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Conserved domains on  [gi|528470586|ref|XP_005163371|]
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rho GTPase-activating protein 29 isoform X2 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 729-939 1.36e-133

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: 408.04  E-value: 1.36e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLR 808
Cdd:cd04409     1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  809 QLPEPLILYRYYNDVIGLAKETQNMDKTDSAKEKSAGEQLGLSTELKRVLFKVRDLLRQLPAPHYKTLQFLVTHLHRVSE 888
Cdd:cd04409    81 QLPEPLILFRLYNEFIGLAKESQHVNETQEAKKNSDKKWPNMCTELNRILLKSKDLLRQLPAPNYNTLQFLIVHLHRVSE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528470586  889 QAEENKMTASNLGIIFGPTLIKPRHLEAEVSLSSLVDYPHQARMVELLIKH 939
Cdd:cd04409   161 QAEENKMSASNLGIIFGPTLIRPRPTDATVSLSSLVDYPHQARLVELLITY 211
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
 672-721 2.70e-28

protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP)-like family; The GMIP-like family includes GMIP, Rho GTPase-activating protein 29 (ARHGAP29) and Rho GTPase-activating protein 45 (ARHGAP45). GMIP is a RhoA-specific GTPase-activating protein that acts as a key factor in saltatory neuronal migration. It associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. ARHGAP29, also called PTPL1-associated RhoGAP protein 1 (PARG1) or Rho-type GTPase-activating protein 29, is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. It has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. ARHGAP29 may act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, ARHGAP29 suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. ARHGAP45, also called minor histocompatibility antigen HA-1 (mHag HA-1), is a Rac-GAP (GTPase-Activating Protein) in endothelial cells. It acts as a novel regulator of endothelial integrity. ARHGAP45 contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, it also contains N-terminally a BAR-domin which can play an autoinhibitory effect on this RhoGAP activity. Members of this family contain a zinc-binding C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410366  Cd Length: 51  Bit Score: 108.11  E-value: 2.70e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  672 THKLRKLRAPSKCRECDSLVVFHGAECEECSLACHKKCLETLAIQCGHKK 721
Cdd:cd20816     2 THRFRRLRTPSKCRECDSYVYFNGAECEECGLACHKKCLETLAIQCGHKR 51
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 247-460 8.10e-07

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


The actual alignment was detected with superfamily member cd07652:

Pssm-ID: 472257 [Multi-domain]  Cd Length: 234  Bit Score: 51.58  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  247 KDVLAWVEKRLSLDMECAKSFAKMAESAKAVASQQDFMPfrDIYVSAFKNEIEYNHVLLQTAAALQT--NKFTQPLLARK 324
Cdd:cd07652    22 KEFATFLKKRAAIEEEHARGLKKLARTTLDTYKRPDHKQ--GSFSNAYHSSLEFHEKLADNGLRFAKalNEMSDELSSLA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  325 NDLDKQRKEIKEQWQRELKKMNESESALKKARLLKMQKREEYEKARSSTSRTEEEQPAAGGRTLEKKrrvEEEALQKAEE 404
Cdd:cd07652   100 KTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDLERVKTGDPGKKLKFGLKGNKSAAQH---EDELLRKVQA 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528470586  405 AQEQYKACVADLEA-KKVSLSNAKSEILAQIRKLVFQCDLTLKAvtvnwfQMQQAQT 460
Cdd:cd07652   177 ADQDYASKVNAAQAlRQELLSRHRPEAVKDLFDLILEIDAALRL------QYQKYAL 227
 
Name Accession Description Interval E-value
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 729-939 1.36e-133

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: 408.04  E-value: 1.36e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLR 808
Cdd:cd04409     1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  809 QLPEPLILYRYYNDVIGLAKETQNMDKTDSAKEKSAGEQLGLSTELKRVLFKVRDLLRQLPAPHYKTLQFLVTHLHRVSE 888
Cdd:cd04409    81 QLPEPLILFRLYNEFIGLAKESQHVNETQEAKKNSDKKWPNMCTELNRILLKSKDLLRQLPAPNYNTLQFLIVHLHRVSE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528470586  889 QAEENKMTASNLGIIFGPTLIKPRHLEAEVSLSSLVDYPHQARMVELLIKH 939
Cdd:cd04409   161 QAEENKMSASNLGIIFGPTLIRPRPTDATVSLSSLVDYPHQARLVELLITY 211
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 744-940 5.01e-54

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: 186.32  E-value: 5.01e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586    744 IPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLV-ELSDLHPHDISNVLKLYLRQLPEPLILYRYYND 822
Cdd:smart00324    3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDlDLSEYDVHDVAGLLKLFLRELPEPLITYELYEE 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586    823 VIGLAKEtqnmdktDSAKEKSAGeqlglstelkrvlfkVRDLLRQLPAPHYKTLQFLVTHLHRVSEQAEENKMTASNLGI 902
Cdd:smart00324   83 FIEAAKL-------EDETERLRA---------------LRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAI 140

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 528470586    903 IFGPTLIKPRHLEAEvslsSLVDYPHQARMVELLIKHH 940
Cdd:smart00324  141 VFGPTLLRPPDGEVA----SLKDIRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 745-913 2.35e-49

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 171.96  E-value: 2.35e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   745 PFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLH-PHDISNVLKLYLRQLPEPLILYRYYNDV 823
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEEdVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   824 IglaketqnmdktDSAKEKSAGEQLGlstelkrvlfKVRDLLRQLPAPHYKTLQFLVTHLHRVSEQAEENKMTASNLGII 903
Cdd:pfam00620   81 I------------EAAKLPDEEERLE----------ALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIV 138

                          170
                   ....*....|
gi 528470586   904 FGPTLIKPRH 913
Cdd:pfam00620  139 FGPTLLRPPD 148
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
 672-721 2.70e-28

protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP)-like family; The GMIP-like family includes GMIP, Rho GTPase-activating protein 29 (ARHGAP29) and Rho GTPase-activating protein 45 (ARHGAP45). GMIP is a RhoA-specific GTPase-activating protein that acts as a key factor in saltatory neuronal migration. It associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. ARHGAP29, also called PTPL1-associated RhoGAP protein 1 (PARG1) or Rho-type GTPase-activating protein 29, is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. It has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. ARHGAP29 may act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, ARHGAP29 suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. ARHGAP45, also called minor histocompatibility antigen HA-1 (mHag HA-1), is a Rac-GAP (GTPase-Activating Protein) in endothelial cells. It acts as a novel regulator of endothelial integrity. ARHGAP45 contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, it also contains N-terminally a BAR-domin which can play an autoinhibitory effect on this RhoGAP activity. Members of this family contain a zinc-binding C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410366  Cd Length: 51  Bit Score: 108.11  E-value: 2.70e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  672 THKLRKLRAPSKCRECDSLVVFHGAECEECSLACHKKCLETLAIQCGHKK 721
Cdd:cd20816     2 THRFRRLRTPSKCRECDSYVYFNGAECEECGLACHKKCLETLAIQCGHKR 51
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 671-717 6.17e-09

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 52.86  E-value: 6.17e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 528470586    671 HTHKLRKLRAPSKCRECDSLVVF---HGAECEECSLACHKKCLETLAIQC 717
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGsfkQGLRCSECKVKCHKKCADKVPKAC 50
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 247-460 8.10e-07

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: 51.58  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  247 KDVLAWVEKRLSLDMECAKSFAKMAESAKAVASQQDFMPfrDIYVSAFKNEIEYNHVLLQTAAALQT--NKFTQPLLARK 324
Cdd:cd07652    22 KEFATFLKKRAAIEEEHARGLKKLARTTLDTYKRPDHKQ--GSFSNAYHSSLEFHEKLADNGLRFAKalNEMSDELSSLA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  325 NDLDKQRKEIKEQWQRELKKMNESESALKKARLLKMQKREEYEKARSSTSRTEEEQPAAGGRTLEKKrrvEEEALQKAEE 404
Cdd:cd07652   100 KTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDLERVKTGDPGKKLKFGLKGNKSAAQH---EDELLRKVQA 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528470586  405 AQEQYKACVADLEA-KKVSLSNAKSEILAQIRKLVFQCDLTLKAvtvnwfQMQQAQT 460
Cdd:cd07652   177 ADQDYASKVNAAQAlRQELLSRHRPEAVKDLFDLILEIDAALRL------QYQKYAL 227
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 671-718 1.08e-06

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 46.67  E-value: 1.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 528470586   671 HTHKLRKLRAPSKCRECDSLV---VFHGAECEECSLACHKKCLETLAIQCG 718
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLwglGKQGLKCSWCKLNVHKRCHEKVPPECG 51
PTZ00121 PTZ00121
MAEBL; Provisional
 322-521 2.26e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  322 ARKNDLDKQRKEIKEQWQRELKKMNESEsalKKARLLKmqKREEYEKArSSTSRTEEEQPAAGGRTLEKKRRVEEeaLQK 401
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAK---KKADEAK--KAEEAKKA-DEAKKAEEAKKADEAKKAEEKKKADE--LKK 1553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  402 AEE---AQEQYKACVADLEAKKVSLSNAKSEILAQIRKlvfqcdltlkavtvnwfqMQQAQTMPLSVNYQAL-SEQAKKY 477
Cdd:PTZ00121 1554 AEElkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE------------------ARIEEVMKLYEEEKKMkAEEAKKA 1615

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 528470586  478 EPGQRYSEFVRSLPKERVWLESLSQDITASSKTGMSLHKRSQNS 521
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 320-437 5.78e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.07  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  320 LLARKNDLDKQRKEIKEQWQRELKKMNESESALKKARLLKMQKREEYEKARSSTSRTEEEQPAAGGR-----------TL 388
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkeieSL 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528470586  389 EKKRRVEE----EALQKAEEAQEQYKACVADLEAKKVSLSNAKSEILAQIRKL 437
Cdd:COG1579   102 KRRISDLEdeilELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 299-433 2.86e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.84  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   299 EYNHVLLQTAAALQTNKFTQPLLARKNDLDKQRKEIKEQWQRELKKMNESESALKKA-----RLLKMQKREEYEKARSST 373
Cdd:TIGR02794   51 QANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAeqaakQAEEKQKQAEEAKAKQAA 130

