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Conserved domains on  [gi|767995437|ref|XP_011523377|]
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rho GTPase-activating protein 23 isoform X5 [Homo sapiens]

Protein Classification

PH_ARHGAP21-like and RhoGAP_ARHGAP21 domain-containing protein( domain architecture ID 10100884)

PH_ARHGAP21-like and RhoGAP_ARHGAP21 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 696-891 2.57e-133

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: 405.63  E-value: 2.57e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  696 AFGVRLEECQPATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDLNVISSLL 775
Cdd:cd04395     1 TFGVPLDDCPPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDPRWRDVNVVSSLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  776 KSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFG 855
Cdd:cd04395    81 KSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767995437  856 PTLVRTSEDNMTDMVTHMPDRYKIVETLIQHSDWFF 891
Cdd:cd04395   161 PTLVRTSDDNMETMVTHMPDQCKIVETLIQHYDWFF 196
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
 484-604 3.78e-52

ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. 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: 269955  Cd Length: 113  Bit Score: 178.33  E-value: 3.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  484 RREGWLYYKQILTKKGKKAGsgLRQWKRVYAALRARSLSLSKERREPGPAAAGAAAAGAgedeaaPVCIGSCLVDISYSE 563
Cdd:cd01253     1 AREGWLHYKQIVTDKGKRVS--DRSWKQAWAVLRGHSLYLYKDKREQTPALSIELGSEQ------RISIRGCIVDIAYSY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767995437  564 TKRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAIRENSRAE 604
Cdd:cd01253    73 TKRKHVFRLTTSDFSEYLFQAEDRDDMLGWIKAIQENSNAE 113
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 3-382 9.67e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 9.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437    3 PEPTSA-LPSDPRSPAAWSDPGLRVPPAARAHLDNSSLGMSQPRPSPGAFPHLSSEPRTPRAFPEPGsRVPPSRLECQQA 81
Cdd:PHA03247 2593 PQSARPrAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLG 2671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437   82 LSHWLSN--QVPRRAGERrcPAMAPRARSASQDRLEEVAAPRPWPCSTSQDA-LSQLGQEGWHRARSDDYLSRATRSAEA 158
Cdd:PHA03247 2672 RAAQASSppQRPRRRAAR--PTVGSLTSLADPPPPPPTPEPAPHALVSATPLpPGPAAARQASPALPAAPAPPAVPAGPA 2749

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  159 LGPGALVSPRFERCGWASQRSSARTPACPtrdlPGPQAPPPSGLQGLDDLGYI-GYRSYSPSFQRRTGLLHALSFRDSPF 237
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPAAG----PPRRLTRPAVASLSESRESLpSPWDPADPPAAVLAPAAALPPAASPA 2825

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  238 GGLPTFNLAQ----SPASFPPEASE----------------PPRVVRPEPSTRAlEPPAEDRGDEVVLRQ-----KPPTG 292
Cdd:PHA03247 2826 GPLPPPTSAQptapPPPPGPPPPSLplggsvapggdvrrrpPSRSPAAKPAAPA-RPPVRRLARPAVSRStesfaLPPDQ 2904

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  293 RKVQLTPARQMNLGFGDESPEPEASGRGERL-GRKVAPLATTEDSLASipfiDEPTSPSIDLQAKHVPASAV------VS 365
Cdd:PHA03247 2905 PERPPQPQAPPPPQPQPQPPPPPQPQPPPPPpPRPQPPLAPTTDPAGA----GEPSGAVPQPWLGALVPGRVavprfrVP 2980

                         410
                  ....*....|....*..
gi 767995437  366 SAMNSAPVLGTSPSSPT 382
Cdd:PHA03247 2981 QPAPSREAPASSTPPLT 2997
 
Name Accession Description Interval E-value
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 696-891 2.57e-133

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: 405.63  E-value: 2.57e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  696 AFGVRLEECQPATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDLNVISSLL 775
Cdd:cd04395     1 TFGVPLDDCPPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDPRWRDVNVVSSLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  776 KSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFG 855
Cdd:cd04395    81 KSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767995437  856 PTLVRTSEDNMTDMVTHMPDRYKIVETLIQHSDWFF 891
Cdd:cd04395   161 PTLVRTSDDNMETMVTHMPDQCKIVETLIQHYDWFF 196
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 711-887 6.42e-60

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 203.27  E-value: 6.42e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437    711 QRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDInlQDERWQDLNVISSLLKSFFRKLPEPLFTDD 790
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPD--LDLSEYDVHDVAGLLKLFLRELPEPLITYE 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437    791 KYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTDMv 870
Cdd:smart00324   79 LYEEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASL- 157

                           170
                    ....*....|....*..
gi 767995437    871 THMPDRYKIVETLIQHS 887
Cdd:smart00324  158 KDIRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 714-862 1.30e-58

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 198.15  E-value: 1.30e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437   714 PLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPgdINLQDERWQDLNVISSLLKSFFRKLPEPLFTDDKYN 793
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGP--DVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767995437   794 DFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTS 862
Cdd:pfam00620   79 EFIEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
 484-604 3.78e-52

ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. 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: 269955  Cd Length: 113  Bit Score: 178.33  E-value: 3.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  484 RREGWLYYKQILTKKGKKAGsgLRQWKRVYAALRARSLSLSKERREPGPAAAGAAAAGAgedeaaPVCIGSCLVDISYSE 563
Cdd:cd01253     1 AREGWLHYKQIVTDKGKRVS--DRSWKQAWAVLRGHSLYLYKDKREQTPALSIELGSEQ------RISIRGCIVDIAYSY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767995437  564 TKRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAIRENSRAE 604
Cdd:cd01253    73 TKRKHVFRLTTSDFSEYLFQAEDRDDMLGWIKAIQENSNAE 113
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
 485-597 1.77e-12

