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Conserved domains on  [gi|2449489708|ref|XP_053665754|]
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uncharacterized protein LOC128714894 [Anopheles marshallii]

Protein Classification

RhoGEF family protein( domain architecture ID 11264326)

RhoGEF (rho guanine nucleotide exchange factor) family protein similar to RhoGEF and PH (pleckstrin homology) domain regions of Drosophila melanogaster RhoGAP1A

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PH_BCR_arthropod cd13368
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
977-1165 4.06e-99

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: 315.24  E-value: 4.06e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  977 FLSEFNVVQTRTMFPSDDKALRRLVKNSFIVELADGHRKLRHLLLFNDVIACAKYKAVGRTgdrnGFEFELKWFIPLRDI 1056
Cdd:cd13368      1 FLNEFNNIQTKSMFPHQDRALRRLVKNSFIVELADGHRKLRHLFLFNDVIACAKYKSSGRT----RITFELKWFIPLNDV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1057 LICEESANDPKETSPINIVHLKSQACTVRDQIMLDEKDRPGGSsragDKHRKKLADLEAQLVLASPNLVFKIGNKaTGKT 1136
Cdd:cd13368     77 TILEEEAPAPKESSPPNIEQLKSNACQVRDQLADRSRASTSGS----DKIRKKLADLEAQLVLASPNLVFRIGNK-NNKT 151
                          170       180
                   ....*....|....*....|....*....
gi 2449489708 1137 MTFFLSSDFERTQWIESILSLQQSCNLPG 1165
Cdd:cd13368    152 YTFFLSSEFERTQWIEAILTLQQTCPLPG 180
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
1335-1530 9.59e-57

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.


The actual alignment was detected with superfamily member cd04387:

Pssm-ID: 470621 [Multi-domain]  Cd Length: 196  Bit Score: 195.15  E-value: 9.59e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEQLLKEVDIHSVTGILKSY 1414
Cdd:cd04387      1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEMDVNAIAGTLKLY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1415 LRDLPEALFTDQYYPKFFDAFN-RHSNLSEGSRIHELQrifaELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVF 1493
Cdd:cd04387     81 FRELPEPLFTDELYPNFAEGIAlSDPVAKESCMLNLLL----SLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVF 156
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2449489708 1494 GPTLLRPGPSATK--QKDLLESSTADVMTQAGILYSFLQ 1530
Cdd:cd04387    157 GPTLLRPSEKESKipTNTMTDSWSLEVMSQVQVLLYFLQ 195
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
793-982 1.38e-31

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: 122.41  E-value: 1.38e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708   793 IVTSIITSETLYVECLNKM-KQYMKAIRATLTtsqpVISEEEFQTIFFKIEDLHEVHSEFLTELQARLAAPDDAtapdtg 871
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLvEVFLKPLKKELK----LLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDS------ 70
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708   872 GLCVGEPFRRLAGQIHLYGAFLHNYGRAIDTVKMCSTHSQqFKEIVSNIvFKNQNEQKLSLEELLHKPVARVQKNALVLE 951
Cdd:smart00325   71 VERIGDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPR-FQKFLKEI-ESSPQCRRLTLESLLLKPVQRLTKYPLLLK 148
                           170       180       190
                    ....*....|....*....|....*....|.
gi 2449489708   952 DLLNQTPEQHPDYHPLRQASKAIRNFLSEFN 982
Cdd:smart00325  149 ELLKHTPEDHEDREDLKKALKAIKELANQVN 179
C2 super family cl14603
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
1207-1316 2.52e-23

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.


The actual alignment was detected with superfamily member cd08686:

Pssm-ID: 472691  Cd Length: 118  Bit Score: 96.42  E-value: 2.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1207 LHLTIQGLSGFDQQCDLFVCVEIDSYGHYFRKAKTKLVCCSATPQWNESFVLELEGSQNLRILLYQ----------ADVQ 1276
Cdd:cd08686      1 LNVIVHSAQGFKQSANLYCTLEVDSFGYFVKKAKTRVCRDTTEPNWNEEFEIELEGSQTLRILCYEkcyskvkldgEGTD 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2449489708 1277 RPILRAKHILKLSRSWMQETpTRKVLQLSEtLSISTIIRF 1316
Cdd:cd08686     81 AIMGKGQIQLDPQSLQTKKW-QEKVISMNG-ITVNLSIKF 118
 
Name Accession Description Interval E-value
PH_BCR_arthropod cd13368
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
977-1165 4.06e-99

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: 315.24  E-value: 4.06e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  977 FLSEFNVVQTRTMFPSDDKALRRLVKNSFIVELADGHRKLRHLLLFNDVIACAKYKAVGRTgdrnGFEFELKWFIPLRDI 1056
Cdd:cd13368      1 FLNEFNNIQTKSMFPHQDRALRRLVKNSFIVELADGHRKLRHLFLFNDVIACAKYKSSGRT----RITFELKWFIPLNDV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1057 LICEESANDPKETSPINIVHLKSQACTVRDQIMLDEKDRPGGSsragDKHRKKLADLEAQLVLASPNLVFKIGNKaTGKT 1136
Cdd:cd13368     77 TILEEEAPAPKESSPPNIEQLKSNACQVRDQLADRSRASTSGS----DKIRKKLADLEAQLVLASPNLVFRIGNK-NNKT 151
                          170       180
                   ....*....|....*....|....*....
gi 2449489708 1137 MTFFLSSDFERTQWIESILSLQQSCNLPG 1165
Cdd:cd13368    152 YTFFLSSEFERTQWIEAILTLQQTCPLPG 180
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
1335-1530 9.59e-57

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: 195.15  E-value: 9.59e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEQLLKEVDIHSVTGILKSY 1414
Cdd:cd04387      1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEMDVNAIAGTLKLY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1415 LRDLPEALFTDQYYPKFFDAFN-RHSNLSEGSRIHELQrifaELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVF 1493
Cdd:cd04387     81 FRELPEPLFTDELYPNFAEGIAlSDPVAKESCMLNLLL----SLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVF 156
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2449489708 1494 GPTLLRPGPSATK--QKDLLESSTADVMTQAGILYSFLQ 1530
Cdd:cd04387    157 GPTLLRPSEKESKipTNTMTDSWSLEVMSQVQVLLYFLQ 195
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
1351-1500 4.28e-54