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528470586   374 SRTEEEQPAAGGRTLEK-KRRVEEEALQKAE-----EAQEQYKACVADLEAKKVSLSNAKSEILAQ 433
Cdd:TIGR02794  131 EAKAKAEAEAERKAKEEaAKQAEEEAKAKAAaeakkKAEEAKKKAEAEAKAKAEAEAKAKAEEAKA 196
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 309-426 9.96e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 43.45  E-value: 9.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   309 AALQTNKFTQPLLARKNDLDKQRKEIKEQWQRE--LKKMNESESALKKARLLKMQKREEYEKARSSTSRTEEEQPAAGGR 386
Cdd:pfam05262  225 KQIDADKAQQKADFAQDNADKQRDEVRQKQQEAknLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHK 304

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 528470586   387 TLEKKRRV---EEEALQKAEEAQEQYKACVADL-------EAKKVSLSNA 426
Cdd:pfam05262  305 AFDLKQESkasEKEAEDKELEAQKKREPVAEDLqktkpqvEAQPTSLNED 354
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 227-282 1.42e-03

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: 38.86  E-value: 1.42e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 528470586    227 KNDSGVESALLYAKAWSKYTKDVLAWVEKRLSLDMECAKSFAKMAESAKAVASQQD 282
Cdd:smart00055    6 ELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAVRDTEP 61
 
Name Accession Description Interval E-value
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 729-939 1.36e-133

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: 408.04  E-value: 1.36e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLR 808
Cdd:cd04409     1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  809 QLPEPLILYRYYNDVIGLAKETQNMDKTDSAKEKSAGEQLGLSTELKRVLFKVRDLLRQLPAPHYKTLQFLVTHLHRVSE 888
Cdd:cd04409    81 QLPEPLILFRLYNEFIGLAKESQHVNETQEAKKNSDKKWPNMCTELNRILLKSKDLLRQLPAPNYNTLQFLIVHLHRVSE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528470586  889 QAEENKMTASNLGIIFGPTLIKPRHLEAEVSLSSLVDYPHQARMVELLIKH 939
Cdd:cd04409   161 QAEENKMSASNLGIIFGPTLIRPRPTDATVSLSSLVDYPHQARLVELLITY 211
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 729-939 1.17e-128

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: 394.48  E-value: 1.17e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLR 808
Cdd:cd04378     1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  809 QLPEPLILYRYYNDVIGLAKETQNMDKTDsakeksagEQLGLSTELKRVLFKVRDLLRQLPAPHYKTLQFLVTHLHRVSE 888
Cdd:cd04378    81 QLPEPLILFRLYNDFIALAKEIQRDTEED--------KAPNTPIEVNRIIRKLKDLLRQLPASNYNTLQHLIAHLYRVAE 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528470586  889 QAEENKMTASNLGIIFGPTLIKPRHLEAEVSLSSLVDYPHQARMVELLIKH 939
Cdd:cd04378   153 QFEENKMSPNNLGIVFGPTLIRPRPGDADVSLSSLVDYGYQARLVEFLITN 203
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 729-939 4.44e-75

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: 247.42  E-value: 4.44e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLR 808
Cdd:cd04408     1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  809 QLPEPLILYRYYNDVIGLAKETQNmDKTDSAKEKSAGEQlglstelkrVLFKVRDLLRQLPAPHYKTLQFLVTHLHRVSE 888
Cdd:cd04408    81 ELPEPVLPFQLYDDFIALAKELQR-DSEKAAESPSIVEN---------IIRSLKELLGRLPVSNYNTLRHLMAHLYRVAE 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528470586  889 QAEENKMTASNLGIIFGPTLIKPRhLEAEVSLSSLVDYPHQARMVELLIKH 939
Cdd:cd04408   151 RFEDNKMSPNNLGIVFGPTLLRPL-VGGDVSMICLLDTGYQAQLVEFLISN 200
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 744-940 5.01e-54

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: 186.32  E-value: 5.01e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586    744 IPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLV-ELSDLHPHDISNVLKLYLRQLPEPLILYRYYND 822
Cdd:smart00324    3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDlDLSEYDVHDVAGLLKLFLRELPEPLITYELYEE 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586    823 VIGLAKEtqnmdktDSAKEKSAGeqlglstelkrvlfkVRDLLRQLPAPHYKTLQFLVTHLHRVSEQAEENKMTASNLGI 902
Cdd:smart00324   83 FIEAAKL-------EDETERLRA---------------LRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAI 140

                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 528470586    903 IFGPTLIKPRHLEAEvslsSLVDYPHQARMVELLIKHH 940
Cdd:smart00324  141 VFGPTLLRPPDGEVA----SLKDIRHQNTVIEFLIENA 174
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 745-939 4.50e-53

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: 183.27  E-value: 4.50e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  745 PFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLRQLPEPLILYRYYNDVI 824
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  825 GLAKETQNMDKTDSAKEksageqlglstelkrvlfkvrdLLRQLPAPHYKTLQFLVTHLHRVSEQAEENKMTASNLGIIF 904
Cdd:cd00159    81 ELAKIEDEEERIEALKE----------------------LLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVF 138

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 528470586  905 GPTLIKPRHLeaevSLSSLVDYPHQARMVELLIKH 939
Cdd:cd00159   139 APTLLRPPDS----DDELLEDIKKLNEIVEFLIEN 169
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 745-913 2.35e-49

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 171.96  E-value: 2.35e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   745 PFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLH-PHDISNVLKLYLRQLPEPLILYRYYNDV 823
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEEdVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   824 IglaketqnmdktDSAKEKSAGEQLGlstelkrvlfKVRDLLRQLPAPHYKTLQFLVTHLHRVSEQAEENKMTASNLGII 903
Cdd:pfam00620   81 I------------EAAKLPDEEERLE----------ALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIV 138

                          170
                   ....*....|
gi 528470586   904 FGPTLIKPRH 913
Cdd:pfam00620  139 FGPTLLRPPD 148
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 729-944 8.97e-43

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: 154.98  E-value: 8.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHD---ISNVLKL 805
Cdd:cd04372     1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVYPDinvITGALKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  806 YLRQLPEPLILYRYYNDVIglaketqnmdktDSAKEKSAGEQLGLstelkrvlfkVRDLLRQLPAPHYKTLQFLVTHLHR 885
Cdd:cd04372    81 YFRDLPIPVITYDTYPKFI------------DAAKISNPDERLEA----------VHEALMLLPPAHYETLRYLMEHLKR 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 528470586  886 VSEQAEENKMTASNLGIIFGPTLIKPRHLEAevsLSSLVDYPHQARMVELLIKHHQMIF 944
Cdd:cd04372   139 VTLHEKDNKMNAENLGIVFGPTLMRPPEDSA---LTTLNDMRYQILIVQLLITNEDVLF 194
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 744-944 1.53e-40

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: 148.70  E-value: 1.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  744 IPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHD---ISNVLKLYLRQLPEPLILYRYY 820
Cdd:cd04395    18 VPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDPRWRDvnvVSSLLKSFFRKLPEPLFTNELY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  821 NDVIglaketqNMDKTDSAKEKsageqlglstelkrvLFKVRDLLRQLPAPHYKTLQFLVTHLHRVSEQAEENKMTASNL 900
Cdd:cd04395    98 PDFI-------EANRIEDPVER---------------LKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 528470586  901 GIIFGPTLIKPrhleAEVSLSSLV-DYPHQARMVELLIKHHQMIF 944
Cdd:cd04395   156 AIVFGPTLVRT----SDDNMETMVtHMPDQCKIVETLIQHYDWFF 196
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 747-939 4.40e-39

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: 144.46  E-value: 4.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  747 IIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELS-DLHPHD-----ISNVLKLYLRQLPEPLILYRYY 820
Cdd:cd04374    31 FVRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGLDPKTSTPGDvDLDNSEweiktITSALKTYLRNLPEPLMTYELH 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  821 NDVIGLAK-ETQNMdktdsakeksageqlglstelkRVlFKVRDLLRQLPAPHYKTLQFLVTHLHRVSEQAEENKMTASN 899
Cdd:cd04374   111 NDFINAAKsENLES----------------------RV-NAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSN 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 528470586  900 LGIIFGPTLIKPRhleaEVSLSSLVDYPHQARMVELLIKH 939
Cdd:cd04374   168 LGVVFGPTLLRPQ----EETVAAIMDIKFQNIVVEILIEN 203
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 740-939 4.53e-38

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: 140.91  E-value: 4.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  740 SPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVEL--SDLHPHDISNVLKLYLRQLPEPL--- 814
Cdd:cd04385    11 TDNDIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLreGEYTVHDVADVLKRFLRDLPDPLlts 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  815 ILYRYYNDVIGLAKETQNMDKtdsakeksageqlglstelkrvlfkVRDLLRQLPAPHYKTLQFLVTHLHRVSEQAEENK 894
Cdd:cd04385    91 ELHAEWIEAAELENKDERIAR-------------------------YKELIRRLPPINRATLKVLIGHLYRVQKHSDENQ 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 528470586  895 MTASNLGIIFGPTLIKPRHLEAEvslsslvDYPHQARMVELLIKH 939
Cdd:cd04385   146 MSVHNLALVFGPTLFQTDEHSVG-------QTSHEVKVIEDLIDN 183
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 729-937 6.33e-36

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: 134.83  E-value: 6.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKL-CQAFENGK---DLVELSDLHPhdISNVLK 804
Cdd:cd04403     1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLrFAVDHDEKldlDDSKWEDIHV--ITGALK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  805 LYLRQLPEPLILYRYYNDVIGLAKETQNMDKtdsakeksageqlglstelkrvLFKVRDLLRQLPAPHYKTLQFLVTHLH 884
Cdd:cd04403    79 LFFRELPEPLFPYSLFNDFVAAIKLSDYEQR----------------------VSAVKDLIKSLPKPNHDTLKMLFRHLC 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528470586  885 RVSEQAEENKMTASNLGIIFGPTLIKPRHLEAEVSLSSLvdYPHQArmVELLI 937
Cdd:cd04403   137 RVIEHGEKNRMTTQNLAIVFGPTLLRPEQETGNIAVHMV--YQNQI--VELIL 185
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 729-944 5.86e-35

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: 132.53  E-value: 5.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVEL--SDLHPHDISNV---L 803
Cdd:cd04398     1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLisPEDYESDIHSVaslL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  804 KLYLRQLPEPLILYRYYNDVIGLAKETQNMDKTDsakeksageqlglstelkrvlfKVRDLLRQLPAPHYKTLQFLVTHL 883
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRD----------------------ALHGLINDLPDANYATLRALMFHL 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528470586  884 HRVSEQAEENKMTASNLGIIFGPTLIKprhleaeVSLSSLVDYPHQARMVELLIKHHQMIF 944
Cdd:cd04398   139 ARIKEHESVNRMSVNNLAIIWGPTLMN-------AAPDNAADMSFQSRVIETLLDNAYQIF 192
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 727-944 2.52e-33

