKWYIPLADLNFQPIDESESCS 666
Cdd:cd01221     15 VKRGELTELVEDG--GSLTFRKKFSKtpvYLFLFNDLLLITKKK-----SEERYLVLDYAPRNLVQVEEVEDPLQLP 84
PH1_FGD5_FGD6 cd13389
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal ...
 598-667 7.19e-03

FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal Pleckstrin Homology (PH) domain; FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. The specific function of FGD6 is unknown. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH 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.


Pssm-ID: 275424  Cd Length: 124  Bit Score: 37.63  E-value: 7.19e-03
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                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2075918467  598 HRQLLKDSfmvELIEGSRK---LRHVFLFTDLLL-CAKLKkqlggKSQQYDCKWYIPLADLNFQPiDESESCSN 667
Cdd:cd13389     11 GRKLIKEG---ELMKVSRKemqPRYFFLFNDCLLyTTPVQ-----SSGMLKLNNELPLSGMKVKL-PEDEEYSN 75
C2_Munc13_fungal cd04043
C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are ...
 818-866 9.43e-03

C2 domain in Munc13 (mammalian uncoordinated) proteins; fungal group; C2-like domains are thought to be involved in phospholipid binding in a Ca2+ independent manner in both Unc13 and Munc13. Caenorabditis elegans Unc13 has a central domain with sequence similarity to PKC, which includes C1 and C2-related domains. Unc13 binds phorbol esters and DAG with high affinity in a phospholipid manner. Mutations in Unc13 results in abnormal neuronal connections and impairment in cholinergic neurotransmission in the nematode. Munc13 is the mammalian homolog which are expressed in the brain. There are 3 isoforms (Munc13-1, -2, -3) and are thought to play a role in neurotransmitter release and are hypothesized to be high-affinity receptors for phorbol esters. Unc13 and Munc13 contain both C1 and C2 domains. There are two C2 related domains present, one central and one at the carboxyl end. Munc13-1 contains a third C2-like domain. Munc13 interacts with syntaxin, synaptobrevin, and synaptotagmin suggesting a role for these as scaffolding proteins. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology.


Pssm-ID: 176008 [Multi-domain]  Cd Length: 126  Bit Score: 37.63  E-value: 9.43e-03
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gi 2075918467  818 SSNLFCTLeVDSFGYfVNKAKTRVYRNTTEPNWNEEFEIELEGSQTLRI 866
Cdd:cd04043     21 LSDPYVTL-VDTNGK-RRIAKTRTIYDTLNPRWDEEFELEVPAGEPLWI 67
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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