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 185.44  E-value: 4.28e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1351 PFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEqLLKEVDIHSVTGILKSYLRDLPEALFTDQYYPK 1430
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDL-DLEEEDVHVVASLLKLFLRELPEPLLTFELYEE 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1431 FFDAFNRHSnlsEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFGPTLLRP 1500
Cdd:pfam00620   80 FIEAAKLPD---EEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRP 146
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
1348-1506 1.14e-51

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: 179.77  E-value: 1.14e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  1348 RDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAeQLLKEVDIHSVTGILKSYLRDLPEALFTDQY 1427
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPD-LDLSEYDVHDVAGLLKLFLRELPEPLITYEL 79
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2449489708  1428 YPKFFDAFNrhsNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFGPTLLRPGPSATK 1506
Cdd:smart00324   80 YEEFIEAAK---LEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVA 155
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
793-982 1.38e-31

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: 122.41  E-value: 1.38e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708   793 IVTSIITSETLYVECLNKM-KQYMKAIRATLTtsqpVISEEEFQTIFFKIEDLHEVHSEFLTELQARLAAPDDAtapdtg 871
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLvEVFLKPLKKELK----LLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDS------ 70
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708   872 GLCVGEPFRRLAGQIHLYGAFLHNYGRAIDTVKMCSTHSQqFKEIVSNIvFKNQNEQKLSLEELLHKPVARVQKNALVLE 951
Cdd:smart00325   71 VERIGDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPR-FQKFLKEI-ESSPQCRRLTLESLLLKPVQRLTKYPLLLK 148
                           170       180       190
                    ....*....|....*....|....*....|.
gi 2449489708   952 DLLNQTPEQHPDYHPLRQASKAIRNFLSEFN 982
Cdd:smart00325  149 ELLKHTPEDHEDREDLKKALKAIKELANQVN 179
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
793-982 4.36e-31

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: 120.87  E-value: 4.36e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  793 IVTSIITSETLYVECLNKM-KQYMKAIRATLTTSqpvisEEEFQTIFFKIEDLHEVHSEFLteLQARLAAPDDATapdtg 871
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILvEVFLPPNSKPLSES-----EEEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQ----- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  872 glCVGEPFRRLAGQIHLYGAFLHNYGRAIDTVKMCSTHSQQFKEIVSNIVfKNQNEQKLSLEELLHKPVARVQKNALVLE 951
Cdd:pfam00621   69 --RIGDIFLKFAPGFKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELE-ANPECRGLDLNSFLIKPVQRIPRYPLLLK 145
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2449489708  952 DLLNQTPEQHPDYHPLRQASKAIRNFLSEFN 982
Cdd:pfam00621  146 ELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
791-982 9.44e-27

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: 108.54  E-value: 9.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  791 RRIVTSIITSETLYVECLNKM-KQYMKAIRATLTTsqpvISEEEFQTIFFKIEDLHEVHSEFLTELQARLAAPDDAtapd 869
Cdd:cd00160      2 QEVIKELLQTERNYVRDLKLLvEVFLKPLDKELLP----LSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKS---- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  870 tgGLCVGEPFRRLAGQIHLYGAFLHNYGRAIDTVKMCSTHSQQFKEIVSNIvfkNQNEQKLSLEELLHKPVARVQKNALV 949
Cdd:cd00160     74 --GPRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKA---ESECGRLKLESLLLKPVQRLTKYPLL 148
                          170       180       190
                   ....*....|....*....|....*....|...
gi 2449489708  950 LEDLLNQTPEQHPDYHPLRQASKAIRNFLSEFN 982
Cdd:cd00160    149 LKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
C2_ABR cd08686
C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is ...
1207-1316 2.52e-23

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: 96.42  E-value: 2.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1207 LHLTIQGLSGFDQQCDLFVCVEIDSYGHYFRKAKTKLVCCSATPQWNESFVLELEGSQNLRILLYQ----------ADVQ 1276
Cdd:cd08686      1 LNVIVHSAQGFKQSANLYCTLEVDSFGYFVKKAKTRVCRDTTEPNWNEEFEIELEGSQTLRILCYEkcyskvkldgEGTD 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2449489708 1277 RPILRAKHILKLSRSWMQETpTRKVLQLSEtLSISTIIRF 1316
Cdd:cd08686     81 AIMGKGQIQLDPQSLQTKKW-QEKVISMNG-ITVNLSIKF 118
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
1207-1274 1.16e-04

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: 42.86  E-value: 1.16e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2449489708  1207 LHLTI---QGLSGFD--QQCDLFVCVEIDSYGHyfRKAKTKLVCCSATPQWNESFVLEL--EGSQNLRILLYQAD 1274
Cdd:smart00239    2 LTVKIisaRNLPPKDkgGKSDPYVKVSLDGDPK--EKKKTKVVKNTLNPVWNETFEFEVppPELAELEIEVYDKD 74
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
793-983 6.98e-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: 41.03  E-value: 6.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  793 IVTSIITSETLYVECLNKMKQYMkaIRATLTTSqpVISE---EEF-QTIFFKIEDLHEVHSEFLTELQARLA-APDDATA 867
Cdd:COG5422    488 AIYEVIYTERDFVKDLEYLRDTW--IKPLEESN--IIPEnarRNFiKHVFANINEIYAVNSKLLKALTNRQClSPIVNGI 563
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  868 PDTGGLCVG--EPFRR-LAGQihLYGAFL--------HNYGRAIDTVKMCSThsqqfkeivsnivfknqnEQKLSLEELL 936
Cdd:COG5422    564 ADIFLDYVPkfEPFIKyGASQ--PYAKYEfereksvnPNFARFDHEVERLDE------------------SRKLELDGYL 623
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2449489708  937 HKPVARVQKNALVLEDLLNQTPEQHPDYHPLRQASKAIRNFLSEFNV 983
Cdd:COG5422    624 TKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNF 670
C2 pfam00168
C2 domain;
1205-1271 9.34e-03

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 37.30  E-value: 9.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2449489708 1205 GDLHLTI---QGL--SGFDQQCDLFVCVEIDSYGHyfrKAKTKLVCCSATPQWNESFVLEL--EGSQNLRILLY 1271
Cdd:pfam00168    1 GRLTVTVieaKNLppKDGNGTSDPYVKVYLLDGKQ---KKKTKVVKNTLNPVWNETFTFSVpdPENAVLEIEVY 71
 
Name Accession Description Interval E-value
PH_BCR_arthropod cd13368
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
977-1165 4.06e-99