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: 127.84  E-value: 2.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  727 HLFGIDFAQVVKNSP--DGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDlVELSDLH-PHDISNVL 803
Cdd:cd04404     4 QQFGVSLQFLKEKNPeqEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEP-VDFDQYEdVHLPAVIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  804 KLYLRQLPEPLILYRYYNDVIGLaketQNMDKTDSAKEksageqlglstelkrvlfkVRDLLRQLPAPHYKTLQFLVTHL 883
Cdd:cd04404    83 KTFLRELPEPLLTFDLYDDIVGF----LNVDKEERVER-------------------VKQLLQTLPEENYQVLKYLIKFL 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528470586  884 HRVSEQAEENKMTASNLGIIFGPTLIKPRhlEAEVSLSSLVdyPHQArMVELLIKHHQMIF 944
Cdd:cd04404   140 VQVSAHSDQNKMTNSNLAVVFGPNLLWAK--DASMSLSAIN--PINT-FTKFLLDHQDEIF 195
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 729-925 2.45e-32

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: 125.04  E-value: 2.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFE-NGKD-LVELSDLHPHDISNVLKLY 806
Cdd:cd04387     1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDtNNKDvSVMLSEMDVNAIAGTLKLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  807 LRQLPEPLILYRYYNDVIGlaketqNMDKTDSAKEKSAgeqlglstelkrvlfkVRDLLRQLPAPHYKTLQFLVTHLHRV 886
Cdd:cd04387    81 FRELPEPLFTDELYPNFAE------GIALSDPVAKESC----------------MLNLLLSLPDPNLVTFLFLLHHLKRV 138

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 528470586  887 SEQAEENKMTASNLGIIFGPTLIKPRHLEAEVSLSSLVD 925
Cdd:cd04387   139 AEREEVNKMSLHNLATVFGPTLLRPSEKESKIPTNTMTD 177
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 744-938 2.47e-31

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: 122.02  E-value: 2.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  744 IPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLRQLPEPLILYRYYNDv 823
Cdd:cd04382    17 IPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSLKEPLITFALWKE- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  824 igLAKETQNMDKTDSakeksageqlglSTELKRVlfkvrdlLRQLPAPHYKTLQFLVTHLHRVSeQAEENKMTASNLGII 903
Cdd:cd04382    96 --FMEAAEILDEDNS------------RAALYQA-------ISELPQPNRDTLAFLILHLQRVA-QSPECKMDINNLARV 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 528470586  904 FGPTLIKprHLEAEVS-LSSLVDYPHQARMVELLIK 938
Cdd:cd04382   154 FGPTIVG--YSVPNPDpMTILQDTVRQPRVVERLLE 187
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 729-916 4.31e-31

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: 121.46  E-value: 4.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDGIPFIIKKCTSEIESRALtIKGIYRVNGAKSRVEKLCQAFENGK--DLVELSDLHP-HDISNVLKL 805
Cdd:cd04384     3 FGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGI-VDGIYRLSGIASNIQRLRHEFDSEQipDLTKDVYIQDiHSVSSLCKL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  806 YLRQLPEPLILYRYYNDVIglaketqnmdktDSAKEKSAGEQLglstelkrvlFKVRDLLRQLPAPHYKTLQFLVTHLHR 885
Cdd:cd04384    82 YFRELPNPLLTYQLYEKFS------------EAVSAASDEERL----------EKIHDVIQQLPPPHYRTLEFLMRHLSR 139

                         170       180       190
                  ....*....|....*....|....*....|.
gi 528470586  886 VSEQAEENKMTASNLGIIFGPTLIKPRHLEA 916
Cdd:cd04384   140 LAKYCSITNMHAKNLAIVWAPNLLRSKQIES 170
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 744-947 8.10e-30

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: 117.93  E-value: 8.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  744 IPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLRQLPEPLILYRYYNDV 823
Cdd:cd04376     9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  824 IGLAKetqnmdktdsakeKSAGEQLGlstelkrvlfKVRDLLRQLPAPHYKTLQFLVTHLHRVSEQAEE----------- 892
Cdd:cd04376    89 IGTAL-------------LEPDEQLE----------ALQLLIYLLPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsg 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528470586  893 NKMTASNLGIIFGPTL---IKPRHLEAEVSLSSLVDYPHQARMVELLIKHHQMIFDVP 947
Cdd:cd04376   146 NKMTSLNLATIFGPNLlhkQKSGEREFVQASLRIEESTAIINVVQTMIDNYEELFMVS 203
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 729-938 8.36e-30

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: 117.15  E-value: 8.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSpDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLR 808
Cdd:cd04377     1 FGVSLSSLTSED-RSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  809 QLPEPLILYRYYNDVIGlAKETQNMdktdsakeksaGEQLglstelkRVLFKVrdlLRQLPAPHYKTLQFLVTHLHRVSE 888
Cdd:cd04377    80 ELPEPLMTFELYENFLR-AMELEEK-----------QERV-------RALYSV---LEQLPRANLNTLERLIFHLVRVAL 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  889 QAEENKMTASNLGIIFGPTLIkpRHLEAEVSLSSLVDYPHQARMVELLIK 938
Cdd:cd04377   138 QEEVNRMSANALAIVFAPCIL--RCPDTADPLQSLQDVSKTTTCVETLIK 185
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 729-945 1.13e-28

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: 114.86  E-value: 1.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLH--PHDISNVLKLY 806
Cdd:cd04386     5 FGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFYsdPHAVASALKSY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  807 LRQLPEPLILYRYYNDVIglaketQNMDKTDSAKEKSAgeqlglstelkrvlfkVRDLLRQLPAPHYKTLQFLVTHLHRV 886
Cdd:cd04386    85 LRELPDPLLTYNLYEDWV------QAANKPDEDERLQA----------------IWRILNKLPRENRDNLRYLIKFLSKL 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 528470586  887 SEQAEENKMTASNLGIIFGPTLIKPRHlEAEVSLSSLVDYPHQARMVELLIKHHQMIFD 945
Cdd:cd04386   143 AQKSDENKMSPSNIAIVLAPNLLWAKN-EGSLAEMAAGTSVHVVAIVELIISHADWFFP 200
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
 672-721 2.70e-28

protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP)-like family; The GMIP-like family includes GMIP, Rho GTPase-activating protein 29 (ARHGAP29) and Rho GTPase-activating protein 45 (ARHGAP45). GMIP is a RhoA-specific GTPase-activating protein that acts as a key factor in saltatory neuronal migration. It associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. ARHGAP29, also called PTPL1-associated RhoGAP protein 1 (PARG1) or Rho-type GTPase-activating protein 29, is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. It has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. ARHGAP29 may act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, ARHGAP29 suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. ARHGAP45, also called minor histocompatibility antigen HA-1 (mHag HA-1), is a Rac-GAP (GTPase-Activating Protein) in endothelial cells. It acts as a novel regulator of endothelial integrity. ARHGAP45 contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, it also contains N-terminally a BAR-domin which can play an autoinhibitory effect on this RhoGAP activity. Members of this family contain a zinc-binding C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410366  Cd Length: 51  Bit Score: 108.11  E-value: 2.70e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  672 THKLRKLRAPSKCRECDSLVVFHGAECEECSLACHKKCLETLAIQCGHKK 721
Cdd:cd20816     2 THRFRRLRTPSKCRECDSYVYFNGAECEECGLACHKKCLETLAIQCGHKR 51
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 729-929 4.01e-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: 109.47  E-value: 4.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVkNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGK--DLVELsDLHPHDISNVLKLY 806
Cdd:cd04373     1 FGVPLANVV-TSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHnlDLVSK-DFTVNAVAGALKSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  807 LRQLPEPLILYRYYNDVIGLAKetqnmdKTDSAKEksageqlglstelkrvLFKVRDLLRQLPAPHYKTLQFLVTHLHRV 886
Cdd:cd04373    79 FSELPDPLIPYSMHLELVEAAK------INDREQR----------------LHALKELLKKFPPENFDVFKYVITHLNKV 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 528470586  887 SEQAEENKMTASNLGIIFGPTLIKP-----RHLEAEVSLSSLVD-YPHQ 929
Cdd:cd04373   137 SQNSKVNLMTSENLSICFWPTLMRPdftsmEALSATRIYQTIIEtFIQQ 185
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 760-947 6.96e-27

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: 109.86  E-value: 6.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  760 LTIKGIYRVNGAKSRVEKLCQAFENGKDL-VELSDLHPHDISNVLKLYLRQLPEPLILYRYYNDVIGLAKETQNMDK--T 836
Cdd:cd04392    24 LRVEGLFRKPGNSARQQELRDLLNSGTDLdLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIADLCQFDEKgnK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  837 DSAKEKsageqlglstelKRVLFKVRDLLRQLPAPHYKTLQFLVTHLHRVSEQAEENKMTASNLGIIFGPTLIKPRHLEA 916
Cdd:cd04392   104 TSAPDK------------ERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPRNLTP 171

                         170       180       190
                  ....*....|....*....|....*....|.
gi 528470586  917 EVSLSSLVdypHQARMVELLIKHHQMIFDVP 947
Cdd:cd04392   172 EDLHENAQ---KLNSIVTFMIKHSQKLFKAP 199
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 729-938 1.39e-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: 105.07  E-value: 1.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSpDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLR 808
Cdd:cd04407     1 FGVRVGSLTSNK-TSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  809 QLPEPLILYRYYNDVIglaketqnmdKTDSAKEKSagEQLglstelkRVLFKVrdlLRQLPAPHYKTLQFLVTHLHRVSE 888
Cdd:cd04407    80 ELPEPLMTFAQYNDFL----------RAVELPEKQ--EQL-------QAIYRV---LEQLPTANHNTLERLIFHLVKVAL 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  889 QAEENKMTASNLGIIFGPTLIkpRHLEAEVSLSSLVDYPHQARMVELLIK 938
Cdd:cd04407   138 EEDVNRMSPNALAIVFAPCLL--RCPDSSDPLTSMKDVAKTTTCVEMLIK 185
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 742-906 4.73e-24

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: 101.00  E-value: 4.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  742 DGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGK--DLVELSDLHPhdISNVLKLYLRQLPEPLILYRY 819
Cdd:cd04393    18 NGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEevDLSKEADVCS--AASLLRLFLQELPEGLIPASL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  820 YNDVIGLAKETQNMDKTDSakeksageqlglstelkrvlfKVRDLLRQLPAPHYKTLQFLVTHLHRVSEQAEENKMTASN 899
Cdd:cd04393    96 QIRLMQLYQDYNGEDEFGR---------------------KLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAEN 154