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 434701  Cd Length: 118  Bit Score: 65.14  E-value: 1.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437   485 REGWLYYKQILTKKGKKAGSGLRQWKRVYAALRARSLSLSKERREPGPAAAGAAAAGAGEDEAApVCIGSCLVDISYSET 564
Cdd:pfam15410    2 KKGIVMRKCCFESKGKKTPRGKRSWKMVYAVLKDLVLYLYKDEHPPESSQFEDKKSLKNAPVGK-IRLHHALATPAPDYT 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 767995437   565 KRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAI 597
Cdd:pfam15410   81 KKSHVFRLQTADGAEYLFQTGSPKELQEWVDTL 113
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 483-599 5.54e-12

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 63.34  E-value: 5.54e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437    483 IRREGWLYykqiltkkgKKAGSGLRQWKRVYAALRARSLSLSKERrepgpaaagaaAAGAGEDEAAPVCIGSCLVDI--S 560
Cdd:smart00233    1 VIKEGWLY---------KKSGGGKKSWKKRYFVLFNSTLLYYKSK-----------KDKKSYKPKGSIDLSGCTVREapD 60

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 767995437    561 YSETKRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAIRE 599
Cdd:smart00233   61 PDSSKKPHCFEIKTSDRKTLLLQAESEEEREKWVEALRK 99
PHA03247 PHA03247
large tegument protein UL36; Provisional
 3-382 9.67e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 9.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437    3 PEPTSA-LPSDPRSPAAWSDPGLRVPPAARAHLDNSSLGMSQPRPSPGAFPHLSSEPRTPRAFPEPGsRVPPSRLECQQA 81
Cdd:PHA03247 2593 PQSARPrAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLG 2671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437   82 LSHWLSN--QVPRRAGERrcPAMAPRARSASQDRLEEVAAPRPWPCSTSQDA-LSQLGQEGWHRARSDDYLSRATRSAEA 158
Cdd:PHA03247 2672 RAAQASSppQRPRRRAAR--PTVGSLTSLADPPPPPPTPEPAPHALVSATPLpPGPAAARQASPALPAAPAPPAVPAGPA 2749

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  159 LGPGALVSPRFERCGWASQRSSARTPACPtrdlPGPQAPPPSGLQGLDDLGYI-GYRSYSPSFQRRTGLLHALSFRDSPF 237
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPAAG----PPRRLTRPAVASLSESRESLpSPWDPADPPAAVLAPAAALPPAASPA 2825

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  238 GGLPTFNLAQ----SPASFPPEASE----------------PPRVVRPEPSTRAlEPPAEDRGDEVVLRQ-----KPPTG 292
Cdd:PHA03247 2826 GPLPPPTSAQptapPPPPGPPPPSLplggsvapggdvrrrpPSRSPAAKPAAPA-RPPVRRLARPAVSRStesfaLPPDQ 2904

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  293 RKVQLTPARQMNLGFGDESPEPEASGRGERL-GRKVAPLATTEDSLASipfiDEPTSPSIDLQAKHVPASAV------VS 365
Cdd:PHA03247 2905 PERPPQPQAPPPPQPQPQPPPPPQPQPPPPPpPRPQPPLAPTTDPAGA----GEPSGAVPQPWLGALVPGRVavprfrVP 2980

                         410
                  ....*....|....*..
gi 767995437  366 SAMNSAPVLGTSPSSPT 382
Cdd:PHA03247 2981 QPAPSREAPASSTPPLT 2997
 
Name Accession Description Interval E-value
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 696-891 2.57e-133

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: 405.63  E-value: 2.57e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  696 AFGVRLEECQPATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDLNVISSLL 775
Cdd:cd04395     1 TFGVPLDDCPPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDPRWRDVNVVSSLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  776 KSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFG 855
Cdd:cd04395    81 KSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767995437  856 PTLVRTSEDNMTDMVTHMPDRYKIVETLIQHSDWFF 891
Cdd:cd04395   161 PTLVRTSDDNMETMVTHMPDQCKIVETLIQHYDWFF 196
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 711-887 6.42e-60

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


Pssm-ID: 214618  Cd Length: 174  Bit Score: 203.27  E-value: 6.42e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437    711 QRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDInlQDERWQDLNVISSLLKSFFRKLPEPLFTDD 790
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPD--LDLSEYDVHDVAGLLKLFLRELPEPLITYE 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437    791 KYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTDMv 870
Cdd:smart00324   79 LYEEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASL- 157

                           170
                    ....*....|....*..
gi 767995437    871 THMPDRYKIVETLIQHS 887
Cdd:smart00324  158 KDIRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 714-862 1.30e-58

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 198.15  E-value: 1.30e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437   714 PLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPgdINLQDERWQDLNVISSLLKSFFRKLPEPLFTDDKYN 793
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGP--DVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYE 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767995437   794 DFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTS 862
Cdd:pfam00620   79 EFIEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 714-886 2.11e-55

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: 189.82  E-value: 2.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  714 PLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPgdiNLQDERWQDLNVISSLLKSFFRKLPEPLFTDDKYN 793
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGE---DIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  794 DFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTDMvTHM 873
Cdd:cd00159    78 EFIELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELL-EDI 156

                         170
                  ....*....|...
gi 767995437  874 PDRYKIVETLIQH 886
Cdd:cd00159   157 KKLNEIVEFLIEN 169
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 697-885 1.22e-54

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: 188.37  E-value: 1.22e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEE-CQpaTENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGdINLQDERWQDLNVISSLL 775
Cdd:cd04403     1 FGCHLEAlCQ--RENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEK-LDLDDSKWEDIHVITGAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  776 KSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFG 855
Cdd:cd04403    78 KLFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFG 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 767995437  856 PTLVRtSEDNMTDMVTHMPDRYKIVETLIQ 885
Cdd:cd04403   158 PTLLR-PEQETGNIAVHMVYQNQIVELILL 186
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
 484-604 3.78e-52

ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. 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: 269955  Cd Length: 113  Bit Score: 178.33  E-value: 3.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  484 RREGWLYYKQILTKKGKKAGsgLRQWKRVYAALRARSLSLSKERREPGPAAAGAAAAGAgedeaaPVCIGSCLVDISYSE 563
Cdd:cd01253     1 AREGWLHYKQIVTDKGKRVS--DRSWKQAWAVLRGHSLYLYKDKREQTPALSIELGSEQ------RISIRGCIVDIAYSY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767995437  564 TKRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAIRENSRAE 604
Cdd:cd01253    73 TKRKHVFRLTTSDFSEYLFQAEDRDDMLGWIKAIQENSNAE 113
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 697-891 1.22e-51

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: 180.29  E-value: 1.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEEcQPATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINL--QDERWQDLNVISSL 774
Cdd:cd04398     1 FGVPLED-LILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLisPEDYESDIHSVASL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  775 LKSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVF 854
Cdd:cd04398    80 LKLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIW 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767995437  855 GPTLVRTSEDNmtdmVTHMPDRYKIVETLIQHSDWFF 891
Cdd:cd04398   160 GPTLMNAAPDN----AADMSFQSRVIETLLDNAYQIF 192
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 709-891 3.41e-47

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


Pssm-ID: 239837 [Multi-domain]  Cd Length: 194  Bit Score: 167.31  E-value: 3.41e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  709 ENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDLNVISSLLKSFFRKLPEPLFT 788
Cdd:cd04372    12 HNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVYPDINVITGALKLYFRDLPIPVIT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  789 DDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTD 868
Cdd:cd04372    92 YDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRPPEDSALT 171

                         170       180
                  ....*....|....*....|...
gi 767995437  869 MVTHMPDRYKIVETLIQHSDWFF 891
Cdd:cd04372   172 TLNDMRYQILIVQLLITNEDVLF 194
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 704-886 1.68e-41

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: 150.92  E-value: 1.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  704 CQPATENQR-----VPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLqdeRWQDLNV--ISSLLK 776
Cdd:cd04385     1 DGPALEDQQltdndIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQL---REGEYTVhdVADVLK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  777 SFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGP 856
Cdd:cd04385    78 RFLRDLPDPLLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGP 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 767995437  857 TLVRTSEDNMTDMVTHMpdryKIVETLIQH 886
Cdd:cd04385   158 TLFQTDEHSVGQTSHEV----KVIEDLIDN 183
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 695-894 8.89e-40

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: 146.45  E-value: 8.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  695 RAFGVRLEECQPATeNQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLqDERWQDLNVISSL 774
Cdd:cd04386     3 PVFGTPLEEHLKRT-GREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPL-DEFYSDPHAVASA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  775 LKSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVF 854
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 767995437  855 GPTLV--RTSEDNMTDMVTHMPDRYKIVETLIQHSDWFFSDE 894
Cdd:cd04386   161 APNLLwaKNEGSLAEMAAGTSVHVVAIVELIISHADWFFPGE 202
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 697-884 1.80e-37

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: 139.11  E-value: 1.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEECqpATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDerwQDLNVISSLLK 776
Cdd:cd04377     1 FGVSLSSL--TSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLED---YPIHVITSVLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  777 SFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGP 856
Cdd:cd04377    76 QWLRELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAP 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 767995437  857 TLVRTSEDnmTDMVTHMPDRYKI---VETLI 884
Cdd:cd04377   156 CILRCPDT--ADPLQSLQDVSKTttcVETLI 184
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 716-886 6.97e-37

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: 138.30  E-value: 6.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  716 IVAACCRIVEARGLESTGIYRVPGnnaVVSSLQEQLNRG-------PGDINLQDERWqDLNVISSLLKSFFRKLPEPLFT 788
Cdd:cd04374    31 FVRKCIEAVETRGINEQGLYRVVG---VNSKVQKLLSLGldpktstPGDVDLDNSEW-EIKTITSALKTYLRNLPEPLMT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  789 DDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTD 868
Cdd:cd04374   107 YELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEETVAA 186

                         170       180
                  ....*....|....*....|
gi 767995437  869 MvthMPDRYK--IVETLIQH 886
Cdd:cd04374   187 I---MDIKFQniVVEILIEN 203
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 697-886 2.74e-36

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: 136.40  E-value: 2.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEECqPATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDlnvISSLLK 776
Cdd:cd04378     1 FGVDFSQV-PRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHD---ISSVLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  777 SFFRKLPEPLFTDDKYNDFI--------------EANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEK 842
Cdd:cd04378    77 LFLRQLPEPLILFRLYNDFIalakeiqrdteedkAPNTPIEVNRIIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEE 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 767995437  843 NKMEPRNLALVFGPTLVR----TSEDNMTDMVTHmPDRYKIVETLIQH 886
Cdd:cd04378   157 NKMSPNNLGIVFGPTLIRprpgDADVSLSSLVDY-GYQARLVEFLITN 203
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 697-867 1.75e-35

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: 134.00  E-value: 1.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEECQP-ATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPgDINLQDErwQDLNVISSLL 775
Cdd:cd04404     6 FGVSLQFLKEkNPEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGE-PVDFDQY--EDVHLPAVIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  776 KSFFRKLPEPLFTDDKYNDFIEANRIEDArERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFG 855
Cdd:cd04404    83 KTFLRELPEPLLTFDLYDDIVGFLNVDKE-ERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFG 161

                         170
                  ....*....|..
gi 767995437  856 PTLVRTSEDNMT 867
Cdd:cd04404   162 PNLLWAKDASMS 173
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 712-883 3.84e-34

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: 130.11  E-value: 3.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  712 RVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDerwQDLNVISSLLKSFFRKLPEPLFTDDK 791
Cdd:cd04382    16 MIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSK---VDIHVICGCLKDFLRSLKEPLITFAL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  792 YNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIAdHSEKNKMEPRNLALVFGPTLV--RTSEDNMTDM 869
Cdd:cd04382    93 WKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVA-QSPECKMDINNLARVFGPTIVgySVPNPDPMTI 171

                         170
                  ....*....|....
gi 767995437  870 VTHMPDRYKIVETL 883
Cdd:cd04382   172 LQDTVRQPRVVERL 185
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 697-885 1.61e-33