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: 315.24  E-value: 4.06e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  977 FLSEFNVVQTRTMFPSDDKALRRLVKNSFIVELADGHRKLRHLLLFNDVIACAKYKAVGRTgdrnGFEFELKWFIPLRDI 1056
Cdd:cd13368      1 FLNEFNNIQTKSMFPHQDRALRRLVKNSFIVELADGHRKLRHLFLFNDVIACAKYKSSGRT----RITFELKWFIPLNDV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1057 LICEESANDPKETSPINIVHLKSQACTVRDQIMLDEKDRPGGSsragDKHRKKLADLEAQLVLASPNLVFKIGNKaTGKT 1136
Cdd:cd13368     77 TILEEEAPAPKESSPPNIEQLKSNACQVRDQLADRSRASTSGS----DKIRKKLADLEAQLVLASPNLVFRIGNK-NNKT 151
                          170       180
                   ....*....|....*....|....*....
gi 2449489708 1137 MTFFLSSDFERTQWIESILSLQQSCNLPG 1165
Cdd:cd13368    152 YTFFLSSEFERTQWIEAILTLQQTCPLPG 180
PH_BCR-related cd01228
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
998-1160 1.72e-65

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: 219.14  E-value: 1.72e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  998 RRLVKNSFIVELADGHRKLRHLLLFNDVIACAKYKAVGRtgDRNGfEFELKWFIPLRDILICEESANDPKETSPINIVH- 1076
Cdd:cd01228      1 RQLVKDGFLVELSEGSRKLRHLFLFTDVLLCAKLKSAGR--GFQG-QYECKWYIPLRDLSLHPKDESEASPIVPVTSDKe 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1077 ---LKSQACTVRDQIMLDEKDRPGGSS---RAGDKHRKKLADLEAQLVLASPNLVFKIGNKaTGKTMTFFLSSDFERTQW 1150
Cdd:cd01228     78 levLKSKIAELKKQIRDDDAQRKKASSsgsKAIEKLRKKLAEQEAALLLASPSLPLRLYHR-NGKTYTFLLSSDYERSEW 156
                          170
                   ....*....|
gi 2449489708 1151 IESILSLQQS 1160
Cdd:cd01228    157 KEAILKLQKK 166
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
1335-1530 9.59e-57

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: 195.15  E-value: 9.59e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEQLLKEVDIHSVTGILKSY 1414
Cdd:cd04387      1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLSEMDVNAIAGTLKLY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1415 LRDLPEALFTDQYYPKFFDAFN-RHSNLSEGSRIHELQrifaELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVF 1493
Cdd:cd04387     81 FRELPEPLFTDELYPNFAEGIAlSDPVAKESCMLNLLL----SLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVF 156
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2449489708 1494 GPTLLRPGPSATK--QKDLLESSTADVMTQAGILYSFLQ 1530
Cdd:cd04387    157 GPTLLRPSEKESKipTNTMTDSWSLEVMSQVQVLLYFLQ 195
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
1351-1500 4.28e-54

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 185.44  E-value: 4.28e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1351 PFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEqLLKEVDIHSVTGILKSYLRDLPEALFTDQYYPK 1430
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDL-DLEEEDVHVVASLLKLFLRELPEPLLTFELYEE 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1431 FFDAFNRHSnlsEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFGPTLLRP 1500
Cdd:pfam00620   80 FIEAAKLPD---EEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRP 146
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
1348-1506 1.14e-51

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: 179.77  E-value: 1.14e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  1348 RDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAeQLLKEVDIHSVTGILKSYLRDLPEALFTDQY 1427
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPD-LDLSEYDVHDVAGLLKLFLRELPEPLITYEL 79
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2449489708  1428 YPKFFDAFNrhsNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFGPTLLRPGPSATK 1506
Cdd:smart00324   80 YEEFIEAAK---LEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVA 155
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
1351-1530 1.35e-46

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: 165.17  E-value: 1.35e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1351 PFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEaeQLLKEVDIHSVTGILKSYLRDLPEALFTDQYYPK 1430
Cdd:cd00159      1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDI--DDLEDYDVHDVASLLKLYLRELPEPLIPFELYDE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1431 FFDAfnrHSNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFGPTLLRPgpsatkqKDL 1510
Cdd:cd00159     79 FIEL---AKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRP-------PDS 148
                          170       180
                   ....*....|....*....|
gi 2449489708 1511 LESSTADVMTQAGILYSFLQ 1530
Cdd:cd00159    149 DDELLEDIKKLNEIVEFLIE 168
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1335-1498 2.36e-40

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: 147.94  E-value: 2.36e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEQLLKEV---DIHSVTGIL 1411
Cdd:cd04398      1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLISPEDyesDIHSVASLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1412 KSYLRDLPEALFTDQYYPKFFDAFNrhsNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAM 1491
Cdd:cd04398     81 KLFFRELPEPLLTKALSREFIEAAK---IEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAI 157

                   ....*..
gi 2449489708 1492 VFGPTLL 1498
Cdd:cd04398    158 IWGPTLM 164
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1335-1533 9.53e-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: 143.72  E-value: 9.53e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEqlLKEVDIHSVTGILKSY 1414
Cdd:cd04378      1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVE--LSELSPHDISSVLKLF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1415 LRDLPEALFTDQYYPKFFDAFNRHSNLSEGSR-----------IHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENK 1483
Cdd:cd04378     79 LRQLPEPLILFRLYNDFIALAKEIQRDTEEDKapntpievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENK 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1484 MSLHNLAMVFGPTLLRPGPsatkqkdllesSTADVMTQAGILYSFlQARL 1533
Cdd:cd04378    159 MSPNNLGIVFGPTLIRPRP-----------GDADVSLSSLVDYGY-QARL 196
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1335-1501 5.84e-38

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: 140.99  E-value: 5.84e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKksFETNAYEAEQLL--KEVDIHSVTGILK 1412
Cdd:cd04403      1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLR--FAVDHDEKLDLDdsKWEDIHVITGALK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1413 SYLRDLPEALFTDQYYPKFFDAFNrhsnLSEG-SRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAM 1491
Cdd:cd04403     79 LFFRELPEPLFPYSLFNDFVAAIK----LSDYeQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAI 154
                          170
                   ....*....|
gi 2449489708 1492 VFGPTLLRPG 1501
Cdd:cd04403    155 VFGPTLLRPE 164
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1335-1505 9.35e-38