                  ....*..
gi 528470586  900 LGIIFGP 906
Cdd:cd04393   155 LAAVFGP 161
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 744-944 6.99e-24

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


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 100.60  E-value: 6.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  744 IPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLRQLPEPLILYRYYNDV 823
Cdd:cd04390    22 VPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLLKLYLRELPEPVIPWAQYEDF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  824 IGLAKetqnmdKTDSAKEKSAGEQLglstelkrvlfkvrDLLRQLPAPHYKTLQFLVTHLHRVSEQAEENKMTASNLGII 903
Cdd:cd04390   102 LSCAQ------LLSKDEEKGLGELM--------------KQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 528470586  904 FGPTLIKPRhleAEVSLSSLVDYPHQARMVELLIKHHQMIF 944
Cdd:cd04390   162 FGPNILRPK---VEDPATIMEGTPQIQQLMTVMISKHEPLF 199
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 729-912 1.45e-23

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: 100.23  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDG--IPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELS-DLHP--HDISNVL 803
Cdd:cd04379     1 FGVPLSRLVEREGESrdVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSeELYPdiNVITGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  804 KLYLRQLPEPLILYRYYNDVIGLAKETQNMDKTDSAKEksageqlglstelkrvlfkVRDLLRQLPAPHYKTLQFLVTHL 883
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHL-------------------TLSIIDCLPLSAKATLLLLLDHL 141

                         170       180
                  ....*....|....*....|....*....
gi 528470586  884 HRVSEQAEENKMTASNLGIIFGPTLIKPR 912
Cdd:cd04379   142 SLVLSNSERNKMTPQNLAVCFGPVLMFCS 170
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 729-908 1.81e-23

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: 99.05  E-value: 1.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSP--DGI--PFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFeNGKDLVELSDLHPHDISNVLK 804
Cdd:cd04381     1 FGASLSLAVERSRchDGIdlPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAY-NRRESPNLEEYEPPTVASLLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  805 LYLRQLPEPLI---LYRYYNDVIGLAKETQnmdktdsaKEKsageqlglstELKRvlfkvrdLLRQLPAPHYKTLQFLVT 881
Cdd:cd04381    80 QYLRELPEPLLtkeLMPRFEEACGRPTEAE--------REQ----------ELQR-------LLKELPECNRLLLAWLIV 134

                         170       180
                  ....*....|....*....|....*..
gi 528470586  882 HLHRVSEQAEENKMTASNLGIIFGPTL 908
Cdd:cd04381   135 HMDHVIAQELETKMNIQNISIVLSPTV 161
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 728-909 7.16e-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: 97.49  E-value: 7.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  728 LFGIDFAQVVKNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVElSDLHPHDISN---VLK 804
Cdd:cd04383     2 LFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLA-DDQNDHDINSvagVLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  805 LYLRQLPEPLILYRYYNDVIGLAKetqnmdktdsakeksageqlgLSTELKRVLfKVRDLLRQLPAPHYKTLQFLVTHLH 884
Cdd:cd04383    81 LYFRGLENPLFPKERFEDLMSCVK---------------------LENPTERVH-QIREILSTLPRSVIIVMRYLFAFLN 138

                         170       180
                  ....*....|....*....|....*
gi 528470586  885 RVSEQAEENKMTASNLGIIFGPTLI 909
Cdd:cd04383   139 HLSQFSDENMMDPYNLAICFGPTLM 163
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 728-947 4.70e-22

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: 95.88  E-value: 4.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  728 LFGIDFAQVVKNS---PDG--IPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFEN--GKDLVELSDLHPHDIS 800
Cdd:cd04391     1 LFGVPLSTLLERDqkkVPGskVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAkfYEGTFLWDQVKQHDAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  801 NVLKLYLRQLPEPLILYRYYndviglaKETQNMDKTDSAKEKSAGEQLglstelkrvlfkvrdLLRQLPAPHYKTLQFLV 880
Cdd:cd04391    81 SLLKLFIRELPQPLLTVEYL-------PAFYSVQGLPSKKDQLQALNL---------------LVLLLPEANRDTLKALL 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  881 THLHRVSEQAEENKMTASNLGIIFGPTLIKPRHLEAEVSLSSLVDYPHQA---RMVELLIKHHQMIFDVP 947
Cdd:cd04391   139 EFLQKVVDHEEKNKMNLWNVAMIMAPNLFPPRGKHSKDNESLQEEVNMAAgcaNIMRLLIRYQDLLWTVP 208
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 728-928 2.05e-20

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: 90.50  E-value: 2.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  728 LFGIDFAQVVK-NSPD----GIPFIIKKCTSEIES-RALTIKGIYRVNGAKSRVEKLCQAFENGKD--LVELSDLH-PHD 798
Cdd:cd04400     1 IFGSPLEEAVElSSHKyngrDLPSVVYRCIEYLDKnRAIYEEGIFRLSGSASVIKQLKERFNTEYDvdLFSSSLYPdVHT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  799 ISNVLKLYLRQLPEPLILYRYYNDVIGLAKEtqNMDKTDSAKEksageqlglstelkrvlfkVRDLLRQLPAPHYKTLQF 878
Cdd:cd04400    81 VAGLLKLYLRELPTLILGGELHNDFKRLVEE--NHDRSQRALE-------------------LKDLVSQLPQANYDLLYV 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  879 LVTHLHRVSEQAEENKMTASNLGIIFGPTLIKPrhleAEVSLSSLVDYPH 928
Cdd:cd04400   140 LFSFLRKIIEHSDVNKMNLRNVCIVFSPTLNIP----AGIFVLFLTDFDC 185
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 744-947 2.59e-20

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: 90.61  E-value: 2.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  744 IP-FIIKKCTSeIESRaLTIKGIYRVNGAKSRVEKLCQAFENGKDLveLSDLHPHDISNVLKLYLRQLPEPLILYRYYND 822
Cdd:cd04394    20 VPkFLVDACTF-LLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEAC--LSSALPCDVAGLLKQFFRELPEPLLPYDLHEA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  823 VIglaketqnmdktdSAKEKSAGEQLGLSTELKRVLfkvrdllrqLPAPHYKTLQFLVTHLHRVSEQAEENKMTASNLGI 902
Cdd:cd04394    96 LL-------------KAQELPTDEERKSATLLLTCL---------LPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAV 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 528470586  903 IFGPTLIKPRHLEAEVSLSSLVDYPHQARMVELLIKHHQMIFDVP 947
Cdd:cd04394   154 IFAPNLFQSEEGGEKMSSSTEKRLRLQAAVVQTLIDNASNIGIVP 198
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 729-937 1.00e-19

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


Pssm-ID: 239871  Cd Length: 186  Bit Score: 88.52  E-value: 1.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSpDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLR 808
Cdd:cd04406     1 FGVELSRLTSED-RSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  809 QLPEPLILYRYYNDVIglaketqnmdktdsakeksagEQLGLStELKRVLFKVRDLLRQLPAPHYKTLQFLVTHLHRVSE 888
Cdd:cd04406    80 DLPNPLMTFELYEEFL---------------------RAMGLQ-ERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIAL 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 528470586  889 QAEENKMTASNLGIIFGPTLIkpRHLEAEVSLSSLVDYPHQARMVELLI 937
Cdd:cd04406   138 QEETNRMSANALAIVFAPCIL--RCPDTTDPLQSVQDISKTTTCVELIV 184
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 744-939 9.54e-19

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: 86.70  E-value: 9.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  744 IPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDL---VELSDLHPHDISNVLKLYLRQLPEPLILYRYY 820
Cdd:cd04396    32 IPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDYgksFDWDGYTVHDAASVLRRYLNNLPEPLVPLDLY 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  821 NDVIGLAKEtqnmdKTDSAKEKSAGEQLGLSTELKRVLFKVRDLLRQLPAPHYKTLQFLVTHLHRVSEQAEENKMTASNL 900
Cdd:cd04396   112 EEFRNPLRK-----RPRILQYMKGRINEPLNTDIDQAIKEYRDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNL 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 528470586  901 GIIFGPTLI-KPRHLEA--EVSLSSLVdyphqarmVELLIKH 939
Cdd:cd04396   187 AAIFQPGILsHPDHEMDpkEYKLSRLV--------VEFLIEH 220
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 729-947 1.26e-18

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: 86.32  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  729 FGIDFAQVVKNSPDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDLVELSDLHPHDISNVLKLYLR 808
Cdd:cd04375     5 FGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYFR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  809 QLPEPLIlyryyndviglakeTQNMDKTDSAKEKSageqlgLSTELKRVLFKVRDLLrqLPAPHYKTLQFLVTHLHRVSE 888
Cdd:cd04375    85 DLPEPLL--------------TNKLSETFIAIFQY------VPKEQRLEAVQCAILL--LPDENREVLQTLLYFLSDVAA 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528470586  889 QAEENKMTASNLGIIFGPTLIKPRHLEAEVSLSSLVDY-------PHQARMVE---------LLIKHHQMIFDVP 947
Cdd:cd04375   143 NSQENQMTATNLAVCLAPSLFHLNTSRRENSSPARRMQrkkslgkPDQKELSEnkaahqclaYMIEECNTLFMVP 217
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 728-944 5.59e-17

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


Pssm-ID: 239867  Cd Length: 192  Bit Score: 80.42  E-value: 5.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  728 LFGIDFAQVVKNspDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFENGKDlVELSDLHPHDISNVLKLYL 807
Cdd:cd04402     1 LFGQPLSNICED--DNLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVE-VDLKAEPVLLLASVLKDFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  808 RQLPEPLILYRYYNDVIglaketqnmdktdSAKEKSAGEQLGLStelkrvlfkVRDLLRQLPAPHYKTLQFLVTHLHRVS 887
Cdd:cd04402    78 RNIPGSLLSSDLYEEWM-------------SALDQENEEEKIAE---------LQRLLDKLPRPNVLLLKHLICVLHNIS 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528470586  888 EQAEENKMTASNLGIIFGPTLI-KPRHLEAEVSLSSLVdyphqARMVELLIKHHQMIF 944
Cdd:cd04402   136 QNSETNKMDAFNLAVCIAPSLLwPPASSELQNEDLKKV-----TSLVQFLIENCQEIF 188
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 741-940 4.25e-14

