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Conserved domains on  [gi|19112658|ref|NP_595866|]
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Rho-type GTPase-activating protein Rga7 [Schizosaccharomyces pombe]

Protein Classification

Rho GTPase-activating protein( domain architecture ID 10166522)

Rho GTPase-activating protein for Rho/Rac/Cdc42-like small GTPases that act as molecular switches, active in their GTP-bound form but inactive when bound to GDP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
504-692 2.47e-105

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: 318.58  E-value: 2.47e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHT-PEDYENDVHAVADLL 582
Cdd:cd04398   1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLIsPEDYESDIHSVASLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 583 KIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWG 662
Cdd:cd04398  81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 19112658 663 PTIIKQAT--IPEISSFSRTIEILIDYCFTIF 692
Cdd:cd04398 161 PTLMNAAPdnAADMSFQSRVIETLLDNAYQIF 192
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
39-277 5.80e-101

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


:

Pssm-ID: 153336 [Multi-domain]  Cd Length: 234  Bit Score: 308.89  E-value: 5.80e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  39 LNSELGLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFSASVITSMEIHEQLANH 118
Cdd:cd07652   1 LNSDVGLSTLLDRLKQSIASAKEFATFLKKRAAIEEEHARGLKKLARTTLDTYKRPDHKQGSFSNAYHSSLEFHEKLADN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 119 SLTLQKTLSAFSDQVIEFHKNAERKRKSIKEYAKKQENAYLEAVMQMDKSKSRFKGAETEYnralDNKNTGDSQKKvGFF 198
Cdd:cd07652  81 GLRFAKALNEMSDELSSLAKTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDL----ERVKTGDPGKK-LKF 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112658 199 KPKSNAQLTKLEDEARLKAENAESDMHSKIENAQNVQKQLLCIHRPNYIKQFFSLQREIESSLIANYLRYTKLCESNTL 277
Cdd:cd07652 156 GLKGNKSAAQHEDELLRKVQAADQDYASKVNAAQALRQELLSRHRPEAVKDLFDLILEIDAALRLQYQKYALPNELLVL 234
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
321-479 3.19e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 50.69  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   321 DNKNPTDASKTKIIQPPSSYGTGSSAGKTNPPVN---PTI---KVTAAIPSPLQN-TNPAPS-TFPNPSVASPAF----P 388
Cdd:pfam05109 500 ESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNatsPTLgktSPTSAVTTPTPNaTSPTPAvTTPTPNATIPTLgktsP 579
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   389 NSSTSNPStaPASASPLASTLKPStANDTNGSSSSSSSNPRTSSPlASNAENKPPVAQQSPPVLLPTLPPIQTTTIQtsr 468
Cdd:pfam05109 580 TSAVTTPT--PNATSPTVGETSPQ-ANTTNHTLGGTSSTPVVTSP-PKNATSAVTTGQHNITSSSTSSMSLRPSSIS--- 652
                         170
                  ....*....|.
gi 19112658   469 EVAPPPSSINS 479
Cdd:pfam05109 653 ETLSPSTSDNS 663
 
Name Accession Description Interval E-value
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
504-692 2.47e-105

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: 318.58  E-value: 2.47e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHT-PEDYENDVHAVADLL 582
Cdd:cd04398   1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLIsPEDYESDIHSVASLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 583 KIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWG 662
Cdd:cd04398  81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 19112658 663 PTIIKQAT--IPEISSFSRTIEILIDYCFTIF 692
Cdd:cd04398 161 PTLMNAAPdnAADMSFQSRVIETLLDNAYQIF 192
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
39-277 5.80e-101

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153336 [Multi-domain]  Cd Length: 234  Bit Score: 308.89  E-value: 5.80e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  39 LNSELGLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFSASVITSMEIHEQLANH 118
Cdd:cd07652   1 LNSDVGLSTLLDRLKQSIASAKEFATFLKKRAAIEEEHARGLKKLARTTLDTYKRPDHKQGSFSNAYHSSLEFHEKLADN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 119 SLTLQKTLSAFSDQVIEFHKNAERKRKSIKEYAKKQENAYLEAVMQMDKSKSRFKGAETEYnralDNKNTGDSQKKvGFF 198
Cdd:cd07652  81 GLRFAKALNEMSDELSSLAKTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDL----ERVKTGDPGKK-LKF 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112658 199 KPKSNAQLTKLEDEARLKAENAESDMHSKIENAQNVQKQLLCIHRPNYIKQFFSLQREIESSLIANYLRYTKLCESNTL 277
Cdd:cd07652 156 GLKGNKSAAQHEDELLRKVQAADQDYASKVNAAQALRQELLSRHRPEAVKDLFDLILEIDAALRLQYQKYALPNELLVL 234
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
517-688 4.27e-57

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: 191.33  E-value: 4.27e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658    517 SNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHtpeDYENDVHAVADLLKIFFRELREPLIPD 596
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLD---LSEYDVHDVAGLLKLFLRELPEPLITY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658    597 NHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGPTII-----KQATI 671
Cdd:smart00324  78 ELYEEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLrppdgEVASL 157
                          170
                   ....*....|....*..
gi 19112658    672 PEISSFSRTIEILIDYC 688
Cdd:smart00324 158 KDIRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
520-666 2.02e-51

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 175.04  E-value: 2.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   520 PNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLhtpEDYENDVHAVADLLKIFFRELREPLIPDNHQ 599
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDL---DLEEEDVHVVASLLKLFLRELPEPLLTFELY 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112658   600 RDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGPTII 666
Cdd:pfam00620  78 EEFIEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLL 144
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
44-118 3.10e-15

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 71.15  E-value: 3.10e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112658    44 GLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFSASVITSMEIHEQLANH 118
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPEDDGGTLKKAWDELLTETEQLAKQ 75
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
44-122 1.51e-06

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 46.57  E-value: 1.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658     44 GLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAK-SYLETFQSKHHSPQSFSASVITSMEihEQLANHSLTL 122
Cdd:smart00055  10 GFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKkLRAVRDTEPEYGSLSKAWEVLLSET--DALAKQHLEL 87
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
321-479 3.19e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 50.69  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   321 DNKNPTDASKTKIIQPPSSYGTGSSAGKTNPPVN---PTI---KVTAAIPSPLQN-TNPAPS-TFPNPSVASPAF----P 388
Cdd:pfam05109 500 ESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNatsPTLgktSPTSAVTTPTPNaTSPTPAvTTPTPNATIPTLgktsP 579
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   389 NSSTSNPStaPASASPLASTLKPStANDTNGSSSSSSSNPRTSSPlASNAENKPPVAQQSPPVLLPTLPPIQTTTIQtsr 468
Cdd:pfam05109 580 TSAVTTPT--PNATSPTVGETSPQ-ANTTNHTLGGTSSTPVVTSP-PKNATSAVTTGQHNITSSSTSSMSLRPSSIS--- 652
                         170
                  ....*....|.
gi 19112658   469 EVAPPPSSINS 479
Cdd:pfam05109 653 ETLSPSTSDNS 663
PHA03247 PHA03247
large tegument protein UL36; Provisional
314-499 6.80e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 6.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   314 HASIKHEDNKNPTDASKTKIIQPPSSYGTGSSAGKTNPPVNPTIKVTAAIPSPLQNT----NPAPSTFPNPSVASPAFPN 389
Cdd:PHA03247 2642 PPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLadppPPPPTPEPAPHALVSATPL 2721
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   390 SSTSNPSTAPASASPLASTLKPS-TANDTNGSSSSSSSNPRTSSPLASNAENKPPVA-QQSPPVLLPTLPPIQTTTIQTS 467
Cdd:PHA03247 2722 PPGPAAARQASPALPAAPAPPAVpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGpPRRLTRPAVASLSESRESLPSP 2801
                         170       180       190
                  ....*....|....*....|....*....|....
gi 19112658   468 REVAPPPSSINSNRAASPF--RPTSVSPQPSSPT 499
Cdd:PHA03247 2802 WDPADPPAAVLAPAAALPPaaSPAGPLPPPTSAQ 2835
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
326-406 9.73e-04

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 42.19  E-value: 9.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   326 TDASKTKIIQPPSSYGTGSSAGkTNPPVNPTIKVTAAIPSPLQntnpaPSTFPNPSVASPAFPNSSTSNPSTAPASASPL 405
Cdd:TIGR00601  77 PKTGTGKVAPPAATPTSAPTPT-PSPPASPASGMSAAPASAVE-----EKSPSEESATATAPESPSTSVPSSGSDAASTL 150

                  .
gi 19112658   406 A 406
Cdd:TIGR00601 151 V 151
 
Name Accession Description Interval E-value
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
504-692 2.47e-105