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: 140.73  E-value: 9.35e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEqLLKEV--DIHSVTGILK 1412
Cdd:cd04372      1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKAD-ISATVypDINVITGALK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1413 SYLRDLPEALFTDQYYPKFFDAfNRHSNLSEgsRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMV 1492
Cdd:cd04372     80 LYFRDLPIPVITYDTYPKFIDA-AKISNPDE--RLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIV 156
                          170
                   ....*....|...
gi 2449489708 1493 FGPTLLRPGPSAT 1505
Cdd:cd04372    157 FGPTLMRPPEDSA 169
PH_ABR cd13366
Active breakpoint cluster region-related protein pleckstrin homology (PH) domain; The ABR ...
977-1159 3.28e-36

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: 135.90  E-value: 3.28e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  977 FLSEFN--VVQTRTMFPSDDKALRRLVKNSFIVELADGHRKLRHLLLFNDVIACAKYK--AVGRTGdrngfEFELKWFIP 1052
Cdd:cd13366      1 FLSSINedIDPRRTAVTTPKGETRQLVKDGFLVEVSEGSRKLRHVFLFTDLLLCAKLKktAVGKHQ-----QYDCKWYIP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1053 LRDILIceesaNDPKETSPINIVH---------LKSQACTVRDQIMlDEKDRPGGSSRAGDKHRKKLADLEAQLVLASPN 1123
Cdd:cd13366     76 LADLVF-----PSPEESESLPQVHtlpdheieeMKMKISAIKSEIQ-KEKKNKKGQSRAIERLKKKMFENESWLLLNSPT 149
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2449489708 1124 LVFKIGNKaTGKTMTFFLSSDFERTQWIESILSLQQ 1159
Cdd:cd13366    150 IPFRIHNK-NGKSYLFLLSSDYERSEWREAIQKLQK 184
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1335-1519 1.05e-35

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: 135.28  E-value: 1.05e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEQLLKEVDIHSVTGILKSY 1414
Cdd:cd04386      5 FGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFYSDPHAVASALKSY 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1415 LRDLPEALFTDQYYPKFFDAFNRHsnlSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFG 1494
Cdd:cd04386     85 LRELPDPLLTYNLYEDWVQAANKP---DEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLA 161
                          170       180
                   ....*....|....*....|....*
gi 2449489708 1495 PTLLRPGPSATKQKDLLESSTADVM 1519
Cdd:cd04386    162 PNLLWAKNEGSLAEMAAGTSVHVVA 186
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1335-1530 2.09e-35

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: 134.06  E-value: 2.09e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQV-IKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAE-QLLKEVDIHSVTGILK 1412
Cdd:cd04395      2 FGVPLDDCpPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDlQDPRWRDVNVVSSLLK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1413 SYLRDLPEALFTDQYYPKFFDAfNRHSNLSEgsRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMV 1492
Cdd:cd04395     82 SFFRKLPEPLFTNELYPDFIEA-NRIEDPVE--RLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIV 158
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2449489708 1493 FGPTLLRPGpsatkqKDLLESSTADVMTQAGILYSFLQ 1530
Cdd:cd04395    159 FGPTLVRTS------DDNMETMVTHMPDQCKIVETLIQ 190
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1350-1529 6.03e-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: 132.42  E-value: 6.03e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1350 IPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSF---ETNAyeaeqLLKEVDIHSVTGILKSYLRDLPEALFTDQ 1426
Cdd:cd04382     17 IPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFlrgKTVP-----NLSKVDIHVICGCLKDFLRSLKEPLITFA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1427 YYPKFFDAFNrhsNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEiENKMSLHNLAMVFGPTLLRPGPSATK 1506
Cdd:cd04382     92 LWKEFMEAAE---ILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSP-ECKMDINNLARVFGPTIVGYSVPNPD 167
                          170       180
                   ....*....|....*....|...
gi 2449489708 1507 QKDLLEsstaDVMTQAGILYSFL 1529
Cdd:cd04382    168 PMTILQ----DTVRQPRVVERLL 186
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1349-1501 1.13e-34

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: 131.28  E-value: 1.13e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1349 DIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEQLLKEVDIHSVTGILKSYLRDLPEALFTDQYY 1428
Cdd:cd04385     14 DIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSELH 93
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2449489708 1429 PKFFDAFN-RHSNlsegSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFGPTLLRPG 1501
Cdd:cd04385     94 AEWIEAAElENKD----ERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTD 163
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1335-1506 4.55e-34

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: 130.66  E-value: 4.55e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKRE--KRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAyEAEQLLKEV--DIHSVTGI 1410
Cdd:cd04379      1 FGVPLSRLVEREgeSRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNS-AAVELSEELypDINVITGV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1411 LKSYLRDLPEALFTDQYYPKFFDAFNRHS-NLSEGSRIHELqRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNL 1489
Cdd:cd04379     80 LKDYLRELPEPLITPQLYEMVLEALAVALpNDVQTNTHLTL-SIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNL 158
                          170
                   ....*....|....*..
gi 2449489708 1490 AMVFGPTLLRPGPSATK 1506
Cdd:cd04379    159 AVCFGPVLMFCSQEFSR 175
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1335-1525 1.85e-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: 126.08  E-value: 1.85e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEqlLKEVDIHSVTGILKSY 1414
Cdd:cd04409      1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVE--LSELSPHDISNVLKLY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1415 LRDLPEALFTDQYYPKFFDAFNRHSNLSEGSRIH------------ELQRI-------FAELPQPNKATINLLLDHLMRV 1475
Cdd:cd04409     79 LRQLPEPLILFRLYNEFIGLAKESQHVNETQEAKknsdkkwpnmctELNRIllkskdlLRQLPAPNYNTLQFLIVHLHRV 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1476 HQQEIENKMSLHNLAMVFGPTLLRPGPSatkQKDLLESSTADVMTQAGIL 1525
Cdd:cd04409    159 SEQAEENKMSASNLGIIFGPTLIRPRPT---DATVSLSSLVDYPHQARLV 205
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1335-1510 1.36e-31

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: 122.55  E-value: 1.36e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKrEKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEqlLKEVDIHSVTGILKSY 1414
Cdd:cd04377      1 FGVSLSSLTS-EDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVN--LEDYPIHVITSVLKQW 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1415 LRDLPEALFTDQYYPKFFDAfnrhSNLSE-GSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVF 1493
Cdd:cd04377     78 LRELPEPLMTFELYENFLRA----MELEEkQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVF 153
                          170
                   ....*....|....*..
gi 2449489708 1494 GPTLLRPGPSATKQKDL 1510
Cdd:cd04377    154 APCILRCPDTADPLQSL 170
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
793-982 1.38e-31