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: 127.96  E-value: 1.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEECqpATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRgpgDINLQ-DERWQDLNVISSLL 775
Cdd:cd04373     1 FGVPLANV--VTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQ---DHNLDlVSKDFTVNAVAGAL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  776 KSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFG 855
Cdd:cd04373    76 KSFFSELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFW 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 767995437  856 PTLVR---TSEDNMTDMVTHMpdryKIVETLIQ 885
Cdd:cd04373   156 PTLMRpdfTSMEALSATRIYQ----TIIETFIQ 184
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 709-885 3.01e-33

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: 127.74  E-value: 3.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  709 ENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQdERWQDLNVISSLLKSFFRKLPEPLFT 788
Cdd:cd04387    12 ERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVM-LSEMDVNAIAGTLKLYFRELPEPLFT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  789 DDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTD 868
Cdd:cd04387    91 DELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPSEKESKI 170

                         170
                  ....*....|....*..
gi 767995437  869 MVTHMPDRYKiVETLIQ 885
Cdd:cd04387   171 PTNTMTDSWS-LEVMSQ 186
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 697-886 1.70e-32

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: 125.23  E-value: 1.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEECQPATeNQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPgDINLQDERWQDLNVISSLLK 776
Cdd:cd04383     3 FNGSLEEYIQDS-GQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGE-DPLADDQNDHDINSVAGVLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  777 SFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGP 856
Cdd:cd04383    81 LYFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGP 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 767995437  857 TLVRTSEDNmtDMVTHMPDRYKIVETLIQH 886
Cdd:cd04383   161 TLMPVPEGQ--DQVSCQAHVNELIKTIIIH 188
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 713-891 4.58e-31

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: 121.78  E-value: 4.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  713 VPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGpGDINLQDErwQDLNVISSLLKSFFRKLPEPLFTDDKY 792
Cdd:cd04376     9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRG-IDVVLDEN--HSVHDVAALLKEFFRDMPDPLLPRELY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  793 NDFIEANRIEDArERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEK-----------NKMEPRNLALVFGPTLVR- 860
Cdd:cd04376    86 TAFIGTALLEPD-EQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsgNKMTSLNLATIFGPNLLHk 164

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767995437  861 --TSEDNMTDMVTHMPDR---YKIVETLIQHSDWFF 891
Cdd:cd04376   165 qkSGEREFVQASLRIEEStaiINVVQTMIDNYEELF 200
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 695-861 4.62e-30

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: 118.37  E-value: 4.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  695 RAFGVRLEECQPATeNQRVPLIVAACCRIVEARGLeSTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDLNVISSL 774
Cdd:cd04384     1 RVFGCDLTEHLLNS-GQDVPQVLKSCTEFIEKHGI-VDGIYRLSGIASNIQRLRHEFDSEQIPDLTKDVYIQDIHSVSSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  775 LKSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVF 854
Cdd:cd04384    79 CKLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVW 158


                  ....*..
gi 767995437  855 GPTLVRT 861
Cdd:cd04384   159 APNLLRS 165
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 713-886 3.02e-29

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: 116.45  E-value: 3.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  713 VPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDlnvISSLLKSFFRKLPEPLFTDDKY 792
Cdd:cd04409    16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHD---ISNVLKLYLRQLPEPLILFRLY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  793 NDFI----EANRIEDARERMRT------------------LRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNL 850
Cdd:cd04409    93 NEFIglakESQHVNETQEAKKNsdkkwpnmctelnrillkSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNL 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767995437  851 ALVFGPTLVR----TSEDNMTDMVTHmPDRYKIVETLIQH 886
Cdd:cd04409   173 GIIFGPTLIRprptDATVSLSSLVDY-PHQARLVELLITY 211
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 697-858 5.19e-29

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: 115.15  E-value: 5.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEEC----QPATENQRVPLIVAACCRIVEA-RGLESTGIYRVPGNNAVVSSLQEQLNRGpGDINL-QDERWQDLNV 770
Cdd:cd04400     2 FGSPLEEAvelsSHKYNGRDLPSVVYRCIEYLDKnRAIYEEGIFRLSGSASVIKQLKERFNTE-YDVDLfSSSLYPDVHT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  771 ISSLLKSFFRKLPEPLFTDDKYNDFIEANRIEDAR-ERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRN 849
Cdd:cd04400    81 VAGLLKLYLRELPTLILGGELHNDFKRLVEENHDRsQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRN 160


                  ....*....
gi 767995437  850 LALVFGPTL 858
Cdd:cd04400   161 VCIVFSPTL 169
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 697-886 6.29e-29

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: 115.30  E-value: 6.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEECqPATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDlnvISSLLK 776
Cdd:cd04408     1 FGVDFSQL-PRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHD---ITSVLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  777 SFFRKLPEPLFTDDKYNDFIEANR--IEDARER----------MRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNK 844
Cdd:cd04408    77 HFLKELPEPVLPFQLYDDFIALAKelQRDSEKAaespsiveniIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNK 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767995437  845 MEPRNLALVFGPTLVRTSEDNMTDMVTHMPDRYK--IVETLIQH 886
Cdd:cd04408   157 MSPNNLGIVFGPTLLRPLVGGDVSMICLLDTGYQaqLVEFLISN 200
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 697-885 1.50e-27

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: 110.85  E-value: 1.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEECqpATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDerwQDLNVISSLLK 776
Cdd:cd04407     1 FGVRVGSL--TSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLEN---YPIHAITGLLK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  777 SFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGP 856
Cdd:cd04407    76 QWLRELPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAP 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 767995437  857 TLVRTSEDnmTDMVTHMPDRYKI---VETLIQ 885
Cdd:cd04407   156 CLLRCPDS--SDPLTSMKDVAKTttcVEMLIK 185
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 697-858 1.62e-27

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: 111.40  E-value: 1.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEE-CQPATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDLNVISSLL 775
Cdd:cd04379     1 FGVPLSRlVEREGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEELYPDINVITGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  776 KSFFRKLPEPLFTDDKYNDFIEA------NRIEDARERMrtlRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRN 849
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEAlavalpNDVQTNTHLT---LSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQN 157