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: 318.58  E-value: 2.47e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHT-PEDYENDVHAVADLL 582
Cdd:cd04398   1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLIsPEDYESDIHSVASLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 583 KIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWG 662
Cdd:cd04398  81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160
                       170       180       190
                ....*....|....*....|....*....|..
gi 19112658 663 PTIIKQAT--IPEISSFSRTIEILIDYCFTIF 692
Cdd:cd04398 161 PTLMNAAPdnAADMSFQSRVIETLLDNAYQIF 192
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
39-277 5.80e-101

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153336 [Multi-domain]  Cd Length: 234  Bit Score: 308.89  E-value: 5.80e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  39 LNSELGLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFSASVITSMEIHEQLANH 118
Cdd:cd07652   1 LNSDVGLSTLLDRLKQSIASAKEFATFLKKRAAIEEEHARGLKKLARTTLDTYKRPDHKQGSFSNAYHSSLEFHEKLADN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 119 SLTLQKTLSAFSDQVIEFHKNAERKRKSIKEYAKKQENAYLEAVMQMDKSKSRFKGAETEYnralDNKNTGDSQKKvGFF 198
Cdd:cd07652  81 GLRFAKALNEMSDELSSLAKTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDL----ERVKTGDPGKK-LKF 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112658 199 KPKSNAQLTKLEDEARLKAENAESDMHSKIENAQNVQKQLLCIHRPNYIKQFFSLQREIESSLIANYLRYTKLCESNTL 277
Cdd:cd07652 156 GLKGNKSAAQHEDELLRKVQAADQDYASKVNAAQALRQELLSRHRPEAVKDLFDLILEIDAALRLQYQKYALPNELLVL 234
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
517-688 4.27e-57

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: 191.33  E-value: 4.27e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658    517 SNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHtpeDYENDVHAVADLLKIFFRELREPLIPD 596
Cdd:smart00324   1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLD---LSEYDVHDVAGLLKLFLRELPEPLITY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658    597 NHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGPTII-----KQATI 671
Cdd:smart00324  78 ELYEEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLrppdgEVASL 157
                          170
                   ....*....|....*..
gi 19112658    672 PEISSFSRTIEILIDYC 688
Cdd:smart00324 158 KDIRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
520-666 2.02e-51

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 175.04  E-value: 2.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   520 PNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLhtpEDYENDVHAVADLLKIFFRELREPLIPDNHQ 599
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDL---DLEEEDVHVVASLLKLFLRELPEPLLTFELY 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112658   600 RDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGPTII 666
Cdd:pfam00620  78 EEFIEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLL 144
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
520-687 1.64e-42

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: 151.30  E-value: 1.64e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 520 PNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPllqlHTPEDYENDVHAVADLLKIFFRELREPLIPDNHQ 599
Cdd:cd00159   1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGE----DIDDLEDYDVHDVASLLKLYLRELPEPLIPFELY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 600 RDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGPTIIK-----QATIPEI 674
Cdd:cd00159  77 DEFIELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRppdsdDELLEDI 156
                       170
                ....*....|...
gi 19112658 675 SSFSRTIEILIDY 687
Cdd:cd00159 157 KKLNEIVEFLIEN 169
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
504-692 1.06e-41

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


Pssm-ID: 239860  Cd Length: 196  Bit Score: 150.24  E-value: 1.06e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIiLREHSN--IPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLlQLHTPEDYENDVHAVADL 581
Cdd:cd04395   2 FGVPLDDC-PPSSENpyVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGF-DIDLQDPRWRDVNVVSSL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 582 LKIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIW 661
Cdd:cd04395  80 LKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVF 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19112658 662 GPTIIKQA------TIPEISSFSRTIEILIDYCFTIF 692
Cdd:cd04395 160 GPTLVRTSddnmetMVTHMPDQCKIVETLIQHYDWFF 196
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
504-667 2.29e-38

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


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 140.60  E-value: 2.29e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHTPEdyENDVHAVADLLK 583
Cdd:cd04403   1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLDLDDSK--WEDIHVITGALK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 584 IFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGP 663
Cdd:cd04403  79 LFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGP 158

                ....
gi 19112658 664 TIIK 667
Cdd:cd04403 159 TLLR 162
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
519-666 1.99e-37

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: 138.20  E-value: 1.99e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 519 IPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQF---ENNPLLQLHtpedyenDVHAVADLLKIFFRELREPLIP 595
Cdd:cd04382  17 IPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFlrgKTVPNLSKV-------DIHVICGCLKDFLRSLKEPLIT 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112658 596 DNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKEnSDVNKMSTNNLAIIWGPTII 666
Cdd:cd04382  90 FALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQ-SPECKMDINNLARVFGPTIV 159
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
517-688 1.02e-35

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: 133.20  E-value: 1.02e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 517 SNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPL-LQLhTPEDYEndVHAVADLLKIFFRELREPLIP 595
Cdd:cd04385  13 NDIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARsVQL-REGEYT--VHDVADVLKRFLRDLPDPLLT 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 596 DNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGPTIIKQATIPEIS 675
Cdd:cd04385  90 SELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTDEHSVGQ 169
                       170
                ....*....|....*
gi 19112658 676 SF--SRTIEILIDYC 688
Cdd:cd04385 170 TSheVKVIEDLIDNY 184
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
504-687 2.66e-35

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: 132.55  E-value: 2.66e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENnpllQLHTPEDYENDVHAVADLLK 583
Cdd:cd04378   1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFEN----GKDLVELSELSPHDISSVLK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 584 IFFRELREPLIPDNHQRDFIDAG----NVEDESRRRDA---VHRAI-------NDLPDANYSTIRHLTIHLAKIKENSDV 649
Cdd:cd04378  77 LFLRQLPEPLILFRLYNDFIALAkeiqRDTEEDKAPNTpieVNRIIrklkdllRQLPASNYNTLQHLIAHLYRVAEQFEE 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 19112658 650 NKMSTNNLAIIWGPTIIK----QATIPeISSF------SRTIEILIDY 687
Cdd:cd04378 157 NKMSPNNLGIVFGPTLIRprpgDADVS-LSSLvdygyqARLVEFLITN 203
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
504-669 2.23e-31

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: 121.19  E-value: 2.23e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENN---PLLQLHtpedyENDVHAVAD 580
Cdd:cd04387   1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNnkdVSVMLS-----EMDVNAIAG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 581 LLKIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAII 660
Cdd:cd04387  76 TLKLYFRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATV 155

                ....*....
gi 19112658 661 WGPTIIKQA 669
Cdd:cd04387 156 FGPTLLRPS 164
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
504-685 2.47e-31

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


Pssm-ID: 239842  Cd Length: 186  Bit Score: 120.62  E-value: 2.47e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSnIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNP-LLQLhtpEDYEndVHAVADLL 582
Cdd:cd04377   1 FGVSLSSLTSEDRS-VPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPdSVNL---EDYP--IHVITSVL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 583 KIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWG 662
Cdd:cd04377  75 KQWLRELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFA 154
                       170       180       190
                ....*....|....*....|....*....|
gi 19112658 663 PTIIK-------QATIPEISSFSRTIEILI 685
Cdd:cd04377 155 PCILRcpdtadpLQSLQDVSKTTTCVETLI 184
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
504-666 3.04e-30

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: 118.33  E-value: 3.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNpllQLHTPED-YENDVHAVADLL 582
Cdd:cd04386   5 FGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAG---TFSLPLDeFYSDPHAVASAL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 583 KIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWG 662
Cdd:cd04386  82 KSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLA 161

                ....
gi 19112658 663 PTII 666
Cdd:cd04386 162 PNLL 165
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
519-675 3.46e-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: 114.91  E-value: 3.46e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 519 IPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENN-PLLQL--HTPedyendvHAVADLLKIFFRELREPLIP 595
Cdd:cd04408  16 VPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGrDLVDLsgHSP-------HDITSVLKHFLKELPEPVLP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 596 DNHQRDFIDAG---------NVEDESRRRDAVHRA---INDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGP 663
Cdd:cd04408  89 FQLYDDFIALAkelqrdsekAAESPSIVENIIRSLkelLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGP 168
                       170
                ....*....|..
gi 19112658 664 TIIKQATIPEIS 675
Cdd:cd04408 169 TLLRPLVGGDVS 180
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
504-692 5.29e-29

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: 114.15  E-value: 5.29e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHTPEDYEnDVHAVADLLK 583
Cdd:cd04372   1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVYP-DINVITGALK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 584 IFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGP 663
Cdd:cd04372  80 LYFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGP 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 19112658 664 TIIK------QATIPEISSFSRTIEILIDYCFTIF 692
Cdd:cd04372 160 TLMRppedsaLTTLNDMRYQILIVQLLITNEDVLF 194
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
504-687 2.65e-28