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: 122.41  E-value: 1.38e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708   793 IVTSIITSETLYVECLNKM-KQYMKAIRATLTtsqpVISEEEFQTIFFKIEDLHEVHSEFLTELQARLAAPDDAtapdtg 871
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLvEVFLKPLKKELK----LLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDS------ 70
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708   872 GLCVGEPFRRLAGQIHLYGAFLHNYGRAIDTVKMCSTHSQqFKEIVSNIvFKNQNEQKLSLEELLHKPVARVQKNALVLE 951
Cdd:smart00325   71 VERIGDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPR-FQKFLKEI-ESSPQCRRLTLESLLLKPVQRLTKYPLLLK 148
                           170       180       190
                    ....*....|....*....|....*....|.
gi 2449489708   952 DLLNQTPEQHPDYHPLRQASKAIRNFLSEFN 982
Cdd:smart00325  149 ELLKHTPEDHEDREDLKKALKAIKELANQVN 179
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
793-982 4.36e-31

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: 120.87  E-value: 4.36e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  793 IVTSIITSETLYVECLNKM-KQYMKAIRATLTTSqpvisEEEFQTIFFKIEDLHEVHSEFLteLQARLAAPDDATapdtg 871
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILvEVFLPPNSKPLSES-----EEEIKTIFSNIEEIYELHRQLL--LEELLKEWISIQ----- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  872 glCVGEPFRRLAGQIHLYGAFLHNYGRAIDTVKMCSTHSQQFKEIVSNIVfKNQNEQKLSLEELLHKPVARVQKNALVLE 951
Cdd:pfam00621   69 --RIGDIFLKFAPGFKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELE-ANPECRGLDLNSFLIKPVQRIPRYPLLLK 145
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2449489708  952 DLLNQTPEQHPDYHPLRQASKAIRNFLSEFN 982
Cdd:pfam00621  146 ELLKHTPPDHPDYEDLKKALEAIKEVAKQIN 176
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
1335-1503 6.55e-31

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: 121.08  E-value: 6.55e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEqlLKEVDIHSVTGILKSY 1414
Cdd:cd04408      1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVD--LSGHSPHDITSVLKHF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1415 LRDLPEALFTDQYYPKFFDAFNRHSNLSEG---------SRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMS 1485
Cdd:cd04408     79 LKELPEPVLPFQLYDDFIALAKELQRDSEKaaespsiveNIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMS 158
                          170
                   ....*....|....*...
gi 2449489708 1486 LHNLAMVFGPTLLRPGPS 1503
Cdd:cd04408    159 PNNLGIVFGPTLLRPLVG 176
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1335-1497 4.44e-30

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: 118.31  E-value: 4.44e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKR----DIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKsfetnAYEAEQL--LKEVDIHSVT 1408
Cdd:cd04381      1 FGASLSLAVERSRChdgiDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKA-----AYNRRESpnLEEYEPPTVA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1409 GILKSYLRDLPEALFTDQYYPKFFDAFNRhsnLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHN 1488
Cdd:cd04381     76 SLLKQYLRELPEPLLTKELMPRFEEACGR---PTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQN 152

                   ....*....
gi 2449489708 1489 LAMVFGPTL 1497
Cdd:cd04381    153 ISIVLSPTV 161
PH_BCR_vertebrate cd13367
Breakpoint Cluster Region-related pleckstrin homology (PH) domain; The BCR gene is one of the ...
998-1161 1.00e-29

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: 117.80  E-value: 1.00e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  998 RRLVKNSFIVELADGHRKLRHLLLFNDVIACAKYKAvgRTGDRnGFEFELKWFIPLRDILIceESANDPKETSPINIV-- 1075
Cdd:cd13367     24 RQLLKDSFMVELVEGARKLRHVFLFTDLLLCAKLKK--QIGGK-SQQYDCKWYIPLADLSF--QTVDESEAVPNIPLIpd 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1076 ----HLKSQACTVRDQIMLDEKDRPGGssRAGDKHRKKLADLEAQLVLASPNLVFKIGNKaTGKTMTFFLSSDFERTQWI 1151
Cdd:cd13367     99 eeidALKVKISQIKSDIQREKRANKGG--KVLERLRKKLSEQESLLLLMSPSMAFRVHNR-NGKSYTFLISSDYERAEWR 175
                          170
                   ....*....|
gi 2449489708 1152 ESILSLQQSC 1161
Cdd:cd13367    176 ENIREQQKKC 185
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1335-1502 1.34e-29

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: 117.22  E-value: 1.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRDIPFIVSACVREVERRGMTEvGIYRVSGSASDVAKLKKSFETNAyeAEQLLKEV---DIHSVTGIL 1411
Cdd:cd04384      3 FGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSEQ--IPDLTKDVyiqDIHSVSSLC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1412 KSYLRDLPEALFTDQYYPKFFDAFnrhSNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAM 1491
Cdd:cd04384     80 KLYFRELPNPLLTYQLYEKFSEAV---SAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAI 156
                          170
                   ....*....|.
gi 2449489708 1492 VFGPTLLRPGP 1502
Cdd:cd04384    157 VWAPNLLRSKQ 167
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
1349-1500 3.47e-29

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: 116.34  E-value: 3.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1349 DIPF-IVSACVREVERRGMTEVGIYRVSGSASDVAKL------KKSFETNAYEAEQllKEVDIHSVTGILKSYLRDLPEA 1421
Cdd:cd04374     26 DIGFkFVRKCIEAVETRGINEQGLYRVVGVNSKVQKLlslgldPKTSTPGDVDLDN--SEWEIKTITSALKTYLRNLPEP 103
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2449489708 1422 LFTDQYYPKFFDAFNrhsNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFGPTLLRP 1500
Cdd:cd04374    104 LMTYELHNDFINAAK---SENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRP 179
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
1334-1497 5.47e-28

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: 112.45  E-value: 5.47e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1334 LFGAKLQQVI-----KREKRDIPFIVSACVREVE-RRGMTEVGIYRVSGSASDVAKLKKSFETNA-YEAEQLLKEVDIHS 1406
Cdd:cd04400      1 IFGSPLEEAVelsshKYNGRDLPSVVYRCIEYLDkNRAIYEEGIFRLSGSASVIKQLKERFNTEYdVDLFSSSLYPDVHT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1407 VTGILKSYLRDLPEALFTDQYYPKFFDAFNRHSNLSEgsRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSL 1486
Cdd:cd04400     81 VAGLLKLYLRELPTLILGGELHNDFKRLVEENHDRSQ--RALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNL 158
                          170
                   ....*....|.
gi 2449489708 1487 HNLAMVFGPTL 1497
Cdd:cd04400    159 RNVCIVFSPTL 169
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1334-1526 3.82e-27