                  ....*....
gi 767995437  850 LALVFGPTL 858
Cdd:cd04379   158 LAVCFGPVL 166
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 695-891 1.04e-23

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: 100.21  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  695 RAFGVRLeecqpatenqrVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRG-----PGDinlqderwQDLN 769
Cdd:cd04390    15 RKFGPRL-----------VPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGerpsfDSD--------TDVH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  770 VISSLLKSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRT--LRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEP 847
Cdd:cd04390    76 TVASLLKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLgeLMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767995437  848 RNLALVFGPTLVRTSEDNMTDMVTHMPDRYKIVETLIQHSDWFF 891
Cdd:cd04390   156 QNLATVFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 697-858 1.14e-23

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: 100.50  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRL----EECQPATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNR--GPGDINLQDERWQDLnv 770
Cdd:cd04391     2 FGVPLstllERDQKKVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAkfYEGTFLWDQVKQHDA-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  771 iSSLLKSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNL 850
Cdd:cd04391    80 -ASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNV 158


                  ....*...
gi 767995437  851 ALVFGPTL 858
Cdd:cd04391   159 AMIMAPNL 166
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 695-868 1.17e-23

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: 99.84  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  695 RAFGVRLEECQPATE-NQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPgDINLQDErwQDLNVISS 773
Cdd:cd04393     1 KVFGVPLQELQQAGQpENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGE-EVDLSKE--ADVCSAAS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  774 LLKSFFRKLPEPLFTDDKYNDFIEA---NRIEDarERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNL 850
Cdd:cd04393    78 LLRLFLQELPEGLIPASLQIRLMQLyqdYNGED--EFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENL 155

                         170       180
                  ....*....|....*....|
gi 767995437  851 ALVFGPTL--VRTSEDNMTD 868
Cdd:cd04393   156 AAVFGPDVfhVYTDVEDMKE 175
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 709-894 1.94e-23

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: 99.30  E-value: 1.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  709 ENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGpGDINLQDErwqDLNVISSLLKSFFRKLPEPLFT 788
Cdd:cd04402    11 EDDNLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSG-VEVDLKAE---PVLLLASVLKDFLRNIPGSLLS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  789 DDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTS-----E 863
Cdd:cd04402    87 SDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWPPasselQ 166

                         170       180       190
                  ....*....|....*....|....*....|.
gi 767995437  864 DNMTDMVThmpdryKIVETLIQHSDWFFSDE 894
Cdd:cd04402   167 NEDLKKVT------SLVQFLIENCQEIFGED 191
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 697-860 1.06e-22

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: 96.99  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEECqpATENQRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDerwQDLNVISSLLK 776
Cdd:cd04406     1 FGVELSRL--TSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDD---YNIHVIASVFK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  777 SFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGP 856
Cdd:cd04406    76 QWLRDLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAP 155


                  ....
gi 767995437  857 TLVR 860
Cdd:cd04406   156 CILR 159
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 697-858 3.05e-22

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: 95.58  E-value: 3.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEEcqpATENQR------VPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRgPGDINLQDerwQDLNV 770
Cdd:cd04381     1 FGASLSL---AVERSRchdgidLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNR-RESPNLEE---YEPPT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  771 ISSLLKSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNL 850
Cdd:cd04381    74 VASLLKQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNI 153


                  ....*...
gi 767995437  851 ALVFGPTL 858
Cdd:cd04381   154 SIVLSPTV 161
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 697-886 7.10e-22

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: 94.38  E-value: 7.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEECQPATENQ----RVPLIVAACC-RIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGpgdiNLQDERWQDLNVI 771
Cdd:cd04389     1 FGSSLEEIMDRQKEKypelKLPWILTFLSeKVLALGGFQTEGIFRVPGDIDEVNELKLRVDQW----DYPLSGLEDPHVP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  772 SSLLKSFFRKLPEPLFTDDKYNDFIEANriEDARERMRtlrkLIRDLPGHYYETLKFLVGHLKTIADHS--EKNKMEPRN 849
Cdd:cd04389    77 ASLLKLWLRELEEPLIPDALYQQCISAS--EDPDKAVE----IVQKLPIINRLVLCYLINFLQVFAQPEnvAHTKMDVSN 150

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767995437  850 LALVFGPTLVRTSEDNMTDMVTHMPDRYKIVETLIQH 886
Cdd:cd04389   151 LAMVFAPNILRCTSDDPRVIFENTRKEMSFLRTLIEH 187
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 697-887 2.96e-21

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: 93.31  E-value: 2.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEeCQPA---TENQRVPLIVAACCRIVEARgLESTGIYRVPGNNAVVSSLQEQLNRGPGdinlQDERWQDLNViSS 773
Cdd:cd04394     2 FGVPLH-SLPHstvPEYGNVPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEA----CLSSALPCDV-AG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  774 LLKSFFRKLPEPLFTDDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALV 853
Cdd:cd04394    75 LLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVI 154

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767995437  854 FGPTLVRTSEDnMTDMVTHMPDRYK----IVETLIQHS 887
Cdd:cd04394   155 FAPNLFQSEEG-GEKMSSSTEKRLRlqaaVVQTLIDNA 191
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 712-890 7.69e-21

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: 92.86  E-value: 7.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  712 RVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPG---DINlqderWQDLNV--ISSLLKSFFRKLPEPL 786
Cdd:cd04396    31 YIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDygkSFD-----WDGYTVhdAASVLRRYLNNLPEPL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  787 FTDDKYNDF----IEANRI-------------EDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRN 849
Cdd:cd04396   106 VPLDLYEEFrnplRKRPRIlqymkgrineplnTDIDQAIKEYRDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASN 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767995437  850 LALVFGPTLVRTSEDNMtdmvthMPDRYKI----VETLIQHSDWF 890
Cdd:cd04396   186 LAAIFQPGILSHPDHEM------DPKEYKLsrlvVEFLIEHQDKF 224
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
 486-597 1.20e-20