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: 112.98  E-value: 2.65e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNpllqLHTPEDYENDVHAVADLLK 583
Cdd:cd04409   1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENG----KDLVELSELSPHDISNVLK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 584 IFFRELREPLIPDNHQRDFID------AGNVEDESRRRDA----------------VHRAINDLPDANYSTIRHLTIHLA 641
Cdd:cd04409  77 LYLRQLPEPLILFRLYNEFIGlakesqHVNETQEAKKNSDkkwpnmctelnrillkSKDLLRQLPAPNYNTLQFLIVHLH 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19112658 642 KIKENSDVNKMSTNNLAIIWGPTIIK----QATIpEISSF------SRTIEILIDY 687
Cdd:cd04409 157 RVSEQAEENKMSASNLGIIFGPTLIRprptDATV-SLSSLvdyphqARLVELLITY 211
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
504-667 1.32e-27

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


Pssm-ID: 239838  Cd Length: 185  Bit Score: 109.85  E-value: 1.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREhSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLhtpEDYENDVHAVADLLK 583
Cdd:cd04373   1 FGVPLANVVTSE-KPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDL---VSKDFTVNAVAGALK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 584 IFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGP 663
Cdd:cd04373  77 SFFSELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWP 156

                ....
gi 19112658 664 TIIK 667
Cdd:cd04373 157 TLMR 160
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
504-671 1.90e-26

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: 107.20  E-value: 1.90e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSNIPNIVMQCTSQVENFGLnLQGIYRVPSSSARVNMLRSQFENNPLLQLHTPEdYENDVHAVADLLK 583
Cdd:cd04384   3 FGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGI-VDGIYRLSGIASNIQRLRHEFDSEQIPDLTKDV-YIQDIHSVSSLCK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 584 IFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGP 663
Cdd:cd04384  81 LYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWAP 160

                ....*...
gi 19112658 664 TIIKQATI 671
Cdd:cd04384 161 NLLRSKQI 168
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
503-667 5.83e-26

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: 105.60  E-value: 5.83e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 503 LFGARLDAIILREHS----NIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFE--NNPLLqlhtpeDYENDVH 576
Cdd:cd04390   2 VFGQRLEDTVAYERKfgprLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDagERPSF------DSDTDVH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 577 AVADLLKIFFRELREPLIPDNHQRDFIDAGNV--EDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMST 654
Cdd:cd04390  76 TVASLLKLYLRELPEPVIPWAQYEDFLSCAQLlsKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSV 155
                       170
                ....*....|...
gi 19112658 655 NNLAIIWGPTIIK 667
Cdd:cd04390 156 QNLATVFGPNILR 168
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
504-685 1.90e-25

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: 103.92  E-value: 1.90e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIIlREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNP-LLQLhtpEDYEndVHAVADLL 582
Cdd:cd04407   1 FGVRVGSLT-SNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPeNVKL---ENYP--IHAITGLL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 583 KIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWG 662
Cdd:cd04407  75 KQWLRELPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFA 154
                       170       180       190
                ....*....|....*....|....*....|
gi 19112658 663 PTIIK-------QATIPEISSFSRTIEILI 685
Cdd:cd04407 155 PCLLRcpdssdpLTSMKDVAKTTTCVEMLI 184
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
519-667 1.93e-24

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


Pssm-ID: 239841  Cd Length: 206  Bit Score: 101.75  E-value: 1.93e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 519 IPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLhtpeDYENDVHAVADLLKIFFRELREPLIPDNH 598
Cdd:cd04376   9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVL----DENHSVHDVAALLKEFFRDMPDPLLPREL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 599 QRDFIDAGNVEDESrRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDV-----------NKMSTNNLAIIWGPTIIK 667
Cdd:cd04376  85 YTAFIGTALLEPDE-QLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsgNKMTSLNLATIFGPNLLH 163
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
503-692 4.20e-24

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: 100.07  E-value: 4.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 503 LFGARLdAIILREHsNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENnpllQLHTPEDYENdVHAVADLL 582
Cdd:cd04402   1 LFGQPL-SNICEDD-NLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNS----GVEVDLKAEP-VLLLASVL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 583 KIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWG 662
Cdd:cd04402  74 KDFLRNIPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIA 153
                       170       180       190
                ....*....|....*....|....*....|....*
gi 19112658 663 PTIIKQATIPE-----ISSFSRTIEILIDYCFTIF 692
Cdd:cd04402 154 PSLLWPPASSElqnedLKKVTSLVQFLIENCQEIF 188
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
504-663 4.36e-24

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: 100.62  E-value: 4.36e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSN--IPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHTPEDYEnDVHAVADL 581
Cdd:cd04379   1 FGVPLSRLVEREGESrdVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEELYP-DINVITGV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 582 LKIFFRELREPLIPDNHQRDFIDAGNV---EDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLA 658
Cdd:cd04379  80 LKDYLRELPEPLITPQLYEMVLEALAValpNDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLA 159

                ....*
gi 19112658 659 IIWGP 663
Cdd:cd04379 160 VCFGP 164
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
503-673 1.06e-23

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: 99.03  E-value: 1.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 503 LFGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFE--NNPLlqlhTPEDYENDVHAVAD 580
Cdd:cd04383   2 LFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFErgEDPL----ADDQNDHDINSVAG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 581 LLKIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAII 660
Cdd:cd04383  78 VLKLYFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAIC 157
                       170
                ....*....|...
gi 19112658 661 WGPTIIKqatIPE 673
Cdd:cd04383 158 FGPTLMP---VPE 167
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
521-686 1.67e-23

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: 98.62  E-value: 1.67e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 521 NIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNpllQLHTP-----EDYENDVHAVADLLKIFFRELREPLIP 595
Cdd:cd04374  30 KFVRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGLDP---KTSTPgdvdlDNSEWEIKTITSALKTYLRNLPEPLMT 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 596 DNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGPTIIKQ-----AT 670
Cdd:cd04374 107 YELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPqeetvAA 186
                       170
                ....*....|....*.
gi 19112658 671 IPEISSFSRTIEILID 686
Cdd:cd04374 187 IMDIKFQNIVVEILIE 202
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
503-673 1.86e-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: 98.30  E-value: 1.86e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 503 LFGARLDAIilrEHS-----NIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHTpedyENDVHA 577
Cdd:cd04393   2 VFGVPLQEL---QQAgqpenGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSK----EADVCS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 578 VADLLKIFFRELREPLIPDNHQRDFIDA---GNVEDESRRRdaVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMST 654
Cdd:cd04393  75 AASLLRLFLQELPEGLIPASLQIRLMQLyqdYNGEDEFGRK--LRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTA 152
                       170
                ....*....|....*....
gi 19112658 655 NNLAIIWGPTIIKQATIPE 673
Cdd:cd04393 153 ENLAAVFGPDVFHVYTDVE 171
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
504-692 2.14e-23

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: 98.18  E-value: 2.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILR--EHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFeNNPLlqlhtPEDY--ENDVHAVA 579
Cdd:cd04404   6 FGVSLQFLKEKnpEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKY-NMGE-----PVDFdqYEDVHLPA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 580 DLLKIFFRELREPLIPDNHQRDFIDAGNVEDESRRRdAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAI 659
Cdd:cd04404  80 VILKTFLRELPEPLLTFDLYDDIVGFLNVDKEERVE-RVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAV 158
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19112658 660 IWGPTII----KQATIPEISSFSRTIEILIDYCFTIF 692
Cdd:cd04404 159 VFGPNLLwakdASMSLSAINPINTFTKFLLDHQDEIF 195
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
503-665 3.06e-22

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: 94.73  E-value: 3.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 503 LFGARLD-AIILREHSN----IPNIVMQCTSQVE-NFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLhTPEDYENDVH 576
Cdd:cd04400   1 IFGSPLEeAVELSSHKYngrdLPSVVYRCIEYLDkNRAIYEEGIFRLSGSASVIKQLKERFNTEYDVDL-FSSSLYPDVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 577 AVADLLKIFFRELREPLIPDNHQRDFIDAGNV-EDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTN 655
Cdd:cd04400  80 TVAGLLKLYLRELPTLILGGELHNDFKRLVEEnHDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLR 159
                       170
                ....*....|
gi 19112658 656 NLAIIWGPTI 665
Cdd:cd04400 160 NVCIVFSPTL 169
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
504-681 5.22e-19