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: 110.90  E-value: 3.82e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1334 LFGAKLQQVIKRE-KRD----IPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEQLLKEVDIHSVT 1408
Cdd:cd04391      1 LFGVPLSTLLERDqKKVpgskVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKFYEGTFLWDQVKQHDAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1409 GILKSYLRDLPEALFTDQYypkfFDAFNRHSNL-SEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLH 1487
Cdd:cd04391     81 SLLKLFIRELPQPLLTVEY----LPAFYSVQGLpSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLW 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2449489708 1488 NLAMVFGPTL-----LRPGPSATKQKDLLESSTADVMTQAGILY 1526
Cdd:cd04391    157 NVAMIMAPNLfpprgKHSKDNESLQEEVNMAAGCANIMRLLIRY 200
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1335-1500 8.35e-27

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: 108.70  E-value: 8.35e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKrDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNaYEAEQLLKEVDIHSVTGILKSY 1414
Cdd:cd04373      1 FGVPLANVVTSEK-PIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQD-HNLDLVSKDFTVNAVAGALKSF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1415 LRDLPEALFTDQYYPKFFDAFnRHSNLSEgsRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFG 1494
Cdd:cd04373     79 FSELPDPLIPYSMHLELVEAA-KINDREQ--RLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFW 155

                   ....*.
gi 2449489708 1495 PTLLRP 1500
Cdd:cd04373    156 PTLMRP 161
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
791-982 9.44e-27

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: 108.54  E-value: 9.44e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  791 RRIVTSIITSETLYVECLNKM-KQYMKAIRATLTTsqpvISEEEFQTIFFKIEDLHEVHSEFLTELQARLAAPDDAtapd 869
Cdd:cd00160      2 QEVIKELLQTERNYVRDLKLLvEVFLKPLDKELLP----LSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKS---- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  870 tgGLCVGEPFRRLAGQIHLYGAFLHNYGRAIDTVKMCSTHSQQFKEIVSNIvfkNQNEQKLSLEELLHKPVARVQKNALV 949
Cdd:cd00160     74 --GPRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKA---ESECGRLKLESLLLKPVQRLTKYPLL 148
                          170       180       190
                   ....*....|....*....|....*....|...
gi 2449489708  950 LEDLLNQTPEQHPDYHPLRQASKAIRNFLSEFN 982
Cdd:cd00160    149 LKELLKHTPDGHEDREDLKKALEAIKEVASQVN 181
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1335-1505 1.79e-26

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: 108.19  E-value: 1.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKR--EKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFetNAYEAEQLLKEVDIHSVTGILK 1412
Cdd:cd04404      6 FGVSLQFLKEKnpEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKY--NMGEPVDFDQYEDVHLPAVILK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1413 SYLRDLPEALFTDQYYPKFFDafnrHSNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMV 1492
Cdd:cd04404     84 TFLRELPEPLLTFDLYDDIVG----FLNVDKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVV 159
                          170
                   ....*....|...
gi 2449489708 1493 FGPTLLRPGPSAT 1505
Cdd:cd04404    160 FGPNLLWAKDASM 172
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1335-1515 2.22e-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: 107.77  E-value: 2.22e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKrEKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAyeAEQLLKEVDIHSVTGILKSY 1414
Cdd:cd04407      1 FGVRVGSLTS-NKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADP--ENVKLENYPIHAITGLLKQW 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1415 LRDLPEALFTDQYYPKFFDAFNrhsnLSEgsRIHELQRIFA---ELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAM 1491
Cdd:cd04407     78 LRELPEPLMTFAQYNDFLRAVE----LPE--KQEQLQAIYRvleQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAI 151
                          170       180
                   ....*....|....*....|....*..
gi 2449489708 1492 VFGPTLLRPGPSA---TKQKDLLESST 1515
Cdd:cd04407    152 VFAPCLLRCPDSSdplTSMKDVAKTTT 178
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1334-1510 1.26e-25

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: 105.62  E-value: 1.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1334 LFGAKLQQVIKREKRD--IPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNayEAEQLLKEVDIHSVTGIL 1411
Cdd:cd04393      2 VFGVPLQELQQAGQPEngVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSG--EEVDLSKEADVCSAASLL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1412 KSYLRDLPEALFTDQYYPKFFDAFNRHSNLSEGSRihELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAM 1491
Cdd:cd04393     80 RLFLQELPEGLIPASLQIRLMQLYQDYNGEDEFGR--KLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAA 157
                          170       180
                   ....*....|....*....|.
gi 2449489708 1492 VFGPTL--LRPGPSATKQKDL 1510
Cdd:cd04393    158 VFGPDVfhVYTDVEDMKEQEI 178
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1334-1507 3.59e-25

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: 104.42  E-value: 3.59e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1334 LFGAKLQQVIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEQLLKEVDIHSVTGILKS 1413
Cdd:cd04383      2 LFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADDQNDHDINSVAGVLKL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1414 YLRDLPEALFTDQYYPKFFDAFnRHSNLSEgsRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVF 1493
Cdd:cd04383     82 YFRGLENPLFPKERFEDLMSCV-KLENPTE--RVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICF 158
                          170
                   ....*....|....
gi 2449489708 1494 GPTLLrPGPSATKQ 1507
Cdd:cd04383    159 GPTLM-PVPEGQDQ 171
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1333-1500 1.09e-24

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: 103.29  E-value: 1.09e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1333 ALFGAKLQQVIKREK----RDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFEtnAYEAEQLLKEVDIHSVT 1408
Cdd:cd04390      1 GVFGQRLEDTVAYERkfgpRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFD--AGERPSFDSDTDVHTVA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1409 GILKSYLRDLPEALFTDQYYPKFFDAFNRhSNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHN 1488
Cdd:cd04390     79 SLLKLYLRELPEPVIPWAQYEDFLSCAQL-LSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQN 157
                          170
                   ....*....|..
gi 2449489708 1489 LAMVFGPTLLRP 1500
Cdd:cd04390    158 LATVFGPNILRP 169
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1348-1518 4.25e-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: 101.75  E-value: 4.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1348 RDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAyeAEQLLKEVDIHSVTGILKSYLRDLPEALFTDQY 1427
Cdd:cd04376      7 RQVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGI--DVVLDENHSVHDVAALLKEFFRDMPDPLLPREL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1428 YPKFFDAfnrhSNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQ----------QEIE-NKMSLHNLAMVFGPT 1496
Cdd:cd04376     85 YTAFIGT----ALLEPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEhaadsidedgQEVSgNKMTSLNLATIFGPN 160
                          170       180
                   ....*....|....*....|....*.
gi 2449489708 1497 LLRPGPSATK----QKDLLESSTADV 1518
Cdd:cd04376    161 LLHKQKSGERefvqASLRIEESTAII 186
C2_ABR cd08686
C2 domain in the Active BCR (Breakpoint cluster region) Related protein; The ABR protein is ...
1207-1316 2.52e-23