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269975  Cd Length: 106  Bit Score: 88.05  E-value: 1.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  486 EGWLYYKQILTKKGKKAGSglRQWKRVYAALRARSLSLSKERREPGPAAAGAAAAgagedeaaPVCIGSCLVDISYSETK 565
Cdd:cd10571     2 EGFLERKHEWESGGKKASN--RSWKNVYTVLRGQELSFYKDQKAAKSGITYAAEP--------PLNLYNAVCEVASDYTK 71

                          90       100       110
                  ....*....|....*....|....*....|..
gi 767995437  566 RRHVFRLTTADFCEYLFQAEDRDDMLGWIRAI 597
Cdd:cd10571    72 KKHVFRLKLSDGAEFLFQAKDEEEMNQWVKKI 103
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 712-890 4.11e-18

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: 84.34  E-value: 4.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  712 RVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGP-GDINLQDErwqdlNVI--SSLLKSFFRKLPEPLFT 788
Cdd:cd04397    26 RIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPtEVPDLSKE-----NPVqlAALLKKFLRELPDPLLT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  789 DDKYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSE-----KNKMEPRNLALVFGPTLVRTSE 863
Cdd:cd04397   101 FKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHideetGSKMDIHNLATVITPNILYSKT 180

                         170       180       190
                  ....*....|....*....|....*....|.
gi 767995437  864 DNMTdmvthMPDRY----KIVETLIQHSDWF 890
Cdd:cd04397   181 DNPN-----TGDEYflaiEAVNYLIENNEEF 206
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 711-878 6.54e-17

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: 81.31  E-value: 6.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  711 QRVPLIVAACCRIVEARGLESTGIYRVPGNNAVVSSLQEQLNRGPGDINLQDERWQDlnvISSLLKSFFRKLPEPLFTDD 790
Cdd:cd04375    18 QPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYD---VADMLKQYFRDLPEPLLTNK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  791 KYNDFIEANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTDMV 870
Cdd:cd04375    95 LSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAPSLFHLNTSRRENSS 174


                  ....*...
gi 767995437  871 THMPDRYK 878
Cdd:cd04375   175 PARRMQRK 182
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 729-891 1.23e-15

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


Pssm-ID: 239857  Cd Length: 208  Bit Score: 77.12  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  729 LESTGIYRVPGNNAVVSSLQEQLNRGpGDINLQDERWQdLNVISSLLKSFFRKLPEPLFTDDKYNDFI----------EA 798
Cdd:cd04392    24 LRVEGLFRKPGNSARQQELRDLLNSG-TDLDLESGGFH-AHDCATVLKGFLGELPEPLLTHAHYPAHLqiadlcqfdeKG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  799 NR--IEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVRTSEDNMTDMVTHMPDR 876
Cdd:cd04392   102 NKtsAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPRNLTPEDLHENAQKL 181

                         170
                  ....*....|....*
gi 767995437  877 YKIVETLIQHSDWFF 891
Cdd:cd04392   182 NSIVTFMIKHSQKLF 196
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
 485-597 3.64e-15

Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. 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: 270107  Cd Length: 126  Bit Score: 73.13  E-value: 3.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  485 REGWLYYKQILTKKGKKAGSGLRQWKRVYAALRARSLSLSKErrepgpaAAGAAAAGAGEDEAAPVCIGSCLVDISYSET 564
Cdd:cd13295     8 KKGYLMRKCCADPDGKKTPFGKRGWKMFYATLKGLVLYLHKD-------EYGCKKALRYESLRNAISVHHSLATKATDYT 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767995437  565 KRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAI 597
Cdd:cd13295    81 KKPHVFRLRTADWREYLFQASDTKEMQSWIEAI 113
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 724-889 2.12e-13

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


Pssm-ID: 239853  Cd Length: 200  Bit Score: 70.29  E-value: 2.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  724 VEARGLESTGIYRvPGNNAVVSSLQEQLNRGPGDINLqdERWqDLNVISSLLKSFFRKLPEPLFTDDKYNDFIE-ANRIE 802
Cdd:cd04388    26 IEKKGLESSTLYR-TQSSSSLTELRQILDCDAASVDL--EQF-DVAALADALKRYLLDLPNPVIPAPVYSEMISrAQEVQ 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  803 DARERMRTLRKLIR--DLPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGPTLVR---TSEDNMTDMVthmpdry 877
Cdd:cd04388   102 SSDEYAQLLRKLIRspNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRfqpASSDSPEFHI------- 174

                         170
                  ....*....|..
gi 767995437  878 KIVETLIQhSDW 889
Cdd:cd04388   175 RIIEVLIT-SEW 185
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
 485-597 1.77e-12

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 434701  Cd Length: 118  Bit Score: 65.14  E-value: 1.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437   485 REGWLYYKQILTKKGKKAGSGLRQWKRVYAALRARSLSLSKERREPGPAAAGAAAAGAGEDEAApVCIGSCLVDISYSET 564
Cdd:pfam15410    2 KKGIVMRKCCFESKGKKTPRGKRSWKMVYAVLKDLVLYLYKDEHPPESSQFEDKKSLKNAPVGK-IRLHHALATPAPDYT 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 767995437   565 KRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAI 597
Cdd:pfam15410   81 KKSHVFRLQTADGAEYLFQTGSPKELQEWVDTL 113
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 483-599 5.54e-12

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 63.34  E-value: 5.54e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437    483 IRREGWLYykqiltkkgKKAGSGLRQWKRVYAALRARSLSLSKERrepgpaaagaaAAGAGEDEAAPVCIGSCLVDI--S 560
Cdd:smart00233    1 VIKEGWLY---------KKSGGGKKSWKKRYFVLFNSTLLYYKSK-----------KDKKSYKPKGSIDLSGCTVREapD 60

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 767995437    561 YSETKRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAIRE 599
Cdd:smart00233   61 PDSSKKPHCFEIKTSDRKTLLLQAESEEEREKWVEALRK 99
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 485-597 6.54e-10