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: 72.60  E-value: 4.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  741 PDGIPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEkLCQAFENGKDLVELSDLHPHDISNVLKLYLRQLPEPLILYRYY 820
Cdd:cd04388    12 PDVAPPLLIKLVEAIEKKGLESSTLYRTQSSSSLTE-LRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  821 NDVIGLAKETQNMDktdsakeksagEQLGLstelkrvlfkVRDLLR--QLPAPHYKTLQFLVTHLHRVSEQAEENKMTAS 898
Cdd:cd04388    91 SEMISRAQEVQSSD-----------EYAQL----------LRKLIRspNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSAR 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 528470586  899 NLGIIFGPTLIKprhleAEVSLSSLVDYPhqARMVELLIKHH 940
Cdd:cd04388   150 ALAEIFSPLLFR-----FQPASSDSPEFH--IRIIEVLITSE 184
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 744-947 1.33e-11

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: 65.46  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  744 IPFIIKKCTSEIESRALTIKGIYRVNGAKSRVEKLCQAFE-NGKDLVELSDLHPHDISNVLKLYLRQLPEPLILYRYYND 822
Cdd:cd04397    27 IPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDkNPTEVPDLSKENPVQLAALLKKFLRELPDPLLTFKLYRL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  823 VIglaketqNMDKTDSAKEKsageqlglstelKRVLFKVRDLlrqLPAPHYKTLQFLVTHLHRV---SEQAEE--NKMTA 897
Cdd:cd04397   107 WI-------SSQKIEDEEER------------KRVLHLVYCL---LPKYHRDTMEVLFSFLKWVssfSHIDEEtgSKMDI 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528470586  898 SNLGIIFGPTLIKPRHLEaevslSSLVDYPHQA-RMVELLIKHHQMIFDVP 947
Cdd:cd04397   165 HNLATVITPNILYSKTDN-----PNTGDEYFLAiEAVNYLIENNEEFCEVP 210
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 764-939 1.77e-10

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: 61.64  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  764 GIYRVNGAKSRVEKLCQAFENGKdlVELSDLH-PHDISNVLKLYLRQLPEPLILYRYYNDVIglaketQNMDKTDSAKEk 842
Cdd:cd04389    42 GIFRVPGDIDEVNELKLRVDQWD--YPLSGLEdPHVPASLLKLWLRELEEPLIPDALYQQCI------SASEDPDKAVE- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  843 sageqlglstelkrvlfkvrdLLRQLPAPHYKTLQFLVTHLHRVSEQA--EENKMTASNLGIIFGPTLIKPRHLEAEVSL 920
Cdd:cd04389   113 ---------------------IVQKLPIINRLVLCYLINFLQVFAQPEnvAHTKMDVSNLAMVFAPNILRCTSDDPRVIF 171

                         170
                  ....*....|....*....
gi 528470586  921 SSLvdyPHQARMVELLIKH 939
Cdd:cd04389   172 ENT---RKEMSFLRTLIEH 187
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 775-944 2.39e-09

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


Pssm-ID: 239864  Cd Length: 212  Bit Score: 58.88  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  775 VEKLCQAFENGKDLVE----LSDLHPHDISNVLKLYLRQLPEPLILYRYYNDVIGLAKETQNMDKTDsakeksageqlgl 850
Cdd:cd04399    53 THQLRNLLNKPKKPDKeviiLKKFEPSTVASVLKLYLLELPDSLIPHDIYDLIRSLYSAYPPSQEDS------------- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  851 stELKRVLfKVRDLLRQLPAPHYKTLQFLVTHLHR---VSEQAEENKMTASNLGIIFGPTLIKPRhleaeVSLSSLVDYP 927
Cdd:cd04399   120 --DTARIQ-GLQSTLSQLPKSHIATLDAIITHFYRlieITKMGESEEEYADKLATSLSREILRPI-----IESLLTIGDK 191

                         170
                  ....*....|....*..
gi 528470586  928 HQARMVELLIKHHQMIF 944
Cdd:cd04399   192 HGYKFFRDLLTHKDQIF 208
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 671-717 6.17e-09

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 52.86  E-value: 6.17e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 528470586    671 HTHKLRKLRAPSKCRECDSLVVF---HGAECEECSLACHKKCLETLAIQC 717
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGsfkQGLRCSECKVKCHKKCADKVPKAC 50
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
 671-719 9.28e-08

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410376  Cd Length: 52  Bit Score: 49.69  E-value: 9.28e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 528470586  671 HTHKLRKLRAPSKCRECDSLVVFHGAECEECSLACHKKCLETLAIQCGH 719
Cdd:cd20826     3 HSFKEKSFRKPRTCDVCKQIIWNEGSSCRVCKYACHRKCEPKVTAACSP 51
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 247-460 8.10e-07

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: 51.58  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  247 KDVLAWVEKRLSLDMECAKSFAKMAESAKAVASQQDFMPfrDIYVSAFKNEIEYNHVLLQTAAALQT--NKFTQPLLARK 324
Cdd:cd07652    22 KEFATFLKKRAAIEEEHARGLKKLARTTLDTYKRPDHKQ--GSFSNAYHSSLEFHEKLADNGLRFAKalNEMSDELSSLA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  325 NDLDKQRKEIKEQWQRELKKMNESESALKKARLLKMQKREEYEKARSSTSRTEEEQPAAGGRTLEKKrrvEEEALQKAEE 404
Cdd:cd07652   100 KTVEKSRKSIKETGKRAEKKVQDAEAAAEKAKARYDSLADDLERVKTGDPGKKLKFGLKGNKSAAQH---EDELLRKVQA 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528470586  405 AQEQYKACVADLEA-KKVSLSNAKSEILAQIRKLVFQCDLTLKAvtvnwfQMQQAQT 460
Cdd:cd07652   177 ADQDYASKVNAAQAlRQELLSRHRPEAVKDLFDLILEIDAALRL------QYQKYAL 227
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 671-718 1.08e-06

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 46.67  E-value: 1.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 528470586   671 HTHKLRKLRAPSKCRECDSLV---VFHGAECEECSLACHKKCLETLAIQCG 718
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLwglGKQGLKCSWCKLNVHKRCHEKVPPECG 51
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 673-717 1.26e-06

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 46.36  E-value: 1.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  673 HKLRK--LRAPSKCRECDSLVVF---HGAECEECSLACHKKCLETLAIQC 717
Cdd:cd00029     1 HRFVPttFSSPTFCDVCGKLIWGlfkQGLKCSDCGLVCHKKCLDKAPSPC 50
PTZ00121 PTZ00121
MAEBL; Provisional
 322-521 2.26e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  322 ARKNDLDKQRKEIKEQWQRELKKMNESEsalKKARLLKmqKREEYEKArSSTSRTEEEQPAAGGRTLEKKRRVEEeaLQK 401
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAK---KKADEAK--KAEEAKKA-DEAKKAEEAKKADEAKKAEEKKKADE--LKK 1553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  402 AEE---AQEQYKACVADLEAKKVSLSNAKSEILAQIRKlvfqcdltlkavtvnwfqMQQAQTMPLSVNYQAL-SEQAKKY 477
Cdd:PTZ00121 1554 AEElkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE------------------ARIEEVMKLYEEEKKMkAEEAKKA 1615

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 528470586  478 EPGQRYSEFVRSLPKERVWLESLSQDITASSKTGMSLHKRSQNS 521
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
 683-717 4.64e-06

first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410372  Cd Length: 52  Bit Score: 44.97  E-value: 4.64e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 528470586  683 KCRECDSLVVFHGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20822    15 RCAVCGEFLVNAGYQCEDCKYTCHKKCYEKVVTKC 49
PRK12704 PRK12704
phosphodiesterase; Provisional
 323-438 1.77e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.01  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  323 RKNDLDKQRKEIKEQWQRELKKMNESESAL-KKARLLKmQKREEYEKARSSTSRTEEEqpaaggrtLEKKRRVEEEALQK 401
Cdd:PRK12704   69 LRNEFEKELRERRNELQKLEKRLLQKEENLdRKLELLE-KREEELEKKEKELEQKQQE--------LEKKEEELEELIEE 139

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 528470586  402 AEEAQEQYKACVADlEAKKVSLSNAKSEILAQIRKLV 438
Cdd:PRK12704  140 QLQELERISGLTAE-EAKEILLEKVEEEARHEAAVLI 175
C1_MRCKalpha cd20864
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
 670-717 3.51e-05

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase alpha (MRCK alpha) and similar proteins; MRCK alpha, also called Cdc42-binding protein kinase alpha, DMPK-like alpha, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK alpha is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410414  Cd Length: 60  Bit Score: 42.70  E-value: 3.51e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528470586  670 AHTHKLRKLRAPSKCRECDSLVV---FHGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20864     2 AHQFVVKSFTTPTKCNQCTSLMVgliRQGCTCEVCGFSCHVTCADKAPSVC 52
PTZ00121 PTZ00121
MAEBL; Provisional
 323-429 4.65e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 4.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  323 RKNDLDKQRKEIKEQWQRELKKmneSESALKKARLLKmQKREEYEKARSSTSRTEEEQPAAGGRTLEKKRRVEEEALQKA 402
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKK---AAAAKKKADEAK-KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466

                          90       100
                  ....*....|....*....|....*..
gi 528470586  403 EEAQEQYKACVADLEAKKVSLSNAKSE 429
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAE 1493
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 320-437 5.78e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 46.07  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  320 LLARKNDLDKQRKEIKEQWQRELKKMNESESALKKARLLKMQKREEYEKARSSTSRTEEEQPAAGGR-----------TL 388
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkeieSL 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528470586  389 EKKRRVEE----EALQKAEEAQEQYKACVADLEAKKVSLSNAKSEILAQIRKL 437
Cdd:COG1579   102 KRRISDLEdeilELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
C1_MRCKgamma cd20866
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
 671-715 6.77e-05

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase gamma (MRCK gamma) and similar proteins; MRCK gamma (MRCKG), also called Cdc42-binding protein kinase gamma, DMPK-like gamma, myotonic dystrophy protein kinase-like gamma, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed in heart and skeletal muscles. It may act as a downstream effector of Cdc42 in cytoskeletal reorganization and contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410416  Cd Length: 52  Bit Score: 41.66  E-value: 6.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 528470586  671 HTHKLRKLRAPSKCRECDSLVV---FHGAECEECSLACHKKCLETLAI 715
Cdd:cd20866     1 HTFKPKTFTSPTKCLRCTSLMVglvRQGLACEACNYVCHVSCAEGAPI 48
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 320-437 7.82e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 7.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  320 LLARKNDLDKQRKEIKEQWQRELKKMNESESALKKARLLKMQKREEYEKARSSTSRTEEEQpaaggRTLEKKRRVEEEAL 399
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL-----ARLEQDIARLEERR 311