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: 96.42  E-value: 2.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1207 LHLTIQGLSGFDQQCDLFVCVEIDSYGHYFRKAKTKLVCCSATPQWNESFVLELEGSQNLRILLYQ----------ADVQ 1276
Cdd:cd08686      1 LNVIVHSAQGFKQSANLYCTLEVDSFGYFVKKAKTRVCRDTTEPNWNEEFEIELEGSQTLRILCYEkcyskvkldgEGTD 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2449489708 1277 RPILRAKHILKLSRSWMQETpTRKVLQLSEtLSISTIIRF 1316
Cdd:cd08686     81 AIMGKGQIQLDPQSLQTKKW-QEKVISMNG-ITVNLSIKF 118
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1335-1499 1.36e-19

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: 88.13  E-value: 1.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQvIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEqlLKEVDIHSVTGILKSY 1414
Cdd:cd04406      1 FGVELSR-LTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVN--LDDYNIHVIASVFKQW 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1415 LRDLPEALFTDQYYPKFFDAFNRHSnlsEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFG 1494
Cdd:cd04406     78 LRDLPNPLMTFELYEEFLRAMGLQE---RRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFA 154

                   ....*
gi 2449489708 1495 PTLLR 1499
Cdd:cd04406    155 PCILR 159
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1335-1499 1.73e-17

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: 82.05  E-value: 1.73e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREK-----RDIPFIVSACVREVERRG--MTEvGIYRVSGSASDVAKLKKSFETNAYEAEQLlkeVDIHSV 1407
Cdd:cd04389      1 FGSSLEEIMDRQKekypeLKLPWILTFLSEKVLALGgfQTE-GIFRVPGDIDEVNELKLRVDQWDYPLSGL---EDPHVP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1408 TGILKSYLRDLPEALFTDQYYPKFFDAFNRHSNLSEgsrihelqrIFAELPQPNKATINLLLDHLMRVHQQEI--ENKMS 1485
Cdd:cd04389     77 ASLLKLWLRELEEPLIPDALYQQCISASEDPDKAVE---------IVQKLPIINRLVLCYLINFLQVFAQPENvaHTKMD 147
                          170
                   ....*....|....
gi 2449489708 1486 LHNLAMVFGPTLLR 1499
Cdd:cd04389    148 VSNLAMVFAPNILR 161
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1334-1512 2.17e-17

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: 81.96  E-value: 2.17e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1334 LFGAKLQQVIKREkrDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAyeaEQLLKEVDIHSVTGILKS 1413
Cdd:cd04402      1 LFGQPLSNICEDD--NLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGV---EVDLKAEPVLLLASVLKD 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1414 YLRDLPEALFTDQYYPKFFDAFNRhSNLSEgsRIHELQRIFAELPQPNKatinLLLDHLMRV-H---QQEIENKMSLHNL 1489
Cdd:cd04402     76 FLRNIPGSLLSSDLYEEWMSALDQ-ENEEE--KIAELQRLLDKLPRPNV----LLLKHLICVlHnisQNSETNKMDAFNL 148
                          170       180
                   ....*....|....*....|...
gi 2449489708 1490 AMVFGPTLLRPGPSATKQKDLLE 1512
Cdd:cd04402    149 AVCIAPSLLWPPASSELQNEDLK 171
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1370-1500 2.25e-17

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: 82.51  E-value: 2.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1370 GIYRVSGSASDVAKLKksfetnayeaEQLLKEVDI---------HSVTGILKSYLRDLPEALFTDQYYP---------KF 1431
Cdd:cd04392     28 GLFRKPGNSARQQELR----------DLLNSGTDLdlesggfhaHDCATVLKGFLGELPEPLLTHAHYPahlqiadlcQF 97
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2449489708 1432 FDAFNRHSNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFGPTLLRP 1500
Cdd:cd04392     98 DEKGNKTSAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICP 166
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1350-1498 4.12e-14

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: 73.21  E-value: 4.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1350 IPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEQLLKE-VDIHSVTGILKSYLRDLPEALFTDQYY 1428
Cdd:cd04396     32 IPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDYGKSFDWDgYTVHDAASVLRRYLNNLPEPLVPLDLY 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1429 PKF--------------FDAFNRHSNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFG 1494
Cdd:cd04396    112 EEFrnplrkrprilqymKGRINEPLNTDIDQAIKEYRDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIFQ 191

                   ....
gi 2449489708 1495 PTLL 1498
Cdd:cd04396    192 PGIL 195
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1332-1497 1.54e-13

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: 71.68  E-value: 1.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1332 GALFGAKLQQVIKREKRDIPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFEtnAYEAEQLLKEVDIHSVTGIL 1411
Cdd:cd04375      2 KNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIE--SSTDNVNYDGQQAYDVADML 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1412 KSYLRDLPEALFTDQYYPKFFDAFnrhSNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAM 1491
Cdd:cd04375     80 KQYFRDLPEPLLTNKLSETFIAIF---QYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAV 156

                   ....*.
gi 2449489708 1492 VFGPTL 1497
Cdd:cd04375    157 CLAPSL 162
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1346-1498 3.64e-11

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: 64.03  E-value: 3.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1346 EKRDIP-FIVSACvREVERRGMTEvGIYRVSGSASDVAKLKKSFEtnayEAEQLLKEVDIHSVTGILKSYLRDLPEALFT 1424
Cdd:cd04394     16 EYGNVPkFLVDAC-TFLLDHLSTE-GLFRKSGSVVRQKELKAKLE----GGEACLSSALPCDVAGLLKQFFRELPEPLLP 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2449489708 1425 DQYYpkffDAFNRHSNLSEG-SRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFGPTLL 1498
Cdd:cd04394     90 YDLH----EALLKAQELPTDeERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAPNLF 160
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1335-1509 9.58e-10