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 57.17  E-value: 6.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  485 REGWLYykqiltkkgKKAGSGLRQWKRVYAALRARSLSLSKERREPGPAAAGAAAagagedeaapvCIGSCLVDISySET 564
Cdd:cd00821     1 KEGYLL---------KRGGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYKPKGSIP-----------LSGILEVEEV-SPK 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767995437  565 KRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAI 597
Cdd:cd00821    60 ERPHCFELVTPDGRTYYLQADSEEERQEWLKAL 92
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 483-602 6.01e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 54.88  E-value: 6.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437   483 IRREGWLYykqiltkkgKKAGSGLRQWKRVYAALRARSLSLSKERREPGPAAAGAAAAgagedeaapvCIGSCLVDISYS 562
Cdd:pfam00169    1 VVKEGWLL---------KKGGGKKKSWKKRYFVLFDGSLLYYKDDKSGKSKEPKGSIS----------LSGCEVVEVVAS 61

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 767995437   563 E-TKRRHVFRLTTADFCE---YLFQAEDRDDMLGWIRAIRENSR 602
Cdd:pfam00169   62 DsPKRKFCFELRTGERTGkrtYLLQAESEEERKDWIKAIQSAIR 105
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 482-601 7.65e-07

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270068  Cd Length: 104  Bit Score: 48.81  E-value: 7.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  482 DIRREGWLYykqiltkkgKKAGSGLRQWKRVYAALRARSLSLSKERREPgpaaagaaaagagedeaapVCIGSCLVdISY 561
Cdd:cd13248     6 PVVMSGWLH---------KQGGSGLKNWRKRWFVLKDNCLYYYKDPEEE-------------------KALGSILL-PSY 56

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767995437  562 S--------ETKRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAIRENS 601
Cdd:cd13248    57 TispappsdEISRKFAFKAEHANMRTYYFAADTAEEMEQWMNAMSLAA 104
PHA03247 PHA03247
large tegument protein UL36; Provisional
 3-382 9.67e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 9.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437    3 PEPTSA-LPSDPRSPAAWSDPGLRVPPAARAHLDNSSLGMSQPRPSPGAFPHLSSEPRTPRAFPEPGsRVPPSRLECQQA 81
Cdd:PHA03247 2593 PQSARPrAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPG-RVSRPRRARRLG 2671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437   82 LSHWLSN--QVPRRAGERrcPAMAPRARSASQDRLEEVAAPRPWPCSTSQDA-LSQLGQEGWHRARSDDYLSRATRSAEA 158
Cdd:PHA03247 2672 RAAQASSppQRPRRRAAR--PTVGSLTSLADPPPPPPTPEPAPHALVSATPLpPGPAAARQASPALPAAPAPPAVPAGPA 2749

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  159 LGPGALVSPRFERCGWASQRSSARTPACPtrdlPGPQAPPPSGLQGLDDLGYI-GYRSYSPSFQRRTGLLHALSFRDSPF 237
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPAAG----PPRRLTRPAVASLSESRESLpSPWDPADPPAAVLAPAAALPPAASPA 2825

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  238 GGLPTFNLAQ----SPASFPPEASE----------------PPRVVRPEPSTRAlEPPAEDRGDEVVLRQ-----KPPTG 292
Cdd:PHA03247 2826 GPLPPPTSAQptapPPPPGPPPPSLplggsvapggdvrrrpPSRSPAAKPAAPA-RPPVRRLARPAVSRStesfaLPPDQ 2904

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  293 RKVQLTPARQMNLGFGDESPEPEASGRGERL-GRKVAPLATTEDSLASipfiDEPTSPSIDLQAKHVPASAV------VS 365
Cdd:PHA03247 2905 PERPPQPQAPPPPQPQPQPPPPPQPQPPPPPpPRPQPPLAPTTDPAGA----GEPSGAVPQPWLGALVPGRVavprfrVP 2980

                         410
                  ....*....|....*..
gi 767995437  366 SAMNSAPVLGTSPSSPT 382
Cdd:PHA03247 2981 QPAPSREAPASSTPPLT 2997
PH1_Tiam1_2 cd01230
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; ...
 483-597 1.03e-04

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2.Neither of these fall in the PHn domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269937  Cd Length: 127  Bit Score: 43.22  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  483 IRREGWLYYKQILT--KKGKKAGSGLRQWKRVYAALRARSLSL--SKERREPGPAAAGAAAagagedeaapVCIGSCLVD 558
Cdd:cd01230     3 VRKAGWLSVKNFLVhkKNKKVELATRRKWKKYWVCLKGCTLLFyeCDERSGIDENSEPKHA----------LFVEGSIVQ 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767995437  559 ISYSETKRRHVFRLTTADFCEYLFQAEDRDDMLGWIRAI 597
Cdd:cd01230    73 AVPEHPKKDFVFCLSNSFGDAYLFQATSQTELENWVTAI 111
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
 483-607 3.31e-04

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270110  Cd Length: 106  Bit Score: 41.46  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  483 IRREGWLYykqiltKKGKKAgsglRQWKRVYAALRARSLSL---SKERREPGpaaagaaaagagedeaapVCIGSCLVDI 559
Cdd:cd13298     6 VLKSGYLL------KRSRKT----KNWKKRWVVLRPCQLSYykdEKEYKLRR------------------VINLSELLAV 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767995437  560 SYSE-TKRRHVFRLTTADFcEYLFQAEDRDDMLGWIRAIRENSRAEGED 607
Cdd:cd13298    58 APLKdKKRKNVFGIYTPSK-NLHFRATSEKDANEWVEALREEFRLDDEE 105
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 697-893 5.57e-04