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: 85.52  E-value: 5.22e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSN-----IPNIVMQCTSQVENF-GLNLQGIYRVPSSSARVNMLRSQFEnnpllQLHTPEDYENDVHA 577
Cdd:cd04389   1 FGSSLEEIMDRQKEKypelkLPWILTFLSEKVLALgGFQTEGIFRVPGDIDEVNELKLRVD-----QWDYPLSGLEDPHV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 578 VADLLKIFFRELREPLIPDNHQRDFIDAgnvedeSRRRDAVHRAINDLPDANYSTIRHLtIHLAKI---KENSDVNKMST 654
Cdd:cd04389  76 PASLLKLWLRELEEPLIPDALYQQCISA------SEDPDKAVEIVQKLPIINRLVLCYL-INFLQVfaqPENVAHTKMDV 148
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19112658 655 NNLAIIWGPTIIK-QATIPEI--------SSFSRTI 681
Cdd:cd04389 149 SNLAMVFAPNILRcTSDDPRVifentrkeMSFLRTL 184
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
503-665 8.09e-18

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: 82.78  E-value: 8.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 503 LFGARLDAIILREH-----SNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENnpllqlhtpEDYEND--- 574
Cdd:cd04391   1 LFGVPLSTLLERDQkkvpgSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEA---------KFYEGTflw 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 575 ----VHAVADLLKIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVN 650
Cdd:cd04391  72 dqvkQHDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKN 151
                       170
                ....*....|....*
gi 19112658 651 KMSTNNLAIIWGPTI 665
Cdd:cd04391 152 KMNLWNVAMIMAPNL 166
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
504-692 6.22e-17

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: 79.40  E-value: 6.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHS----NIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLhtpEDYEndVHAVA 579
Cdd:cd04381   1 FGASLSLAVERSRChdgiDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNL---EEYE--PPTVA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 580 DLLKIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAI 659
Cdd:cd04381  76 SLLKQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISI 155
                       170       180       190
                ....*....|....*....|....*....|...
gi 19112658 660 IWGPTIikqatipEISsfSRTIEILIDYCFTIF 692
Cdd:cd04381 156 VLSPTV-------QIS--NRLLYALLTHCQELF 179
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
503-687 1.12e-16

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: 79.05  E-value: 1.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 503 LFGARLDAI---ILREHSNIPNIVMQCTSQVENFgLNLQGIYRVPSSSARVNMLRSQFENNP-LLQLHTPEDyendvhaV 578
Cdd:cd04394   1 VFGVPLHSLphsTVPEYGNVPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEaCLSSALPCD-------V 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 579 ADLLKIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLA 658
Cdd:cd04394  73 AGLLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLA 152
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19112658 659 IIWGPTI---------IKQATIPEISSFSRTIEILIDY 687
Cdd:cd04394 153 VIFAPNLfqseeggekMSSSTEKRLRLQAAVVQTLIDN 190
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
504-665 8.78e-16

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: 77.07  E-value: 8.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHtpEDYEndVHAVADLLK 583
Cdd:cd04375   5 FGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNY--DGQQ--AYDVADMLK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 584 IFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGP 663
Cdd:cd04375  81 QYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAP 160

                ..
gi 19112658 664 TI 665
Cdd:cd04375 161 SL 162
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
44-118 3.10e-15

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 71.15  E-value: 3.10e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112658    44 GLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFSASVITSMEIHEQLANH 118
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKFLKKKKKPEDDGGTLKKAWDELLTETEQLAKQ 75
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
504-685 2.03e-14

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: 71.96  E-value: 2.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILREHSnIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNplLQLHTPEDYenDVHAVADLLK 583
Cdd:cd04406   1 FGVELSRLTSEDRS-VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTD--ANSVNLDDY--NIHVIASVFK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 584 IFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGP 663
Cdd:cd04406  76 QWLRDLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAP 155
                       170       180
                ....*....|....*....|....*....
gi 19112658 664 TIIK-------QATIPEISSFSRTIEILI 685
Cdd:cd04406 156 CILRcpdttdpLQSVQDISKTTTCVELIV 184
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
519-687 3.84e-14

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


Pssm-ID: 239861  Cd Length: 225  Bit Score: 72.06  E-value: 3.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 519 IPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFEnnpllqlhTPEDYEND-------VHAVADLLKIFFRELRE 591
Cdd:cd04396  32 IPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFS--------TPPDYGKSfdwdgytVHDAASVLRRYLNNLPE 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 592 PLIP-----------------DNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANystiRHLTIH----LAKIKENSDVN 650
Cdd:cd04396 104 PLVPldlyeefrnplrkrpriLQYMKGRINEPLNTDIDQAIKEYRDLITRLPNLN----RQLLLYlldlLAVFARNSDKN 179
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19112658 651 KMSTNNLAIIWGPTII---KQATIPEISSFSRT-IEILIDY 687
Cdd:cd04396 180 LMTASNLAAIFQPGILshpDHEMDPKEYKLSRLvVEFLIEH 220
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
535-666 1.91e-13

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: 69.80  E-value: 1.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 535 LNLQGIYRVPSSSARVNMLRSQFENNPLLQLHTPEDYENDVhavADLLKIFFRELREPLIPDNHQR---------DFIDA 605
Cdd:cd04392  24 LRVEGLFRKPGNSARQQELRDLLNSGTDLDLESGGFHAHDC---ATVLKGFLGELPEPLLTHAHYPahlqiadlcQFDEK 100
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112658 606 GN---VEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGPTII 666
Cdd:cd04392 101 GNktsAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLI 164
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
40-229 3.50e-13

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153331 [Multi-domain]  Cd Length: 239  Bit Score: 69.81  E-value: 3.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  40 NSELGLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKhhspqSFSASVITSMEIHEQLANHS 119
Cdd:cd07647   2 TSTTGFDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPGDEIG-----TLKSSWDSLRKETENVANAH 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 120 LTLQKTLSAFSDQVIEFHKNAERKRK----SIKEYAKKQENAYlEAVMQMDKS---KSRFK-GAETEYnraldnkntgds 191
Cdd:cd07647  77 IQLAQSLREEAEKLEEFREKQKEERKktedIMKRSQKNKKELY-KKTMKAKKSyeqKCREKdKAEQAY------------ 143
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19112658 192 QKKVGFFKPKSNAQLTKLEDEARLKAENAESDMHSKIE 229
Cdd:cd07647 144 EKSSSGAQPKEAEKLKKKAAQCKTSAEEADSAYKSSIG 181
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
58-227 1.84e-11

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proteins in this group have been named FCH domain Only (FCHO) proteins. Vertebrates have two members, FCHO1 and FCHO2. These proteins contain an F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153332 [Multi-domain]  Cd Length: 261  Bit Score: 65.06  E-value: 1.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  58 TCKELAGFFKKRSILEEESGKNLQKLAKsyletfQSKHHSPQS-FSA--SVITSMEihEQLANHSLTLQKTLSAFSDQVI 134
Cdd:cd07648  20 AVKELADFLRERATIEETYSKALNKLAK------QASNSSQLGtFAPlwLVLRVST--EKLSELHLQLVQKLQELIKDVQ 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 135 EFHKNAERKRKSIKEyakkQENAYLEAVMQMD-------KSKSRFKGAETEYNRaldNKNTGDSQKKVgffkPKSNAQLT 207
Cdd:cd07648  92 KYGEEQHKKHKKVKE----EESGTAEAVQAIQtttaalqKAKEAYHARCLELER---LRRENASPKEI----EKAEAKLK 160
                       170       180
                ....*....|....*....|...
gi 19112658 208 KLEDEARL---KAENAESDMHSK 227
Cdd:cd07648 161 KAQDEYKAlveKYNNIRADFETK 183
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
504-666 1.39e-09

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: 58.53  E-value: 1.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 504 FGARLDAIILRE-----------HSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLlqlHTPEDYE 572
Cdd:cd04397   1 FGVPLEILVEKFgadstlgvgpgKLRIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPT---EVPDLSK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 573 NDVHAVADLLKIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIR------HLTIHLAKIKEN 646
Cdd:cd04397  78 ENPVQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEvlfsflKWVSSFSHIDEE 157
                       170       180
                ....*....|....*....|
gi 19112658 647 SDvNKMSTNNLAIIWGPTII 666
Cdd:cd04397 158 TG-SKMDIHNLATVITPNIL 176
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
48-188 2.04e-09

The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.