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: 60.07  E-value: 9.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRD-----------IPFIVSACVREVERRGMTEVGIYRVSGSASDVAKLKKSFETNAYEAEQLLKEVD 1403
Cdd:cd04397      1 FGVPLEILVEKFGADstlgvgpgklrIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPDLSKENP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1404 IHsVTGILKSYLRDLPEALFTDQYYpKFFDAFNRHSNLSEGSRIheLQRIFAELPQPNKATINLLLDHLMRV---HQ--Q 1478
Cdd:cd04397     81 VQ-LAALLKKFLRELPDPLLTFKLY-RLWISSQKIEDEEERKRV--LHLVYCLLPKYHRDTMEVLFSFLKWVssfSHidE 156
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2449489708 1479 EIENKMSLHNLAMVFGPTLLRPGPSATKQKD 1509
Cdd:cd04397    157 ETGSKMDIHNLATVITPNILYSKTDNPNTGD 187
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1351-1509 6.74e-09

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: 57.58  E-value: 6.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1351 PFIVSACVREVERRGMTEVGIYRvSGSASDVAKLKKSFETNAyeAEQLLKEVDIHSVTGILKSYLRDLPEALFTDQYYPK 1430
Cdd:cd04388     16 PPLLIKLVEAIEKKGLESSTLYR-TQSSSSLTELRQILDCDA--ASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYSE 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2449489708 1431 FFDAFNRHSNLSEGSRIHELQRIFAELPQPNKATINLLLDHLMRVHQQEIENKMSLHNLAMVFGPTLLRPGPSATKQKD 1509
Cdd:cd04388     93 MISRAQEVQSSDEYAQLLRKLIRSPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQPASSDSPE 171
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1335-1500 4.05e-07

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: 52.33  E-value: 4.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1335 FGAKLQQVIKREKRDIPFIVSAC-----------VREVERRGmtevgIYRVSGSASDVAKLKKSFETNAYEAEQL--LKE 1401
Cdd:cd04399      1 FGVDLETRCRLDKKVVPLIVSAIlsyldqlypdlINDEVRRN-----VWTDPVSLKETHQLRNLLNKPKKPDKEViiLKK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708 1402 VDIHSVTGILKSYLRDLPEALFTDQYYPKFFDAFNRHSNLSEGS---RIHELQRIFAELPQPNKATINLLLDHLMR---- 1474
Cdd:cd04399     76 FEPSTVASVLKLYLLELPDSLIPHDIYDLIRSLYSAYPPSQEDSdtaRIQGLQSTLSQLPKSHIATLDAIITHFYRliei 155
                          170       180
                   ....*....|....*....|....*.
gi 2449489708 1475 VHQQEIENKMSLHnLAMVFGPTLLRP 1500
Cdd:cd04399    156 TKMGESEEEYADK-LATSLSREILRP 180
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
1207-1274 1.16e-04

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: 42.86  E-value: 1.16e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2449489708  1207 LHLTI---QGLSGFD--QQCDLFVCVEIDSYGHyfRKAKTKLVCCSATPQWNESFVLEL--EGSQNLRILLYQAD 1274
Cdd:smart00239    2 LTVKIisaRNLPPKDkgGKSDPYVKVSLDGDPK--EKKKTKVVKNTLNPVWNETFEFEVppPELAELEIEVYDKD 74
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
1207-1275 2.74e-04

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: 41.67  E-value: 2.74e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2449489708 1207 LHLTI---QGLSGFDQQ--CDLFVCVEIDSyghyFRKAKTKLVCCSATPQWNESFVLELE--GSQNLRILLYQADV 1275
Cdd:cd00030      1 LRVTVieaRNLPAKDLNgkSDPYVKVSLGG----KQKFKTKVVKNTLNPVWNETFEFPVLdpESDTLTVEVWDKDR 72
PH_RARhoGAP cd13319
RA and RhoGAP domain-containing protein Pleckstrin homology PH domain; RARhoGAP (also called ...
1007-1056 5.85e-03

RA and RhoGAP domain-containing protein Pleckstrin homology PH domain; RARhoGAP (also called Rho GTPase-activating protein 20 and ARHGAP20 ) is thought to function in rearrangements of the cytoskeleton and cell signaling events that occur during spermatogenesis. RARhoGAP was also shown to be activated by Rap1 and to induce inactivation of Rho, resulting in the neurite outgrowth. Recent findings show that ARHGAP20, even although it is located in the middle of the MDR on 11q22-23, is expressed at higher levels in chronic lymphocytic leukemia patients with 11q22-23 and/or 13q14 deletions and its expression pattern suggests a functional link between cases with 11q22-23 and 13q14 deletions. The mechanism needs to be further studied. RARhoGAP contains a PH domain, a Ras-associating domain, a Rho-GAP domain, and ANXL repeats. 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: 270129  Cd Length: 97  Bit Score: 37.60  E-value: 5.85e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2449489708 1007 VELADGH-RKLRHLLLFNDVIACAKYKavgrtgdrNGFEFELKWFIPLRDI 1056
Cdd:cd13319      9 VQLTRGLqTQERHLFLFSDVLVVAKPK--------SKNSFKLKHKIRLSEL 51
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
793-983 6.98e-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: 41.03  E-value: 6.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  793 IVTSIITSETLYVECLNKMKQYMkaIRATLTTSqpVISE---EEF-QTIFFKIEDLHEVHSEFLTELQARLA-APDDATA 867
Cdd:COG5422    488 AIYEVIYTERDFVKDLEYLRDTW--IKPLEESN--IIPEnarRNFiKHVFANINEIYAVNSKLLKALTNRQClSPIVNGI 563
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2449489708  868 PDTGGLCVG--EPFRR-LAGQihLYGAFL--------HNYGRAIDTVKMCSThsqqfkeivsnivfknqnEQKLSLEELL 936
Cdd:COG5422    564 ADIFLDYVPkfEPFIKyGASQ--PYAKYEfereksvnPNFARFDHEVERLDE------------------SRKLELDGYL 623
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2449489708  937 HKPVARVQKNALVLEDLLNQTPEQHPDYHPLRQASKAIRNFLSEFNV 983
Cdd:COG5422    624 TKPTTRLARYPLLLEEVLKFTDPDNPDTEDIPKVIDMLREFLSRLNF 670
C2 pfam00168
C2 domain;
1205-1271 9.34e-03

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 37.30  E-value: 9.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2449489708 1205 GDLHLTI---QGL--SGFDQQCDLFVCVEIDSYGHyfrKAKTKLVCCSATPQWNESFVLEL--EGSQNLRILLY 1271
Cdd:pfam00168    1 GRLTVTVieaKNLppKDGNGTSDPYVKVYLLDGKQ---KKKTKVVKNTLNPVWNETFTFSVpdPENAVLEIEVY 71
 
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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