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 528470586  400 QKAEEAQEQYKACVADLEAKKVSLSNAKSEILAQIRKL 437
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
 671-718 8.49e-05

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 41.49  E-value: 8.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528470586  671 HTHKLRKLRAPSKCRECDSLVV---FHGAECEECSLACHKKCLETLAIQCG 718
Cdd:cd20809     1 HKFIVRTFSTPTKCNHCTSLMVglvRQGLVCEVCGYACHVSCADKAPQVCP 51
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 322-437 9.63e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.30  E-value: 9.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  322 ARKNDLDKQRKEIK---EQWQRELKKMNESESALKKARLLK-MQKREEYEKARSSTSRTEEeqpaaggrtLEKKRRVEEe 397
Cdd:COG1579    52 TELEDLEKEIKRLEleiEEVEARIKKYEEQLGNVRNNKEYEaLQKEIESLKRRISDLEDEI---------LELMERIEE- 121

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 528470586  398 ALQKAEEAQEQYKACVADLEAKKVSLSNAKSEILAQIRKL 437
Cdd:COG1579   122 LEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
C1_CeDKF1-like_rpt2 cd20798
second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
 671-717 1.17e-04

second protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group contain two copies of the C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410348  Cd Length: 54  Bit Score: 40.95  E-value: 1.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  671 HTHKLRKLRAPSKCRECDSL---VVFHGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20798     2 HTLAEHNYKKPTVCKVCDKLlvgLVRQGLKCRDCGVNVHKKCASLLPSNC 51
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
 670-717 1.41e-04

protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar proteins; Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. This model corresponds to the C1 domain found in TNS1 variant. Typical TNS1 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410438  Cd Length: 57  Bit Score: 41.01  E-value: 1.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 528470586  670 AHTHKLRKLRAPSKCRECDSLVVFHGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20888     5 THTFKVKTFKKVKSCGICKQAITREGSTCRVCKLSCHKKCEAKVATPC 52
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 671-717 1.57e-04

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 40.50  E-value: 1.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  671 HTHKLRKLRAPSKCRECDSLV---VFHGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20837     1 HRFKVYNYMSPTFCDHCGSLLwglFRQGLKCEECGMNVHHKCQKKVANLC 50
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
 669-718 1.66e-04

protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar proteins; Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. This model corresponds to the C1 domain found in TNS3 variant. Typical TNS3 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410439  Cd Length: 56  Bit Score: 40.64  E-value: 1.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  669 AAHTHKLRKLRAPSKCRECDSLVVFHGAECEECSLACHKKCLETLAIQCG 718
Cdd:cd20889     1 SSHTFKNKTFKKPKVCSICKQVIDSQGISCRVCKYACHKKCEAKVVTPCF 50
C1_RASGRP2 cd20861
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 2 ...
 671-717 2.06e-04

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 2 (RASGRP2) and similar proteins; RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. It may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is also involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410411  Cd Length: 56  Bit Score: 40.64  E-value: 2.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  671 HTHKLRKLRAPSKCRECDSLVV---FHGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20861     4 HNFAERTFLRPVACRHCKNLILgiyKQGLKCRACGVNCHKQCKDHLSIEC 53
PTZ00121 PTZ00121
MAEBL; Provisional
 268-570 2.14e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  268 AKMAESAKAVASQ-QDFMPFRDIYVSAFKNEIEYNHVLLQTAAALQTNKFTQPLLARKNDLDKQRKEikeqwqrELKKMN 346
Cdd:PTZ00121 1612 AKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-------EAKKAE 1684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  347 ESESalKKARLLKmQKREEYEKARSSTSRTEEEQpaaggRTLEKKRRVEEEALQKAEEA-----QEQYKA---CVADLEA 418
Cdd:PTZ00121 1685 EDEK--KAAEALK-KEAEEAKKAEELKKKEAEEK-----KKAEELKKAEEENKIKAEEAkkeaeEDKKKAeeaKKDEEEK 1756

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  419 KKVSLSNAKSEILAQIRKLVFQCDLT--LKAVTVNWFQMQQAQTMPLSVNYQALSEQAKKYEPGQRYS-EFVRSLPKERV 495
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIEeeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSkEMEDSAIKEVA 1836

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528470586  496 wlesLSQDITASSKTGMSLHKRSQNSTRSSHGNLSQGSATSMDNHSADEVEgnmqPCKAKIAERRSNSSIDMQVP 570
Cdd:PTZ00121 1837 ----DSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE----IEEADEIEKIDKDDIEREIP 1903
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 671-717 2.41e-04

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 40.31  E-value: 2.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  671 HTHKLRKLRAPSKCRECDSL---VVFHGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20792     2 HKFVATFFKQPTFCSHCKDFiwgLGKQGYQCQVCRFVVHKRCHEYVVFKC 51
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
 671-717 2.69e-04

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 39.96  E-value: 2.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  671 HTHKLRKLRAPSKCRECDSLV--VF-HGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20796     2 HTFVVHTYTKPTVCQHCKKLLkgLFrQGLQCKDCKFNCHKKCAEKVPKDC 51
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
 673-718 2.78e-04

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 40.00  E-value: 2.78e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 528470586  673 HKL-RKLRAPSKCRECDSlVVFHGAECEECSLACHKKCLETLAIQCG 718
Cdd:cd20812     3 HRFsKKLFMRQTCDYCHK-QMFFGLKCKDCKYKCHKKCAKKAPPSCG 48
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 299-433 2.86e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.84  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   299 EYNHVLLQTAAALQTNKFTQPLLARKNDLDKQRKEIKEQWQRELKKMNESESALKKA-----RLLKMQKREEYEKARSST 373
Cdd:TIGR02794   51 QANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAeqaakQAEEKQKQAEEAKAKQAA 130

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528470586   374 SRTEEEQPAAGGRTLEK-KRRVEEEALQKAE-----EAQEQYKACVADLEAKKVSLSNAKSEILAQ 433
Cdd:TIGR02794  131 EAKAKAEAEAERKAKEEaAKQAEEEAKAKAAaeakkKAEEAKKKAEAEAKAKAEAEAKAKAEEAKA 196
C1_Munc13-1 cd20858
protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; ...
 671-717 3.09e-04

protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; Munc13-1, also called protein unc-13 homolog A (Unc13A), is a diacylglycerol (DAG) receptor that plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Loss of MUNC13-1 function causes microcephaly, cortical hyperexcitability, and fatal myasthenia. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410408  Cd Length: 60  Bit Score: 40.07  E-value: 3.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  671 HTHKLRKLRAPSKCRECDSL---VVFHGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20858     8 HNFEVWTATTPTYCYECEGLlwgIARQGMRCTECGVKCHEKCQDLLNADC 57
C1_Myosin-IXa cd20883
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ...
 671-720 5.54e-04

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar proteins; Myosin-IXa, also called unconventional myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation, such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410433  Cd Length: 58  Bit Score: 39.18  E-value: 5.54e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528470586  671 HTHKLRKLRAPSKCRECDSLV--VFHGAECEECSLACHKKCLETLAIQCGHK 720
Cdd:cd20883     6 HIFKSTQYSIPTYCEYCSSLIwmMDRAYVCKLCRYACHKKCCLKTTTKCSKK 57
PTZ00121 PTZ00121
MAEBL; Provisional
 323-559 6.17e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 6.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  323 RKNDLDKQRKEIKEQWQRELKKMNESESALKKARLLKMQKREEYEKARSSTSRTEEEQPAAGGRTLEKKRRVEE----EA 398
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDakrvEI 1156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  399 LQKAEEAQEQYKACVADlEAKKVSLSNAKSEI--LAQIRKlvfqcdltlkavtvnwfqMQQAQTMPLSVNYQAL--SEQA 474
Cdd:PTZ00121 1157 ARKAEDARKAEEARKAE-DAKKAEAARKAEEVrkAEELRK------------------AEDARKAEAARKAEEErkAEEA 1217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  475 KKYEPGQRySEFVRSLPKERvwleSLSQDITASSKTGMSLHKRSQNSTRSSHGNLSQGSATSMDNHSADEVEGNMQPCKA 554
Cdd:PTZ00121 1218 RKAEDAKK-AEAVKKAEEAK----KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292


                  ....*
gi 528470586  555 KIAER 559
Cdd:PTZ00121 1293 DEAKK 1297
C1_Munc13 cd20807
protein kinase C conserved region 1 (C1 domain) found in the Munc13 family; The Munc13 gene ...
 681-717 6.28e-04

protein kinase C conserved region 1 (C1 domain) found in the Munc13 family; The Munc13 gene family encodes a family of neuron-specific, synaptic molecules that bind to syntaxin, an essential mediator of neurotransmitter release. Munc13-1 is a component of presynaptic active zones in which it acts as an essential synaptic vesicle priming protein. Munc13-2 is essential for normal release probability at hippocampal mossy fiber synapses. Munc13-3 is almost exclusively expressed in the cerebellum. It acts as a tumor suppressor and plays a critical role in the formation of release sites with calcium channel nanodomains. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410357  Cd Length: 53  Bit Score: 39.00  E-value: 6.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 528470586  681 PSKCRECDSL---VVFHGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20807    11 PTYCYECEGLlwgIARQGVRCTECGVKCHEKCKDLLNADC 50
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
 671-719 7.38e-04

second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410386  Cd Length: 54  Bit Score: 38.86  E-value: 7.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 528470586  671 HTHKLRKLRAPSKCRECDSLV--VFH-GAECEECSLACHKKCLETLAIQCGH 719
Cdd:cd20836     1 HKFKVHTYSSPTFCDHCGSLLygLIHqGMKCDTCDMNVHKRCVKNVPSLCGT 52
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
 680-718 8.26e-04

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410360  Cd Length: 52  Bit Score: 38.78  E-value: 8.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 528470586  680 APSKCRECDSL---VVFHGAECEECSLACHKKCLETLAiQCG 718
Cdd:cd20810    12 EPTTCSVCKKLlkgLFFQGYKCSVCGAAVHKECIAKVK-RCG 52
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 309-426 9.96e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 43.45  E-value: 9.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   309 AALQTNKFTQPLLARKNDLDKQRKEIKEQWQRE--LKKMNESESALKKARLLKMQKREEYEKARSSTSRTEEEQPAAGGR 386
Cdd:pfam05262  225 KQIDADKAQQKADFAQDNADKQRDEVRQKQQEAknLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHK 304