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: 42.70  E-value: 5.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  697 FGVRLEEcQPATENQRVPLIVAAccrIVEARGL---------ESTGIYRVPGNNAVVSSLQEQLNRGPgDINLQDERWQD 767
Cdd:cd04399     1 FGVDLET-RCRLDKKVVPLIVSA---ILSYLDQlypdlindeVRRNVWTDPVSLKETHQLRNLLNKPK-KPDKEVIILKK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  768 LN--VISSLLKSFFRKLPEPLFTDDKYNDFIE------ANRIEDARERMRTLRKLIRDLPGHYYETLKFLVGHLKT---I 836
Cdd:cd04399    76 FEpsTVASVLKLYLLELPDSLIPHDIYDLIRSlysaypPSQEDSDTARIQGLQSTLSQLPKSHIATLDAIITHFYRlieI 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767995437  837 ADHSEKNKMEPRNLALVFGPTLVRTsednMTDMVTHMPDR--YKIVETLIQHSDWFFSD 893
Cdd:cd04399   156 TKMGESEEEYADKLATSLSREILRP----IIESLLTIGDKhgYKFFRDLLTHKDQIFSE 210
PHA03247 PHA03247
large tegument protein UL36; Provisional
 2-386 2.77e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437    2 VPEPTSALPSDPRSPAAWSDPGLRVPPAARAHLDNSSlgmSQPRPSPGAFPHLSSEPRTPRAFPEPGSRVPP--SRLECQ 79
Cdd:PHA03247 2719 TPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPA---RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAvaSLSESR 2795

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437   80 QALSHWLSNQVPRRAGERRCPAMAPRARSASQDRLEEVAAPRPwPCSTSQDALSQLGQEGWhRARSDDYLSRATRSAEAL 159
Cdd:PHA03247 2796 ESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA-PPPPPGPPPPSLPLGGS-VAPGGDVRRRPPSRSPAA 2873

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  160 GPGALVSPRfercgwaSQRSSARTPACPTRDLPGPQAPPPsglqglddlgyigyRSYSPSFQRRTGLLHALSFRDSPFGG 239
Cdd:PHA03247 2874 KPAAPARPP-------VRRLARPAVSRSTESFALPPDQPE--------------RPPQPQAPPPPQPQPQPPPPPQPQPP 2932

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  240 LPTFNLAQSPA--SFPPEASEPPRVVRPEPSTRALEPpaedrGDEVVLRQKPPTGRKVQLTPArqmnlgfgdESPEPEAS 317
Cdd:PHA03247 2933 PPPPPRPQPPLapTTDPAGAGEPSGAVPQPWLGALVP-----GRVAVPRFRVPQPAPSREAPA---------SSTPPLTG 2998

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767995437  318 GRGERLGRKVAPLATTEDSLASIPFIDEPTSPSIDLQAKHVPASAVVSSAMNSAPVLGTSPSSPTFTFT 386
Cdd:PHA03247 2999 HSLSRVSSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPEPHDPFA 3067
PH2_PH_fungal cd13299
Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal ...
 486-528 2.80e-03

Fungal proteins Pleckstrin homology (PH) domain, repeat 2; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the second PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270111  Cd Length: 102  Bit Score: 38.38  E-value: 2.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 767995437  486 EGWLYYkqiLTKKGkkagsgLRQWKRVYAALRARSLSLSKERR 528
Cdd:cd13299     9 QGYLQV---LKKKG------VNQWKKYWLVLRNRSLSFYKDQS 42
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
3-205 3.12e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437    3 PEPTSALPSDPRSPAAWSdPGLRVPPAARAHLDNSSLGMSQPRPSPGAFPhlssEPRTPRAFPEPGSRVPPsrlecqqal 82
Cdd:PRK12323  410 PAAAAAARAVAAAPARRS-PAPEALAAARQASARGPGGAPAPAPAPAAAP----AAAARPAAAGPRPVAAA--------- 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437   83 shwlSNQVPRRAGERRCPAMAPRARSASQDRLEEVAAPRPWPCSTS-QDALSQLGQEGWHRARSDDYLSRATRSAEALGP 161
Cdd:PRK12323  476 ----AAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAApAGWVAESIPDPATADPDDAFETLAPAPAAAPAP 551

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767995437  162 GALVSPRFERCGWASQRSSARTPACPTRDLPGPQAPPPsgLQGL 205
Cdd:PRK12323  552 RAAAATEPVVAPRPPRASASGLPDMFDGDWPALAARLP--VRGL 593
PHA03247 PHA03247
large tegument protein UL36; Provisional
 21-276 3.50e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437   21 DPGLRVPPAARAHLDNSSLGMSQPRPSPGAfPHLSSEPRTPRAFPEPGS-RVPPSRLECQQALSHwlSNQVPRRAGERRC 99
Cdd:PHA03247 2550 DPPPPLPPAAPPAAPDRSVPPPRPAPRPSE-PAVTSRARRPDAPPQSARpRAPVDDRGDPRGPAP--PSPLPPDTHAPDP 2626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  100 PAMAPRARSASQDRLEEVAAPRPwPCSTSQDALSqlgqegwhRARSDDYLSRATRSAEALGPGALVSPRFERCGWASQRS 179
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPPTVPPP-ERPRDDPAPG--------RVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTS 2697

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  180 SARTPACPtrdlPGPQAPPPSGLQGLD-DLGYIGYRSYSPSFQRRTGLLHALSFRDSPFGGLPTfnlAQSPASFPPEASE 258
Cdd:PHA03247 2698 LADPPPPP----PTPEPAPHALVSATPlPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARP---ARPPTTAGPPAPA 2770

                         250
                  ....*....|....*...
gi 767995437  259 PPRvVRPEPSTRALEPPA 276
Cdd:PHA03247 2771 PPA-APAAGPPRRLTRPA 2787
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 778-867 6.90e-03

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


Pssm-ID: 239845  Cd Length: 220  Bit Score: 39.63  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767995437  778 FFRKLPEPLFTDDKYNDFIEANRIEDarermRTLRKLIRD-LPGHYYETLKFLVGHLKTIADHSEKNKMEPRNLALVFGP 856
Cdd:cd04380   114 FLESLPDPIIPYSLYERLLEAVANNE-----EDKRQVIRIsLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGR 188

                          90
                  ....*....|.
gi 767995437  857 TLVRTSEDNMT 867
Cdd:cd04380   189 VLLRDPPRAGG 199
 
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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