Pssm-ID: 153294 [Multi-domain]  Cd Length: 191  Bit Score: 57.73  E-value: 2.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  48 LNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFSASVitsMEIHEQLANHSLTLQKTLS 127
Cdd:cd07610   5 LEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKPESGKTSLGTSWNSL---REETESAATVHEELSEKLS 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112658 128 AFSDQVIefhknaeRKRKSIKEYAKKQENAYLEAVMQ--MDKSKSRFKGAETEYNRALDNKNT 188
Cdd:cd07610  82 QLIREPL-------EKVKEDKEQARKKELAEGEKLKKklQELWAKLAKKADEEYREQVEKLNP 137
F-BAR_NOSTRIN cd07658
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic ...
59-256 1.35e-07

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic INducer (NOSTRIN); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Nitric Oxide Synthase TRaffic INducer (NOSTRIN) is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). NOSTRIN facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of NOSTRIN may be correlated to preeclampsia. NOSTRIN contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. The F-BAR domain of NOSTRIN is necessary and sufficient for its membrane association and is responsible for its subcellular localization.


Pssm-ID: 153342 [Multi-domain]  Cd Length: 239  Bit Score: 53.15  E-value: 1.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  59 CKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFSASVITSME----IHEQLANhSLTLQ--KTLSAFSDq 132
Cdd:cd07658  21 CKELATVLQERAELELNYAKGLSKLSGKLSKASKSVSGTLSSAWTCVAEEMEseadIHRNLGS-ALTEEaiKPLRQVLD- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 133 viefhkNAERKRKSIKEYAKKQENAYLEAVMQMDKSKSR----FKGAETEYNRALDNKNTGDSQK---KVGFFKPKSNAQ 205
Cdd:cd07658  99 ------EQHKTRKPVENEVDKAAKLLTDWRSEQIKVKKKlhglARENEKLQDQVEDNKQSCTKQKmlnKLKKSAEVQDKE 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19112658 206 LTKLED------EARLKAENAESDMHSKIENAQNVQKQLLCihrpNYIKQFFSLQRE 256
Cdd:cd07658 173 DEKLEAkrkkgeESRLKAENEYYTCCVRLERLRLEWESALR----KGLNQYESLEEE 225
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
44-172 6.79e-07

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 50.76  E-value: 6.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  44 GLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYL---ETFQSKhHSPQSFSASVitsmeihEQLANHSL 120
Cdd:cd07651   6 GFDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRLEKLSRKSLggsEEGGLK-NSLDTLRLET-------ESMAKSHL 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19112658 121 TLQKTL-SAFSDQVIEFHKNAERKRKSI-----KEYAKKQE-NAYLEavmqmdKSKSRF 172
Cdd:cd07651  78 KFAKQIrQDLEEKLAAFASSYTQKRKKIqshmeKLLKKKQDqEKYLE------KAREKY 130
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
44-122 1.51e-06

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 46.57  E-value: 1.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658     44 GLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAK-SYLETFQSKHHSPQSFSASVITSMEihEQLANHSLTL 122
Cdd:smart00055  10 GFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKkLRAVRDTEPEYGSLSKAWEVLLSET--DALAKQHLEL 87
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
65-236 1.66e-06

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153337 [Multi-domain]  Cd Length: 251  Bit Score: 49.94  E-value: 1.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  65 FFKKRSILEEESGKNLQKLAKSYLETfqSKHHSPQSFSASVITSMEIHE--QLANhsltlQKTLSA--FSDQVI-EFHKN 139
Cdd:cd07653  27 FVKERAAIEQEYAKKLRKLVKKYLPK--KKEEDEYSFSSVKAFRSILNEvnDIAG-----QHELIAenLNSNVCkELKTL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 140 AERKRKSIKEYAK--KQENAYLEAVM-QMDKSKSRFKGAETEYNRALDNKNTGDSQKKVgffkpkSNAQLTKLEDEARLK 216
Cdd:cd07653 100 ISELRQERKKHLSegSKLQQKLESSIkQLEKSKKAYEKAFKEAEKAKQKYEKADADMNL------TKADVEKAKANANLK 173
                       170       180
                ....*....|....*....|
gi 19112658 217 AENAEsdmHSKIENAQNVQK 236
Cdd:cd07653 174 TQAAE---EAKNEYAAQLQK 190
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
520-685 2.02e-06

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: 49.10  E-value: 2.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 520 PNIVMQCTSQVENFGLNLQGIYRVPSSSARVNmLRSQFENNPllqlhTPEDYEN-DVHAVADLLKIFFRELREPLIPDNH 598
Cdd:cd04388  16 PPLLIKLVEAIEKKGLESSTLYRTQSSSSLTE-LRQILDCDA-----ASVDLEQfDVAALADALKRYLLDLPNPVIPAPV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 599 QRDFIDAGNVEDESRRRDAVHRAI---NDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGPTIIK-QATIPEI 674
Cdd:cd04388  90 YSEMISRAQEVQSSDEYAQLLRKLirsPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRfQPASSDS 169
                       170
                ....*....|..
gi 19112658 675 SSFS-RTIEILI 685
Cdd:cd04388 170 PEFHiRIIEVLI 181
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
321-479 3.19e-06

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 50.69  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   321 DNKNPTDASKTKIIQPPSSYGTGSSAGKTNPPVN---PTI---KVTAAIPSPLQN-TNPAPS-TFPNPSVASPAF----P 388
Cdd:pfam05109 500 ESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNatsPTLgktSPTSAVTTPTPNaTSPTPAvTTPTPNATIPTLgktsP 579
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   389 NSSTSNPStaPASASPLASTLKPStANDTNGSSSSSSSNPRTSSPlASNAENKPPVAQQSPPVLLPTLPPIQTTTIQtsr 468
Cdd:pfam05109 580 TSAVTTPT--PNATSPTVGETSPQ-ANTTNHTLGGTSSTPVVTSP-PKNATSAVTTGQHNITSSSTSSMSLRPSSIS--- 652
                         170
                  ....*....|.
gi 19112658   469 EVAPPPSSINS 479
Cdd:pfam05109 653 ETLSPSTSDNS 663
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
574-666 3.22e-06

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: 48.88  E-value: 3.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 574 DVHAVADLLKIFFRELREPLIPDNHQRDFIDAGNVeDESRRRDAVHRAindLPDANYSTIRHLTIHLAKIKENSDVNKMS 653
Cdd:cd04380 103 SAESVAEALLLFLESLPDPIIPYSLYERLLEAVAN-NEEDKRQVIRIS---LPPVHRNVFVYLCSFLRELLSESADRGLD 178
                        90
                ....*....|...
gi 19112658 654 TNNLAIIWGPTII 666
Cdd:cd04380 179 ENTLATIFGRVLL 191
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
44-235 5.25e-06