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 528470586   387 TLEKKRRV---EEEALQKAEEAQEQYKACVADL-------EAKKVSLSNA 426
Cdd:pfam05262  305 AFDLKQESkasEKEAEDKELEAQKKREPVAEDLqktkpqvEAQPTSLNED 354
PTZ00121 PTZ00121
MAEBL; Provisional
 323-429 1.04e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  323 RKNDLDKQRKEIKEQwqRELKKMNESEsalKKARLLKmQKREEYEKARSSTSRTEEEQPAAGGRTLEKKRRVEEEALQKA 402
Cdd:PTZ00121 1419 KADEAKKKAEEKKKA--DEAKKKAEEA---KKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492

                          90       100
                  ....*....|....*....|....*..
gi 528470586  403 EEAQEQYKACVADLEAKKVSLSNAKSE 429
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAE 1519
PTZ00121 PTZ00121
MAEBL; Provisional
 321-429 1.19e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  321 LARKNDLDKQRKEIKEQwqRELKKMNESESALKKARLLKMQKREEYEKARSSTSRTEEEQPA--AGGRTLEKKRRVEE-- 396
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKA--EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdeAKKKAEEDKKKADElk 1411

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 528470586  397 ----------EALQKAEEAQEQYKACVADLEAKKVSLSNAKSE 429
Cdd:PTZ00121 1412 kaaaakkkadEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1454
PTZ00121 PTZ00121
MAEBL; Provisional
 324-437 1.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  324 KNDLDKQRKEIKEQWQRELKKMNESESAlKKARLLKMQKREEYEKArSSTSRTEEEQPAAGGRTLEKKRRVEE------- 396
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMA-HFARRQAAIKAEEARKA-DELKKAEEKKKADEAKKAEEKKKADEakkkaee 1313

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 528470586  397 -----EALQKAEEAQEQYKACVADLEAKKVSLSNAKSEILAQIRKL 437
Cdd:PTZ00121 1314 akkadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA 1359
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 796-911 1.36e-03

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


Pssm-ID: 239845  Cd Length: 220  Bit Score: 41.56  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  796 PHDISNVLKLYLRQLPEPLILYRYYNDVIglaketQNMDKTDSAKeksageqlglstelkrvlfkvRDLLR-QLPAPHYK 874
Cdd:cd04380   104 AESVAEALLLFLESLPDPIIPYSLYERLL------EAVANNEEDK---------------------RQVIRiSLPPVHRN 156

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 528470586  875 TLQFLVTHLHRVSEQAEENKMTASNLGIIFGPTLIKP 911
Cdd:cd04380   157 VFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRD 193
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 227-282 1.42e-03

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: 38.86  E-value: 1.42e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 528470586    227 KNDSGVESALLYAKAWSKYTKDVLAWVEKRLSLDMECAKSFAKMAESAKAVASQQD 282
Cdd:smart00055    6 ELDDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAVRDTEP 61
PTZ00121 PTZ00121
MAEBL; Provisional
 321-436 1.46e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  321 LARKNDLDKQRKEIKEQwqRELKKMNESESALKKARLLKMQKREEYEKArSSTSRTEEEQPAAGGRTLEKKRRVEEE--- 397
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAEEKKKA-DELKKAEELKKAEEKKKAEEAKKAEEDknm 1578

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 528470586  398 ALQKAEEAQEQYKACVADLEAKKVSLSNAKSEilaQIRK 436
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE---EAKK 1614
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
 670-709 1.61e-03

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410374  Cd Length: 53  Bit Score: 37.68  E-value: 1.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 528470586  670 AHTHKLRKLRAPSKCREC-DSL--VVFHGAECEECSLACHKKC 709
Cdd:cd20824     1 PHNFKPHSFSIPTKCDYCgEKIwgLSKKGLSCKDCGFNCHIKC 43
PTZ00121 PTZ00121
MAEBL; Provisional
 323-429 1.80e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  323 RKNDLDKQRKEIKEQWQRELKKMNESesaLKKARLLKMQKREEYEKARSSTSRTEEEQPAAGGRTLEKKRRVEEEALQKA 402
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEE---KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440

                          90       100
                  ....*....|....*....|....*..
gi 528470586  403 EEAQEQYKACVADLEAKKVSLSNAKSE 429
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAE 1467
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
 671-717 1.96e-03

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410381  Cd Length: 58  Bit Score: 37.71  E-value: 1.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528470586  671 HTHKLRKLRAPSKCRECDSLVVF----HGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20831     6 HTFVATHFKGGPSCAVCNKLIPGrfgkQGYQCRDCGLICHKRCHVKVETHC 56
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 327-408 1.98e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.41  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   327 LDKQRKEIKEQWQRELKKMNESESaLKKARLLKMQKREEYEKARsstsRTEEEQPAAggrtlEKKRRVEEEALQKAEEAQ 406
Cdd:pfam05672   16 LAEKRRQAREQREREEQERLEKEE-EERLRKEELRRRAEEERAR----REEEARRLE-----EERRREEEERQRKAEEEA 85


                   ..
gi 528470586   407 EQ 408
Cdd:pfam05672   86 EE 87
3a0801s03tim44 TIGR00984
mitochondrial import inner membrane, translocase subunit; The mitochondrial protein ...
 329-427 2.11e-03

mitochondrial import inner membrane, translocase subunit; The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tim proteins. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 130057 [Multi-domain]  Cd Length: 378  Bit Score: 42.17  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   329 KQRKEIKE---QWQRELKKMNESEsALKKARllkmqkrEEYEKARSSTSRTEEeqpaAGGRTLEKKRRVEEEALQKAEEA 405
Cdd:TIGR00984    8 QKSQELQEsikQLQDRSGKLNESD-ALKKAR-------KAYEKAESGTLKSSE----VVGKTLGKLGDTMKKMAHKAWES 75

                           90       100
                   ....*....|....*....|....*..
gi 528470586   406 QEQYK-----ACVADLEAKKVSLSNAK 427
Cdd:TIGR00984   76 ELGKKmkkagAETAKTAAEHVDKSAEP 102
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
 668-717 2.12e-03

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410393  Cd Length: 79  Bit Score: 38.42  E-value: 2.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528470586  668 KAAHTHKLRKLRAPSKCRECDSLV--VF-HGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20843     9 KVPHTFVIHSYTRPTVCQFCKKLLkgLFrQGLQCKDCKFNCHKRCATRVPNDC 61
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
 680-718 2.13e-03

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410378  Cd Length: 57  Bit Score: 37.81  E-value: 2.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 528470586  680 APSKCRECDSL---VVFHGAECEECSLACHKKCLETLAIQCG 718
Cdd:cd20828    15 TPTNCDYCLQIlwgIVKKGMKCSECGYNCHEKCQPQVPKQCS 56
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
328-578 2.18e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 42.33  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  328 DKQRKEIKEQWQRELKKMN-ESESALKKA--RLLKMQKREEYEKARSST------SRTEEEQPAAGGRTLEKKRRVEEEA 398
Cdd:COG3064    54 EEEAREAKAEAEQRAAELAaEAAKKLAEAekAAAEAEKKAAAEKAKAAKeaeaaaAAEKAAAAAEKEKAEEAKRKAEEEA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  399 LQKAEEAQ---EQYKACVADLEAKKVSLSNAKSEILAQIRKLVFQCDLTLKAVTVNWFQMQQAQTMPLSVNYQALSEQAK 475
Cdd:COG3064   134 KRKAEEERkaaEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  476 KYEPGQRYSEFVRSLPKERVWLESLSQDITASSKTGMSLHKRSQNSTRSSHGNLSQGSATSMDNHSADEVEGNMQPCKAK 555
Cdd:COG3064   214 AALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293

                         250       260
                  ....*....|....*....|...
gi 528470586  556 IAERRSNSSIDMQVPRTQGSQRA 578
Cdd:COG3064   294 GLVLDDSAALAAELLGAVAAEEA 316
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 369-511 2.54e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  369 ARSSTSRTEEEQPAaggRTLEKKR----RVEEEALQKAEEAQEQYKACVADLE--AKKVsLSNAKSEILAQIRKLVFQCD 442
Cdd:PRK00409  523 ASLEELERELEQKA---EEAEALLkeaeKLKEELEEKKEKLQEEEDKLLEEAEkeAQQA-IKEAKKEADEIIKELRQLQK 598

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528470586  443 LTLKAVTVNwfQMQQAQTMpLSVNYQALSEqaKKYEPGQRYSEFVrslPKERVWLESLSQDITASSKTG 511
Cdd:PRK00409  599 GGYASVKAH--ELIEARKR-LNKANEKKEK--KKKKQKEKQEELK---VGDEVKYLSLGQKGEVLSIPD 659
C1_MRCKbeta cd20865
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
 671-709 2.67e-03

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase beta (MRCK beta) and similar proteins; MRCK beta, also called Cdc42-binding protein kinase beta (Cdc42BP-beta), DMPK-like beta, or myotonic dystrophy protein kinase-like beta, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. MRCK beta is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410415  Cd Length: 53  Bit Score: 37.27  E-value: 2.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 528470586  671 HTHKLRKLRAPSKCRECDSLVV---FHGAECEECSLACHKKC 709
Cdd:cd20865     1 HQLSIKSFSSPTQCSHCTSLMVglvRQGYACEVCSFACHVSC 42
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
 671-718 2.84e-03

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, 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; and 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 an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410371  Cd Length: 55  Bit Score: 37.39  E-value: 2.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  671 HTHKLRKLRAPSKCRECDSLVVFHGAE--CEECSLACHKKCLETLAIQCG 718
Cdd:cd20821     3 HRFVSKTVIKPETCVVCGKRIKFGKKAlkCKDCRVVCHPDCKDKLPLPCV 52
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 327-506 2.88e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   327 LDKQRKEIKEQWQRELKKMNESESALKKARLLKMQKREEYEKArsstsrtEEEQPAAGGRTLEKKRRVEEEALQKAEEAQ 406
Cdd:TIGR02169  796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL-------QEQRIDLKEQIKSIEKEIENLNGKKEELEE 868

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   407 E--QYKACVADLEAKKVSLSNAKSEILAQIRKLvfQCDLTLKAVTVNWFQMQQAQtmpLSVNYQALSEQAKKYEP----G 480
Cdd:TIGR02169  869 EleELEAALRDLESRLGDLKKERDELEAQLREL--ERKIEELEAQIEKKRKRLSE---LKAKLEALEEELSEIEDpkgeD 943