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. The specific function of FCH domain Only 2 (FCHO2) is still unknown. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO1 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153357 [Multi-domain]  Cd Length: 269  Bit Score: 48.52  E-value: 5.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  44 GLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSP--QSFSASVitsmeihEQLANHSLT 121
Cdd:cd07673  13 GFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLAKSASNYSQLGTFAPvwDVFKTST-------EKLANCHLE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 122 LQKTLsafSDQVIEFHKNAERKRKSIKEyAKKQENAYLEAVMQMDK-SKSRFKGAETEYNRALDN---KNTGDSQKKVgf 197
Cdd:cd07673  86 LVRKL---QELIKEVQKYGEEQVKSHKK-TKEEVAGTLEAVQNIQSiTQALQKSKENYNAKCLEQerlKKEGATQREI-- 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19112658 198 fkPKSNAQLTKLEDEARLKAEN---AESDMHSKI-ENAQNVQ 235
Cdd:cd07673 160 --EKAAVKSKKATESYKLYVEKyalAKADFEQKMtETAQKFQ 199
PHA03247 PHA03247
large tegument protein UL36; Provisional
314-499 6.80e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 6.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   314 HASIKHEDNKNPTDASKTKIIQPPSSYGTGSSAGKTNPPVNPTIKVTAAIPSPLQNT----NPAPSTFPNPSVASPAFPN 389
Cdd:PHA03247 2642 PPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLadppPPPPTPEPAPHALVSATPL 2721
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   390 SSTSNPSTAPASASPLASTLKPS-TANDTNGSSSSSSSNPRTSSPLASNAENKPPVA-QQSPPVLLPTLPPIQTTTIQTS 467
Cdd:PHA03247 2722 PPGPAAARQASPALPAAPAPPAVpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGpPRRLTRPAVASLSESRESLPSP 2801
                         170       180       190
                  ....*....|....*....|....*....|....
gi 19112658   468 REVAPPPSSINSNRAASPF--RPTSVSPQPSSPT 499
Cdd:PHA03247 2802 WDPADPPAAVLAPAAALPPaaSPAGPLPPPTSAQ 2835
PHA03247 PHA03247
large tegument protein UL36; Provisional
326-499 1.03e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   326 TDASKTKIIQPPSSYGTGSSAGKTNPPVNPTIKVTAAIPSPLQNTNPAPSTFPNPS-VASPAFPNSSTSNPSTAPASASP 404
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAdPPAAVLAPAAALPPAASPAGPLP 2829
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   405 LASTLKPSTANDTNGSSSSSSS-------------NPRTSSPLASNAEN---------KPPVAQQSPPVLLPTLPPIQTT 462
Cdd:PHA03247 2830 PPTSAQPTAPPPPPGPPPPSLPlggsvapggdvrrRPPSRSPAAKPAAParppvrrlaRPAVSRSTESFALPPDQPERPP 2909
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 19112658   463 TIQTSREVAPPPSSINSNRAASPFRPTSVSPQPSSPT 499
Cdd:PHA03247 2910 QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPT 2946
PHA03247 PHA03247
large tegument protein UL36; Provisional
334-502 1.40e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   334 IQPPSSYGTGSSAGKTNPPVNPTikvTAAIPSPLQNTNPA---PSTFPNPSVAS-----PAFPnsSTSNPSTAPASASPL 405
Cdd:PHA03247 2740 APPAVPAGPATPGGPARPARPPT---TAGPPAPAPPAAPAagpPRRLTRPAVASlsesrESLP--SPWDPADPPAAVLAP 2814
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   406 ASTLKPSTANDTngsssssSSNPRTSSPLASNAENKPPVAqqsppvllptlppiqtTTIQTSREVAP-------PPSSIN 478
Cdd:PHA03247 2815 AAALPPAASPAG-------PLPPPTSAQPTAPPPPPGPPP----------------PSLPLGGSVAPggdvrrrPPSRSP 2871
                         170       180
                  ....*....|....*....|....*..
gi 19112658   479 SNRAASPFRPTSVS---PQPSSPTKSL 502
Cdd:PHA03247 2872 AAKPAAPARPPVRRlarPAVSRSTESF 2898
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
337-485 3.20e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 47.15  E-value: 3.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  337 PSSYGTGSSAGKTNPPVNPTIKVTAAIPSPlQNTNPAPSTFPNPSVASPAFPNSSTS------NPSTAPASAS-PLASTL 409
Cdd:PRK07003 383 PGARAAAAVGASAVPAVTAVTGAAGAALAP-KAAAAAAATRAEAPPAAPAPPATADRgddaadGDAPVPAKANaRASADS 461
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112658  410 KPSTANDTNGSSSSSSSNPRTSSPLASNAENKPPVAQQSPPVLLPTLPPIQTTTIQTSREVAPPPSSINSNRAASP 485
Cdd:PRK07003 462 RCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTP 537
PHA03379 PHA03379
EBNA-3A; Provisional
335-572 5.14e-05

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 46.59  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  335 QPPSSYGTGSSAGKTNPPVNPTIKVTAA---------IPSPLQNTNPAPSTFPNPSVASPAFPNSSTSNPSTAPASASPL 405
Cdd:PHA03379 426 EVPQSLETATSHGSAQVPEPPPVHDLEPgplhdqhsmAPCPVAQLPPGPLQDLEPGDQLPGVVQDGRPACAPVPAPAGPI 505
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  406 ASTLKPSTANdtngsSSSSSSNPRTSSPLASNAENKPPVAQQSPPVLLPTLPPIQ-----TTTIQTSREVAPPPSSINSN 480
Cdd:PHA03379 506 VRPWEASLSQ-----VPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAPPLIAMQgpgetSGIVRVRERWRPAPWTPNPP 580
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  481 RAASPF---------RP----------------TSVSPQ-----PSSPTKSLLFGARLD--AIILREhSNIPniVMQCTS 528
Cdd:PHA03379 581 RSPSQMsvrdrlarlRAeaqpyqasvevqppqlTQVSPQqpmeyPLEPEQQMFPGSPFSqvADVMRA-GGVP--AMQPQY 657
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 19112658  529 qvenFGLNLQgiyRVPSSSARVNMLRSQFENNPLLQLHTPEDYE 572
Cdd:PHA03379 658 ----FDLPLQ---QPISQGAPLAPLRASMGPVPPVPATQPQYFD 694
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
316-501 8.85e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.06  E-value: 8.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   316 SIKHEDNKNPTDASKTKIIQP----PSSYGTGSSAgKTNPPVNPTIKVTAAIPSPlqnTNPAPS-TFPNPSVASPAF--- 387
Cdd:pfam05109 467 TVSTADVTSPTPAGTTSGASPvtpsPSPRDNGTES-KAPDMTSPTSAVTTPTPNA---TSPTPAvTTPTPNATSPTLgkt 542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   388 -PNSSTSNPSTAPASASPLASTLKPS----TANDTNGSSSSSSSNPRTSSPLASNAENKPPVAQQSPPVLLPTLPPIQTT 462
Cdd:pfam05109 543 sPTSAVTTPTPNATSPTPAVTTPTPNatipTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPVVTSPP 622
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 19112658   463 TIQTSREVAPPPSSINSNRAASPFRPTSVSpQPSSPTKS 501
Cdd:pfam05109 623 KNATSAVTTGQHNITSSSTSSMSLRPSSIS-ETLSPSTS 660
PHA03247 PHA03247
large tegument protein UL36; Provisional
325-498 1.66e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   325 PTDASKTKIIQPPSSYGTGSSAGKTNPPVNPTIKVTAAI--PSPLQNTNPAPSTFPNPSVAsPAFPNSSTSNPSTA--PA 400
Cdd:PHA03247 2690 PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAArqASPALPAAPAPPAVPAGPAT-PGGPARPARPPTTAgpPA 2768
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   401 SASPLASTLKP---STANDTNGSSSSSSSNPRTSSPLASNAENKPPVAQQSPPVLLPTLPPIQTTTIQTSREVA--PPPS 475
Cdd:PHA03247 2769 PAPPAAPAAGPprrLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPpgPPPP 2848
                         170       180
                  ....*....|....*....|...
gi 19112658   476 SINSNRAASPFRPTSVSPQPSSP 498
Cdd:PHA03247 2849 SLPLGGSVAPGGDVRRRPPSRSP 2871
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
44-195 1.96e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153358 [Multi-domain]  Cd Length: 261  Bit Score: 43.78  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  44 GLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAK-----SYLETFqskhhSP--QSFSASVITSMEIHEQLA 116
Cdd:cd07674   6 GFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKmasngSPLGTF-----APmwEVFRVSSDKLALCHLELM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 117 NHSLTLQKTLSAFSDQVIEFHK------------------NAERKRKSIKEYAKK---QENAYLEAVMQ--MDKSKSRFK 173
Cdd:cd07674  81 RKLNDLIKDINRYGDEQVKIHKktkeeaigtleavqslqvQSQHLQKSRENYHSKcveQERLRREGVPQkeLEKAELKTK 160
                       170       180
                ....*....|....*....|....
gi 19112658 174 GAETEYNRALDNKNT--GDSQKKV 195
Cdd:cd07674 161 KAAESLRGSVEKYNRarGDFEQKM 184
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
60-192 1.99e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153333 [Multi-domain]  Cd Length: 233  Bit Score: 43.46  E-value: 1.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  60 KELAGFFKKRSILEEESGKNLQKLAKSYL---------ETF-QSKHHSPQS------FSASVitSMEIHEQLANHSLTLQ 123
Cdd:cd07649  22 KEMAEFIRERIKIEEEYAKNLSKLSQSSLaaqeegtlgEAWaQVKKSLADEaevhlkFSSKL--QSEVEKPLLNFRENFK 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 124 KTLSAFSDQVIEFHKN-------AERKRKSIKEYAK------KQENAYLEAVMQMDKSKSRFKGAET--EYNRALDNKNT 188
Cdd:cd07649 100 KDMKKLDHHIADLRKQlasryaaVEKARKALLERQKdlegktQQLEIKLSNKTEEDIKKARRKSTQAgdDLMRCVDLYNQ 179

                ....
gi 19112658 189 GDSQ 192
Cdd:cd07649 180 AQSK 183
PHA03247 PHA03247
large tegument protein UL36; Provisional
346-500 2.22e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   346 AGKTNPPVNPtikvtAAIPSPLQNTNPAPSTFPNPSvaSPAFpNSSTSNPSTAPASASPlastlkpSTANDTNGSSSSSS 425
Cdd:PHA03247 2548 AGDPPPPLPP-----AAPPAAPDRSVPPPRPAPRPS--EPAV-TSRARRPDAPPQSARP-------RAPVDDRGDPRGPA 2612
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112658   426 snPRTSSPLASNAENKPPVAQQSPPVLLPTLPPIQTTTIQTSREVAPPPSSINSNRAASPFRPTSVSPQPSSPTK 500
Cdd:PHA03247 2613 --PPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR 2685
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
325-497 3.22e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.80  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   325 PTDASKTKIIQPPSSYGTGSSAGKTNPP-VNPTIKVTAAIPSPLQNTNPAPSTF---------------PNPSVASPAFP 388
Cdd:pfam17823 153 NASAAPRAAIAAASAPHAASPAPRTAASsTTAASSTTAASSAPTTAASSAPATLtpargistaatatghPAAGTALAAVG 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   389 NSSTSNPSTAPASASPLASTLKPSTAN-----DTNGSSSSSSSNPRTSSPLASNAENKPPVAQQSPPVLLPTLPPIQTTT 463
Cdd:pfam17823 233 NSSPAAGTVTAAVGTVTPAALATLAAAagtvaSAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVST 312
                         170       180       190
                  ....*....|....*....|....*....|....
gi 19112658   464 IQTSREVAPPPSSINSNRAASPFRPTSVSPQPSS 497
Cdd:pfam17823 313 DQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLA 346
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
361-496 4.27e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 43.54  E-value: 4.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  361 AAIPSPLQNTNPAPSTFPNPSVASPAFPnSSTSNPSTAPASASPLASTLKPSTAndtngsssSSSSNPRTSSP--LASNA 438
Cdd:PRK08691 361 LAAASCDANAVIENTELQSPSAQTAEKE-TAAKKPQPRPEAETAQTPVQTASAA--------AMPSEGKTAGPvsNQENN 431
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19112658  439 ENKPPVAQQSPPVLLPTLPPIQTTTIQTSREVA-PPPSSINSNRAASPFRPTSVSPQPS 496
Cdd:PRK08691 432 DVPPWEDAPDEAQTAAGTAQTSAKSIQTASEAEtPPENQVSKNKAADNETDAPLSEVPS 490
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
316-492 4.46e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.41  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   316 SIKHEDNKNPTDASKTKIIQPPS--SYGTGSSAGKTNppvnpTIKVTAAIPSPLQNTN-PAPSTFPNPSVASPAFPNSST 392
Cdd:pfam17823  46 AVPRADNKSSEQ*NFCAATAAPApvTLTKGTSAAHLN-----STEVTAEHTPHGTDLSePATREGAADGAASRALAAAAS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   393 SNPSTApASASPLASTLKPSTANDTngSSSSSSSNPRTSSPLASNAENKPPVAQQSPPVLLPTLPPIQTTTiqTSREVAP 472
Cdd:pfam17823 121 SSPSSA-AQSLPAAIAALPSEAFSA--PRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASST--TAASSAP 195
                         170       180
                  ....*....|....*....|
gi 19112658   473 PPSSINSNRAASPFRPTSVS 492
Cdd:pfam17823 196 TTAASSAPATLTPARGISTA 215
F-BAR_FBP17 cd07676
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; ...
65-249 4.61e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Formin Binding Protein 17 (FBP17), also called FormiN Binding Protein 1 (FNBP1), is involved in dynamin-mediated endocytosis. It is recruited to clathrin-coated pits late in the endocytosis process and may play a role in the invagination and scission steps. FBP17 binds in vivo to tankyrase, a protein involved in telomere maintenance and mitogen activated protein kinase (MAPK) signaling. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153360 [Multi-domain]  Cd Length: 253  Bit Score: 42.34  E-value: 4.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  65 FFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFS---ASVITSMEIHEQLANHSLTLQKTLSAFSDQVIEFHKNAE 141
Cdd:cd07676  27 FVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTscrAFLMTLNEMNDYAGQHEVISENLASQIIVELTRYVQELK 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 142 RKRKSIKEYAKKQENAYLEAVMQMDKSKSRFKGAETEYNRALDNKNTGDSQKKVgffkpkSNAQLTKLEDEARLK---AE 218
Cdd:cd07676 107 QERKSHFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINV------TKADVEKARQQAQIRhqmAE 180
                       170       180       190
                ....*....|....*....|....*....|.
gi 19112658 219 NAESDMHSKIENAQNVQKQLLCIHRPNYIKQ 249
Cdd:cd07676 181 DSKAEYSSYLQKFNKEQHEHYYTHIPNIFQK 211
F-BAR_FCHSD1 cd07678
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 ...
60-221 5.05e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH and double SH3 domains 1 (FCHSD1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH and double SH3 domains 1 (FCHSD1) contains an N-terminal F-BAR domain and two SH3 domains at the C-terminus. It has been characterized only in silico, and its biological function is still unknown. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153362 [Multi-domain]  Cd Length: 263  Bit Score: 42.30  E-value: 5.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  60 KELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFSASVITSME-IHEQLANHSLTLQKTLSAFSDQVIEFHK 138
Cdd:cd07678  22 EDIRSYSKQRAAIEREYGQALQRLASQFLKRDWHRGGNETEMDRSVRTVWGaWREGTAATGQGRVTRLEAYRRLRDEAGK 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 139 NA----ERKRKSIKEYAKKQENAYLEAVMQMDKSKSRFkgAETEYNRALDNKNTGDSQKKV-----GFFkpKSNAQLTKL 209
Cdd:cd07678 102 TGrsakEQVLKKSTEQLQKAQAELLETVKELSKSKKLY--GQLERVSEVAKEKAADVEARLnksdhGIF--HSKASLQKL 177
                       170
                ....*....|..
gi 19112658 210 edEARLKAENAE 221
Cdd:cd07678 178 --SAKFSAQSAE 187
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
337-504 6.04e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.16  E-value: 6.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  337 PSSYGTGSSAGKTNPPVNPTIKVTAAIPSPLQNTNPAPSTFPnPSVASPafpnsstsnPSTAPASASPlastlkpstand 416
Cdd:PRK14951 366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAP-AAAASA---------PAAPPAAAPP------------ 423
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  417 tngsssssssnPRTSSPLASNAENKPPVAQQSPPVLLPTLPPIQTTTIQTSREVAPPPSsinsnrAASPFRPTSVSPQPS 496
Cdd:PRK14951 424 -----------APVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPA------VASAAPAPAAAPAAA 486

                 ....*...
gi 19112658  497 SPTKSLLF 504
Cdd:PRK14951 487 RLTPTEEG 494
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
326-406 9.73e-04

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 42.19  E-value: 9.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   326 TDASKTKIIQPPSSYGTGSSAGkTNPPVNPTIKVTAAIPSPLQntnpaPSTFPNPSVASPAFPNSSTSNPSTAPASASPL 405
Cdd:TIGR00601  77 PKTGTGKVAPPAATPTSAPTPT-PSPPASPASGMSAAPASAVE-----EKSPSEESATATAPESPSTSVPSSGSDAASTL 150

                  .
gi 19112658   406 A 406
Cdd:TIGR00601 151 V 151
PHA03255 PHA03255
BDLF3; Provisional
330-504 1.03e-03