                          170       180
                   ....*....|....*....|....*.
gi 528470586   481 QRYSEFVRSLPKERVWLESLSQDITA 506
Cdd:TIGR02169  944 EEIPEEELSLEDVQAELQRVEEEIRA 969
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
314-437 3.00e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  314 NKFTQPLLARKNDLDKQ----RKEIKEqWQRELKKMNESESALK--KARLLKMQKR--------EEYEKARSSTSRTEEE 379
Cdd:PRK03918  299 SEFYEEYLDELREIEKRlsrlEEEING-IEERIKELEEKEERLEelKKKLKELEKRleeleerhELYEEAKAKKEELERL 377

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528470586  380 QPAAGGRTLEKkrrVEEEaLQKAEEAQEQYKACVADLEAKKVSLSNAKSEILAQIRKL 437
Cdd:PRK03918  378 KKRLTGLTPEK---LEKE-LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 671-720 3.12e-03

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 37.25  E-value: 3.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528470586  671 HTHKLRKLRAPSKCRECDSLV---VFHGAECEECSLACHKKCLETLAIQCGHK 720
Cdd:cd20838     3 HRFSVHNYKRPTFCDHCGSLLyglYKQGLQCKVCKMNVHKRCQKNVANNCGVN 55
PRK12472 PRK12472
hypothetical protein; Provisional
 341-429 3.33e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 41.78  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  341 ELKKMNeSESALKKARLLKMQKREEYEKARSSTSRTEEEQPAAGGRTLEKKRRVEE---EALQKAEEAQEQYKACVADLE 417
Cdd:PRK12472  208 EAKTAA-AAAAREAAPLKASLRKLERAKARADAELKRADKALAAAKTDEAKARAEErqqKAAQQAAEAATQLDTAKADAE 286

                          90
                  ....*....|..
gi 528470586  418 AKKVSLSNAKSE 429
Cdd:PRK12472  287 AKRAAAAATKEA 298
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
 668-726 3.48e-03

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410392  Cd Length: 94  Bit Score: 38.07  E-value: 3.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528470586  668 KAAHTHKLRKLRAPSKCRECDSLV--VF-HGAECEECSLACHKKCLETLAIQC-GHKKLQGRL 726
Cdd:cd20842    32 KVPHTFVIHSYTRPTVCQYCKKLLkgLFrQGLQCKDCKFNCHKRCAPKVPNNClGEVAINGDL 94
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 323-433 3.75e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  323 RKNDLDKQRKEIKEQWQRELKKMNESESALKKARLLKMQKREEYEKARSSTSRTEEEQpAAGGRTLEKKRRVEEEALQK- 401
Cdd:PRK09510  117 KKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAE-AAKKAAAEAKKKAEAEAAAKa 195

                          90       100       110
                  ....*....|....*....|....*....|..
gi 528470586  402 AEEAQEQykacvADLEAKKVSLSNAKSEILAQ 433
Cdd:PRK09510  196 AAEAKKK-----AEAEAKKKAAAEAKKKAAAE 222
C1_RASGRP4 cd20863
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 ...
 671-717 4.04e-03

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 (RASGRP4) and similar proteins; RASGRP4 functions as a cation- and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. It may function in mast cell differentiation. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410413  Cd Length: 57  Bit Score: 36.68  E-value: 4.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 528470586  671 HTHKLRKLRAPSKCRECDSL---VVFHGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20863     4 HNFHETTFKKPTFCDSCSGFlwgVTKQGYRCQDCGINCHKHCKDQVDVEC 53
PTZ00121 PTZ00121
MAEBL; Provisional
 268-436 4.21e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  268 AKMAESAKAVASQQDFMPFRDIYVSAFKNEIEYNHVLLQTAAALQTNKFTQPLLARKNDLDKQRKEIKEQwqRELKKMNE 347
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA--EEKKKADE 1294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  348 SESA--LKKARLLKmQKREEYEKARSSTSRTEEEQPAAGG--RTLEKKRRVEEEALQKAEEAQEQYKACVADLEAKKVSL 423
Cdd:PTZ00121 1295 AKKAeeKKKADEAK-KKAEEAKKADEAKKKAEEAKKKADAakKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373

                         170
                  ....*....|...
gi 528470586  424 SNAKSEILAQIRK 436
Cdd:PTZ00121 1374 EEAKKKADAAKKK 1386
C1_Munc13-2-like cd20859
protein kinase C conserved region 1 (C1 domain) found in Munc13-2, Munc13-3 and similar ...
 667-717 4.22e-03

protein kinase C conserved region 1 (C1 domain) found in Munc13-2, Munc13-3 and similar proteins; Munc13-2, also called protein unc-13 homolog B (Unc13B), plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Munc13-2 is essential for normal release probability at hippocampal mossy fiber synapses. Munc13-3 is almost exclusively expressed in the cerebellum. It acts as a tumor suppressor and plays a critical role in the formation of release sites with calcium channel nanodomains. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410409  Cd Length: 82  Bit Score: 37.74  E-value: 4.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528470586  667 SKAAHTHKLRKLRAPSKCRECDSL---VVFHGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20859    16 CTTPHNFEVWTATTPTYCYECEGLlwgIARQGMRCSECGVKCHEKCQDLLNADC 69
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 245-457 5.72e-03

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: 40.02  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  245 YTKDVLAWVEKRLSLDMECAKSFAKMAESAKAVASQQDFMPFRDIyvsaFKNEIE-YNHVLLQTAAALQtnKFTQPLLAR 323
Cdd:cd07648    20 AVKELADFLRERATIEETYSKALNKLAKQASNSSQLGTFAPLWLV----LRVSTEkLSELHLQLVQKLQ--ELIKDVQKY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  324 KNDLDKQRKEIKEQWQREL---KKMNESESALKKARLLKMQKREEYEKARSSTSRTEEeqpaaggrtLEKkrrveeeALQ 400
Cdd:cd07648    94 GEEQHKKHKKVKEEESGTAeavQAIQTTTAALQKAKEAYHARCLELERLRRENASPKE---------IEK-------AEA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528470586  401 KAEEAQEQYKACV-------ADLEAKKVSLSNAKSEI----LAQIRKLVfqcDLTLKAVTVNWFQMQQ 457
Cdd:cd07648   158 KLKKAQDEYKALVekynnirADFETKMTDSCKRFQEIeeshLRQMKEFL---ASYAEVLSENHSAVGQ 222
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
321-485 5.83e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  321 LARKNDLDKQRKEIKEQWQRELKKMNESESALKKARllkmqkrEEYEKARSSTSRTEEEQpaaggRTLEKKRRVEEEALQ 400
Cdd:COG4372    37 LFELDKLQEELEQLREELEQAREELEQLEEELEQAR-------SELEQLEEELEELNEQL-----QAAQAELAQAQEELE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  401 KAEEAQEQYKACVADLEAKKVSLSNAKSEILAQIRKLVFQcdltlkavtvnwFQMQQAQTMPLSVNYQALSEQAKKYEPG 480
Cdd:COG4372   105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE------------IAEREEELKELEEQLESLQEELAALEQE 172


                  ....*
gi 528470586  481 QRYSE 485
Cdd:COG4372   173 LQALS 177
C1_RASGRP1 cd20860
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 ...
 681-720 6.04e-03

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 (RASGRP1) and similar proteins; RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. It activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410410  Cd Length: 55  Bit Score: 36.45  E-value: 6.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 528470586  681 PSKCRECDSL---VVFHGAECEECSLACHKKCLETLAIQCGHK 720
Cdd:cd20860    13 PTFCDNCAGFlwgVIKQGYRCKDCGMNCHKQCKDLVVFECKKR 55
C1_PKD3_rpt2 cd20844
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
 668-717 6.57e-03

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410394  Cd Length: 69  Bit Score: 36.53  E-value: 6.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528470586  668 KAAHTHKLRKLRAPSKCRECDSLV--VF-HGAECEECSLACHKKCLETLAIQC 717
Cdd:cd20844     3 KVPHTFAVHSYTRPTICQYCKRLLkgLFrQGMQCKDCRFNCHKRCASKVPRDC 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 314-434 7.06e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 7.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   314 NKFTQPLLARKNDLDKQRKEIKEQWQRElkkmNESESALKKARllkmQKREEYEKARSSTSRTEEEQPAAGGRTLEKKRR 393
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKI----AELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLAR 737

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 528470586   394 VEEEAlQKAEEAQEQYKACVADLEAKKVSLSNAKSEILAQI 434
Cdd:TIGR02168  738 LEAEV-EQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 299-436 7.55e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 7.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  299 EYNHVLLQTAAALQTNKFTQPLLARKND-----LDKQRKEIKEQWQRELKKMNESESALKKARLLKMQKREEYEKARSST 373
Cdd:PRK09510   63 QYNRQQQQQKSAKRAEEQRKKKEQQQAEelqqkQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAA 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528470586  374 SRTEEEQPAAGGRTLEKKRRVEEEALQKAE-EAQEQYKAcvadlEAKKVSLSNAKSEILAQIRK 436
Cdd:PRK09510  143 AAAKAKAEAEAKRAAAAAKKAAAEAKKKAEaEAAKKAAA-----EAKKKAEAEAAAKAAAEAKK 201
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 320-437 7.69e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  320 LLARKNDLDKQRKEIKEQWQRELKKMNESESAL--KKARLLKMQKREEYEKARSSTSRTEEEQPAAGGRTLEKKRRVEEE 397
Cdd:COG1196   363 AEEALLEAEAELAEAEEELEELAEELLEALRAAaeLAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 528470586  398 ALQKAEEAQEQYKACVADLEAKKVSLSNAKSEILAQIRKL 437
Cdd:COG1196   443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 320-437 7.89e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 7.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586  320 LLARKNDLDKQRKEIKEQwQRELKKMNESESALKKARLLKMQKREEYEKARSSTSRTEEEQpAAGGRTLEKKRRVEEEAL 399
Cdd:COG1196   269 LEELRLELEELELELEEA-QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEEL 346

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 528470586  400 QKAEEAQEQYKACVADLEAKKVSLSNAKSEILAQIRKL 437
Cdd:COG1196   347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 320-437 7.93e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 7.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528470586   320 LLARKNDLDKQRKEIKEQWQRELKKMNESESALKKARLLKMQKRE----------EYEKARSSTSRTEEEQPAAGgrTLE 389
Cdd:TIGR02169  880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAklealeeelsEIEDPKGEDEEIPEEELSLE--DVQ 957

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 528470586   390 KKRRVEEEALQKAEE----AQEQYKACVA---DLEAKKVSLSNAKSEILAQIRKL 437
Cdd:TIGR02169  958 AELQRVEEEIRALEPvnmlAIQEYEEVLKrldELKEKRAKLEEERKAILERIEEY 1012
 
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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