BDLF3; Provisional


Pssm-ID: 165513 [Multi-domain]  Cd Length: 234  Bit Score: 41.43  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  330 KTKIIQPPSSYGTGSSAGKTNPPVNPTIKVTAAIPSPLQNTNPAPSTFPnpsVASPAFPNSSTSNPSTAPASASPLASTL 409
Cdd:PHA03255  19 ETSLIWTSSGSSTASAGNVTGTTAVTTPSPSASGPSTNQSTTLTTTSAP---ITTTAILSTNTTTVTSTGTTVTPVPTTS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  410 KPSTANDTNgsssssSSNPRTSSPLASNAENKPPVAqqSPPVLLPTLPPIQTTTIQTSREVAPPPSSINSNRAASPFRPT 489
Cdd:PHA03255  96 NASTINVTT------KVTAQNITATEAGTGTSTGVT--SNVTTRSSSTTSATTRITNATTLAPTLSSKGTSNATKTTAEL 167
                        170       180
                 ....*....|....*....|..
gi 19112658  490 SVSP---QPSS----PTKSLLF 504
Cdd:PHA03255 168 PTVPderQPSLsyglPLWTLVF 189
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
324-498 1.05e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   324 NPTDASKTKIIQPPSSYGTGSSAGKTNPPVNPTIKvTAAIPSPLQNTNPAPSTFPNPSVAS-------PAFPNSSTSNPS 396
Cdd:PHA03307  105 SPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLR-PVGSPGPPPAASPPAAGASPAAVASdaassrqAALPLSSPEETA 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   397 TAPASASPLASTLKPSTANDTNGSSSSSSSNPRTSSPLASNAENK--PPVAQQSPPVLLPTLPPIQTTTIQTSREVAPPP 474
Cdd:PHA03307  184 RAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAadDAGASSSDSSSSESSGCGWGPENECPLPRPAPI 263
                         170       180
                  ....*....|....*....|....
gi 19112658   475 SSINSNRAASPFRPTSVSPQPSSP 498
Cdd:PHA03307  264 TLPTRIWEASGWNGPSSRPGPASS 287
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
351-448 1.05e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.10  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  351 PPVNPTIKVTAAIPSPLQNTnPAPSTFPNPSVASPAFPNSSTSNPSTAPASASPLASTLKPSTandtngsSSSSSSNPRT 430
Cdd:PRK14950 363 VPAPQPAKPTAAAPSPVRPT-PAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHT-------PESAPKLTRA 434
                         90
                 ....*....|....*...
gi 19112658  431 SSPLASNAENKPPVAQQS 448
Cdd:PRK14950 435 AIPVDEKPKYTPPAPPKE 452
F-BAR_srGAP cd07656
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating ...
61-131 1.48e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Slit-Robo GTPase Activating Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs, all of which are expressed during embryonic and early development in the nervous system but with different localization and timing. srGAPs contain an N-terminal F-BAR domain, a Rho GAP domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153340 [Multi-domain]  Cd Length: 241  Bit Score: 40.78  E-value: 1.48e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112658  61 ELAGFFKKRSILEEESGKNLQKLAKSyletFQSKHHSPQS--FSASVITSMEIHEQLANHSLTLQKTLSAFSD 131
Cdd:cd07656  23 DLQDYFRRRAEIELEYSRSLEKLADR----FSSKHKNEKSkrEDWSLLSPVNCWNTLLVQTKQESRDHSTLSD 91
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
269-500 2.70e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 40.71  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   269 TKLCESNTllnglTIRPQKPTPTNCGLQHAldnINANTDFVQYVLHASIKHEDNKNPTDASKTKIIQPPSSYGTGSSAGK 348
Cdd:pfam17823 147 AAACRANA-----SAAPRAAIAAASAPHAA---SPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAATA 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   349 TNPPVNPTikVTAAIPsplqNTNPAPSTFPNP-SVASPAFPNSSTSNPSTAPASA------SPLASTLKPS--TANDTNG 419
Cdd:pfam17823 219 TGHPAAGT--ALAAVG----NSSPAAGTVTAAvGTVTPAALATLAAAAGTVASAAgtinmgDPHARRLSPAkhMPSDTMA 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   420 SSSSSSSNPRTSSPLASNAENKP-------PVAQQSPPVLLPTLPP---------IQTTTIQTSREVA-----PPPSSIN 478
Cdd:pfam17823 293 RNPAAPMGAQAQGPIIQVSTDQPvhntagePTPSPSNTTLEPNTPKsvastnlavVTTTKAQAKEPSAspvpvLHTSMIP 372
                         250       260
                  ....*....|....*....|..
gi 19112658   479 SNRAASPfrptSVSPQPSSPTK 500
Cdd:pfam17823 373 EVEATSP----TTQPSPLLPTQ 390
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
44-237 5.35e-03

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 1 (PSTPIP1), also known as CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153355 [Multi-domain]  Cd Length: 242  Bit Score: 39.17  E-value: 5.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  44 GLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSyletfQSKHHSPQSFSASVITSMEIHEQLANHSLTLQ 123
Cdd:cd07671   6 GYEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIARK-----AGGQTEINTLKASFDQLKQQIENIGNSHIQLA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658 124 KTLSAFSDQVIEFHknaERKRKSIKEYakkqenaylEAVMQ-MDKSKSrfkgaeTEYNRALDNKntgdsqkkvgffkpKS 202
Cdd:cd07671  81 GMLREELKSLEEFR---ERQKEQRKKY---------EAVMErVQKSKV------SLYKKTMESK--------------KT 128
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 19112658 203 NAQLTKLEDEARLKAENAESDMHSK-IENAQNVQKQ 237
Cdd:cd07671 129 YEQRCREADEAEQTFERSSSTGNPKqSEKSQNKAKQ 164
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
336-507 5.44e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   336 PPSSYGTGSSAGK--TNPPVNPTIKVTAAIP---SPLQNTNPAPSTFPNPSV-ASPAfpnsstsnPSTAPASASPLASTL 409
Cdd:PHA03307   71 PPPGPGTEAPANEsrSTPTWSLSTLAPASPAregSPTPPGPSSPDPPPPTPPpASPP--------PSPAPDLSEMLRPVG 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   410 KPSTANDTN----GSSSSSSSNPRTSSPLASNAENKPPVAQQSPPVLLPTLPpiqtttIQTSREVAPPPSSinsnRAASP 485
Cdd:PHA03307  143 SPGPPPAASppaaGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPP------PSTPPAAASPRPP----RRSSP 212
                         170       180
                  ....*....|....*....|..
gi 19112658   486 FRPTSVSPQPsSPTKSLLFGAR 507
Cdd:PHA03307  213 ISASASSPAP-APGRSAADDAG 233
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
344-416 5.64e-03

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 39.49  E-value: 5.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112658   344 SSAGKTNPPVNPTikvtaAIPSPLQNTNPAPSTFPNPSVASPAFPNSSTSNPSTAPASASPLASTlkPSTAND 416
Cdd:TIGR00601  80 GTGKVAPPAATPT-----SAPTPTPSPPASPASGMSAAPASAVEEKSPSEESATATAPESPSTSV--PSSGSD 145
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
317-443 5.67e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 39.91  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658  317 IKHEDNKNPTDASKTKIIQPPSSYGTGSSAGKTNPPVNPTIKVTAAIPSPLQNT---------NPAPSTFPNPSVASPAF 387
Cdd:PLN03209 442 ARYEDLKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATAATDAAAPPPANMRplspyavydDLKPPTSPSPAAPVGKV 521
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19112658  388 PNSSTSNPSTAPASASPLASTLKPSTANdtngssssssSNPRTSSPLASNAENKPP 443
Cdd:PLN03209 522 APSSTNEVVKVGNSAPPTALADEQHHAQ----------PKPRPLSPYTMYEDLKPP 567
PRK10856 PRK10856
cytoskeleton protein RodZ;
337-414 6.09e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 39.24  E-value: 6.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112658  337 PSSYGTGSSAGKTNPPVNPTIKVTAAIPSPLQNTNPAPSTFP-NPSVASPAFPNSSTSNPSTAPASASPLASTLKPSTA 414
Cdd:PRK10856 163 PLDTSTTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPqQNAVVAPSQANVDTAATPAPAAPATPDGAAPLPTDQ 241
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
300-507 6.79e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.77  E-value: 6.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   300 DNINANTDFVQYVLHASIKHEDNknPTDAsktkiIQPPSSYGTGSSAGKTNPPVNPTIKVTaaipsplqnTNPAPSTFPN 379
Cdd:PHA03307    9 DLIEAAAEGGEFFPRPPATPGDA--ADDL-----LSGSQGQLVSDSAELAAVTVVAGAAAC---------DRFEPPTGPP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   380 PSVASPAFPNSSTSNPSTAPasaSPLASTLKPSTANDTNGSSSSSSSNPRTSSPlASNAENKPPVAQQSPPVLLPTLPPI 459
Cdd:PHA03307   73 PGPGTEAPANESRSTPTWSL---STLAPASPAREGSPTPPGPSSPDPPPPTPPP-ASPPPSPAPDLSEMLRPVGSPGPPP 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 19112658   460 QTTTIQTSREVAPPPSSINSNRAASPF-------RPTSVSPQPSSPTKSLLFGAR 507
Cdd:PHA03307  149 AASPPAAGASPAAVASDAASSRQAALPlsspeetARAPSSPPAEPPPSTPPAAAS 203
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
336-498 7.77e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 39.75  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   336 PPSSYGTGSSAGKTNPPVNPTikvtAAIPSPLQNTNPAPSTFPNPSVASPA----FPNSSTSNPSTAPASASPLASTLKP 411
Cdd:pfam03154 294 PPQPFPLTPQSSQSQVPPGPS----PAAPGQSQQRIHTPPSQSQLQSQQPPreqpLPPAPLSMPHIKPPPTTPIPQLPNP 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112658   412 ST----ANDTNGSSSSSSSN---PRTSSPLASNAENKPPVA-----------QQSPPVLLPTLPPIQTTTIQTSREVAPP 473
Cdd:pfam03154 370 QShkhpPHLSGPSPFQMNSNlppPPALKPLSSLSTHHPPSAhppplqlmpqsQQLPPPPAQPPVLTQSQSLPPPAASHPP 449
                         170       180
                  ....*....|....*....|....*
gi 19112658   474 PSSINSNRAASPFRPTSVSPQPSSP 498
Cdd:pfam03154 450 TSGLHQVPSQSPFPQHPFVPGGPPP 474
 
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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